data_3TBJ # _entry.id 3TBJ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3TBJ RCSB RCSB067277 WWPDB D_1000067277 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 3d3z _pdbx_database_related.details . _pdbx_database_related.content_type unspecified # _pdbx_database_status.entry_id 3TBJ _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2011-08-07 _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Almog, O.' 1 'Gonzalez, A.' 2 # _citation.id primary _citation.title 'The 1.8 A crystal structure of ACTIBIND suggests a mode of action for T2 ribonucleases as antitumorigenic agents.' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 55 _citation.page_first 1013 _citation.page_last 1020 _citation.year 2012 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 22216760 _citation.pdbx_database_id_DOI 10.1021/jm1015507 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'de Leeuw, M.' 1 primary 'Gonzalez, A.' 2 primary 'Lanir, A.' 3 primary 'Roiz, L.' 4 primary 'Smirnoff, P.' 5 primary 'Schwartz, B.' 6 primary 'Shoseyov, O.' 7 primary 'Almog, O.' 8 # _cell.entry_id 3TBJ _cell.length_a 78.457 _cell.length_b 78.457 _cell.length_c 103.708 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? # _symmetry.entry_id 3TBJ _symmetry.space_group_name_H-M 'P 32 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 154 # 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 Actibind 26709.584 1 ? ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 3 non-polymer syn 'PHOSPHATE ION' 94.971 2 ? ? ? ? 4 non-polymer syn 1,2-ETHANEDIOL 62.068 3 ? ? ? ? 5 water nat water 18.015 278 ? ? ? ? # _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 ;TIDTCSSDSPLSCQTDNEASCCFNSPGGSLLQTQFWDYDPSDGPSDSWTIHGLWPDNCDGTYQEYCDESREYSNITSILE AQNRTELLSYMKEYWPDYEGADEDESFWEHEWNKHGTCINTIEPSCYTDYYAQEEVGDFFQQVVDLFKTLDSYTALSDAG ITPSEDATYKLSDIEDALAAIHDGYPPYVGCEDGALSQLYYYFNVKGSAIGGTYVASERLEDSNCKDSGIKYPPKYS ; _entity_poly.pdbx_seq_one_letter_code_can ;TIDTCSSDSPLSCQTDNEASCCFNSPGGSLLQTQFWDYDPSDGPSDSWTIHGLWPDNCDGTYQEYCDESREYSNITSILE AQNRTELLSYMKEYWPDYEGADEDESFWEHEWNKHGTCINTIEPSCYTDYYAQEEVGDFFQQVVDLFKTLDSYTALSDAG ITPSEDATYKLSDIEDALAAIHDGYPPYVGCEDGALSQLYYYFNVKGSAIGGTYVASERLEDSNCKDSGIKYPPKYS ; _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 THR n 1 2 ILE n 1 3 ASP n 1 4 THR n 1 5 CYS n 1 6 SER n 1 7 SER n 1 8 ASP n 1 9 SER n 1 10 PRO n 1 11 LEU n 1 12 SER n 1 13 CYS n 1 14 GLN n 1 15 THR n 1 16 ASP n 1 17 ASN n 1 18 GLU n 1 19 ALA n 1 20 SER n 1 21 CYS n 1 22 CYS n 1 23 PHE n 1 24 ASN n 1 25 SER n 1 26 PRO n 1 27 GLY n 1 28 GLY n 1 29 SER n 1 30 LEU n 1 31 LEU n 1 32 GLN n 1 33 THR n 1 34 GLN n 1 35 PHE n 1 36 TRP n 1 37 ASP n 1 38 TYR n 1 39 ASP n 1 40 PRO n 1 41 SER n 1 42 ASP n 1 43 GLY n 1 44 PRO n 1 45 SER n 1 46 ASP n 1 47 SER n 1 48 TRP n 1 49 THR n 1 50 ILE n 1 51 HIS n 1 52 GLY n 1 53 LEU n 1 54 TRP n 1 55 PRO n 1 56 ASP n 1 57 ASN n 1 58 CYS n 1 59 ASP n 1 60 GLY n 1 61 THR n 1 62 TYR n 1 63 GLN n 1 64 GLU n 1 65 TYR n 1 66 CYS n 1 67 ASP n 1 68 GLU n 1 69 SER n 1 70 ARG n 1 71 GLU n 1 72 TYR n 1 73 SER n 1 74 ASN n 1 75 ILE n 1 76 THR n 1 77 SER n 1 78 ILE n 1 79 LEU n 1 80 GLU n 1 81 ALA n 1 82 GLN n 1 83 ASN n 1 84 ARG n 1 85 THR n 1 86 GLU n 1 87 LEU n 1 88 LEU n 1 89 SER n 1 90 TYR n 1 91 MET n 1 92 LYS n 1 93 GLU n 1 94 TYR n 1 95 TRP n 1 96 PRO n 1 97 ASP n 1 98 TYR n 1 99 GLU n 1 100 GLY n 1 101 ALA n 1 102 ASP n 1 103 GLU n 1 104 ASP n 1 105 GLU n 1 106 SER n 1 107 PHE n 1 108 TRP n 1 109 GLU n 1 110 HIS n 1 111 GLU n 1 112 TRP n 1 113 ASN n 1 114 LYS n 1 115 HIS n 1 116 GLY n 1 117 THR n 1 118 CYS n 1 119 ILE n 1 120 ASN n 1 121 THR n 1 122 ILE n 1 123 GLU n 1 124 PRO n 1 125 SER n 1 126 CYS n 1 127 TYR n 1 128 THR n 1 129 ASP n 1 130 TYR n 1 131 TYR n 1 132 ALA n 1 133 GLN n 1 134 GLU n 1 135 GLU n 1 136 VAL n 1 137 GLY n 1 138 ASP n 1 139 PHE n 1 140 PHE n 1 141 GLN n 1 142 GLN n 1 143 VAL n 1 144 VAL n 1 145 ASP n 1 146 LEU n 1 147 PHE n 1 148 LYS n 1 149 THR n 1 150 LEU n 1 151 ASP n 1 152 SER n 1 153 TYR n 1 154 THR n 1 155 ALA n 1 156 LEU n 1 157 SER n 1 158 ASP n 1 159 ALA n 1 160 GLY n 1 161 ILE n 1 162 THR n 1 163 PRO n 1 164 SER n 1 165 GLU n 1 166 ASP n 1 167 ALA n 1 168 THR n 1 169 TYR n 1 170 LYS n 1 171 LEU n 1 172 SER n 1 173 ASP n 1 174 ILE n 1 175 GLU n 1 176 ASP n 1 177 ALA n 1 178 LEU n 1 179 ALA n 1 180 ALA n 1 181 ILE n 1 182 HIS n 1 183 ASP n 1 184 GLY n 1 185 TYR n 1 186 PRO n 1 187 PRO n 1 188 TYR n 1 189 VAL n 1 190 GLY n 1 191 CYS n 1 192 GLU n 1 193 ASP n 1 194 GLY n 1 195 ALA n 1 196 LEU n 1 197 SER n 1 198 GLN n 1 199 LEU n 1 200 TYR n 1 201 TYR n 1 202 TYR n 1 203 PHE n 1 204 ASN n 1 205 VAL n 1 206 LYS n 1 207 GLY n 1 208 SER n 1 209 ALA n 1 210 ILE n 1 211 GLY n 1 212 GLY n 1 213 THR n 1 214 TYR n 1 215 VAL n 1 216 ALA n 1 217 SER n 1 218 GLU n 1 219 ARG n 1 220 LEU n 1 221 GLU n 1 222 ASP n 1 223 SER n 1 224 ASN n 1 225 CYS n 1 226 LYS n 1 227 ASP n 1 228 SER n 1 229 GLY n 1 230 ILE n 1 231 LYS n 1 232 TYR n 1 233 PRO n 1 234 PRO n 1 235 LYS n 1 236 TYR n 1 237 SER n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name ? _entity_src_nat.pdbx_organism_scientific 'Aspergillus niger' _entity_src_nat.pdbx_ncbi_taxonomy_id 5061 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code Q45U61_ASPNG _struct_ref.pdbx_db_accession Q45U61 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;TIDTCSSDSPLSCQTDNEASCCFNSPGGSLLQTQFWDYDPSDGPSGSWTIHGLWPDNCDGTYQEYCDESREYSNITSILE AQNRTELLSYMKEYWPDYEGADEDESFWEHEWNKHGTCINTIEPSCYTDYYAQEEVGDFFQQVVDLFKTLDSYTALSDAG ITPSEDATYKLSDIEDALAAIHDGYPPYVGCEDGALSQLYYYFNVKGSAIGGTYVASERLEDSNCKDSGIKYPPKYS ; _struct_ref.pdbx_align_begin 24 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3TBJ _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 237 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q45U61 _struct_ref_seq.db_align_beg 24 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 260 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 24 _struct_ref_seq.pdbx_auth_seq_align_end 260 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 3TBJ _struct_ref_seq_dif.mon_id ASP _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 46 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code Q45U61 _struct_ref_seq_dif.db_mon_id GLY _struct_ref_seq_dif.pdbx_seq_db_seq_num 69 _struct_ref_seq_dif.details 'SEE REMARK 999' _struct_ref_seq_dif.pdbx_auth_seq_num 69 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 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 PO4 non-polymer . 'PHOSPHATE ION' ? 'O4 P -3' 94.971 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 3TBJ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.45 _exptl_crystal.density_percent_sol 64.35 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _diffrn.id 1 _diffrn.ambient_temp ? _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength . _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SSRL BEAMLINE BL7-1' _diffrn_source.pdbx_synchrotron_site SSRL _diffrn_source.pdbx_synchrotron_beamline BL7-1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 3TBJ _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 34.569 _reflns.d_resolution_high 1.77 _reflns.number_obs 35832 _reflns.number_all 35832 _reflns.percent_possible_obs 98.600 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.061 _reflns.pdbx_netI_over_sigmaI 18.200 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.200 _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 ? # loop_ _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_ordinal _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.percent_possible_all _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 1 1 1.770 1.870 91.000 0.807 0.807 1.000 4.200 ? ? ? ? ? ? 1 2 1.870 1.980 100.000 0.499 0.499 1.600 5.400 ? ? ? ? ? ? 1 3 1.980 2.120 100.000 0.281 0.281 2.800 5.400 ? ? ? ? ? ? 1 4 2.120 2.290 100.000 0.170 0.170 4.600 5.500 ? ? ? ? ? ? 1 5 2.290 2.510 100.000 0.116 0.116 6.700 5.500 ? ? ? ? ? ? 1 6 2.510 2.810 100.000 0.073 0.073 10.500 5.400 ? ? ? ? ? ? 1 7 2.810 3.240 100.000 0.044 0.044 16.700 5.400 ? ? ? ? ? ? 1 8 3.240 3.970 100.000 0.027 0.027 25.500 5.300 ? ? ? ? ? ? 1 9 3.970 5.610 99.700 0.022 0.022 27.400 5.100 ? ? ? ? ? ? 1 10 5.610 34.569 99.000 0.018 0.018 32.800 5.000 ? ? ? ? ? ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3TBJ _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 32945 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 33.97 _refine.ls_d_res_high 1.80 _refine.ls_percent_reflns_obs 99.67 _refine.ls_R_factor_obs 0.15544 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.15378 _refine.ls_R_factor_R_free 0.18736 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 1738 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min 0.300 _refine.occupancy_max 1.000 _refine.correlation_coeff_Fo_to_Fc 0.972 _refine.correlation_coeff_Fo_to_Fc_free 0.961 _refine.B_iso_mean 27.343 _refine.aniso_B[1][1] 1.63 _refine.aniso_B[2][2] 1.63 _refine.aniso_B[3][3] -2.45 _refine.aniso_B[1][2] 0.82 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ;(1) There is unmodelled electron density in the active site that can be interpreted as a disordered nucleotide. (2) HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ; _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.091 _refine.pdbx_overall_ESU_R_Free 0.093 _refine.overall_SU_ML 0.066 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 4.766 _refine.overall_SU_R_Cruickshank_DPI 0.0903 _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1878 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 64 _refine_hist.number_atoms_solvent 278 _refine_hist.number_atoms_total 2220 _refine_hist.d_res_high 1.80 _refine_hist.d_res_low 33.97 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.026 0.021 ? 2185 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 1376 'X-RAY DIFFRACTION' ? r_angle_refined_deg 2.095 1.982 ? 3013 'X-RAY DIFFRACTION' ? r_angle_other_deg 1.061 3.000 ? 3372 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.905 5.000 ? 273 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.990 26.161 ? 112 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 12.223 15.000 ? 310 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 25.273 15.000 ? 3 'X-RAY DIFFRACTION' ? r_chiral_restr 0.126 0.200 ? 309 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.012 0.021 ? 2554 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.002 0.020 ? 431 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.245 1.500 ? 1297 'X-RAY DIFFRACTION' ? r_mcbond_other 0.426 1.500 ? 517 'X-RAY DIFFRACTION' ? r_mcangle_it 1.998 2.000 ? 2115 'X-RAY DIFFRACTION' ? r_scbond_it 3.338 3.000 ? 888 'X-RAY DIFFRACTION' ? r_scangle_it 4.785 4.500 ? 898 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.800 _refine_ls_shell.d_res_low 1.847 _refine_ls_shell.number_reflns_R_work 2325 _refine_ls_shell.R_factor_R_work 0.333 _refine_ls_shell.percent_reflns_obs 96.52 _refine_ls_shell.R_factor_R_free 0.357 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 115 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # _struct.entry_id 3TBJ _struct.title 'The 1.7A crystal structure of Actibind a T2 ribonucleases as antitumorigenic agents' _struct.pdbx_descriptor Actibind _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3TBJ _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'Hydrolase, ribonuclease' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 3 ? G N N 4 ? H N N 4 ? I N N 4 ? J N N 5 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 67 ? GLU A 71 ? ASP A 90 GLU A 94 5 ? 5 HELX_P HELX_P2 2 ASN A 74 ? GLN A 82 ? ASN A 97 GLN A 105 1 ? 9 HELX_P HELX_P3 3 ARG A 84 ? TRP A 95 ? ARG A 107 TRP A 118 1 ? 12 HELX_P HELX_P4 4 GLY A 100 ? ASP A 102 ? GLY A 123 ASP A 125 5 ? 3 HELX_P HELX_P5 5 GLU A 103 ? HIS A 115 ? GLU A 126 HIS A 138 1 ? 13 HELX_P HELX_P6 6 GLY A 116 ? TYR A 127 ? GLY A 139 TYR A 150 5 ? 12 HELX_P HELX_P7 7 GLN A 133 ? THR A 149 ? GLN A 156 THR A 172 1 ? 17 HELX_P HELX_P8 8 ASP A 151 ? ASP A 158 ? ASP A 174 ASP A 181 1 ? 8 HELX_P HELX_P9 9 LYS A 170 ? ALA A 180 ? LYS A 193 ALA A 203 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 5 SG ? ? ? 1_555 A CYS 22 SG ? ? A CYS 28 A CYS 45 1_555 ? ? ? ? ? ? ? 2.039 ? disulf2 disulf ? ? A CYS 13 SG ? ? ? 1_555 A CYS 58 SG ? ? A CYS 36 A CYS 81 1_555 ? ? ? ? ? ? ? 2.058 ? disulf3 disulf ? ? A CYS 21 SG ? ? ? 1_555 A CYS 126 SG ? ? A CYS 44 A CYS 149 1_555 ? ? ? ? ? ? ? 2.059 ? disulf4 disulf ? ? A CYS 66 SG ? ? ? 1_555 A CYS 118 SG ? ? A CYS 89 A CYS 141 1_555 ? ? ? ? ? ? ? 2.125 ? disulf5 disulf ? ? A CYS 191 SG ? ? ? 1_555 A CYS 225 SG ? ? A CYS 214 A CYS 248 1_555 ? ? ? ? ? ? ? 2.009 ? covale1 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 301 A NAG 302 1_555 ? ? ? ? ? ? ? 1.453 ? covale2 covale ? ? A ASN 83 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 106 A NAG 303 1_555 ? ? ? ? ? ? ? 1.466 ? covale3 covale ? ? A ASN 74 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 97 A NAG 301 1_555 ? ? ? ? ? ? ? 1.490 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 SER 25 A . ? SER 48 A PRO 26 A ? PRO 49 A 1 1.42 2 ASP 39 A . ? ASP 62 A PRO 40 A ? PRO 63 A 1 -3.06 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 4 ? # 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 B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? 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 THR A 49 ? ASP A 56 ? THR A 72 ASP A 79 A 2 SER A 29 ? PHE A 35 ? SER A 52 PHE A 58 A 3 ALA A 195 ? LYS A 206 ? ALA A 218 LYS A 229 A 4 TYR A 188 ? GLU A 192 ? TYR A 211 GLU A 215 B 1 THR A 49 ? ASP A 56 ? THR A 72 ASP A 79 B 2 SER A 29 ? PHE A 35 ? SER A 52 PHE A 58 B 3 ALA A 195 ? LYS A 206 ? ALA A 218 LYS A 229 B 4 THR A 213 ? ALA A 216 ? THR A 236 ALA A 239 # 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 ASP A 56 ? O ASP A 79 N SER A 29 ? N SER A 52 A 2 3 N LEU A 30 ? N LEU A 53 O PHE A 203 ? O PHE A 226 A 3 4 O GLN A 198 ? O GLN A 221 N GLY A 190 ? N GLY A 213 B 1 2 O ASP A 56 ? O ASP A 79 N SER A 29 ? N SER A 52 B 2 3 N LEU A 30 ? N LEU A 53 O PHE A 203 ? O PHE A 226 B 3 4 N ASN A 204 ? N ASN A 227 O VAL A 215 ? O VAL A 238 # 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 ? ? ? ? 11 'BINDING SITE FOR RESIDUE NAG A 301' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 302' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 303' AC4 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE PO4 A 304' AC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE PO4 A 305' AC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 306' AC7 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 307' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO A 308' # 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 11 ASN A 74 ? ASN A 97 . ? 1_555 ? 2 AC1 11 SER A 77 ? SER A 100 . ? 1_555 ? 3 AC1 11 ALA A 81 ? ALA A 104 . ? 1_555 ? 4 AC1 11 GLN A 133 ? GLN A 156 . ? 1_555 ? 5 AC1 11 NAG C . ? NAG A 302 . ? 1_555 ? 6 AC1 11 HOH J . ? HOH A 439 . ? 1_555 ? 7 AC1 11 HOH J . ? HOH A 440 . ? 1_555 ? 8 AC1 11 HOH J . ? HOH A 490 . ? 1_555 ? 9 AC1 11 HOH J . ? HOH A 538 . ? 1_555 ? 10 AC1 11 HOH J . ? HOH A 610 . ? 1_555 ? 11 AC1 11 HOH J . ? HOH A 617 . ? 1_555 ? 12 AC2 6 GLN A 133 ? GLN A 156 . ? 1_555 ? 13 AC2 6 NAG B . ? NAG A 301 . ? 1_555 ? 14 AC2 6 HOH J . ? HOH A 440 . ? 1_555 ? 15 AC2 6 HOH J . ? HOH A 462 . ? 1_555 ? 16 AC2 6 HOH J . ? HOH A 476 . ? 1_555 ? 17 AC2 6 HOH J . ? HOH A 648 . ? 1_555 ? 18 AC3 5 GLN A 14 ? GLN A 37 . ? 4_546 ? 19 AC3 5 GLN A 82 ? GLN A 105 . ? 1_555 ? 20 AC3 5 ASN A 83 ? ASN A 106 . ? 1_555 ? 21 AC3 5 TYR A 131 ? TYR A 154 . ? 1_555 ? 22 AC3 5 HOH J . ? HOH A 596 . ? 1_555 ? 23 AC4 10 HIS A 51 ? HIS A 74 . ? 1_555 ? 24 AC4 10 TRP A 54 ? TRP A 77 . ? 1_555 ? 25 AC4 10 HIS A 110 ? HIS A 133 . ? 1_555 ? 26 AC4 10 GLU A 111 ? GLU A 134 . ? 1_555 ? 27 AC4 10 LYS A 114 ? LYS A 137 . ? 1_555 ? 28 AC4 10 HIS A 115 ? HIS A 138 . ? 1_555 ? 29 AC4 10 HOH J . ? HOH A 410 . ? 1_555 ? 30 AC4 10 HOH J . ? HOH A 506 . ? 1_555 ? 31 AC4 10 HOH J . ? HOH A 578 . ? 1_555 ? 32 AC4 10 HOH J . ? HOH A 612 . ? 1_555 ? 33 AC5 8 GLU A 86 ? GLU A 109 . ? 1_555 ? 34 AC5 8 LEU A 87 ? LEU A 110 . ? 1_555 ? 35 AC5 8 TYR A 90 ? TYR A 113 . ? 1_555 ? 36 AC5 8 GLN A 141 ? GLN A 164 . ? 1_555 ? 37 AC5 8 LYS A 148 ? LYS A 171 . ? 1_555 ? 38 AC5 8 TYR A 236 ? TYR A 259 . ? 6_555 ? 39 AC5 8 HOH J . ? HOH A 444 . ? 6_555 ? 40 AC5 8 HOH J . ? HOH A 580 . ? 1_555 ? 41 AC6 7 ASP A 42 ? ASP A 65 . ? 1_555 ? 42 AC6 7 GLY A 43 ? GLY A 66 . ? 1_555 ? 43 AC6 7 LYS A 92 ? LYS A 115 . ? 1_555 ? 44 AC6 7 GLU A 93 ? GLU A 116 . ? 1_555 ? 45 AC6 7 GLU A 93 ? GLU A 116 . ? 6_555 ? 46 AC6 7 HOH J . ? HOH A 619 . ? 1_555 ? 47 AC6 7 HOH J . ? HOH A 621 . ? 6_555 ? 48 AC7 7 SER A 20 ? SER A 43 . ? 2_544 ? 49 AC7 7 CYS A 22 ? CYS A 45 . ? 2_544 ? 50 AC7 7 ASP A 37 ? ASP A 60 . ? 1_555 ? 51 AC7 7 ASP A 39 ? ASP A 62 . ? 1_555 ? 52 AC7 7 PRO A 40 ? PRO A 63 . ? 1_555 ? 53 AC7 7 HOH J . ? HOH A 459 . ? 1_555 ? 54 AC7 7 HOH J . ? HOH A 651 . ? 1_555 ? 55 AC8 4 THR A 1 ? THR A 24 . ? 1_555 ? 56 AC8 4 ILE A 2 ? ILE A 25 . ? 1_555 ? 57 AC8 4 ASP A 138 ? ASP A 161 . ? 1_555 ? 58 AC8 4 HOH J . ? HOH A 402 . ? 1_555 ? # _atom_sites.entry_id 3TBJ _atom_sites.fract_transf_matrix[1][1] 0.012746 _atom_sites.fract_transf_matrix[1][2] 0.007359 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.014718 _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] 0.009642 _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 P 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 . THR A 1 1 ? 33.511 -20.357 60.072 1.00 23.73 ? 24 THR A N 1 ATOM 2 C CA . THR A 1 1 ? 33.089 -19.976 58.691 1.00 23.50 ? 24 THR A CA 1 ATOM 3 C C . THR A 1 1 ? 34.062 -18.888 58.235 1.00 22.44 ? 24 THR A C 1 ATOM 4 O O . THR A 1 1 ? 35.096 -18.618 58.906 1.00 24.23 ? 24 THR A O 1 ATOM 5 C CB . THR A 1 1 ? 31.602 -19.504 58.685 1.00 24.39 ? 24 THR A CB 1 ATOM 6 O OG1 . THR A 1 1 ? 31.463 -18.536 59.710 1.00 25.65 ? 24 THR A OG1 1 ATOM 7 C CG2 . THR A 1 1 ? 30.626 -20.662 59.067 1.00 25.50 ? 24 THR A CG2 1 ATOM 8 N N A ILE A 1 2 ? 33.833 -18.311 57.076 0.50 23.42 ? 25 ILE A N 1 ATOM 9 N N B ILE A 1 2 ? 33.743 -18.222 57.133 0.50 23.39 ? 25 ILE A N 1 ATOM 10 C CA A ILE A 1 2 ? 34.831 -17.405 56.508 0.50 22.34 ? 25 ILE A CA 1 ATOM 11 C CA B ILE A 1 2 ? 34.655 -17.257 56.464 0.50 22.32 ? 25 ILE A CA 1 ATOM 12 C C A ILE A 1 2 ? 34.905 -16.184 57.409 0.50 22.51 ? 25 ILE A C 1 ATOM 13 C C B ILE A 1 2 ? 34.942 -16.074 57.383 0.50 23.03 ? 25 ILE A C 1 ATOM 14 O O A ILE A 1 2 ? 33.946 -15.775 58.054 0.50 21.07 ? 25 ILE A O 1 ATOM 15 O O B ILE A 1 2 ? 34.058 -15.604 58.066 0.50 22.06 ? 25 ILE A O 1 ATOM 16 C CB A ILE A 1 2 ? 34.526 -17.038 55.018 0.50 22.13 ? 25 ILE A CB 1 ATOM 17 C CB B ILE A 1 2 ? 34.006 -16.741 55.118 0.50 21.98 ? 25 ILE A CB 1 ATOM 18 C CG1 A ILE A 1 2 ? 35.835 -16.738 54.253 0.50 23.05 ? 25 ILE A CG1 1 ATOM 19 C CG1 B ILE A 1 2 ? 34.993 -15.936 54.260 0.50 20.09 ? 25 ILE A CG1 1 ATOM 20 C CG2 A ILE A 1 2 ? 33.459 -15.949 54.961 0.50 22.39 ? 25 ILE A CG2 1 ATOM 21 C CG2 B ILE A 1 2 ? 32.741 -15.912 55.418 0.50 22.42 ? 25 ILE A CG2 1 ATOM 22 C CD1 A ILE A 1 2 ? 35.769 -16.756 52.700 0.50 21.15 ? 25 ILE A CD1 1 ATOM 23 C CD1 B ILE A 1 2 ? 36.161 -16.772 53.608 0.50 18.40 ? 25 ILE A CD1 1 ATOM 24 N N A ASP A 1 3 ? 36.085 -15.647 57.459 0.50 24.08 ? 26 ASP A N 1 ATOM 25 N N B ASP A 1 3 ? 36.169 -15.596 57.371 0.50 25.11 ? 26 ASP A N 1 ATOM 26 C CA A ASP A 1 3 ? 36.281 -14.413 58.109 0.50 26.58 ? 26 ASP A CA 1 ATOM 27 C CA B ASP A 1 3 ? 36.453 -14.368 58.072 0.50 27.90 ? 26 ASP A CA 1 ATOM 28 C C A ASP A 1 3 ? 35.467 -13.319 57.454 0.50 27.30 ? 26 ASP A C 1 ATOM 29 C C B ASP A 1 3 ? 35.767 -13.159 57.408 0.50 27.76 ? 26 ASP A C 1 ATOM 30 O O A ASP A 1 3 ? 34.984 -13.451 56.326 0.50 26.27 ? 26 ASP A O 1 ATOM 31 O O B ASP A 1 3 ? 35.644 -13.064 56.202 0.50 27.31 ? 26 ASP A O 1 ATOM 32 C CB A ASP A 1 3 ? 37.761 -14.119 58.104 0.50 27.73 ? 26 ASP A CB 1 ATOM 33 C CB B ASP A 1 3 ? 37.967 -14.226 58.411 0.50 29.75 ? 26 ASP A CB 1 ATOM 34 C CG A ASP A 1 3 ? 38.534 -15.035 59.087 0.50 26.27 ? 26 ASP A CG 1 ATOM 35 C CG B ASP A 1 3 ? 38.850 -13.926 57.226 0.50 30.62 ? 26 ASP A CG 1 ATOM 36 O OD1 A ASP A 1 3 ? 37.973 -15.675 60.013 0.50 30.63 ? 26 ASP A OD1 1 ATOM 37 O OD1 B ASP A 1 3 ? 38.332 -13.562 56.116 0.50 38.57 ? 26 ASP A OD1 1 ATOM 38 O OD2 A ASP A 1 3 ? 39.700 -15.116 58.894 0.50 30.07 ? 26 ASP A OD2 1 ATOM 39 O OD2 B ASP A 1 3 ? 40.096 -14.059 57.428 0.50 31.46 ? 26 ASP A OD2 1 ATOM 40 N N . THR A 1 4 ? 35.210 -12.285 58.245 1.00 27.35 ? 27 THR A N 1 ATOM 41 C CA . THR A 1 4 ? 34.433 -11.192 57.812 1.00 27.34 ? 27 THR A CA 1 ATOM 42 C C . THR A 1 4 ? 35.364 -10.011 57.763 1.00 28.14 ? 27 THR A C 1 ATOM 43 O O . THR A 1 4 ? 36.382 -9.932 58.473 1.00 31.61 ? 27 THR A O 1 ATOM 44 C CB . THR A 1 4 ? 33.261 -10.893 58.758 1.00 29.11 ? 27 THR A CB 1 ATOM 45 O OG1 . THR A 1 4 ? 33.727 -10.787 60.095 1.00 30.07 ? 27 THR A OG1 1 ATOM 46 C CG2 . THR A 1 4 ? 32.250 -12.051 58.722 1.00 30.62 ? 27 THR A CG2 1 ATOM 47 N N . CYS A 1 5 ? 35.079 -9.125 56.855 1.00 27.69 ? 28 CYS A N 1 ATOM 48 C CA . CYS A 1 5 ? 35.843 -7.929 56.680 1.00 27.26 ? 28 CYS A CA 1 ATOM 49 C C . CYS A 1 5 ? 34.892 -6.750 56.796 1.00 30.96 ? 28 CYS A C 1 ATOM 50 O O . CYS A 1 5 ? 33.658 -6.847 56.574 1.00 29.17 ? 28 CYS A O 1 ATOM 51 C CB . CYS A 1 5 ? 36.489 -7.949 55.282 1.00 27.32 ? 28 CYS A CB 1 ATOM 52 S SG . CYS A 1 5 ? 37.411 -9.440 54.860 1.00 27.40 ? 28 CYS A SG 1 ATOM 53 N N . SER A 1 6 ? 35.457 -5.598 57.133 1.00 31.53 ? 29 SER A N 1 ATOM 54 C CA . SER A 1 6 ? 34.641 -4.403 57.264 1.00 34.19 ? 29 SER A CA 1 ATOM 55 C C . SER A 1 6 ? 33.924 -4.056 55.927 1.00 35.48 ? 29 SER A C 1 ATOM 56 O O . SER A 1 6 ? 34.458 -4.252 54.830 1.00 34.24 ? 29 SER A O 1 ATOM 57 C CB . SER A 1 6 ? 35.485 -3.230 57.692 1.00 35.19 ? 29 SER A CB 1 ATOM 58 O OG . SER A 1 6 ? 34.788 -2.028 57.352 1.00 39.86 ? 29 SER A OG 1 ATOM 59 N N . SER A 1 7 ? 32.691 -3.550 56.030 1.00 36.70 ? 30 SER A N 1 ATOM 60 C CA . SER A 1 7 ? 31.958 -3.130 54.811 1.00 39.28 ? 30 SER A CA 1 ATOM 61 C C . SER A 1 7 ? 32.566 -1.867 54.179 1.00 38.30 ? 30 SER A C 1 ATOM 62 O O . SER A 1 7 ? 32.231 -1.528 52.982 1.00 38.86 ? 30 SER A O 1 ATOM 63 C CB . SER A 1 7 ? 30.447 -2.957 55.077 1.00 41.11 ? 30 SER A CB 1 ATOM 64 O OG . SER A 1 7 ? 30.212 -1.919 55.996 1.00 47.05 ? 30 SER A OG 1 ATOM 65 N N A ASP A 1 8 ? 33.470 -1.199 54.886 0.50 37.80 ? 31 ASP A N 1 ATOM 66 N N B ASP A 1 8 ? 33.461 -1.197 54.948 0.50 37.49 ? 31 ASP A N 1 ATOM 67 C CA A ASP A 1 8 ? 34.228 -0.154 54.234 0.50 38.02 ? 31 ASP A CA 1 ATOM 68 C CA B ASP A 1 8 ? 34.351 -0.120 54.437 0.50 37.59 ? 31 ASP A CA 1 ATOM 69 C C A ASP A 1 8 ? 35.692 -0.612 53.914 0.50 36.14 ? 31 ASP A C 1 ATOM 70 C C B ASP A 1 8 ? 35.636 -0.599 53.714 0.50 35.49 ? 31 ASP A C 1 ATOM 71 O O A ASP A 1 8 ? 36.652 0.184 53.959 0.50 37.12 ? 31 ASP A O 1 ATOM 72 O O B ASP A 1 8 ? 36.417 0.236 53.234 0.50 35.65 ? 31 ASP A O 1 ATOM 73 C CB A ASP A 1 8 ? 34.063 1.141 55.035 0.50 39.22 ? 31 ASP A CB 1 ATOM 74 C CB B ASP A 1 8 ? 34.717 0.930 55.528 0.50 38.54 ? 31 ASP A CB 1 ATOM 75 C CG A ASP A 1 8 ? 32.590 1.652 55.016 0.50 40.34 ? 31 ASP A CG 1 ATOM 76 C CG B ASP A 1 8 ? 35.919 0.525 56.448 0.50 40.06 ? 31 ASP A CG 1 ATOM 77 O OD1 A ASP A 1 8 ? 32.222 2.290 54.026 0.50 37.24 ? 31 ASP A OD1 1 ATOM 78 O OD1 B ASP A 1 8 ? 36.355 -0.650 56.432 0.50 37.50 ? 31 ASP A OD1 1 ATOM 79 O OD2 A ASP A 1 8 ? 31.820 1.397 55.972 0.50 40.10 ? 31 ASP A OD2 1 ATOM 80 O OD2 B ASP A 1 8 ? 36.392 1.423 57.238 0.50 41.77 ? 31 ASP A OD2 1 ATOM 81 N N . SER A 1 9 ? 35.847 -1.910 53.619 1.00 32.79 ? 32 SER A N 1 ATOM 82 C CA . SER A 1 9 ? 37.111 -2.427 53.102 1.00 31.12 ? 32 SER A CA 1 ATOM 83 C C . SER A 1 9 ? 37.407 -1.807 51.740 1.00 30.18 ? 32 SER A C 1 ATOM 84 O O . SER A 1 9 ? 36.459 -1.511 50.987 1.00 31.06 ? 32 SER A O 1 ATOM 85 C CB . SER A 1 9 ? 37.018 -3.934 52.954 1.00 31.48 ? 32 SER A CB 1 ATOM 86 O OG . SER A 1 9 ? 36.947 -4.584 54.185 1.00 27.78 ? 32 SER A OG 1 ATOM 87 N N . PRO A 1 10 ? 38.688 -1.633 51.403 1.00 29.03 ? 33 PRO A N 1 ATOM 88 C CA . PRO A 1 10 ? 38.991 -1.004 50.129 1.00 30.66 ? 33 PRO A CA 1 ATOM 89 C C . PRO A 1 10 ? 38.688 -1.883 48.893 1.00 30.06 ? 33 PRO A C 1 ATOM 90 O O . PRO A 1 10 ? 38.918 -3.136 48.866 1.00 28.29 ? 33 PRO A O 1 ATOM 91 C CB . PRO A 1 10 ? 40.504 -0.739 50.245 1.00 29.17 ? 33 PRO A CB 1 ATOM 92 C CG . PRO A 1 10 ? 40.965 -1.857 51.075 1.00 32.68 ? 33 PRO A CG 1 ATOM 93 C CD . PRO A 1 10 ? 39.929 -2.041 52.083 1.00 29.18 ? 33 PRO A CD 1 ATOM 94 N N . LEU A 1 11 ? 38.188 -1.214 47.849 1.00 31.05 ? 34 LEU A N 1 ATOM 95 C CA . LEU A 1 11 ? 37.778 -1.850 46.651 1.00 29.81 ? 34 LEU A CA 1 ATOM 96 C C . LEU A 1 11 ? 38.940 -2.429 45.886 1.00 27.89 ? 34 LEU A C 1 ATOM 97 O O . LEU A 1 11 ? 39.958 -1.755 45.615 1.00 28.43 ? 34 LEU A O 1 ATOM 98 C CB . LEU A 1 11 ? 37.075 -0.820 45.773 1.00 31.59 ? 34 LEU A CB 1 ATOM 99 C CG . LEU A 1 11 ? 36.015 -1.113 44.786 1.00 35.61 ? 34 LEU A CG 1 ATOM 100 C CD1 . LEU A 1 11 ? 35.116 -2.217 45.186 1.00 31.27 ? 34 LEU A CD1 1 ATOM 101 C CD2 . LEU A 1 11 ? 35.286 0.273 44.589 1.00 43.88 ? 34 LEU A CD2 1 ATOM 102 N N . SER A 1 12 ? 38.765 -3.689 45.479 1.00 26.10 ? 35 SER A N 1 ATOM 103 C CA . SER A 1 12 ? 39.794 -4.339 44.679 1.00 26.21 ? 35 SER A CA 1 ATOM 104 C C . SER A 1 12 ? 39.900 -3.586 43.304 1.00 27.26 ? 35 SER A C 1 ATOM 105 O O . SER A 1 12 ? 38.944 -2.993 42.846 1.00 26.48 ? 35 SER A O 1 ATOM 106 C CB . SER A 1 12 ? 39.473 -5.804 44.449 1.00 23.81 ? 35 SER A CB 1 ATOM 107 O OG . SER A 1 12 ? 38.228 -6.005 43.809 1.00 24.53 ? 35 SER A OG 1 ATOM 108 N N . CYS A 1 13 ? 41.076 -3.658 42.714 1.00 27.23 ? 36 CYS A N 1 ATOM 109 C CA . CYS A 1 13 ? 41.489 -2.984 41.477 1.00 30.55 ? 36 CYS A CA 1 ATOM 110 C C . CYS A 1 13 ? 41.517 -1.440 41.517 1.00 32.23 ? 36 CYS A C 1 ATOM 111 O O . CYS A 1 13 ? 42.409 -0.868 40.940 1.00 34.09 ? 36 CYS A O 1 ATOM 112 C CB . CYS A 1 13 ? 40.663 -3.452 40.254 1.00 31.20 ? 36 CYS A CB 1 ATOM 113 S SG . CYS A 1 13 ? 40.988 -5.108 39.764 1.00 30.32 ? 36 CYS A SG 1 ATOM 114 N N . GLN A 1 14 ? 40.500 -0.843 42.128 1.00 33.29 ? 37 GLN A N 1 ATOM 115 C CA . GLN A 1 14 ? 40.305 0.562 42.181 1.00 35.97 ? 37 GLN A CA 1 ATOM 116 C C . GLN A 1 14 ? 41.166 1.174 43.227 1.00 37.06 ? 37 GLN A C 1 ATOM 117 O O . GLN A 1 14 ? 41.327 2.381 43.211 1.00 37.96 ? 37 GLN A O 1 ATOM 118 C CB . GLN A 1 14 ? 38.806 0.900 42.341 1.00 37.34 ? 37 GLN A CB 1 ATOM 119 C CG . GLN A 1 14 ? 37.973 0.442 41.163 1.00 41.40 ? 37 GLN A CG 1 ATOM 120 C CD . GLN A 1 14 ? 36.489 0.940 41.092 1.00 49.20 ? 37 GLN A CD 1 ATOM 121 O OE1 . GLN A 1 14 ? 36.221 2.158 41.131 1.00 51.55 ? 37 GLN A OE1 1 ATOM 122 N NE2 . GLN A 1 14 ? 35.524 -0.021 40.867 1.00 44.93 ? 37 GLN A NE2 1 ATOM 123 N N . THR A 1 15 ? 41.755 0.371 44.126 1.00 35.84 ? 38 THR A N 1 ATOM 124 C CA . THR A 1 15 ? 42.685 0.901 45.106 1.00 35.32 ? 38 THR A CA 1 ATOM 125 C C . THR A 1 15 ? 44.005 0.121 45.083 1.00 34.72 ? 38 THR A C 1 ATOM 126 O O . THR A 1 15 ? 44.103 -0.926 44.527 1.00 33.78 ? 38 THR A O 1 ATOM 127 C CB . THR A 1 15 ? 42.052 0.880 46.551 1.00 36.85 ? 38 THR A CB 1 ATOM 128 O OG1 . THR A 1 15 ? 41.866 -0.480 46.998 1.00 30.74 ? 38 THR A OG1 1 ATOM 129 C CG2 . THR A 1 15 ? 40.647 1.624 46.581 1.00 36.60 ? 38 THR A CG2 1 ATOM 130 N N A ASP A 1 16 ? 44.999 0.643 45.751 0.70 35.00 ? 39 ASP A N 1 ATOM 131 N N B ASP A 1 16 ? 45.041 0.710 45.657 0.30 35.34 ? 39 ASP A N 1 ATOM 132 C CA A ASP A 1 16 ? 46.295 0.035 45.772 0.70 36.49 ? 39 ASP A CA 1 ATOM 133 C CA B ASP A 1 16 ? 46.337 0.067 45.803 0.30 36.01 ? 39 ASP A CA 1 ATOM 134 C C A ASP A 1 16 ? 46.498 -0.562 47.195 0.70 36.01 ? 39 ASP A C 1 ATOM 135 C C B ASP A 1 16 ? 46.314 -0.535 47.220 0.30 35.29 ? 39 ASP A C 1 ATOM 136 O O A ASP A 1 16 ? 46.871 0.143 48.143 0.70 36.96 ? 39 ASP A O 1 ATOM 137 O O B ASP A 1 16 ? 46.258 0.211 48.203 0.30 35.01 ? 39 ASP A O 1 ATOM 138 C CB A ASP A 1 16 ? 47.410 1.087 45.484 0.70 38.63 ? 39 ASP A CB 1 ATOM 139 C CB B ASP A 1 16 ? 47.503 1.100 45.696 0.30 37.58 ? 39 ASP A CB 1 ATOM 140 C CG A ASP A 1 16 ? 48.783 0.475 45.529 0.70 39.87 ? 39 ASP A CG 1 ATOM 141 C CG B ASP A 1 16 ? 47.836 1.510 44.245 0.30 39.50 ? 39 ASP A CG 1 ATOM 142 O OD1 A ASP A 1 16 ? 48.876 -0.732 45.364 0.70 44.06 ? 39 ASP A OD1 1 ATOM 143 O OD1 B ASP A 1 16 ? 48.067 0.643 43.370 0.30 43.53 ? 39 ASP A OD1 1 ATOM 144 O OD2 A ASP A 1 16 ? 49.756 1.183 45.767 0.70 47.57 ? 39 ASP A OD2 1 ATOM 145 O OD2 B ASP A 1 16 ? 47.916 2.730 43.980 0.30 43.20 ? 39 ASP A OD2 1 ATOM 146 N N . ASN A 1 17 ? 46.281 -1.865 47.333 1.00 34.35 ? 40 ASN A N 1 ATOM 147 C CA . ASN A 1 17 ? 46.444 -2.524 48.632 1.00 33.82 ? 40 ASN A CA 1 ATOM 148 C C . ASN A 1 17 ? 47.051 -3.887 48.492 1.00 33.67 ? 40 ASN A C 1 ATOM 149 O O . ASN A 1 17 ? 47.161 -4.401 47.367 1.00 32.98 ? 40 ASN A O 1 ATOM 150 C CB . ASN A 1 17 ? 45.094 -2.627 49.298 1.00 33.29 ? 40 ASN A CB 1 ATOM 151 C CG . ASN A 1 17 ? 44.621 -1.300 49.843 1.00 34.64 ? 40 ASN A CG 1 ATOM 152 O OD1 . ASN A 1 17 ? 43.739 -0.656 49.247 1.00 36.43 ? 40 ASN A OD1 1 ATOM 153 N ND2 . ASN A 1 17 ? 45.196 -0.868 50.984 1.00 31.09 ? 40 ASN A ND2 1 ATOM 154 N N . GLU A 1 18 ? 47.461 -4.446 49.627 1.00 32.54 ? 41 GLU A N 1 ATOM 155 C CA . GLU A 1 18 ? 48.175 -5.710 49.675 1.00 33.01 ? 41 GLU A CA 1 ATOM 156 C C . GLU A 1 18 ? 47.238 -6.897 49.839 1.00 29.85 ? 41 GLU A C 1 ATOM 157 O O . GLU A 1 18 ? 46.376 -6.922 50.718 1.00 29.97 ? 41 GLU A O 1 ATOM 158 C CB . GLU A 1 18 ? 49.205 -5.698 50.807 1.00 35.01 ? 41 GLU A CB 1 ATOM 159 C CG . GLU A 1 18 ? 50.548 -5.101 50.417 1.00 44.66 ? 41 GLU A CG 1 ATOM 160 C CD . GLU A 1 18 ? 51.442 -6.095 49.703 1.00 48.91 ? 41 GLU A CD 1 ATOM 161 O OE1 . GLU A 1 18 ? 50.910 -6.959 48.975 1.00 57.23 ? 41 GLU A OE1 1 ATOM 162 O OE2 . GLU A 1 18 ? 52.678 -6.013 49.870 1.00 57.09 ? 41 GLU A OE2 1 ATOM 163 N N . ALA A 1 19 ? 47.433 -7.878 48.971 1.00 27.51 ? 42 ALA A N 1 ATOM 164 C CA . ALA A 1 19 ? 46.679 -9.140 48.980 1.00 26.23 ? 42 ALA A CA 1 ATOM 165 C C . ALA A 1 19 ? 46.609 -9.744 50.385 1.00 25.35 ? 42 ALA A C 1 ATOM 166 O O . ALA A 1 19 ? 47.640 -9.903 51.037 1.00 25.55 ? 42 ALA A O 1 ATOM 167 C CB . ALA A 1 19 ? 47.309 -10.176 48.044 1.00 26.46 ? 42 ALA A CB 1 ATOM 168 N N . SER A 1 20 ? 45.415 -10.129 50.772 1.00 24.62 ? 43 SER A N 1 ATOM 169 C CA . SER A 1 20 ? 45.146 -10.672 52.088 1.00 23.51 ? 43 SER A CA 1 ATOM 170 C C . SER A 1 20 ? 43.790 -11.325 52.019 1.00 23.27 ? 43 SER A C 1 ATOM 171 O O . SER A 1 20 ? 43.106 -11.243 50.998 1.00 24.09 ? 43 SER A O 1 ATOM 172 C CB . SER A 1 20 ? 45.111 -9.626 53.210 1.00 23.46 ? 43 SER A CB 1 ATOM 173 O OG . SER A 1 20 ? 43.898 -8.838 53.135 1.00 22.24 ? 43 SER A OG 1 ATOM 174 N N . CYS A 1 21 ? 43.375 -11.932 53.135 1.00 24.58 ? 44 CYS A N 1 ATOM 175 C CA . CYS A 1 21 ? 42.018 -12.431 53.214 1.00 23.26 ? 44 CYS A CA 1 ATOM 176 C C . CYS A 1 21 ? 40.905 -11.373 53.040 1.00 24.44 ? 44 CYS A C 1 ATOM 177 O O . CYS A 1 21 ? 39.774 -11.717 52.724 1.00 25.35 ? 44 CYS A O 1 ATOM 178 C CB . CYS A 1 21 ? 41.824 -13.207 54.524 1.00 25.05 ? 44 CYS A CB 1 ATOM 179 S SG . CYS A 1 21 ? 42.729 -14.698 54.596 1.00 24.90 ? 44 CYS A SG 1 ATOM 180 N N . CYS A 1 22 ? 41.208 -10.090 53.211 1.00 24.19 ? 45 CYS A N 1 ATOM 181 C CA . CYS A 1 22 ? 40.256 -9.048 52.996 1.00 23.12 ? 45 CYS A CA 1 ATOM 182 C C . CYS A 1 22 ? 40.548 -8.132 51.762 1.00 23.40 ? 45 CYS A C 1 ATOM 183 O O . CYS A 1 22 ? 40.078 -6.975 51.698 1.00 24.22 ? 45 CYS A O 1 ATOM 184 C CB . CYS A 1 22 ? 40.194 -8.167 54.258 1.00 24.31 ? 45 CYS A CB 1 ATOM 185 S SG . CYS A 1 22 ? 39.268 -9.060 55.611 1.00 25.62 ? 45 CYS A SG 1 ATOM 186 N N . PHE A 1 23 ? 41.365 -8.624 50.841 1.00 23.21 ? 46 PHE A N 1 ATOM 187 C CA . PHE A 1 23 ? 41.684 -7.871 49.608 1.00 22.90 ? 46 PHE A CA 1 ATOM 188 C C . PHE A 1 23 ? 41.926 -8.827 48.446 1.00 24.11 ? 46 PHE A C 1 ATOM 189 O O . PHE A 1 23 ? 42.905 -9.523 48.424 1.00 25.38 ? 46 PHE A O 1 ATOM 190 C CB . PHE A 1 23 ? 42.893 -6.924 49.800 1.00 22.73 ? 46 PHE A CB 1 ATOM 191 C CG . PHE A 1 23 ? 43.003 -5.896 48.700 1.00 24.19 ? 46 PHE A CG 1 ATOM 192 C CD1 . PHE A 1 23 ? 41.976 -4.951 48.533 1.00 26.16 ? 46 PHE A CD1 1 ATOM 193 C CD2 . PHE A 1 23 ? 44.018 -5.957 47.801 1.00 25.72 ? 46 PHE A CD2 1 ATOM 194 C CE1 . PHE A 1 23 ? 42.037 -3.997 47.528 1.00 26.31 ? 46 PHE A CE1 1 ATOM 195 C CE2 . PHE A 1 23 ? 44.085 -4.994 46.690 1.00 26.72 ? 46 PHE A CE2 1 ATOM 196 C CZ . PHE A 1 23 ? 43.085 -4.064 46.596 1.00 25.79 ? 46 PHE A CZ 1 ATOM 197 N N . ASN A 1 24 ? 40.983 -8.877 47.479 1.00 24.06 ? 47 ASN A N 1 ATOM 198 C CA . ASN A 1 24 ? 41.175 -9.676 46.289 1.00 23.71 ? 47 ASN A CA 1 ATOM 199 C C . ASN A 1 24 ? 42.199 -9.118 45.340 1.00 23.71 ? 47 ASN A C 1 ATOM 200 O O . ASN A 1 24 ? 42.003 -8.045 44.733 1.00 23.88 ? 47 ASN A O 1 ATOM 201 C CB . ASN A 1 24 ? 39.817 -9.856 45.564 1.00 21.85 ? 47 ASN A CB 1 ATOM 202 C CG . ASN A 1 24 ? 38.918 -10.801 46.337 1.00 20.30 ? 47 ASN A CG 1 ATOM 203 O OD1 . ASN A 1 24 ? 39.083 -12.034 46.231 1.00 23.47 ? 47 ASN A OD1 1 ATOM 204 N ND2 . ASN A 1 24 ? 37.947 -10.240 47.119 1.00 22.73 ? 47 ASN A ND2 1 ATOM 205 N N . SER A 1 25 ? 43.316 -9.847 45.229 1.00 26.21 ? 48 SER A N 1 ATOM 206 C CA . SER A 1 25 ? 44.509 -9.382 44.458 1.00 24.99 ? 48 SER A CA 1 ATOM 207 C C . SER A 1 25 ? 45.353 -10.585 44.285 1.00 27.06 ? 48 SER A C 1 ATOM 208 O O . SER A 1 25 ? 45.520 -11.359 45.254 1.00 27.65 ? 48 SER A O 1 ATOM 209 C CB . SER A 1 25 ? 45.309 -8.313 45.183 1.00 28.55 ? 48 SER A CB 1 ATOM 210 O OG . SER A 1 25 ? 46.378 -7.838 44.398 1.00 27.83 ? 48 SER A OG 1 ATOM 211 N N . PRO A 1 26 ? 45.933 -10.773 43.084 1.00 25.69 ? 49 PRO A N 1 ATOM 212 C CA . PRO A 1 26 ? 45.856 -9.912 41.920 1.00 26.92 ? 49 PRO A CA 1 ATOM 213 C C . PRO A 1 26 ? 44.521 -10.003 41.158 1.00 26.41 ? 49 PRO A C 1 ATOM 214 O O . PRO A 1 26 ? 44.230 -9.134 40.313 1.00 27.48 ? 49 PRO A O 1 ATOM 215 C CB . PRO A 1 26 ? 47.003 -10.440 41.015 1.00 28.87 ? 49 PRO A CB 1 ATOM 216 C CG . PRO A 1 26 ? 47.072 -11.883 41.329 1.00 27.98 ? 49 PRO A CG 1 ATOM 217 C CD . PRO A 1 26 ? 46.792 -11.952 42.856 1.00 26.50 ? 49 PRO A CD 1 ATOM 218 N N . GLY A 1 27 ? 43.736 -11.008 41.500 1.00 24.98 ? 50 GLY A N 1 ATOM 219 C CA . GLY A 1 27 ? 42.404 -11.280 40.911 1.00 25.52 ? 50 GLY A CA 1 ATOM 220 C C . GLY A 1 27 ? 41.308 -10.404 41.522 1.00 24.04 ? 50 GLY A C 1 ATOM 221 O O . GLY A 1 27 ? 40.409 -10.875 42.162 1.00 24.29 ? 50 GLY A O 1 ATOM 222 N N . GLY A 1 28 ? 41.386 -9.125 41.220 1.00 25.34 ? 51 GLY A N 1 ATOM 223 C CA . GLY A 1 28 ? 40.504 -8.098 41.787 1.00 24.94 ? 51 GLY A CA 1 ATOM 224 C C . GLY A 1 28 ? 39.266 -7.796 40.947 1.00 24.81 ? 51 GLY A C 1 ATOM 225 O O . GLY A 1 28 ? 38.388 -6.999 41.378 1.00 25.42 ? 51 GLY A O 1 ATOM 226 N N . SER A 1 29 ? 39.239 -8.300 39.728 1.00 22.62 ? 52 SER A N 1 ATOM 227 C CA . SER A 1 29 ? 38.073 -8.092 38.846 1.00 24.34 ? 52 SER A CA 1 ATOM 228 C C . SER A 1 29 ? 37.361 -9.394 38.820 1.00 22.86 ? 52 SER A C 1 ATOM 229 O O . SER A 1 29 ? 37.938 -10.388 38.349 1.00 25.78 ? 52 SER A O 1 ATOM 230 C CB . SER A 1 29 ? 38.520 -7.723 37.438 1.00 24.14 ? 52 SER A CB 1 ATOM 231 O OG . SER A 1 29 ? 37.350 -7.492 36.716 1.00 28.72 ? 52 SER A OG 1 ATOM 232 N N . LEU A 1 30 ? 36.203 -9.455 39.426 1.00 22.57 ? 53 LEU A N 1 ATOM 233 C CA . LEU A 1 30 ? 35.446 -10.716 39.516 1.00 22.18 ? 53 LEU A CA 1 ATOM 234 C C . LEU A 1 30 ? 34.300 -10.725 38.494 1.00 21.68 ? 53 LEU A C 1 ATOM 235 O O . LEU A 1 30 ? 33.481 -9.833 38.475 1.00 24.51 ? 53 LEU A O 1 ATOM 236 C CB . LEU A 1 30 ? 34.851 -10.900 40.929 1.00 22.30 ? 53 LEU A CB 1 ATOM 237 C CG . LEU A 1 30 ? 35.699 -11.465 42.104 1.00 24.45 ? 53 LEU A CG 1 ATOM 238 C CD1 . LEU A 1 30 ? 35.968 -12.956 41.833 1.00 23.10 ? 53 LEU A CD1 1 ATOM 239 C CD2 . LEU A 1 30 ? 36.945 -10.757 42.161 1.00 23.80 ? 53 LEU A CD2 1 ATOM 240 N N . LEU A 1 31 ? 34.247 -11.748 37.648 1.00 20.47 ? 54 LEU A N 1 ATOM 241 C CA . LEU A 1 31 ? 33.343 -11.858 36.510 1.00 20.38 ? 54 LEU A CA 1 ATOM 242 C C . LEU A 1 31 ? 32.304 -12.935 36.813 1.00 20.48 ? 54 LEU A C 1 ATOM 243 O O . LEU A 1 31 ? 32.625 -14.064 36.979 1.00 21.41 ? 54 LEU A O 1 ATOM 244 C CB . LEU A 1 31 ? 34.065 -12.241 35.234 1.00 21.11 ? 54 LEU A CB 1 ATOM 245 C CG . LEU A 1 31 ? 34.940 -11.196 34.509 1.00 21.56 ? 54 LEU A CG 1 ATOM 246 C CD1 . LEU A 1 31 ? 36.011 -10.613 35.477 1.00 21.66 ? 54 LEU A CD1 1 ATOM 247 C CD2 . LEU A 1 31 ? 35.526 -11.856 33.305 1.00 23.18 ? 54 LEU A CD2 1 ATOM 248 N N . GLN A 1 32 ? 31.061 -12.518 36.943 1.00 21.30 ? 55 GLN A N 1 ATOM 249 C CA . GLN A 1 32 ? 29.974 -13.469 37.018 1.00 19.97 ? 55 GLN A CA 1 ATOM 250 C C . GLN A 1 32 ? 29.515 -13.681 35.607 1.00 19.83 ? 55 GLN A C 1 ATOM 251 O O . GLN A 1 32 ? 28.991 -12.778 34.942 1.00 19.46 ? 55 GLN A O 1 ATOM 252 C CB . GLN A 1 32 ? 28.850 -13.016 37.914 1.00 20.47 ? 55 GLN A CB 1 ATOM 253 C CG . GLN A 1 32 ? 27.936 -14.118 38.497 1.00 18.58 ? 55 GLN A CG 1 ATOM 254 C CD . GLN A 1 32 ? 27.119 -14.863 37.443 1.00 21.14 ? 55 GLN A CD 1 ATOM 255 O OE1 . GLN A 1 32 ? 26.141 -14.347 36.918 1.00 20.74 ? 55 GLN A OE1 1 ATOM 256 N NE2 . GLN A 1 32 ? 27.489 -16.137 37.202 1.00 18.55 ? 55 GLN A NE2 1 ATOM 257 N N . THR A 1 33 ? 29.722 -14.896 35.129 1.00 19.94 ? 56 THR A N 1 ATOM 258 C CA . THR A 1 33 ? 29.483 -15.215 33.697 1.00 20.15 ? 56 THR A CA 1 ATOM 259 C C . THR A 1 33 ? 28.274 -16.142 33.534 1.00 19.37 ? 56 THR A C 1 ATOM 260 O O . THR A 1 33 ? 28.029 -17.004 34.383 1.00 18.05 ? 56 THR A O 1 ATOM 261 C CB . THR A 1 33 ? 30.734 -15.898 33.047 1.00 20.38 ? 56 THR A CB 1 ATOM 262 O OG1 . THR A 1 33 ? 31.038 -17.087 33.781 1.00 18.96 ? 56 THR A OG1 1 ATOM 263 C CG2 . THR A 1 33 ? 31.929 -14.926 33.236 1.00 19.12 ? 56 THR A CG2 1 ATOM 264 N N . GLN A 1 34 ? 27.577 -15.986 32.423 1.00 19.34 ? 57 GLN A N 1 ATOM 265 C CA . GLN A 1 34 ? 26.327 -16.651 32.111 1.00 19.25 ? 57 GLN A CA 1 ATOM 266 C C . GLN A 1 34 ? 26.280 -17.164 30.674 1.00 18.56 ? 57 GLN A C 1 ATOM 267 O O . GLN A 1 34 ? 26.969 -16.680 29.779 1.00 19.63 ? 57 GLN A O 1 ATOM 268 C CB . GLN A 1 34 ? 25.155 -15.687 32.360 1.00 21.76 ? 57 GLN A CB 1 ATOM 269 C CG . GLN A 1 34 ? 25.113 -15.131 33.792 1.00 21.31 ? 57 GLN A CG 1 ATOM 270 C CD . GLN A 1 34 ? 23.903 -14.203 34.032 1.00 21.38 ? 57 GLN A CD 1 ATOM 271 O OE1 . GLN A 1 34 ? 22.949 -14.161 33.205 1.00 20.92 ? 57 GLN A OE1 1 ATOM 272 N NE2 . GLN A 1 34 ? 23.877 -13.534 35.210 1.00 19.21 ? 57 GLN A NE2 1 ATOM 273 N N . PHE A 1 35 ? 25.423 -18.119 30.430 1.00 16.42 ? 58 PHE A N 1 ATOM 274 C CA . PHE A 1 35 ? 25.223 -18.666 29.116 1.00 17.77 ? 58 PHE A CA 1 ATOM 275 C C . PHE A 1 35 ? 23.757 -18.615 28.725 1.00 20.05 ? 58 PHE A C 1 ATOM 276 O O . PHE A 1 35 ? 22.888 -18.694 29.582 1.00 18.34 ? 58 PHE A O 1 ATOM 277 C CB . PHE A 1 35 ? 25.415 -20.186 29.181 1.00 17.81 ? 58 PHE A CB 1 ATOM 278 C CG . PHE A 1 35 ? 26.835 -20.639 29.154 1.00 20.69 ? 58 PHE A CG 1 ATOM 279 C CD1 . PHE A 1 35 ? 27.683 -20.221 28.186 1.00 21.67 ? 58 PHE A CD1 1 ATOM 280 C CD2 . PHE A 1 35 ? 27.251 -21.604 30.047 1.00 20.82 ? 58 PHE A CD2 1 ATOM 281 C CE1 . PHE A 1 35 ? 28.954 -20.771 28.112 1.00 25.44 ? 58 PHE A CE1 1 ATOM 282 C CE2 . PHE A 1 35 ? 28.503 -22.133 29.938 1.00 22.57 ? 58 PHE A CE2 1 ATOM 283 C CZ . PHE A 1 35 ? 29.352 -21.682 29.016 1.00 24.41 ? 58 PHE A CZ 1 ATOM 284 N N . TRP A 1 36 ? 23.513 -18.526 27.425 1.00 20.02 ? 59 TRP A N 1 ATOM 285 C CA . TRP A 1 36 ? 22.202 -18.725 26.814 1.00 18.83 ? 59 TRP A CA 1 ATOM 286 C C . TRP A 1 36 ? 22.401 -19.939 25.897 1.00 19.71 ? 59 TRP A C 1 ATOM 287 O O . TRP A 1 36 ? 22.899 -19.823 24.712 1.00 19.23 ? 59 TRP A O 1 ATOM 288 C CB . TRP A 1 36 ? 21.780 -17.432 26.040 1.00 20.27 ? 59 TRP A CB 1 ATOM 289 C CG . TRP A 1 36 ? 20.455 -17.626 25.412 1.00 21.29 ? 59 TRP A CG 1 ATOM 290 C CD1 . TRP A 1 36 ? 20.197 -17.769 24.046 1.00 24.11 ? 59 TRP A CD1 1 ATOM 291 C CD2 . TRP A 1 36 ? 19.203 -17.670 26.071 1.00 21.22 ? 59 TRP A CD2 1 ATOM 292 N NE1 . TRP A 1 36 ? 18.870 -17.951 23.857 1.00 21.80 ? 59 TRP A NE1 1 ATOM 293 C CE2 . TRP A 1 36 ? 18.217 -17.841 25.055 1.00 21.63 ? 59 TRP A CE2 1 ATOM 294 C CE3 . TRP A 1 36 ? 18.789 -17.514 27.401 1.00 23.42 ? 59 TRP A CE3 1 ATOM 295 C CZ2 . TRP A 1 36 ? 16.902 -17.923 25.332 1.00 19.88 ? 59 TRP A CZ2 1 ATOM 296 C CZ3 . TRP A 1 36 ? 17.415 -17.609 27.689 1.00 21.18 ? 59 TRP A CZ3 1 ATOM 297 C CH2 . TRP A 1 36 ? 16.480 -17.837 26.628 1.00 19.55 ? 59 TRP A CH2 1 ATOM 298 N N . ASP A 1 37 ? 22.002 -21.126 26.369 1.00 18.90 ? 60 ASP A N 1 ATOM 299 C CA . ASP A 1 37 ? 22.266 -22.371 25.674 1.00 19.05 ? 60 ASP A CA 1 ATOM 300 C C . ASP A 1 37 ? 20.966 -22.747 24.943 1.00 20.08 ? 60 ASP A C 1 ATOM 301 O O . ASP A 1 37 ? 19.948 -23.061 25.595 1.00 19.90 ? 60 ASP A O 1 ATOM 302 C CB . ASP A 1 37 ? 22.572 -23.485 26.657 1.00 19.37 ? 60 ASP A CB 1 ATOM 303 C CG . ASP A 1 37 ? 23.975 -23.436 27.272 1.00 24.99 ? 60 ASP A CG 1 ATOM 304 O OD1 . ASP A 1 37 ? 24.829 -22.701 26.760 1.00 26.44 ? 60 ASP A OD1 1 ATOM 305 O OD2 . ASP A 1 37 ? 24.161 -24.123 28.343 1.00 23.29 ? 60 ASP A OD2 1 ATOM 306 N N . TYR A 1 38 ? 20.968 -22.631 23.604 1.00 20.55 ? 61 TYR A N 1 ATOM 307 C CA . TYR A 1 38 ? 19.767 -22.879 22.769 1.00 20.63 ? 61 TYR A CA 1 ATOM 308 C C . TYR A 1 38 ? 19.841 -24.113 21.938 1.00 21.17 ? 61 TYR A C 1 ATOM 309 O O . TYR A 1 38 ? 18.804 -24.733 21.586 1.00 22.96 ? 61 TYR A O 1 ATOM 310 C CB . TYR A 1 38 ? 19.413 -21.608 21.947 1.00 22.26 ? 61 TYR A CB 1 ATOM 311 C CG . TYR A 1 38 ? 20.538 -21.182 21.067 1.00 21.28 ? 61 TYR A CG 1 ATOM 312 C CD1 . TYR A 1 38 ? 21.515 -20.247 21.518 1.00 22.55 ? 61 TYR A CD1 1 ATOM 313 C CD2 . TYR A 1 38 ? 20.772 -21.840 19.869 1.00 24.88 ? 61 TYR A CD2 1 ATOM 314 C CE1 . TYR A 1 38 ? 22.635 -19.891 20.740 1.00 22.65 ? 61 TYR A CE1 1 ATOM 315 C CE2 . TYR A 1 38 ? 21.920 -21.495 19.074 1.00 26.25 ? 61 TYR A CE2 1 ATOM 316 C CZ . TYR A 1 38 ? 22.825 -20.502 19.542 1.00 21.89 ? 61 TYR A CZ 1 ATOM 317 O OH . TYR A 1 38 ? 23.946 -20.181 18.816 1.00 27.80 ? 61 TYR A OH 1 ATOM 318 N N . ASP A 1 39 ? 21.046 -24.581 21.568 1.00 22.85 ? 62 ASP A N 1 ATOM 319 C CA . ASP A 1 39 ? 21.126 -25.789 20.789 1.00 22.62 ? 62 ASP A CA 1 ATOM 320 C C . ASP A 1 39 ? 22.372 -26.591 21.140 1.00 24.01 ? 62 ASP A C 1 ATOM 321 O O . ASP A 1 39 ? 23.452 -26.337 20.595 1.00 22.85 ? 62 ASP A O 1 ATOM 322 C CB . ASP A 1 39 ? 21.146 -25.472 19.266 1.00 24.95 ? 62 ASP A CB 1 ATOM 323 C CG . ASP A 1 39 ? 21.254 -26.755 18.357 1.00 23.43 ? 62 ASP A CG 1 ATOM 324 O OD1 . ASP A 1 39 ? 21.208 -27.909 18.835 1.00 23.77 ? 62 ASP A OD1 1 ATOM 325 O OD2 . ASP A 1 39 ? 21.378 -26.604 17.080 1.00 25.31 ? 62 ASP A OD2 1 ATOM 326 N N . PRO A 1 40 ? 22.230 -27.561 22.032 1.00 22.73 ? 63 PRO A N 1 ATOM 327 C CA . PRO A 1 40 ? 21.002 -27.891 22.756 1.00 22.68 ? 63 PRO A CA 1 ATOM 328 C C . PRO A 1 40 ? 20.638 -26.862 23.841 1.00 22.59 ? 63 PRO A C 1 ATOM 329 O O . PRO A 1 40 ? 21.480 -26.190 24.444 1.00 22.03 ? 63 PRO A O 1 ATOM 330 C CB . PRO A 1 40 ? 21.312 -29.220 23.381 1.00 23.99 ? 63 PRO A CB 1 ATOM 331 C CG . PRO A 1 40 ? 22.760 -29.138 23.671 1.00 26.12 ? 63 PRO A CG 1 ATOM 332 C CD . PRO A 1 40 ? 23.383 -28.317 22.549 1.00 22.79 ? 63 PRO A CD 1 ATOM 333 N N . SER A 1 41 ? 19.348 -26.791 24.127 1.00 20.55 ? 64 SER A N 1 ATOM 334 C CA . SER A 1 41 ? 18.797 -25.946 25.148 1.00 20.44 ? 64 SER A CA 1 ATOM 335 C C . SER A 1 41 ? 18.929 -26.605 26.573 1.00 21.22 ? 64 SER A C 1 ATOM 336 O O . SER A 1 41 ? 18.799 -27.849 26.700 1.00 21.84 ? 64 SER A O 1 ATOM 337 C CB . SER A 1 41 ? 17.311 -25.731 24.864 1.00 19.96 ? 64 SER A CB 1 ATOM 338 O OG . SER A 1 41 ? 17.102 -24.904 23.705 1.00 21.01 ? 64 SER A OG 1 ATOM 339 N N . ASP A 1 42 ? 19.099 -25.758 27.601 1.00 20.72 ? 65 ASP A N 1 ATOM 340 C CA . ASP A 1 42 ? 19.074 -26.207 29.006 1.00 20.69 ? 65 ASP A CA 1 ATOM 341 C C . ASP A 1 42 ? 18.425 -25.071 29.817 1.00 19.82 ? 65 ASP A C 1 ATOM 342 O O . ASP A 1 42 ? 18.149 -23.960 29.296 1.00 19.42 ? 65 ASP A O 1 ATOM 343 C CB . ASP A 1 42 ? 20.447 -26.564 29.519 1.00 20.04 ? 65 ASP A CB 1 ATOM 344 C CG . ASP A 1 42 ? 21.413 -25.388 29.420 1.00 14.85 ? 65 ASP A CG 1 ATOM 345 O OD1 . ASP A 1 42 ? 20.954 -24.231 29.645 1.00 23.38 ? 65 ASP A OD1 1 ATOM 346 O OD2 . ASP A 1 42 ? 22.587 -25.676 29.084 1.00 23.04 ? 65 ASP A OD2 1 ATOM 347 N N . GLY A 1 43 ? 18.093 -25.425 31.044 1.00 18.87 ? 66 GLY A N 1 ATOM 348 C CA . GLY A 1 43 ? 17.545 -24.448 31.986 1.00 17.54 ? 66 GLY A CA 1 ATOM 349 C C . GLY A 1 43 ? 16.170 -24.056 31.601 1.00 19.01 ? 66 GLY A C 1 ATOM 350 O O . GLY A 1 43 ? 15.555 -24.653 30.716 1.00 18.13 ? 66 GLY A O 1 ATOM 351 N N . PRO A 1 44 ? 15.598 -23.087 32.342 1.00 18.46 ? 67 PRO A N 1 ATOM 352 C CA . PRO A 1 44 ? 14.251 -22.672 32.006 1.00 18.41 ? 67 PRO A CA 1 ATOM 353 C C . PRO A 1 44 ? 14.240 -21.926 30.626 1.00 21.22 ? 67 PRO A C 1 ATOM 354 O O . PRO A 1 44 ? 15.275 -21.306 30.255 1.00 19.98 ? 67 PRO A O 1 ATOM 355 C CB . PRO A 1 44 ? 13.926 -21.633 33.075 1.00 19.96 ? 67 PRO A CB 1 ATOM 356 C CG . PRO A 1 44 ? 14.898 -21.807 34.233 1.00 19.78 ? 67 PRO A CG 1 ATOM 357 C CD . PRO A 1 44 ? 16.147 -22.445 33.545 1.00 16.66 ? 67 PRO A CD 1 ATOM 358 N N A SER A 1 45 ? 13.106 -21.953 29.914 0.70 20.58 ? 68 SER A N 1 ATOM 359 N N B SER A 1 45 ? 13.116 -21.976 29.905 0.30 20.89 ? 68 SER A N 1 ATOM 360 C CA A SER A 1 45 ? 12.973 -21.289 28.655 0.70 22.09 ? 68 SER A CA 1 ATOM 361 C CA B SER A 1 45 ? 12.951 -21.247 28.660 0.30 21.74 ? 68 SER A CA 1 ATOM 362 C C A SER A 1 45 ? 13.136 -19.786 28.759 0.70 22.78 ? 68 SER A C 1 ATOM 363 C C B SER A 1 45 ? 13.308 -19.786 28.802 0.30 22.45 ? 68 SER A C 1 ATOM 364 O O A SER A 1 45 ? 13.419 -19.152 27.734 0.70 23.60 ? 68 SER A O 1 ATOM 365 O O B SER A 1 45 ? 13.901 -19.193 27.890 0.30 22.59 ? 68 SER A O 1 ATOM 366 C CB A SER A 1 45 ? 11.630 -21.645 28.017 0.70 22.72 ? 68 SER A CB 1 ATOM 367 C CB B SER A 1 45 ? 11.509 -21.355 28.181 0.30 22.31 ? 68 SER A CB 1 ATOM 368 O OG A SER A 1 45 ? 10.612 -20.936 28.670 0.70 24.81 ? 68 SER A OG 1 ATOM 369 O OG B SER A 1 45 ? 11.173 -22.691 27.922 0.30 21.98 ? 68 SER A OG 1 ATOM 370 N N . ASP A 1 46 ? 12.986 -19.228 29.961 1.00 22.79 ? 69 ASP A N 1 ATOM 371 C CA . ASP A 1 46 ? 13.065 -17.801 30.201 1.00 24.05 ? 69 ASP A CA 1 ATOM 372 C C . ASP A 1 46 ? 14.082 -17.455 31.251 1.00 23.29 ? 69 ASP A C 1 ATOM 373 O O . ASP A 1 46 ? 13.843 -16.565 32.044 1.00 23.81 ? 69 ASP A O 1 ATOM 374 C CB . ASP A 1 46 ? 11.687 -17.259 30.643 1.00 26.04 ? 69 ASP A CB 1 ATOM 375 C CG . ASP A 1 46 ? 11.166 -17.913 31.888 1.00 28.47 ? 69 ASP A CG 1 ATOM 376 O OD1 . ASP A 1 46 ? 11.660 -18.987 32.370 1.00 25.52 ? 69 ASP A OD1 1 ATOM 377 O OD2 . ASP A 1 46 ? 10.175 -17.372 32.382 1.00 34.11 ? 69 ASP A OD2 1 ATOM 378 N N . SER A 1 47 ? 15.207 -18.183 31.290 1.00 21.74 ? 70 SER A N 1 ATOM 379 C CA . SER A 1 47 ? 16.328 -17.793 32.125 1.00 19.39 ? 70 SER A CA 1 ATOM 380 C C . SER A 1 47 ? 17.607 -18.173 31.457 1.00 20.22 ? 70 SER A C 1 ATOM 381 O O . SER A 1 47 ? 17.698 -19.228 30.837 1.00 20.37 ? 70 SER A O 1 ATOM 382 C CB . SER A 1 47 ? 16.247 -18.425 33.505 1.00 19.05 ? 70 SER A CB 1 ATOM 383 O OG . SER A 1 47 ? 17.382 -18.101 34.356 1.00 20.05 ? 70 SER A OG 1 ATOM 384 N N . TRP A 1 48 ? 18.628 -17.327 31.638 1.00 18.89 ? 71 TRP A N 1 ATOM 385 C CA . TRP A 1 48 ? 19.968 -17.679 31.315 1.00 18.57 ? 71 TRP A CA 1 ATOM 386 C C . TRP A 1 48 ? 20.412 -18.586 32.452 1.00 18.65 ? 71 TRP A C 1 ATOM 387 O O . TRP A 1 48 ? 19.647 -18.789 33.437 1.00 20.55 ? 71 TRP A O 1 ATOM 388 C CB . TRP A 1 48 ? 20.806 -16.443 31.299 1.00 19.42 ? 71 TRP A CB 1 ATOM 389 C CG . TRP A 1 48 ? 20.532 -15.534 30.056 1.00 20.38 ? 71 TRP A CG 1 ATOM 390 C CD1 . TRP A 1 48 ? 19.349 -14.967 29.654 1.00 20.80 ? 71 TRP A CD1 1 ATOM 391 C CD2 . TRP A 1 48 ? 21.506 -15.171 29.082 1.00 22.25 ? 71 TRP A CD2 1 ATOM 392 N NE1 . TRP A 1 48 ? 19.559 -14.240 28.480 1.00 23.22 ? 71 TRP A NE1 1 ATOM 393 C CE2 . TRP A 1 48 ? 20.873 -14.363 28.117 1.00 22.95 ? 71 TRP A CE2 1 ATOM 394 C CE3 . TRP A 1 48 ? 22.875 -15.402 28.966 1.00 20.09 ? 71 TRP A CE3 1 ATOM 395 C CZ2 . TRP A 1 48 ? 21.544 -13.839 27.042 1.00 24.59 ? 71 TRP A CZ2 1 ATOM 396 C CZ3 . TRP A 1 48 ? 23.546 -14.887 27.852 1.00 22.54 ? 71 TRP A CZ3 1 ATOM 397 C CH2 . TRP A 1 48 ? 22.871 -14.160 26.901 1.00 22.37 ? 71 TRP A CH2 1 ATOM 398 N N . THR A 1 49 ? 21.593 -19.191 32.259 1.00 16.55 ? 72 THR A N 1 ATOM 399 C CA . THR A 1 49 ? 22.177 -20.087 33.241 1.00 17.71 ? 72 THR A CA 1 ATOM 400 C C . THR A 1 49 ? 23.592 -19.689 33.592 1.00 16.11 ? 72 THR A C 1 ATOM 401 O O . THR A 1 49 ? 24.189 -18.793 32.961 1.00 19.04 ? 72 THR A O 1 ATOM 402 C CB . THR A 1 49 ? 22.133 -21.498 32.695 1.00 15.46 ? 72 THR A CB 1 ATOM 403 O OG1 . THR A 1 49 ? 22.831 -21.555 31.477 1.00 17.16 ? 72 THR A OG1 1 ATOM 404 C CG2 . THR A 1 49 ? 20.733 -22.017 32.473 1.00 15.21 ? 72 THR A CG2 1 ATOM 405 N N . ILE A 1 50 ? 24.151 -20.280 34.639 1.00 17.74 ? 73 ILE A N 1 ATOM 406 C CA . ILE A 1 50 ? 25.439 -19.957 35.167 1.00 14.73 ? 73 ILE A CA 1 ATOM 407 C C . ILE A 1 50 ? 26.544 -20.603 34.345 1.00 16.26 ? 73 ILE A C 1 ATOM 408 O O . ILE A 1 50 ? 26.499 -21.782 33.998 1.00 17.85 ? 73 ILE A O 1 ATOM 409 C CB . ILE A 1 50 ? 25.629 -20.418 36.638 1.00 15.77 ? 73 ILE A CB 1 ATOM 410 C CG1 . ILE A 1 50 ? 24.594 -19.711 37.618 1.00 16.65 ? 73 ILE A CG1 1 ATOM 411 C CG2 . ILE A 1 50 ? 27.097 -20.251 37.143 1.00 14.93 ? 73 ILE A CG2 1 ATOM 412 C CD1 . ILE A 1 50 ? 24.359 -20.431 38.987 1.00 17.06 ? 73 ILE A CD1 1 ATOM 413 N N . HIS A 1 51 ? 27.571 -19.822 34.053 1.00 17.01 ? 74 HIS A N 1 ATOM 414 C CA . HIS A 1 51 ? 28.824 -20.369 33.531 1.00 16.49 ? 74 HIS A CA 1 ATOM 415 C C . HIS A 1 51 ? 29.768 -20.470 34.774 1.00 18.41 ? 74 HIS A C 1 ATOM 416 O O . HIS A 1 51 ? 30.266 -21.542 35.028 1.00 17.37 ? 74 HIS A O 1 ATOM 417 C CB . HIS A 1 51 ? 29.384 -19.513 32.421 1.00 17.35 ? 74 HIS A CB 1 ATOM 418 C CG . HIS A 1 51 ? 30.605 -20.065 31.734 1.00 17.08 ? 74 HIS A CG 1 ATOM 419 N ND1 . HIS A 1 51 ? 31.166 -19.419 30.643 1.00 18.95 ? 74 HIS A ND1 1 ATOM 420 C CD2 . HIS A 1 51 ? 31.330 -21.195 31.931 1.00 21.50 ? 74 HIS A CD2 1 ATOM 421 C CE1 . HIS A 1 51 ? 32.186 -20.164 30.207 1.00 18.81 ? 74 HIS A CE1 1 ATOM 422 N NE2 . HIS A 1 51 ? 32.298 -21.238 30.978 1.00 20.13 ? 74 HIS A NE2 1 ATOM 423 N N . GLY A 1 52 ? 30.050 -19.343 35.445 1.00 18.31 ? 75 GLY A N 1 ATOM 424 C CA . GLY A 1 52 ? 30.888 -19.335 36.657 1.00 18.31 ? 75 GLY A CA 1 ATOM 425 C C . GLY A 1 52 ? 31.103 -17.977 37.311 1.00 19.43 ? 75 GLY A C 1 ATOM 426 O O . GLY A 1 52 ? 30.356 -17.034 37.034 1.00 19.09 ? 75 GLY A O 1 ATOM 427 N N . LEU A 1 53 ? 32.214 -17.919 38.053 1.00 19.91 ? 76 LEU A N 1 ATOM 428 C CA . LEU A 1 53 ? 32.751 -16.771 38.733 1.00 20.31 ? 76 LEU A CA 1 ATOM 429 C C . LEU A 1 53 ? 34.244 -16.817 38.610 1.00 20.25 ? 76 LEU A C 1 ATOM 430 O O . LEU A 1 53 ? 34.901 -17.784 39.046 1.00 19.45 ? 76 LEU A O 1 ATOM 431 C CB . LEU A 1 53 ? 32.303 -16.736 40.196 1.00 21.35 ? 76 LEU A CB 1 ATOM 432 C CG . LEU A 1 53 ? 32.825 -15.481 40.920 1.00 20.54 ? 76 LEU A CG 1 ATOM 433 C CD1 . LEU A 1 53 ? 32.188 -14.165 40.344 1.00 18.87 ? 76 LEU A CD1 1 ATOM 434 C CD2 . LEU A 1 53 ? 32.598 -15.691 42.451 1.00 22.63 ? 76 LEU A CD2 1 ATOM 435 N N . TRP A 1 54 ? 34.785 -15.833 37.912 1.00 19.82 ? 77 TRP A N 1 ATOM 436 C CA . TRP A 1 54 ? 36.205 -15.831 37.560 1.00 20.64 ? 77 TRP A CA 1 ATOM 437 C C . TRP A 1 54 ? 36.924 -14.637 38.106 1.00 21.64 ? 77 TRP A C 1 ATOM 438 O O . TRP A 1 54 ? 36.483 -13.485 37.854 1.00 21.85 ? 77 TRP A O 1 ATOM 439 C CB . TRP A 1 54 ? 36.378 -15.750 36.030 1.00 22.07 ? 77 TRP A CB 1 ATOM 440 C CG . TRP A 1 54 ? 35.598 -16.723 35.216 1.00 20.73 ? 77 TRP A CG 1 ATOM 441 C CD1 . TRP A 1 54 ? 35.057 -17.960 35.632 1.00 20.67 ? 77 TRP A CD1 1 ATOM 442 C CD2 . TRP A 1 54 ? 35.286 -16.632 33.806 1.00 21.69 ? 77 TRP A CD2 1 ATOM 443 N NE1 . TRP A 1 54 ? 34.442 -18.575 34.593 1.00 22.30 ? 77 TRP A NE1 1 ATOM 444 C CE2 . TRP A 1 54 ? 34.550 -17.803 33.462 1.00 19.63 ? 77 TRP A CE2 1 ATOM 445 C CE3 . TRP A 1 54 ? 35.509 -15.671 32.824 1.00 22.81 ? 77 TRP A CE3 1 ATOM 446 C CZ2 . TRP A 1 54 ? 34.028 -18.029 32.177 1.00 22.57 ? 77 TRP A CZ2 1 ATOM 447 C CZ3 . TRP A 1 54 ? 35.014 -15.927 31.520 1.00 24.56 ? 77 TRP A CZ3 1 ATOM 448 C CH2 . TRP A 1 54 ? 34.304 -17.080 31.221 1.00 23.10 ? 77 TRP A CH2 1 ATOM 449 N N . PRO A 1 55 ? 38.080 -14.862 38.750 1.00 23.58 ? 78 PRO A N 1 ATOM 450 C CA . PRO A 1 55 ? 38.940 -13.751 39.132 1.00 26.76 ? 78 PRO A CA 1 ATOM 451 C C . PRO A 1 55 ? 39.850 -13.344 37.965 1.00 27.65 ? 78 PRO A C 1 ATOM 452 O O . PRO A 1 55 ? 40.645 -14.145 37.511 1.00 31.71 ? 78 PRO A O 1 ATOM 453 C CB . PRO A 1 55 ? 39.800 -14.347 40.287 1.00 26.43 ? 78 PRO A CB 1 ATOM 454 C CG . PRO A 1 55 ? 39.839 -15.916 40.020 1.00 25.77 ? 78 PRO A CG 1 ATOM 455 C CD . PRO A 1 55 ? 38.542 -16.185 39.258 1.00 23.81 ? 78 PRO A CD 1 ATOM 456 N N . ASP A 1 56 ? 39.682 -12.172 37.387 1.00 26.36 ? 79 ASP A N 1 ATOM 457 C CA . ASP A 1 56 ? 40.649 -11.667 36.455 1.00 26.56 ? 79 ASP A CA 1 ATOM 458 C C . ASP A 1 56 ? 41.571 -10.708 37.192 1.00 26.71 ? 79 ASP A C 1 ATOM 459 O O . ASP A 1 56 ? 41.153 -10.049 38.186 1.00 24.78 ? 79 ASP A O 1 ATOM 460 C CB . ASP A 1 56 ? 39.942 -10.811 35.381 1.00 27.82 ? 79 ASP A CB 1 ATOM 461 C CG . ASP A 1 56 ? 39.377 -11.600 34.157 1.00 32.68 ? 79 ASP A CG 1 ATOM 462 O OD1 . ASP A 1 56 ? 39.171 -12.849 34.235 1.00 33.26 ? 79 ASP A OD1 1 ATOM 463 O OD2 . ASP A 1 56 ? 39.109 -10.807 33.152 1.00 34.55 ? 79 ASP A OD2 1 ATOM 464 N N . ASN A 1 57 ? 42.797 -10.582 36.673 1.00 25.22 ? 80 ASN A N 1 ATOM 465 C CA . ASN A 1 57 ? 43.661 -9.478 36.960 1.00 27.30 ? 80 ASN A CA 1 ATOM 466 C C . ASN A 1 57 ? 43.037 -8.128 36.538 1.00 27.35 ? 80 ASN A C 1 ATOM 467 O O . ASN A 1 57 ? 42.097 -8.077 35.695 1.00 27.84 ? 80 ASN A O 1 ATOM 468 C CB . ASN A 1 57 ? 45.018 -9.682 36.328 1.00 28.37 ? 80 ASN A CB 1 ATOM 469 C CG . ASN A 1 57 ? 45.668 -10.913 36.838 1.00 31.06 ? 80 ASN A CG 1 ATOM 470 O OD1 . ASN A 1 57 ? 45.457 -11.244 37.992 1.00 32.35 ? 80 ASN A OD1 1 ATOM 471 N ND2 . ASN A 1 57 ? 46.313 -11.710 35.937 1.00 33.93 ? 80 ASN A ND2 1 ATOM 472 N N . CYS A 1 58 ? 43.496 -7.062 37.165 1.00 27.93 ? 81 CYS A N 1 ATOM 473 C CA . CYS A 1 58 ? 42.942 -5.732 36.923 1.00 29.20 ? 81 CYS A CA 1 ATOM 474 C C . CYS A 1 58 ? 43.138 -5.285 35.452 1.00 30.68 ? 81 CYS A C 1 ATOM 475 O O . CYS A 1 58 ? 42.374 -4.444 34.957 1.00 30.27 ? 81 CYS A O 1 ATOM 476 C CB . CYS A 1 58 ? 43.454 -4.726 37.965 1.00 32.07 ? 81 CYS A CB 1 ATOM 477 S SG . CYS A 1 58 ? 43.035 -5.282 39.646 1.00 33.52 ? 81 CYS A SG 1 ATOM 478 N N . ASP A 1 59 ? 44.136 -5.851 34.774 1.00 31.87 ? 82 ASP A N 1 ATOM 479 C CA . ASP A 1 59 ? 44.406 -5.527 33.382 1.00 34.47 ? 82 ASP A CA 1 ATOM 480 C C . ASP A 1 59 ? 43.632 -6.424 32.410 1.00 34.07 ? 82 ASP A C 1 ATOM 481 O O . ASP A 1 59 ? 43.790 -6.297 31.216 1.00 35.81 ? 82 ASP A O 1 ATOM 482 C CB . ASP A 1 59 ? 45.928 -5.526 33.046 1.00 34.85 ? 82 ASP A CB 1 ATOM 483 C CG . ASP A 1 59 ? 46.566 -6.870 33.141 1.00 38.61 ? 82 ASP A CG 1 ATOM 484 O OD1 . ASP A 1 59 ? 45.834 -7.830 33.468 1.00 38.00 ? 82 ASP A OD1 1 ATOM 485 O OD2 . ASP A 1 59 ? 47.810 -7.004 32.871 1.00 45.24 ? 82 ASP A OD2 1 ATOM 486 N N . GLY A 1 60 ? 42.787 -7.318 32.889 1.00 32.14 ? 83 GLY A N 1 ATOM 487 C CA . GLY A 1 60 ? 42.093 -8.251 32.024 1.00 32.90 ? 83 GLY A CA 1 ATOM 488 C C . GLY A 1 60 ? 42.778 -9.573 31.702 1.00 32.05 ? 83 GLY A C 1 ATOM 489 O O . GLY A 1 60 ? 42.143 -10.441 31.101 1.00 32.08 ? 83 GLY A O 1 ATOM 490 N N . THR A 1 61 ? 44.046 -9.747 32.076 1.00 31.80 ? 84 THR A N 1 ATOM 491 C CA . THR A 1 61 ? 44.651 -11.056 31.971 1.00 32.19 ? 84 THR A CA 1 ATOM 492 C C . THR A 1 61 ? 44.049 -11.910 33.086 1.00 32.20 ? 84 THR A C 1 ATOM 493 O O . THR A 1 61 ? 43.234 -11.419 33.900 1.00 28.82 ? 84 THR A O 1 ATOM 494 C CB . THR A 1 61 ? 46.199 -10.975 32.059 1.00 34.25 ? 84 THR A CB 1 ATOM 495 O OG1 . THR A 1 61 ? 46.555 -10.316 33.285 1.00 33.31 ? 84 THR A OG1 1 ATOM 496 C CG2 . THR A 1 61 ? 46.790 -10.212 30.747 1.00 32.15 ? 84 THR A CG2 1 ATOM 497 N N . TYR A 1 62 ? 44.409 -13.173 33.193 1.00 32.73 ? 85 TYR A N 1 ATOM 498 C CA . TYR A 1 62 ? 43.869 -13.924 34.365 1.00 34.08 ? 85 TYR A CA 1 ATOM 499 C C . TYR A 1 62 ? 44.776 -15.026 34.668 1.00 34.22 ? 85 TYR A C 1 ATOM 500 O O . TYR A 1 62 ? 45.584 -15.352 33.826 1.00 34.13 ? 85 TYR A O 1 ATOM 501 C CB . TYR A 1 62 ? 42.497 -14.471 34.092 1.00 35.36 ? 85 TYR A CB 1 ATOM 502 C CG . TYR A 1 62 ? 42.404 -15.290 32.798 1.00 35.96 ? 85 TYR A CG 1 ATOM 503 C CD1 . TYR A 1 62 ? 42.451 -16.692 32.857 1.00 41.04 ? 85 TYR A CD1 1 ATOM 504 C CD2 . TYR A 1 62 ? 42.223 -14.663 31.539 1.00 38.38 ? 85 TYR A CD2 1 ATOM 505 C CE1 . TYR A 1 62 ? 42.305 -17.493 31.688 1.00 43.28 ? 85 TYR A CE1 1 ATOM 506 C CE2 . TYR A 1 62 ? 42.083 -15.427 30.368 1.00 43.04 ? 85 TYR A CE2 1 ATOM 507 C CZ . TYR A 1 62 ? 42.158 -16.849 30.453 1.00 47.01 ? 85 TYR A CZ 1 ATOM 508 O OH . TYR A 1 62 ? 42.010 -17.700 29.366 1.00 49.35 ? 85 TYR A OH 1 ATOM 509 N N A GLN A 1 63 ? 44.752 -15.493 35.930 0.50 34.13 ? 86 GLN A N 1 ATOM 510 N N B GLN A 1 63 ? 44.680 -15.569 35.871 0.50 34.17 ? 86 GLN A N 1 ATOM 511 C CA A GLN A 1 63 ? 45.443 -16.715 36.361 0.50 33.81 ? 86 GLN A CA 1 ATOM 512 C CA B GLN A 1 63 ? 45.420 -16.756 36.216 0.50 33.93 ? 86 GLN A CA 1 ATOM 513 C C A GLN A 1 63 ? 44.415 -17.874 36.174 0.50 30.75 ? 86 GLN A C 1 ATOM 514 C C B GLN A 1 63 ? 44.396 -17.894 36.154 0.50 30.76 ? 86 GLN A C 1 ATOM 515 O O A GLN A 1 63 ? 43.234 -17.645 36.035 0.50 28.18 ? 86 GLN A O 1 ATOM 516 O O B GLN A 1 63 ? 43.207 -17.676 36.071 0.50 28.32 ? 86 GLN A O 1 ATOM 517 C CB A GLN A 1 63 ? 45.947 -16.695 37.847 0.50 34.87 ? 86 GLN A CB 1 ATOM 518 C CB B GLN A 1 63 ? 46.064 -16.658 37.606 0.50 34.93 ? 86 GLN A CB 1 ATOM 519 C CG A GLN A 1 63 ? 46.463 -15.324 38.542 0.50 37.88 ? 86 GLN A CG 1 ATOM 520 C CG B GLN A 1 63 ? 46.856 -15.348 37.893 0.50 37.88 ? 86 GLN A CG 1 ATOM 521 C CD A GLN A 1 63 ? 47.218 -15.572 39.867 0.50 38.10 ? 86 GLN A CD 1 ATOM 522 C CD B GLN A 1 63 ? 48.053 -15.218 37.045 0.50 41.07 ? 86 GLN A CD 1 ATOM 523 O OE1 A GLN A 1 63 ? 46.698 -15.380 40.991 0.50 40.61 ? 86 GLN A OE1 1 ATOM 524 O OE1 B GLN A 1 63 ? 48.925 -16.094 37.061 0.50 45.65 ? 86 GLN A OE1 1 ATOM 525 N NE2 A GLN A 1 63 ? 48.437 -16.025 39.729 0.50 36.08 ? 86 GLN A NE2 1 ATOM 526 N NE2 B GLN A 1 63 ? 48.132 -14.121 36.287 0.50 38.21 ? 86 GLN A NE2 1 ATOM 527 N N . GLU A 1 64 ? 44.906 -19.103 36.190 1.00 29.96 ? 87 GLU A N 1 ATOM 528 C CA . GLU A 1 64 ? 44.075 -20.298 36.063 1.00 28.14 ? 87 GLU A CA 1 ATOM 529 C C . GLU A 1 64 ? 44.746 -21.438 36.790 1.00 28.16 ? 87 GLU A C 1 ATOM 530 O O . GLU A 1 64 ? 45.992 -21.523 36.805 1.00 31.06 ? 87 GLU A O 1 ATOM 531 C CB . GLU A 1 64 ? 43.839 -20.618 34.567 1.00 27.19 ? 87 GLU A CB 1 ATOM 532 C CG . GLU A 1 64 ? 45.033 -20.772 33.686 1.00 33.11 ? 87 GLU A CG 1 ATOM 533 C CD . GLU A 1 64 ? 44.549 -21.077 32.243 1.00 38.00 ? 87 GLU A CD 1 ATOM 534 O OE1 . GLU A 1 64 ? 44.274 -20.131 31.485 1.00 49.26 ? 87 GLU A OE1 1 ATOM 535 O OE2 . GLU A 1 64 ? 44.226 -22.194 31.942 1.00 40.82 ? 87 GLU A OE2 1 ATOM 536 N N . TYR A 1 65 ? 43.966 -22.324 37.405 1.00 26.80 ? 88 TYR A N 1 ATOM 537 C CA . TYR A 1 65 ? 44.545 -23.528 38.008 1.00 25.67 ? 88 TYR A CA 1 ATOM 538 C C . TYR A 1 65 ? 45.600 -23.212 39.041 1.00 26.61 ? 88 TYR A C 1 ATOM 539 O O . TYR A 1 65 ? 46.757 -23.656 38.921 1.00 25.46 ? 88 TYR A O 1 ATOM 540 C CB . TYR A 1 65 ? 45.106 -24.466 36.947 1.00 27.79 ? 88 TYR A CB 1 ATOM 541 C CG . TYR A 1 65 ? 44.003 -24.974 35.966 1.00 26.10 ? 88 TYR A CG 1 ATOM 542 C CD1 . TYR A 1 65 ? 43.014 -25.847 36.406 1.00 21.19 ? 88 TYR A CD1 1 ATOM 543 C CD2 . TYR A 1 65 ? 43.931 -24.510 34.674 1.00 26.08 ? 88 TYR A CD2 1 ATOM 544 C CE1 . TYR A 1 65 ? 42.060 -26.351 35.567 1.00 23.13 ? 88 TYR A CE1 1 ATOM 545 C CE2 . TYR A 1 65 ? 42.888 -24.935 33.804 1.00 24.19 ? 88 TYR A CE2 1 ATOM 546 C CZ . TYR A 1 65 ? 42.003 -25.879 34.218 1.00 22.69 ? 88 TYR A CZ 1 ATOM 547 O OH . TYR A 1 65 ? 40.955 -26.312 33.429 1.00 21.38 ? 88 TYR A OH 1 ATOM 548 N N . CYS A 1 66 ? 45.208 -22.419 40.036 1.00 26.76 ? 89 CYS A N 1 ATOM 549 C CA . CYS A 1 66 ? 46.219 -21.793 40.928 1.00 27.83 ? 89 CYS A CA 1 ATOM 550 C C . CYS A 1 66 ? 46.652 -22.688 42.080 1.00 27.34 ? 89 CYS A C 1 ATOM 551 O O . CYS A 1 66 ? 47.643 -22.397 42.763 1.00 28.47 ? 89 CYS A O 1 ATOM 552 C CB . CYS A 1 66 ? 45.719 -20.481 41.459 1.00 28.34 ? 89 CYS A CB 1 ATOM 553 S SG . CYS A 1 66 ? 45.477 -19.160 40.226 1.00 32.44 ? 89 CYS A SG 1 ATOM 554 N N . ASP A 1 67 ? 45.941 -23.792 42.310 1.00 26.36 ? 90 ASP A N 1 ATOM 555 C CA . ASP A 1 67 ? 46.301 -24.638 43.452 1.00 27.50 ? 90 ASP A CA 1 ATOM 556 C C . ASP A 1 67 ? 45.968 -26.085 43.258 1.00 26.80 ? 90 ASP A C 1 ATOM 557 O O . ASP A 1 67 ? 44.868 -26.486 43.615 1.00 24.95 ? 90 ASP A O 1 ATOM 558 C CB . ASP A 1 67 ? 45.667 -24.141 44.735 1.00 25.98 ? 90 ASP A CB 1 ATOM 559 C CG . ASP A 1 67 ? 46.299 -24.776 46.000 1.00 30.17 ? 90 ASP A CG 1 ATOM 560 O OD1 . ASP A 1 67 ? 47.087 -25.759 45.870 1.00 29.06 ? 90 ASP A OD1 1 ATOM 561 O OD2 . ASP A 1 67 ? 45.971 -24.266 47.111 1.00 29.48 ? 90 ASP A OD2 1 ATOM 562 N N A GLU A 1 68 ? 46.906 -26.862 42.721 0.50 27.85 ? 91 GLU A N 1 ATOM 563 N N B GLU A 1 68 ? 46.935 -26.835 42.718 0.50 28.18 ? 91 GLU A N 1 ATOM 564 C CA A GLU A 1 68 ? 46.685 -28.275 42.452 0.50 29.23 ? 91 GLU A CA 1 ATOM 565 C CA B GLU A 1 68 ? 46.833 -28.268 42.453 0.50 29.85 ? 91 GLU A CA 1 ATOM 566 C C A GLU A 1 68 ? 46.355 -29.042 43.731 0.50 29.57 ? 91 GLU A C 1 ATOM 567 C C B GLU A 1 68 ? 46.404 -29.033 43.708 0.50 29.91 ? 91 GLU A C 1 ATOM 568 O O A GLU A 1 68 ? 45.647 -30.065 43.693 0.50 30.02 ? 91 GLU A O 1 ATOM 569 O O B GLU A 1 68 ? 45.683 -30.044 43.625 0.50 30.47 ? 91 GLU A O 1 ATOM 570 C CB A GLU A 1 68 ? 47.891 -28.918 41.747 0.50 31.13 ? 91 GLU A CB 1 ATOM 571 C CB B GLU A 1 68 ? 48.182 -28.842 41.925 0.50 32.15 ? 91 GLU A CB 1 ATOM 572 C CG A GLU A 1 68 ? 47.741 -30.412 41.475 0.50 34.10 ? 91 GLU A CG 1 ATOM 573 C CG B GLU A 1 68 ? 48.714 -28.171 40.636 0.50 36.51 ? 91 GLU A CG 1 ATOM 574 C CD A GLU A 1 68 ? 48.743 -30.921 40.467 0.50 39.17 ? 91 GLU A CD 1 ATOM 575 C CD B GLU A 1 68 ? 50.200 -28.480 40.301 0.50 43.85 ? 91 GLU A CD 1 ATOM 576 O OE1 A GLU A 1 68 ? 49.585 -30.115 39.996 0.50 39.77 ? 91 GLU A OE1 1 ATOM 577 O OE1 B GLU A 1 68 ? 50.788 -29.433 40.874 0.50 43.09 ? 91 GLU A OE1 1 ATOM 578 O OE2 A GLU A 1 68 ? 48.666 -32.118 40.140 0.50 44.16 ? 91 GLU A OE2 1 ATOM 579 O OE2 B GLU A 1 68 ? 50.757 -27.735 39.436 0.50 48.52 ? 91 GLU A OE2 1 ATOM 580 N N . SER A 1 69 ? 46.825 -28.554 44.871 1.00 29.07 ? 92 SER A N 1 ATOM 581 C CA . SER A 1 69 ? 46.531 -29.244 46.115 1.00 30.50 ? 92 SER A CA 1 ATOM 582 C C . SER A 1 69 ? 45.047 -29.102 46.525 1.00 28.40 ? 92 SER A C 1 ATOM 583 O O . SER A 1 69 ? 44.558 -29.835 47.362 1.00 28.70 ? 92 SER A O 1 ATOM 584 C CB . SER A 1 69 ? 47.473 -28.731 47.226 1.00 30.32 ? 92 SER A CB 1 ATOM 585 O OG . SER A 1 69 ? 46.977 -27.526 47.813 1.00 30.06 ? 92 SER A OG 1 ATOM 586 N N . ARG A 1 70 ? 44.330 -28.161 45.911 1.00 26.10 ? 93 ARG A N 1 ATOM 587 C CA . ARG A 1 70 ? 42.900 -27.991 46.202 1.00 23.92 ? 93 ARG A CA 1 ATOM 588 C C . ARG A 1 70 ? 42.057 -28.140 44.921 1.00 25.28 ? 93 ARG A C 1 ATOM 589 O O . ARG A 1 70 ? 41.024 -27.517 44.804 1.00 23.24 ? 93 ARG A O 1 ATOM 590 C CB . ARG A 1 70 ? 42.580 -26.665 46.859 1.00 24.18 ? 93 ARG A CB 1 ATOM 591 C CG . ARG A 1 70 ? 43.210 -26.510 48.248 1.00 25.49 ? 93 ARG A CG 1 ATOM 592 C CD . ARG A 1 70 ? 42.831 -25.210 48.927 1.00 26.03 ? 93 ARG A CD 1 ATOM 593 N NE . ARG A 1 70 ? 43.197 -24.081 48.135 1.00 23.42 ? 93 ARG A NE 1 ATOM 594 C CZ . ARG A 1 70 ? 42.386 -23.120 47.676 1.00 22.84 ? 93 ARG A CZ 1 ATOM 595 N NH1 . ARG A 1 70 ? 41.094 -23.052 47.934 1.00 20.48 ? 93 ARG A NH1 1 ATOM 596 N NH2 . ARG A 1 70 ? 42.920 -22.140 46.943 1.00 22.80 ? 93 ARG A NH2 1 ATOM 597 N N . GLU A 1 71 ? 42.504 -28.993 44.013 1.00 25.15 ? 94 GLU A N 1 ATOM 598 C CA . GLU A 1 71 ? 41.688 -29.406 42.865 1.00 25.27 ? 94 GLU A CA 1 ATOM 599 C C . GLU A 1 71 ? 41.019 -30.731 43.169 1.00 24.64 ? 94 GLU A C 1 ATOM 600 O O . GLU A 1 71 ? 41.601 -31.620 43.818 1.00 24.54 ? 94 GLU A O 1 ATOM 601 C CB . GLU A 1 71 ? 42.571 -29.544 41.643 1.00 25.27 ? 94 GLU A CB 1 ATOM 602 C CG . GLU A 1 71 ? 42.982 -28.179 41.135 1.00 28.72 ? 94 GLU A CG 1 ATOM 603 C CD . GLU A 1 71 ? 43.887 -28.344 39.854 1.00 35.82 ? 94 GLU A CD 1 ATOM 604 O OE1 . GLU A 1 71 ? 43.914 -29.408 39.282 1.00 45.72 ? 94 GLU A OE1 1 ATOM 605 O OE2 . GLU A 1 71 ? 44.647 -27.460 39.524 1.00 39.23 ? 94 GLU A OE2 1 ATOM 606 N N . TYR A 1 72 ? 39.768 -30.849 42.751 1.00 21.84 ? 95 TYR A N 1 ATOM 607 C CA . TYR A 1 72 ? 38.913 -31.971 43.101 1.00 21.96 ? 95 TYR A CA 1 ATOM 608 C C . TYR A 1 72 ? 38.198 -32.619 41.955 1.00 22.70 ? 95 TYR A C 1 ATOM 609 O O . TYR A 1 72 ? 37.979 -31.974 40.892 1.00 22.57 ? 95 TYR A O 1 ATOM 610 C CB . TYR A 1 72 ? 37.837 -31.457 44.126 1.00 22.32 ? 95 TYR A CB 1 ATOM 611 C CG . TYR A 1 72 ? 38.569 -30.957 45.404 1.00 20.25 ? 95 TYR A CG 1 ATOM 612 C CD1 . TYR A 1 72 ? 39.287 -31.861 46.213 1.00 22.75 ? 95 TYR A CD1 1 ATOM 613 C CD2 . TYR A 1 72 ? 38.546 -29.638 45.770 1.00 24.39 ? 95 TYR A CD2 1 ATOM 614 C CE1 . TYR A 1 72 ? 40.016 -31.423 47.309 1.00 25.51 ? 95 TYR A CE1 1 ATOM 615 C CE2 . TYR A 1 72 ? 39.237 -29.197 46.868 1.00 22.92 ? 95 TYR A CE2 1 ATOM 616 C CZ . TYR A 1 72 ? 39.941 -30.060 47.654 1.00 24.48 ? 95 TYR A CZ 1 ATOM 617 O OH . TYR A 1 72 ? 40.665 -29.582 48.752 1.00 23.51 ? 95 TYR A OH 1 ATOM 618 N N A SER A 1 73 ? 37.847 -33.905 42.127 0.50 21.91 ? 96 SER A N 1 ATOM 619 N N B SER A 1 73 ? 37.819 -33.881 42.169 0.50 22.45 ? 96 SER A N 1 ATOM 620 C CA A SER A 1 73 ? 37.054 -34.648 41.146 0.50 22.36 ? 96 SER A CA 1 ATOM 621 C CA B SER A 1 73 ? 37.102 -34.651 41.190 0.50 23.45 ? 96 SER A CA 1 ATOM 622 C C A SER A 1 73 ? 35.773 -35.136 41.789 0.50 22.41 ? 96 SER A C 1 ATOM 623 C C B SER A 1 73 ? 35.810 -35.154 41.811 0.50 22.90 ? 96 SER A C 1 ATOM 624 O O A SER A 1 73 ? 35.163 -36.103 41.318 0.50 21.86 ? 96 SER A O 1 ATOM 625 O O B SER A 1 73 ? 35.223 -36.130 41.335 0.50 22.54 ? 96 SER A O 1 ATOM 626 C CB A SER A 1 73 ? 37.828 -35.873 40.597 0.50 24.23 ? 96 SER A CB 1 ATOM 627 C CB B SER A 1 73 ? 38.012 -35.799 40.683 0.50 25.44 ? 96 SER A CB 1 ATOM 628 O OG A SER A 1 73 ? 38.371 -36.609 41.656 0.50 23.69 ? 96 SER A OG 1 ATOM 629 O OG B SER A 1 73 ? 39.169 -35.209 40.078 0.50 28.26 ? 96 SER A OG 1 ATOM 630 N N . ASN A 1 74 ? 35.300 -34.424 42.798 1.00 21.36 ? 97 ASN A N 1 ATOM 631 C CA . ASN A 1 74 ? 34.126 -34.903 43.569 1.00 22.94 ? 97 ASN A CA 1 ATOM 632 C C . ASN A 1 74 ? 33.343 -33.782 44.162 1.00 22.29 ? 97 ASN A C 1 ATOM 633 O O . ASN A 1 74 ? 32.948 -33.843 45.327 1.00 20.94 ? 97 ASN A O 1 ATOM 634 C CB . ASN A 1 74 ? 34.534 -35.851 44.676 1.00 22.74 ? 97 ASN A CB 1 ATOM 635 C CG . ASN A 1 74 ? 35.478 -35.155 45.725 1.00 24.84 ? 97 ASN A CG 1 ATOM 636 O OD1 . ASN A 1 74 ? 35.994 -34.066 45.512 1.00 20.70 ? 97 ASN A OD1 1 ATOM 637 N ND2 . ASN A 1 74 ? 35.719 -35.826 46.818 1.00 29.21 ? 97 ASN A ND2 1 ATOM 638 N N . ILE A 1 75 ? 33.020 -32.797 43.317 1.00 21.46 ? 98 ILE A N 1 ATOM 639 C CA . ILE A 1 75 ? 32.272 -31.640 43.787 1.00 19.42 ? 98 ILE A CA 1 ATOM 640 C C . ILE A 1 75 ? 30.902 -32.010 44.297 1.00 20.10 ? 98 ILE A C 1 ATOM 641 O O . ILE A 1 75 ? 30.461 -31.505 45.332 1.00 19.07 ? 98 ILE A O 1 ATOM 642 C CB . ILE A 1 75 ? 32.097 -30.580 42.633 1.00 17.74 ? 98 ILE A CB 1 ATOM 643 C CG1 . ILE A 1 75 ? 33.422 -29.953 42.162 1.00 19.63 ? 98 ILE A CG1 1 ATOM 644 C CG2 . ILE A 1 75 ? 31.095 -29.451 43.068 1.00 17.78 ? 98 ILE A CG2 1 ATOM 645 C CD1 . ILE A 1 75 ? 34.257 -29.260 43.277 1.00 16.51 ? 98 ILE A CD1 1 ATOM 646 N N . THR A 1 76 ? 30.189 -32.911 43.612 1.00 20.08 ? 99 THR A N 1 ATOM 647 C CA . THR A 1 76 ? 28.839 -33.288 44.019 1.00 20.94 ? 99 THR A CA 1 ATOM 648 C C . THR A 1 76 ? 28.899 -33.963 45.401 1.00 21.84 ? 99 THR A C 1 ATOM 649 O O . THR A 1 76 ? 28.105 -33.711 46.318 1.00 21.11 ? 99 THR A O 1 ATOM 650 C CB . THR A 1 76 ? 28.256 -34.326 43.033 1.00 22.29 ? 99 THR A CB 1 ATOM 651 O OG1 . THR A 1 76 ? 28.101 -33.672 41.797 1.00 22.85 ? 99 THR A OG1 1 ATOM 652 C CG2 . THR A 1 76 ? 26.866 -34.851 43.484 1.00 23.87 ? 99 THR A CG2 1 ATOM 653 N N . SER A 1 77 ? 29.900 -34.800 45.599 1.00 22.13 ? 100 SER A N 1 ATOM 654 C CA . SER A 1 77 ? 30.069 -35.439 46.920 1.00 22.13 ? 100 SER A CA 1 ATOM 655 C C . SER A 1 77 ? 30.409 -34.447 48.019 1.00 22.93 ? 100 SER A C 1 ATOM 656 O O . SER A 1 77 ? 29.973 -34.597 49.193 1.00 20.15 ? 100 SER A O 1 ATOM 657 C CB . SER A 1 77 ? 31.158 -36.528 46.875 1.00 24.75 ? 100 SER A CB 1 ATOM 658 O OG . SER A 1 77 ? 30.733 -37.536 45.960 1.00 28.04 ? 100 SER A OG 1 ATOM 659 N N . ILE A 1 78 ? 31.239 -33.444 47.686 1.00 20.94 ? 101 ILE A N 1 ATOM 660 C CA . ILE A 1 78 ? 31.604 -32.384 48.664 1.00 19.89 ? 101 ILE A CA 1 ATOM 661 C C . ILE A 1 78 ? 30.359 -31.613 49.048 1.00 18.69 ? 101 ILE A C 1 ATOM 662 O O . ILE A 1 78 ? 30.084 -31.439 50.248 1.00 21.03 ? 101 ILE A O 1 ATOM 663 C CB . ILE A 1 78 ? 32.635 -31.448 48.078 1.00 19.70 ? 101 ILE A CB 1 ATOM 664 C CG1 . ILE A 1 78 ? 33.992 -32.109 48.003 1.00 21.23 ? 101 ILE A CG1 1 ATOM 665 C CG2 . ILE A 1 78 ? 32.654 -30.101 48.866 1.00 20.06 ? 101 ILE A CG2 1 ATOM 666 C CD1 . ILE A 1 78 ? 34.969 -31.383 47.085 1.00 20.41 ? 101 ILE A CD1 1 ATOM 667 N N . LEU A 1 79 ? 29.532 -31.237 48.089 1.00 18.45 ? 102 LEU A N 1 ATOM 668 C CA . LEU A 1 79 ? 28.322 -30.506 48.433 1.00 20.34 ? 102 LEU A CA 1 ATOM 669 C C . LEU A 1 79 ? 27.333 -31.349 49.273 1.00 19.27 ? 102 LEU A C 1 ATOM 670 O O . LEU A 1 79 ? 26.686 -30.830 50.233 1.00 20.15 ? 102 LEU A O 1 ATOM 671 C CB . LEU A 1 79 ? 27.602 -29.933 47.203 1.00 20.55 ? 102 LEU A CB 1 ATOM 672 C CG . LEU A 1 79 ? 28.468 -28.981 46.325 1.00 22.57 ? 102 LEU A CG 1 ATOM 673 C CD1 . LEU A 1 79 ? 27.733 -28.525 45.010 1.00 22.22 ? 102 LEU A CD1 1 ATOM 674 C CD2 . LEU A 1 79 ? 28.868 -27.753 47.053 1.00 20.33 ? 102 LEU A CD2 1 ATOM 675 N N . GLU A 1 80 ? 27.152 -32.592 48.930 1.00 22.51 ? 103 GLU A N 1 ATOM 676 C CA . GLU A 1 80 ? 26.292 -33.480 49.751 1.00 23.65 ? 103 GLU A CA 1 ATOM 677 C C . GLU A 1 80 ? 26.772 -33.696 51.163 1.00 26.09 ? 103 GLU A C 1 ATOM 678 O O . GLU A 1 80 ? 25.971 -33.634 52.072 1.00 24.47 ? 103 GLU A O 1 ATOM 679 C CB . GLU A 1 80 ? 26.205 -34.855 49.093 1.00 25.66 ? 103 GLU A CB 1 ATOM 680 C CG . GLU A 1 80 ? 25.378 -34.783 47.777 1.00 27.95 ? 103 GLU A CG 1 ATOM 681 C CD . GLU A 1 80 ? 25.533 -36.019 46.812 1.00 32.29 ? 103 GLU A CD 1 ATOM 682 O OE1 . GLU A 1 80 ? 26.550 -36.752 46.892 1.00 34.88 ? 103 GLU A OE1 1 ATOM 683 O OE2 . GLU A 1 80 ? 24.631 -36.154 45.895 1.00 35.98 ? 103 GLU A OE2 1 ATOM 684 N N . ALA A 1 81 ? 28.089 -33.902 51.352 1.00 26.27 ? 104 ALA A N 1 ATOM 685 C CA . ALA A 1 81 ? 28.667 -34.086 52.676 1.00 26.29 ? 104 ALA A CA 1 ATOM 686 C C . ALA A 1 81 ? 28.475 -32.799 53.513 1.00 26.07 ? 104 ALA A C 1 ATOM 687 O O . ALA A 1 81 ? 28.422 -32.826 54.724 1.00 26.17 ? 104 ALA A O 1 ATOM 688 C CB . ALA A 1 81 ? 30.141 -34.435 52.543 1.00 27.08 ? 104 ALA A CB 1 ATOM 689 N N . GLN A 1 82 ? 28.362 -31.664 52.866 1.00 23.00 ? 105 GLN A N 1 ATOM 690 C CA . GLN A 1 82 ? 28.194 -30.385 53.558 1.00 22.79 ? 105 GLN A CA 1 ATOM 691 C C . GLN A 1 82 ? 26.724 -30.078 53.747 1.00 24.14 ? 105 GLN A C 1 ATOM 692 O O . GLN A 1 82 ? 26.404 -28.976 54.207 1.00 22.64 ? 105 GLN A O 1 ATOM 693 C CB . GLN A 1 82 ? 28.913 -29.269 52.817 1.00 22.89 ? 105 GLN A CB 1 ATOM 694 C CG . GLN A 1 82 ? 30.434 -29.481 52.863 1.00 20.17 ? 105 GLN A CG 1 ATOM 695 C CD . GLN A 1 82 ? 31.249 -28.508 52.087 1.00 21.85 ? 105 GLN A CD 1 ATOM 696 O OE1 . GLN A 1 82 ? 30.787 -27.443 51.666 1.00 21.91 ? 105 GLN A OE1 1 ATOM 697 N NE2 . GLN A 1 82 ? 32.520 -28.846 51.936 1.00 20.84 ? 105 GLN A NE2 1 ATOM 698 N N . ASN A 1 83 ? 25.857 -31.019 53.341 1.00 21.79 ? 106 ASN A N 1 ATOM 699 C CA . ASN A 1 83 ? 24.374 -30.849 53.426 1.00 25.34 ? 106 ASN A CA 1 ATOM 700 C C . ASN A 1 83 ? 23.860 -29.706 52.622 1.00 25.42 ? 106 ASN A C 1 ATOM 701 O O . ASN A 1 83 ? 22.842 -29.096 52.967 1.00 25.15 ? 106 ASN A O 1 ATOM 702 C CB . ASN A 1 83 ? 23.886 -30.765 54.830 1.00 27.68 ? 106 ASN A CB 1 ATOM 703 C CG . ASN A 1 83 ? 24.605 -31.804 55.725 1.00 31.67 ? 106 ASN A CG 1 ATOM 704 O OD1 . ASN A 1 83 ? 24.618 -33.007 55.368 1.00 29.42 ? 106 ASN A OD1 1 ATOM 705 N ND2 . ASN A 1 83 ? 25.280 -31.333 56.805 1.00 33.07 ? 106 ASN A ND2 1 ATOM 706 N N . ARG A 1 84 ? 24.529 -29.407 51.516 1.00 22.33 ? 107 ARG A N 1 ATOM 707 C CA . ARG A 1 84 ? 24.054 -28.289 50.688 1.00 22.08 ? 107 ARG A CA 1 ATOM 708 C C . ARG A 1 84 ? 23.140 -28.789 49.543 1.00 23.63 ? 107 ARG A C 1 ATOM 709 O O . ARG A 1 84 ? 23.441 -28.600 48.338 1.00 21.87 ? 107 ARG A O 1 ATOM 710 C CB . ARG A 1 84 ? 25.242 -27.546 50.087 1.00 21.26 ? 107 ARG A CB 1 ATOM 711 C CG . ARG A 1 84 ? 26.193 -27.034 51.189 1.00 22.06 ? 107 ARG A CG 1 ATOM 712 C CD . ARG A 1 84 ? 27.218 -26.135 50.616 1.00 22.47 ? 107 ARG A CD 1 ATOM 713 N NE . ARG A 1 84 ? 28.417 -25.899 51.432 1.00 23.32 ? 107 ARG A NE 1 ATOM 714 C CZ . ARG A 1 84 ? 28.870 -24.761 51.906 1.00 25.71 ? 107 ARG A CZ 1 ATOM 715 N NH1 . ARG A 1 84 ? 28.197 -23.669 51.751 1.00 23.86 ? 107 ARG A NH1 1 ATOM 716 N NH2 . ARG A 1 84 ? 30.036 -24.744 52.567 1.00 26.67 ? 107 ARG A NH2 1 ATOM 717 N N . THR A 1 85 ? 22.082 -29.481 49.939 1.00 23.26 ? 108 THR A N 1 ATOM 718 C CA . THR A 1 85 ? 21.212 -30.234 49.064 1.00 23.86 ? 108 THR A CA 1 ATOM 719 C C . THR A 1 85 ? 20.359 -29.262 48.206 1.00 22.58 ? 108 THR A C 1 ATOM 720 O O . THR A 1 85 ? 20.156 -29.519 46.999 1.00 23.24 ? 108 THR A O 1 ATOM 721 C CB . THR A 1 85 ? 20.327 -31.268 49.881 1.00 25.32 ? 108 THR A CB 1 ATOM 722 O OG1 . THR A 1 85 ? 19.637 -30.505 50.921 1.00 30.45 ? 108 THR A OG1 1 ATOM 723 C CG2 . THR A 1 85 ? 21.179 -32.321 50.485 1.00 25.01 ? 108 THR A CG2 1 ATOM 724 N N A GLU A 1 86 ? 19.911 -28.143 48.747 0.60 21.89 ? 109 GLU A N 1 ATOM 725 N N B GLU A 1 86 ? 19.902 -28.176 48.816 0.40 22.14 ? 109 GLU A N 1 ATOM 726 C CA A GLU A 1 86 ? 19.172 -27.190 47.923 0.60 22.93 ? 109 GLU A CA 1 ATOM 727 C CA B GLU A 1 86 ? 19.204 -27.120 48.110 0.40 22.60 ? 109 GLU A CA 1 ATOM 728 C C A GLU A 1 86 ? 20.063 -26.453 46.920 0.60 21.91 ? 109 GLU A C 1 ATOM 729 C C B GLU A 1 86 ? 20.084 -26.603 46.950 0.40 21.93 ? 109 GLU A C 1 ATOM 730 O O A GLU A 1 86 ? 19.615 -26.074 45.845 0.60 20.36 ? 109 GLU A O 1 ATOM 731 O O B GLU A 1 86 ? 19.687 -26.629 45.774 0.40 20.54 ? 109 GLU A O 1 ATOM 732 C CB A GLU A 1 86 ? 18.490 -26.112 48.765 0.60 23.78 ? 109 GLU A CB 1 ATOM 733 C CB B GLU A 1 86 ? 18.861 -25.948 49.065 0.40 23.27 ? 109 GLU A CB 1 ATOM 734 C CG A GLU A 1 86 ? 17.443 -26.665 49.656 0.60 27.77 ? 109 GLU A CG 1 ATOM 735 C CG B GLU A 1 86 ? 17.905 -26.281 50.230 0.40 25.44 ? 109 GLU A CG 1 ATOM 736 C CD A GLU A 1 86 ? 16.111 -26.797 49.045 0.60 28.05 ? 109 GLU A CD 1 ATOM 737 C CD B GLU A 1 86 ? 18.581 -26.779 51.527 0.40 27.27 ? 109 GLU A CD 1 ATOM 738 O OE1 A GLU A 1 86 ? 15.972 -27.117 47.804 0.60 29.17 ? 109 GLU A OE1 1 ATOM 739 O OE1 B GLU A 1 86 ? 19.807 -26.976 51.558 0.40 21.21 ? 109 GLU A OE1 1 ATOM 740 O OE2 A GLU A 1 86 ? 15.180 -26.598 49.918 0.60 33.37 ? 109 GLU A OE2 1 ATOM 741 O OE2 B GLU A 1 86 ? 17.829 -26.956 52.530 0.40 30.34 ? 109 GLU A OE2 1 ATOM 742 N N . LEU A 1 87 ? 21.304 -26.212 47.316 1.00 21.34 ? 110 LEU A N 1 ATOM 743 C CA . LEU A 1 87 ? 22.277 -25.630 46.432 1.00 21.58 ? 110 LEU A CA 1 ATOM 744 C C . LEU A 1 87 ? 22.551 -26.616 45.275 1.00 20.09 ? 110 LEU A C 1 ATOM 745 O O . LEU A 1 87 ? 22.588 -26.176 44.113 1.00 17.82 ? 110 LEU A O 1 ATOM 746 C CB . LEU A 1 87 ? 23.591 -25.303 47.144 1.00 20.61 ? 110 LEU A CB 1 ATOM 747 C CG . LEU A 1 87 ? 24.782 -24.838 46.274 1.00 21.60 ? 110 LEU A CG 1 ATOM 748 C CD1 . LEU A 1 87 ? 24.400 -23.500 45.591 1.00 18.46 ? 110 LEU A CD1 1 ATOM 749 C CD2 . LEU A 1 87 ? 25.985 -24.755 47.146 1.00 19.23 ? 110 LEU A CD2 1 ATOM 750 N N . LEU A 1 88 ? 22.767 -27.909 45.593 1.00 19.28 ? 111 LEU A N 1 ATOM 751 C CA . LEU A 1 88 ? 23.013 -28.867 44.555 1.00 20.69 ? 111 LEU A CA 1 ATOM 752 C C . LEU A 1 88 ? 21.824 -28.972 43.532 1.00 21.68 ? 111 LEU A C 1 ATOM 753 O O . LEU A 1 88 ? 22.058 -28.967 42.327 1.00 19.48 ? 111 LEU A O 1 ATOM 754 C CB . LEU A 1 88 ? 23.463 -30.204 45.115 1.00 20.81 ? 111 LEU A CB 1 ATOM 755 C CG . LEU A 1 88 ? 23.685 -31.366 44.237 1.00 26.04 ? 111 LEU A CG 1 ATOM 756 C CD1 . LEU A 1 88 ? 24.881 -31.024 43.297 1.00 24.80 ? 111 LEU A CD1 1 ATOM 757 C CD2 . LEU A 1 88 ? 24.011 -32.741 45.101 1.00 26.96 ? 111 LEU A CD2 1 ATOM 758 N N A SER A 1 89 ? 20.584 -28.989 44.036 0.50 20.93 ? 112 SER A N 1 ATOM 759 N N B SER A 1 89 ? 20.591 -29.028 44.006 0.50 21.63 ? 112 SER A N 1 ATOM 760 C CA A SER A 1 89 ? 19.387 -29.067 43.201 0.50 20.89 ? 112 SER A CA 1 ATOM 761 C CA B SER A 1 89 ? 19.483 -29.155 43.097 0.50 22.24 ? 112 SER A CA 1 ATOM 762 C C A SER A 1 89 ? 19.312 -27.818 42.336 0.50 20.47 ? 112 SER A C 1 ATOM 763 C C B SER A 1 89 ? 19.360 -27.829 42.305 0.50 21.16 ? 112 SER A C 1 ATOM 764 O O A SER A 1 89 ? 18.987 -27.902 41.158 0.50 20.69 ? 112 SER A O 1 ATOM 765 O O B SER A 1 89 ? 19.100 -27.884 41.112 0.50 21.26 ? 112 SER A O 1 ATOM 766 C CB A SER A 1 89 ? 18.087 -29.193 44.037 0.50 21.69 ? 112 SER A CB 1 ATOM 767 C CB B SER A 1 89 ? 18.201 -29.554 43.839 0.50 23.49 ? 112 SER A CB 1 ATOM 768 O OG A SER A 1 89 ? 18.110 -30.344 44.863 0.50 19.22 ? 112 SER A OG 1 ATOM 769 O OG B SER A 1 89 ? 17.959 -28.613 44.846 0.50 26.19 ? 112 SER A OG 1 ATOM 770 N N . TYR A 1 90 ? 19.637 -26.664 42.913 1.00 20.11 ? 113 TYR A N 1 ATOM 771 C CA . TYR A 1 90 ? 19.592 -25.422 42.198 1.00 19.23 ? 113 TYR A CA 1 ATOM 772 C C . TYR A 1 90 ? 20.691 -25.469 41.052 1.00 17.48 ? 113 TYR A C 1 ATOM 773 O O . TYR A 1 90 ? 20.457 -25.049 39.918 1.00 17.60 ? 113 TYR A O 1 ATOM 774 C CB . TYR A 1 90 ? 19.795 -24.250 43.129 1.00 19.71 ? 113 TYR A CB 1 ATOM 775 C CG . TYR A 1 90 ? 19.740 -22.904 42.460 1.00 19.15 ? 113 TYR A CG 1 ATOM 776 C CD1 . TYR A 1 90 ? 18.619 -22.130 42.472 1.00 18.53 ? 113 TYR A CD1 1 ATOM 777 C CD2 . TYR A 1 90 ? 20.868 -22.384 41.828 1.00 19.43 ? 113 TYR A CD2 1 ATOM 778 C CE1 . TYR A 1 90 ? 18.589 -20.871 41.849 1.00 21.74 ? 113 TYR A CE1 1 ATOM 779 C CE2 . TYR A 1 90 ? 20.801 -21.149 41.186 1.00 15.57 ? 113 TYR A CE2 1 ATOM 780 C CZ . TYR A 1 90 ? 19.684 -20.429 41.204 1.00 20.52 ? 113 TYR A CZ 1 ATOM 781 O OH . TYR A 1 90 ? 19.717 -19.242 40.583 1.00 21.80 ? 113 TYR A OH 1 ATOM 782 N N . MET A 1 91 ? 21.844 -26.027 41.371 1.00 17.59 ? 114 MET A N 1 ATOM 783 C CA . MET A 1 91 ? 22.912 -26.125 40.414 1.00 15.59 ? 114 MET A CA 1 ATOM 784 C C . MET A 1 91 ? 22.520 -26.943 39.229 1.00 16.46 ? 114 MET A C 1 ATOM 785 O O . MET A 1 91 ? 22.917 -26.634 38.055 1.00 17.61 ? 114 MET A O 1 ATOM 786 C CB . MET A 1 91 ? 24.249 -26.521 41.082 1.00 15.70 ? 114 MET A CB 1 ATOM 787 C CG . MET A 1 91 ? 24.799 -25.462 41.974 1.00 16.06 ? 114 MET A CG 1 ATOM 788 S SD . MET A 1 91 ? 26.199 -26.070 42.901 1.00 20.10 ? 114 MET A SD 1 ATOM 789 C CE . MET A 1 91 ? 27.245 -26.966 41.618 1.00 16.28 ? 114 MET A CE 1 ATOM 790 N N . LYS A 1 92 ? 21.823 -28.048 39.498 1.00 17.59 ? 115 LYS A N 1 ATOM 791 C CA . LYS A 1 92 ? 21.382 -28.961 38.444 1.00 18.31 ? 115 LYS A CA 1 ATOM 792 C C . LYS A 1 92 ? 20.468 -28.227 37.493 1.00 19.61 ? 115 LYS A C 1 ATOM 793 O O . LYS A 1 92 ? 20.548 -28.424 36.271 1.00 18.65 ? 115 LYS A O 1 ATOM 794 C CB . LYS A 1 92 ? 20.615 -30.173 39.035 1.00 18.98 ? 115 LYS A CB 1 ATOM 795 C CG . LYS A 1 92 ? 21.581 -31.127 39.679 1.00 22.20 ? 115 LYS A CG 1 ATOM 796 C CD . LYS A 1 92 ? 20.853 -32.218 40.513 1.00 30.01 ? 115 LYS A CD 1 ATOM 797 C CE . LYS A 1 92 ? 21.788 -33.312 41.066 1.00 34.32 ? 115 LYS A CE 1 ATOM 798 N NZ . LYS A 1 92 ? 21.091 -34.038 42.257 1.00 35.78 ? 115 LYS A NZ 1 ATOM 799 N N . GLU A 1 93 ? 19.687 -27.276 38.006 1.00 18.05 ? 116 GLU A N 1 ATOM 800 C CA . GLU A 1 93 ? 18.678 -26.557 37.184 1.00 16.92 ? 116 GLU A CA 1 ATOM 801 C C . GLU A 1 93 ? 19.292 -25.292 36.501 1.00 17.69 ? 116 GLU A C 1 ATOM 802 O O . GLU A 1 93 ? 19.113 -25.097 35.297 1.00 17.67 ? 116 GLU A O 1 ATOM 803 C CB . GLU A 1 93 ? 17.512 -26.139 38.111 1.00 17.19 ? 116 GLU A CB 1 ATOM 804 C CG . GLU A 1 93 ? 16.648 -25.078 37.447 1.00 18.61 ? 116 GLU A CG 1 ATOM 805 C CD . GLU A 1 93 ? 15.890 -25.628 36.239 1.00 23.73 ? 116 GLU A CD 1 ATOM 806 O OE1 . GLU A 1 93 ? 15.937 -26.842 36.085 1.00 24.92 ? 116 GLU A OE1 1 ATOM 807 O OE2 . GLU A 1 93 ? 15.254 -24.863 35.532 1.00 19.30 ? 116 GLU A OE2 1 ATOM 808 N N . TYR A 1 94 ? 20.118 -24.522 37.239 1.00 17.51 ? 117 TYR A N 1 ATOM 809 C CA . TYR A 1 94 ? 20.609 -23.241 36.797 1.00 18.39 ? 117 TYR A CA 1 ATOM 810 C C . TYR A 1 94 ? 22.108 -23.177 36.497 1.00 17.05 ? 117 TYR A C 1 ATOM 811 O O . TYR A 1 94 ? 22.543 -22.191 35.888 1.00 16.10 ? 117 TYR A O 1 ATOM 812 C CB . TYR A 1 94 ? 20.250 -22.105 37.815 1.00 18.31 ? 117 TYR A CB 1 ATOM 813 C CG . TYR A 1 94 ? 18.795 -21.791 37.886 1.00 18.75 ? 117 TYR A CG 1 ATOM 814 C CD1 . TYR A 1 94 ? 18.221 -20.917 36.974 1.00 18.53 ? 117 TYR A CD1 1 ATOM 815 C CD2 . TYR A 1 94 ? 17.984 -22.336 38.900 1.00 17.73 ? 117 TYR A CD2 1 ATOM 816 C CE1 . TYR A 1 94 ? 16.845 -20.605 37.062 1.00 19.62 ? 117 TYR A CE1 1 ATOM 817 C CE2 . TYR A 1 94 ? 16.625 -22.059 38.952 1.00 16.69 ? 117 TYR A CE2 1 ATOM 818 C CZ . TYR A 1 94 ? 16.086 -21.157 38.028 1.00 18.06 ? 117 TYR A CZ 1 ATOM 819 O OH . TYR A 1 94 ? 14.724 -20.897 38.072 1.00 18.33 ? 117 TYR A OH 1 ATOM 820 N N . TRP A 1 95 ? 22.863 -24.214 36.836 1.00 15.92 ? 118 TRP A N 1 ATOM 821 C CA . TRP A 1 95 ? 24.273 -24.354 36.395 1.00 17.44 ? 118 TRP A CA 1 ATOM 822 C C . TRP A 1 95 ? 24.469 -25.720 35.637 1.00 16.86 ? 118 TRP A C 1 ATOM 823 O O . TRP A 1 95 ? 25.465 -26.471 35.822 1.00 19.16 ? 118 TRP A O 1 ATOM 824 C CB . TRP A 1 95 ? 25.143 -24.277 37.623 1.00 15.41 ? 118 TRP A CB 1 ATOM 825 C CG . TRP A 1 95 ? 26.579 -23.867 37.402 1.00 15.32 ? 118 TRP A CG 1 ATOM 826 C CD1 . TRP A 1 95 ? 27.331 -24.064 36.291 1.00 17.22 ? 118 TRP A CD1 1 ATOM 827 C CD2 . TRP A 1 95 ? 27.459 -23.332 38.387 1.00 18.23 ? 118 TRP A CD2 1 ATOM 828 N NE1 . TRP A 1 95 ? 28.606 -23.606 36.473 1.00 15.39 ? 118 TRP A NE1 1 ATOM 829 C CE2 . TRP A 1 95 ? 28.709 -23.160 37.771 1.00 16.60 ? 118 TRP A CE2 1 ATOM 830 C CE3 . TRP A 1 95 ? 27.289 -22.915 39.704 1.00 20.41 ? 118 TRP A CE3 1 ATOM 831 C CZ2 . TRP A 1 95 ? 29.784 -22.622 38.406 1.00 18.26 ? 118 TRP A CZ2 1 ATOM 832 C CZ3 . TRP A 1 95 ? 28.443 -22.330 40.363 1.00 18.63 ? 118 TRP A CZ3 1 ATOM 833 C CH2 . TRP A 1 95 ? 29.637 -22.217 39.692 1.00 21.16 ? 118 TRP A CH2 1 ATOM 834 N N . PRO A 1 96 ? 23.556 -26.002 34.661 1.00 16.47 ? 119 PRO A N 1 ATOM 835 C CA . PRO A 1 96 ? 23.743 -27.203 33.905 1.00 17.28 ? 119 PRO A CA 1 ATOM 836 C C . PRO A 1 96 ? 24.932 -27.189 32.950 1.00 17.78 ? 119 PRO A C 1 ATOM 837 O O . PRO A 1 96 ? 25.315 -26.132 32.417 1.00 17.85 ? 119 PRO A O 1 ATOM 838 C CB . PRO A 1 96 ? 22.411 -27.291 33.146 1.00 17.49 ? 119 PRO A CB 1 ATOM 839 C CG . PRO A 1 96 ? 22.146 -25.869 32.738 1.00 18.48 ? 119 PRO A CG 1 ATOM 840 C CD . PRO A 1 96 ? 22.554 -25.148 34.039 1.00 18.77 ? 119 PRO A CD 1 ATOM 841 N N . ASP A 1 97 ? 25.488 -28.367 32.710 1.00 19.04 ? 120 ASP A N 1 ATOM 842 C CA . ASP A 1 97 ? 26.279 -28.596 31.528 1.00 19.39 ? 120 ASP A CA 1 ATOM 843 C C . ASP A 1 97 ? 25.253 -28.897 30.374 1.00 21.50 ? 120 ASP A C 1 ATOM 844 O O . ASP A 1 97 ? 24.354 -29.752 30.500 1.00 21.82 ? 120 ASP A O 1 ATOM 845 C CB . ASP A 1 97 ? 27.253 -29.746 31.773 1.00 19.40 ? 120 ASP A CB 1 ATOM 846 C CG . ASP A 1 97 ? 28.213 -29.985 30.614 1.00 23.10 ? 120 ASP A CG 1 ATOM 847 O OD1 . ASP A 1 97 ? 27.734 -30.410 29.542 1.00 25.49 ? 120 ASP A OD1 1 ATOM 848 O OD2 . ASP A 1 97 ? 29.407 -29.682 30.801 1.00 24.82 ? 120 ASP A OD2 1 ATOM 849 N N . TYR A 1 98 ? 25.373 -28.168 29.279 1.00 22.97 ? 121 TYR A N 1 ATOM 850 C CA . TYR A 1 98 ? 24.414 -28.346 28.144 1.00 23.49 ? 121 TYR A CA 1 ATOM 851 C C . TYR A 1 98 ? 24.241 -29.760 27.649 1.00 24.65 ? 121 TYR A C 1 ATOM 852 O O . TYR A 1 98 ? 23.165 -30.105 27.082 1.00 25.14 ? 121 TYR A O 1 ATOM 853 C CB . TYR A 1 98 ? 24.737 -27.402 26.962 1.00 24.40 ? 121 TYR A CB 1 ATOM 854 C CG . TYR A 1 98 ? 26.037 -27.771 26.335 1.00 26.70 ? 121 TYR A CG 1 ATOM 855 C CD1 . TYR A 1 98 ? 26.105 -28.810 25.403 1.00 28.10 ? 121 TYR A CD1 1 ATOM 856 C CD2 . TYR A 1 98 ? 27.168 -27.083 26.644 1.00 27.12 ? 121 TYR A CD2 1 ATOM 857 C CE1 . TYR A 1 98 ? 27.319 -29.215 24.803 1.00 27.60 ? 121 TYR A CE1 1 ATOM 858 C CE2 . TYR A 1 98 ? 28.435 -27.496 26.102 1.00 28.15 ? 121 TYR A CE2 1 ATOM 859 C CZ . TYR A 1 98 ? 28.495 -28.549 25.175 1.00 31.13 ? 121 TYR A CZ 1 ATOM 860 O OH . TYR A 1 98 ? 29.715 -28.950 24.704 1.00 32.96 ? 121 TYR A OH 1 ATOM 861 N N . GLU A 1 99 ? 25.304 -30.550 27.792 1.00 25.79 ? 122 GLU A N 1 ATOM 862 C CA . GLU A 1 99 ? 25.305 -31.906 27.271 1.00 27.92 ? 122 GLU A CA 1 ATOM 863 C C . GLU A 1 99 ? 24.421 -32.857 28.054 1.00 29.20 ? 122 GLU A C 1 ATOM 864 O O . GLU A 1 99 ? 23.866 -33.838 27.517 1.00 30.71 ? 122 GLU A O 1 ATOM 865 C CB . GLU A 1 99 ? 26.706 -32.417 27.127 1.00 28.77 ? 122 GLU A CB 1 ATOM 866 C CG . GLU A 1 99 ? 26.722 -33.583 26.295 1.00 31.61 ? 122 GLU A CG 1 ATOM 867 C CD . GLU A 1 99 ? 28.163 -34.143 26.118 1.00 34.25 ? 122 GLU A CD 1 ATOM 868 O OE1 . GLU A 1 99 ? 29.159 -33.506 26.535 1.00 33.99 ? 122 GLU A OE1 1 ATOM 869 O OE2 . GLU A 1 99 ? 28.218 -35.265 25.611 1.00 39.97 ? 122 GLU A OE2 1 ATOM 870 N N . GLY A 1 100 ? 24.255 -32.561 29.315 1.00 26.58 ? 123 GLY A N 1 ATOM 871 C CA . GLY A 1 100 ? 23.273 -33.286 30.130 1.00 27.20 ? 123 GLY A CA 1 ATOM 872 C C . GLY A 1 100 ? 23.767 -33.333 31.549 1.00 27.45 ? 123 GLY A C 1 ATOM 873 O O . GLY A 1 100 ? 24.926 -32.989 31.823 1.00 25.13 ? 123 GLY A O 1 ATOM 874 N N . ALA A 1 101 ? 22.875 -33.728 32.452 1.00 25.43 ? 124 ALA A N 1 ATOM 875 C CA . ALA A 1 101 ? 23.154 -33.730 33.880 1.00 27.13 ? 124 ALA A CA 1 ATOM 876 C C . ALA A 1 101 ? 24.359 -34.588 34.228 1.00 26.14 ? 124 ALA A C 1 ATOM 877 O O . ALA A 1 101 ? 25.072 -34.300 35.190 1.00 24.59 ? 124 ALA A O 1 ATOM 878 C CB . ALA A 1 101 ? 21.929 -34.194 34.656 1.00 27.03 ? 124 ALA A CB 1 ATOM 879 N N . ASP A 1 102 ? 24.591 -35.644 33.455 1.00 27.99 ? 125 ASP A N 1 ATOM 880 C CA . ASP A 1 102 ? 25.720 -36.536 33.763 1.00 27.86 ? 125 ASP A CA 1 ATOM 881 C C . ASP A 1 102 ? 27.061 -35.834 33.560 1.00 25.38 ? 125 ASP A C 1 ATOM 882 O O . ASP A 1 102 ? 28.097 -36.326 34.041 1.00 25.09 ? 125 ASP A O 1 ATOM 883 C CB . ASP A 1 102 ? 25.677 -37.859 32.957 1.00 30.63 ? 125 ASP A CB 1 ATOM 884 C CG . ASP A 1 102 ? 24.543 -38.813 33.404 1.00 36.10 ? 125 ASP A CG 1 ATOM 885 O OD1 . ASP A 1 102 ? 23.851 -38.568 34.453 1.00 37.79 ? 125 ASP A OD1 1 ATOM 886 O OD2 . ASP A 1 102 ? 24.330 -39.775 32.630 1.00 45.23 ? 125 ASP A OD2 1 ATOM 887 N N . GLU A 1 103 ? 27.064 -34.712 32.803 1.00 22.76 ? 126 GLU A N 1 ATOM 888 C CA . GLU A 1 103 ? 28.273 -33.919 32.629 1.00 23.15 ? 126 GLU A CA 1 ATOM 889 C C . GLU A 1 103 ? 28.383 -32.726 33.595 1.00 19.94 ? 126 GLU A C 1 ATOM 890 O O . GLU A 1 103 ? 29.392 -32.012 33.602 1.00 17.25 ? 126 GLU A O 1 ATOM 891 C CB . GLU A 1 103 ? 28.350 -33.445 31.164 1.00 23.35 ? 126 GLU A CB 1 ATOM 892 C CG . GLU A 1 103 ? 28.650 -34.608 30.131 1.00 26.13 ? 126 GLU A CG 1 ATOM 893 C CD . GLU A 1 103 ? 27.460 -35.639 29.990 1.00 36.59 ? 126 GLU A CD 1 ATOM 894 O OE1 . GLU A 1 103 ? 26.282 -35.241 29.688 1.00 35.08 ? 126 GLU A OE1 1 ATOM 895 O OE2 . GLU A 1 103 ? 27.704 -36.863 30.246 1.00 42.68 ? 126 GLU A OE2 1 ATOM 896 N N . ASP A 1 104 ? 27.357 -32.539 34.436 1.00 20.18 ? 127 ASP A N 1 ATOM 897 C CA . ASP A 1 104 ? 27.396 -31.446 35.404 1.00 17.99 ? 127 ASP A CA 1 ATOM 898 C C . ASP A 1 104 ? 28.650 -31.562 36.289 1.00 18.05 ? 127 ASP A C 1 ATOM 899 O O . ASP A 1 104 ? 29.354 -30.541 36.457 1.00 17.78 ? 127 ASP A O 1 ATOM 900 C CB . ASP A 1 104 ? 26.180 -31.452 36.302 1.00 17.93 ? 127 ASP A CB 1 ATOM 901 C CG . ASP A 1 104 ? 24.943 -31.086 35.615 1.00 20.21 ? 127 ASP A CG 1 ATOM 902 O OD1 . ASP A 1 104 ? 25.018 -30.584 34.442 1.00 20.33 ? 127 ASP A OD1 1 ATOM 903 O OD2 . ASP A 1 104 ? 23.862 -31.221 36.289 1.00 21.82 ? 127 ASP A OD2 1 ATOM 904 N N . GLU A 1 105 ? 28.967 -32.737 36.820 1.00 16.30 ? 128 GLU A N 1 ATOM 905 C CA . GLU A 1 105 ? 30.072 -32.922 37.777 1.00 16.90 ? 128 GLU A CA 1 ATOM 906 C C . GLU A 1 105 ? 31.385 -32.423 37.136 1.00 18.66 ? 128 GLU A C 1 ATOM 907 O O . GLU A 1 105 ? 32.126 -31.627 37.738 1.00 17.75 ? 128 GLU A O 1 ATOM 908 C CB . GLU A 1 105 ? 30.188 -34.382 38.179 1.00 16.27 ? 128 GLU A CB 1 ATOM 909 C CG . GLU A 1 105 ? 31.473 -34.753 38.938 1.00 20.36 ? 128 GLU A CG 1 ATOM 910 C CD . GLU A 1 105 ? 31.691 -33.960 40.241 1.00 21.33 ? 128 GLU A CD 1 ATOM 911 O OE1 . GLU A 1 105 ? 30.701 -33.542 40.870 1.00 21.34 ? 128 GLU A OE1 1 ATOM 912 O OE2 . GLU A 1 105 ? 32.900 -33.740 40.609 1.00 21.13 ? 128 GLU A OE2 1 ATOM 913 N N A SER A 1 106 ? 31.675 -32.840 35.892 0.70 20.22 ? 129 SER A N 1 ATOM 914 N N B SER A 1 106 ? 31.668 -32.841 35.895 0.30 18.66 ? 129 SER A N 1 ATOM 915 C CA A SER A 1 106 ? 32.960 -32.459 35.278 0.70 19.68 ? 129 SER A CA 1 ATOM 916 C CA B SER A 1 106 ? 32.938 -32.463 35.237 0.30 17.97 ? 129 SER A CA 1 ATOM 917 C C A SER A 1 106 ? 32.963 -30.946 35.074 0.70 18.13 ? 129 SER A C 1 ATOM 918 C C B SER A 1 106 ? 32.982 -30.955 34.929 0.30 17.72 ? 129 SER A C 1 ATOM 919 O O A SER A 1 106 ? 33.997 -30.316 35.307 0.70 17.76 ? 129 SER A O 1 ATOM 920 O O B SER A 1 106 ? 34.051 -30.355 34.880 0.30 17.56 ? 129 SER A O 1 ATOM 921 C CB A SER A 1 106 ? 33.217 -33.162 33.908 0.70 21.97 ? 129 SER A CB 1 ATOM 922 C CB B SER A 1 106 ? 33.173 -33.253 33.922 0.30 19.01 ? 129 SER A CB 1 ATOM 923 O OG A SER A 1 106 ? 32.124 -32.925 33.036 0.70 23.93 ? 129 SER A OG 1 ATOM 924 O OG B SER A 1 106 ? 32.699 -34.581 34.001 0.30 15.66 ? 129 SER A OG 1 ATOM 925 N N . PHE A 1 107 ? 31.830 -30.338 34.700 1.00 18.23 ? 130 PHE A N 1 ATOM 926 C CA . PHE A 1 107 ? 31.746 -28.866 34.489 1.00 18.68 ? 130 PHE A CA 1 ATOM 927 C C . PHE A 1 107 ? 32.063 -28.129 35.797 1.00 18.36 ? 130 PHE A C 1 ATOM 928 O O . PHE A 1 107 ? 32.822 -27.113 35.835 1.00 17.58 ? 130 PHE A O 1 ATOM 929 C CB . PHE A 1 107 ? 30.335 -28.486 33.962 1.00 16.96 ? 130 PHE A CB 1 ATOM 930 C CG . PHE A 1 107 ? 30.126 -27.039 33.579 1.00 17.25 ? 130 PHE A CG 1 ATOM 931 C CD1 . PHE A 1 107 ? 31.104 -26.189 33.227 1.00 19.14 ? 130 PHE A CD1 1 ATOM 932 C CD2 . PHE A 1 107 ? 28.860 -26.532 33.624 1.00 17.05 ? 130 PHE A CD2 1 ATOM 933 C CE1 . PHE A 1 107 ? 30.818 -24.881 32.858 1.00 19.20 ? 130 PHE A CE1 1 ATOM 934 C CE2 . PHE A 1 107 ? 28.563 -25.285 33.227 1.00 17.18 ? 130 PHE A CE2 1 ATOM 935 C CZ . PHE A 1 107 ? 29.506 -24.435 32.881 1.00 18.12 ? 130 PHE A CZ 1 ATOM 936 N N . TRP A 1 108 ? 31.428 -28.588 36.894 1.00 18.13 ? 131 TRP A N 1 ATOM 937 C CA . TRP A 1 108 ? 31.656 -27.908 38.191 1.00 17.36 ? 131 TRP A CA 1 ATOM 938 C C . TRP A 1 108 ? 33.063 -28.101 38.687 1.00 16.84 ? 131 TRP A C 1 ATOM 939 O O . TRP A 1 108 ? 33.676 -27.176 39.220 1.00 17.71 ? 131 TRP A O 1 ATOM 940 C CB . TRP A 1 108 ? 30.639 -28.429 39.174 1.00 18.18 ? 131 TRP A CB 1 ATOM 941 C CG . TRP A 1 108 ? 29.224 -28.227 38.741 1.00 15.00 ? 131 TRP A CG 1 ATOM 942 C CD1 . TRP A 1 108 ? 28.695 -27.192 37.970 1.00 19.23 ? 131 TRP A CD1 1 ATOM 943 C CD2 . TRP A 1 108 ? 28.068 -28.989 39.171 1.00 16.53 ? 131 TRP A CD2 1 ATOM 944 N NE1 . TRP A 1 108 ? 27.344 -27.358 37.821 1.00 17.12 ? 131 TRP A NE1 1 ATOM 945 C CE2 . TRP A 1 108 ? 26.927 -28.394 38.593 1.00 17.77 ? 131 TRP A CE2 1 ATOM 946 C CE3 . TRP A 1 108 ? 27.897 -30.074 40.009 1.00 21.72 ? 131 TRP A CE3 1 ATOM 947 C CZ2 . TRP A 1 108 ? 25.663 -28.935 38.732 1.00 17.23 ? 131 TRP A CZ2 1 ATOM 948 C CZ3 . TRP A 1 108 ? 26.607 -30.604 40.171 1.00 16.98 ? 131 TRP A CZ3 1 ATOM 949 C CH2 . TRP A 1 108 ? 25.510 -30.006 39.553 1.00 19.59 ? 131 TRP A CH2 1 ATOM 950 N N . GLU A 1 109 ? 33.604 -29.302 38.476 1.00 18.37 ? 132 GLU A N 1 ATOM 951 C CA . GLU A 1 109 ? 35.031 -29.507 38.769 1.00 19.45 ? 132 GLU A CA 1 ATOM 952 C C . GLU A 1 109 ? 35.848 -28.453 37.987 1.00 18.37 ? 132 GLU A C 1 ATOM 953 O O . GLU A 1 109 ? 36.805 -27.843 38.513 1.00 18.22 ? 132 GLU A O 1 ATOM 954 C CB . GLU A 1 109 ? 35.490 -30.898 38.319 1.00 20.65 ? 132 GLU A CB 1 ATOM 955 C CG . GLU A 1 109 ? 34.910 -31.965 39.190 1.00 21.60 ? 132 GLU A CG 1 ATOM 956 C CD . GLU A 1 109 ? 35.156 -33.374 38.586 1.00 25.80 ? 132 GLU A CD 1 ATOM 957 O OE1 . GLU A 1 109 ? 35.957 -33.474 37.643 1.00 23.00 ? 132 GLU A OE1 1 ATOM 958 O OE2 . GLU A 1 109 ? 34.497 -34.353 39.006 1.00 20.14 ? 132 GLU A OE2 1 ATOM 959 N N . HIS A 1 110 ? 35.575 -28.333 36.706 1.00 19.38 ? 133 HIS A N 1 ATOM 960 C CA . HIS A 1 110 ? 36.355 -27.381 35.826 1.00 16.53 ? 133 HIS A CA 1 ATOM 961 C C . HIS A 1 110 ? 36.322 -25.984 36.389 1.00 16.74 ? 133 HIS A C 1 ATOM 962 O O . HIS A 1 110 ? 37.350 -25.298 36.549 1.00 18.86 ? 133 HIS A O 1 ATOM 963 C CB . HIS A 1 110 ? 35.846 -27.431 34.399 1.00 17.75 ? 133 HIS A CB 1 ATOM 964 C CG . HIS A 1 110 ? 36.456 -26.399 33.501 1.00 18.79 ? 133 HIS A CG 1 ATOM 965 N ND1 . HIS A 1 110 ? 37.755 -26.501 33.050 1.00 19.72 ? 133 HIS A ND1 1 ATOM 966 C CD2 . HIS A 1 110 ? 35.958 -25.248 32.989 1.00 20.40 ? 133 HIS A CD2 1 ATOM 967 C CE1 . HIS A 1 110 ? 38.053 -25.414 32.346 1.00 24.77 ? 133 HIS A CE1 1 ATOM 968 N NE2 . HIS A 1 110 ? 36.971 -24.643 32.275 1.00 20.49 ? 133 HIS A NE2 1 ATOM 969 N N . GLU A 1 111 ? 35.114 -25.488 36.695 1.00 16.17 ? 134 GLU A N 1 ATOM 970 C CA . GLU A 1 111 ? 34.991 -24.165 37.251 1.00 16.73 ? 134 GLU A CA 1 ATOM 971 C C . GLU A 1 111 ? 35.737 -23.943 38.585 1.00 18.18 ? 134 GLU A C 1 ATOM 972 O O . GLU A 1 111 ? 36.489 -22.972 38.713 1.00 18.81 ? 134 GLU A O 1 ATOM 973 C CB . GLU A 1 111 ? 33.515 -23.764 37.382 1.00 16.63 ? 134 GLU A CB 1 ATOM 974 C CG . GLU A 1 111 ? 32.918 -23.563 35.929 1.00 16.99 ? 134 GLU A CG 1 ATOM 975 C CD . GLU A 1 111 ? 33.624 -22.496 35.021 1.00 18.12 ? 134 GLU A CD 1 ATOM 976 O OE1 . GLU A 1 111 ? 33.968 -21.389 35.580 1.00 18.61 ? 134 GLU A OE1 1 ATOM 977 O OE2 . GLU A 1 111 ? 33.893 -22.755 33.769 1.00 18.25 ? 134 GLU A OE2 1 ATOM 978 N N . TRP A 1 112 ? 35.569 -24.859 39.544 1.00 19.78 ? 135 TRP A N 1 ATOM 979 C CA . TRP A 1 112 ? 36.313 -24.748 40.831 1.00 18.04 ? 135 TRP A CA 1 ATOM 980 C C . TRP A 1 112 ? 37.831 -24.856 40.522 1.00 18.19 ? 135 TRP A C 1 ATOM 981 O O . TRP A 1 112 ? 38.613 -24.056 41.028 1.00 19.12 ? 135 TRP A O 1 ATOM 982 C CB . TRP A 1 112 ? 35.847 -25.841 41.845 1.00 17.71 ? 135 TRP A CB 1 ATOM 983 C CG . TRP A 1 112 ? 36.804 -25.897 42.943 1.00 18.24 ? 135 TRP A CG 1 ATOM 984 C CD1 . TRP A 1 112 ? 37.782 -26.783 43.102 1.00 18.71 ? 135 TRP A CD1 1 ATOM 985 C CD2 . TRP A 1 112 ? 37.031 -24.857 43.908 1.00 19.86 ? 135 TRP A CD2 1 ATOM 986 N NE1 . TRP A 1 112 ? 38.579 -26.428 44.195 1.00 19.11 ? 135 TRP A NE1 1 ATOM 987 C CE2 . TRP A 1 112 ? 38.172 -25.190 44.636 1.00 17.83 ? 135 TRP A CE2 1 ATOM 988 C CE3 . TRP A 1 112 ? 36.388 -23.676 44.177 1.00 18.02 ? 135 TRP A CE3 1 ATOM 989 C CZ2 . TRP A 1 112 ? 38.649 -24.391 45.687 1.00 16.32 ? 135 TRP A CZ2 1 ATOM 990 C CZ3 . TRP A 1 112 ? 36.892 -22.821 45.168 1.00 21.82 ? 135 TRP A CZ3 1 ATOM 991 C CH2 . TRP A 1 112 ? 38.022 -23.186 45.877 1.00 20.38 ? 135 TRP A CH2 1 ATOM 992 N N . ASN A 1 113 ? 38.238 -25.937 39.851 1.00 17.65 ? 136 ASN A N 1 ATOM 993 C CA . ASN A 1 113 ? 39.647 -26.189 39.618 1.00 18.18 ? 136 ASN A CA 1 ATOM 994 C C . ASN A 1 113 ? 40.363 -25.037 38.914 1.00 20.56 ? 136 ASN A C 1 ATOM 995 O O . ASN A 1 113 ? 41.425 -24.564 39.334 1.00 19.08 ? 136 ASN A O 1 ATOM 996 C CB . ASN A 1 113 ? 39.833 -27.540 38.922 1.00 19.41 ? 136 ASN A CB 1 ATOM 997 C CG . ASN A 1 113 ? 39.371 -28.660 39.782 1.00 17.68 ? 136 ASN A CG 1 ATOM 998 O OD1 . ASN A 1 113 ? 39.262 -28.475 41.035 1.00 19.56 ? 136 ASN A OD1 1 ATOM 999 N ND2 . ASN A 1 113 ? 39.171 -29.885 39.186 1.00 19.37 ? 136 ASN A ND2 1 ATOM 1000 N N . LYS A 1 114 ? 39.737 -24.549 37.878 1.00 21.55 ? 137 LYS A N 1 ATOM 1001 C CA . LYS A 1 114 ? 40.335 -23.526 37.063 1.00 21.32 ? 137 LYS A CA 1 ATOM 1002 C C . LYS A 1 114 ? 40.293 -22.176 37.710 1.00 19.84 ? 137 LYS A C 1 ATOM 1003 O O . LYS A 1 114 ? 41.262 -21.435 37.699 1.00 19.61 ? 137 LYS A O 1 ATOM 1004 C CB . LYS A 1 114 ? 39.579 -23.438 35.692 1.00 19.75 ? 137 LYS A CB 1 ATOM 1005 C CG . LYS A 1 114 ? 40.305 -22.416 34.731 1.00 19.29 ? 137 LYS A CG 1 ATOM 1006 C CD . LYS A 1 114 ? 39.737 -22.545 33.319 1.00 18.02 ? 137 LYS A CD 1 ATOM 1007 C CE . LYS A 1 114 ? 40.468 -21.475 32.415 1.00 22.68 ? 137 LYS A CE 1 ATOM 1008 N NZ . LYS A 1 114 ? 39.979 -21.603 31.019 1.00 23.99 ? 137 LYS A NZ 1 ATOM 1009 N N . HIS A 1 115 ? 39.132 -21.807 38.222 1.00 20.03 ? 138 HIS A N 1 ATOM 1010 C CA . HIS A 1 115 ? 38.942 -20.453 38.626 1.00 19.16 ? 138 HIS A CA 1 ATOM 1011 C C . HIS A 1 115 ? 38.792 -20.225 40.157 1.00 20.94 ? 138 HIS A C 1 ATOM 1012 O O . HIS A 1 115 ? 39.287 -19.220 40.730 1.00 22.40 ? 138 HIS A O 1 ATOM 1013 C CB . HIS A 1 115 ? 37.692 -19.907 37.948 1.00 20.48 ? 138 HIS A CB 1 ATOM 1014 C CG . HIS A 1 115 ? 37.834 -19.680 36.476 1.00 21.40 ? 138 HIS A CG 1 ATOM 1015 N ND1 . HIS A 1 115 ? 38.724 -18.756 35.942 1.00 21.38 ? 138 HIS A ND1 1 ATOM 1016 C CD2 . HIS A 1 115 ? 37.185 -20.234 35.426 1.00 21.02 ? 138 HIS A CD2 1 ATOM 1017 C CE1 . HIS A 1 115 ? 38.561 -18.731 34.621 1.00 25.29 ? 138 HIS A CE1 1 ATOM 1018 N NE2 . HIS A 1 115 ? 37.662 -19.650 34.287 1.00 24.27 ? 138 HIS A NE2 1 ATOM 1019 N N . GLY A 1 116 ? 38.026 -21.090 40.809 1.00 20.37 ? 139 GLY A N 1 ATOM 1020 C CA . GLY A 1 116 ? 37.796 -20.983 42.256 1.00 21.13 ? 139 GLY A CA 1 ATOM 1021 C C . GLY A 1 116 ? 39.126 -21.014 43.010 1.00 21.43 ? 139 GLY A C 1 ATOM 1022 O O . GLY A 1 116 ? 39.299 -20.299 44.004 1.00 22.16 ? 139 GLY A O 1 ATOM 1023 N N . THR A 1 117 ? 40.053 -21.875 42.567 1.00 20.94 ? 140 THR A N 1 ATOM 1024 C CA . THR A 1 117 ? 41.357 -21.959 43.227 1.00 21.59 ? 140 THR A CA 1 ATOM 1025 C C . THR A 1 117 ? 42.176 -20.717 43.077 1.00 24.39 ? 140 THR A C 1 ATOM 1026 O O . THR A 1 117 ? 43.177 -20.598 43.797 1.00 24.74 ? 140 THR A O 1 ATOM 1027 C CB . THR A 1 117 ? 42.183 -23.120 42.686 1.00 21.90 ? 140 THR A CB 1 ATOM 1028 O OG1 . THR A 1 117 ? 42.399 -22.917 41.313 1.00 20.19 ? 140 THR A OG1 1 ATOM 1029 C CG2 . THR A 1 117 ? 41.471 -24.454 42.904 1.00 20.83 ? 140 THR A CG2 1 ATOM 1030 N N . CYS A 1 118 ? 41.760 -19.753 42.211 1.00 23.56 ? 141 CYS A N 1 ATOM 1031 C CA . CYS A 1 118 ? 42.531 -18.551 41.970 1.00 24.47 ? 141 CYS A CA 1 ATOM 1032 C C . CYS A 1 118 ? 41.970 -17.349 42.713 1.00 23.21 ? 141 CYS A C 1 ATOM 1033 O O . CYS A 1 118 ? 42.457 -16.214 42.536 1.00 24.55 ? 141 CYS A O 1 ATOM 1034 C CB . CYS A 1 118 ? 42.579 -18.304 40.458 1.00 23.08 ? 141 CYS A CB 1 ATOM 1035 S SG . CYS A 1 118 ? 43.503 -19.498 39.517 1.00 25.85 ? 141 CYS A SG 1 ATOM 1036 N N . ILE A 1 119 ? 40.920 -17.554 43.485 1.00 23.95 ? 142 ILE A N 1 ATOM 1037 C CA . ILE A 1 119 ? 40.281 -16.481 44.262 1.00 23.89 ? 142 ILE A CA 1 ATOM 1038 C C . ILE A 1 119 ? 41.049 -16.453 45.610 1.00 24.79 ? 142 ILE A C 1 ATOM 1039 O O . ILE A 1 119 ? 40.882 -17.347 46.467 1.00 24.79 ? 142 ILE A O 1 ATOM 1040 C CB . ILE A 1 119 ? 38.796 -16.653 44.451 1.00 22.63 ? 142 ILE A CB 1 ATOM 1041 C CG1 . ILE A 1 119 ? 38.092 -16.658 43.100 1.00 26.59 ? 142 ILE A CG1 1 ATOM 1042 C CG2 . ILE A 1 119 ? 38.207 -15.525 45.389 1.00 25.04 ? 142 ILE A CG2 1 ATOM 1043 C CD1 . ILE A 1 119 ? 36.609 -16.988 43.167 1.00 26.92 ? 142 ILE A CD1 1 ATOM 1044 N N . ASN A 1 120 ? 41.941 -15.484 45.758 1.00 26.53 ? 143 ASN A N 1 ATOM 1045 C CA . ASN A 1 120 ? 42.851 -15.527 46.958 1.00 26.99 ? 143 ASN A CA 1 ATOM 1046 C C . ASN A 1 120 ? 42.178 -15.435 48.282 1.00 25.65 ? 143 ASN A C 1 ATOM 1047 O O . ASN A 1 120 ? 42.657 -16.028 49.306 1.00 28.47 ? 143 ASN A O 1 ATOM 1048 C CB . ASN A 1 120 ? 43.953 -14.459 46.813 1.00 26.97 ? 143 ASN A CB 1 ATOM 1049 C CG . ASN A 1 120 ? 43.427 -13.061 47.096 1.00 28.41 ? 143 ASN A CG 1 ATOM 1050 O OD1 . ASN A 1 120 ? 42.652 -12.539 46.328 1.00 25.26 ? 143 ASN A OD1 1 ATOM 1051 N ND2 . ASN A 1 120 ? 43.830 -12.470 48.225 1.00 26.39 ? 143 ASN A ND2 1 ATOM 1052 N N . THR A 1 121 ? 41.035 -14.761 48.353 1.00 23.96 ? 144 THR A N 1 ATOM 1053 C CA . THR A 1 121 ? 40.387 -14.547 49.601 1.00 23.27 ? 144 THR A CA 1 ATOM 1054 C C . THR A 1 121 ? 39.526 -15.748 50.135 1.00 23.56 ? 144 THR A C 1 ATOM 1055 O O . THR A 1 121 ? 38.969 -15.651 51.181 1.00 26.83 ? 144 THR A O 1 ATOM 1056 C CB . THR A 1 121 ? 39.483 -13.311 49.569 1.00 23.81 ? 144 THR A CB 1 ATOM 1057 O OG1 . THR A 1 121 ? 38.515 -13.488 48.501 1.00 24.30 ? 144 THR A OG1 1 ATOM 1058 C CG2 . THR A 1 121 ? 40.334 -11.960 49.329 1.00 19.62 ? 144 THR A CG2 1 ATOM 1059 N N A ILE A 1 122 ? 39.546 -16.847 49.388 0.50 24.29 ? 145 ILE A N 1 ATOM 1060 N N B ILE A 1 122 ? 39.386 -16.792 49.363 0.50 25.20 ? 145 ILE A N 1 ATOM 1061 C CA A ILE A 1 122 ? 38.742 -18.068 49.613 0.50 23.40 ? 145 ILE A CA 1 ATOM 1062 C CA B ILE A 1 122 ? 38.779 -18.004 49.869 0.50 24.63 ? 145 ILE A CA 1 ATOM 1063 C C A ILE A 1 122 ? 39.599 -19.172 50.300 0.50 21.01 ? 145 ILE A C 1 ATOM 1064 C C B ILE A 1 122 ? 39.967 -18.969 49.766 0.50 25.54 ? 145 ILE A C 1 ATOM 1065 O O A ILE A 1 122 ? 39.126 -20.236 50.581 0.50 18.32 ? 145 ILE A O 1 ATOM 1066 O O B ILE A 1 122 ? 40.345 -19.502 48.721 0.50 28.19 ? 145 ILE A O 1 ATOM 1067 C CB A ILE A 1 122 ? 38.199 -18.566 48.217 0.50 21.29 ? 145 ILE A CB 1 ATOM 1068 C CB B ILE A 1 122 ? 37.475 -18.342 49.105 0.50 22.15 ? 145 ILE A CB 1 ATOM 1069 C CG1 A ILE A 1 122 ? 37.130 -17.589 47.704 0.50 25.26 ? 145 ILE A CG1 1 ATOM 1070 C CG1 B ILE A 1 122 ? 37.762 -18.991 47.729 0.50 19.32 ? 145 ILE A CG1 1 ATOM 1071 C CG2 A ILE A 1 122 ? 37.543 -19.959 48.267 0.50 24.41 ? 145 ILE A CG2 1 ATOM 1072 C CG2 B ILE A 1 122 ? 36.681 -17.091 49.008 0.50 18.93 ? 145 ILE A CG2 1 ATOM 1073 C CD1 A ILE A 1 122 ? 36.390 -18.041 46.438 0.50 18.57 ? 145 ILE A CD1 1 ATOM 1074 C CD1 B ILE A 1 122 ? 36.435 -19.596 47.085 0.50 14.21 ? 145 ILE A CD1 1 ATOM 1075 N N A GLU A 1 123 ? 40.898 -18.941 50.414 0.50 21.12 ? 146 GLU A N 1 ATOM 1076 N N B GLU A 1 123 ? 40.660 -18.994 50.865 0.50 25.40 ? 146 GLU A N 1 ATOM 1077 C CA A GLU A 1 123 ? 41.785 -20.000 50.885 0.50 22.25 ? 146 GLU A CA 1 ATOM 1078 C CA B GLU A 1 123 ? 41.767 -19.858 51.099 0.50 25.09 ? 146 GLU A CA 1 ATOM 1079 C C A GLU A 1 123 ? 41.419 -20.406 52.318 0.50 22.27 ? 146 GLU A C 1 ATOM 1080 C C B GLU A 1 123 ? 41.361 -20.416 52.423 0.50 24.16 ? 146 GLU A C 1 ATOM 1081 O O A GLU A 1 123 ? 40.828 -19.613 53.055 0.50 20.34 ? 146 GLU A O 1 ATOM 1082 O O B GLU A 1 123 ? 40.697 -19.729 53.192 0.50 22.87 ? 146 GLU A O 1 ATOM 1083 C CB A GLU A 1 123 ? 43.250 -19.562 50.763 0.50 23.79 ? 146 GLU A CB 1 ATOM 1084 C CB B GLU A 1 123 ? 43.052 -19.042 51.252 0.50 26.17 ? 146 GLU A CB 1 ATOM 1085 C CG A GLU A 1 123 ? 43.551 -19.199 49.320 0.50 23.96 ? 146 GLU A CG 1 ATOM 1086 C CG B GLU A 1 123 ? 43.626 -18.644 49.947 0.50 25.76 ? 146 GLU A CG 1 ATOM 1087 C CD A GLU A 1 123 ? 44.867 -18.493 49.141 0.50 27.71 ? 146 GLU A CD 1 ATOM 1088 C CD B GLU A 1 123 ? 44.212 -19.824 49.209 0.50 29.10 ? 146 GLU A CD 1 ATOM 1089 O OE1 A GLU A 1 123 ? 45.656 -18.494 50.104 0.50 26.63 ? 146 GLU A OE1 1 ATOM 1090 O OE1 B GLU A 1 123 ? 43.970 -20.988 49.601 0.50 30.73 ? 146 GLU A OE1 1 ATOM 1091 O OE2 A GLU A 1 123 ? 45.063 -17.941 48.026 0.50 25.53 ? 146 GLU A OE2 1 ATOM 1092 O OE2 B GLU A 1 123 ? 44.957 -19.580 48.251 0.50 36.44 ? 146 GLU A OE2 1 ATOM 1093 N N . PRO A 1 124 ? 41.741 -21.657 52.701 1.00 23.74 ? 147 PRO A N 1 ATOM 1094 C CA . PRO A 1 124 ? 41.443 -22.146 54.031 1.00 25.05 ? 147 PRO A CA 1 ATOM 1095 C C . PRO A 1 124 ? 41.911 -21.289 55.199 1.00 24.65 ? 147 PRO A C 1 ATOM 1096 O O . PRO A 1 124 ? 41.201 -21.204 56.225 1.00 22.22 ? 147 PRO A O 1 ATOM 1097 C CB . PRO A 1 124 ? 42.129 -23.534 54.054 1.00 26.34 ? 147 PRO A CB 1 ATOM 1098 C CG . PRO A 1 124 ? 42.096 -24.000 52.646 1.00 26.82 ? 147 PRO A CG 1 ATOM 1099 C CD . PRO A 1 124 ? 42.239 -22.719 51.814 1.00 24.42 ? 147 PRO A CD 1 ATOM 1100 N N A SER A 1 125 ? 43.054 -20.631 55.006 0.50 24.88 ? 148 SER A N 1 ATOM 1101 N N B SER A 1 125 ? 43.054 -20.600 55.066 0.50 24.72 ? 148 SER A N 1 ATOM 1102 C CA A SER A 1 125 ? 43.597 -19.737 56.004 0.50 24.66 ? 148 SER A CA 1 ATOM 1103 C CA B SER A 1 125 ? 43.513 -19.689 56.135 0.50 24.13 ? 148 SER A CA 1 ATOM 1104 C C A SER A 1 125 ? 42.755 -18.483 56.276 0.50 23.94 ? 148 SER A C 1 ATOM 1105 C C B SER A 1 125 ? 42.579 -18.535 56.419 0.50 23.65 ? 148 SER A C 1 ATOM 1106 O O A SER A 1 125 ? 43.092 -17.765 57.177 0.50 23.87 ? 148 SER A O 1 ATOM 1107 O O B SER A 1 125 ? 42.644 -17.941 57.471 0.50 23.12 ? 148 SER A O 1 ATOM 1108 C CB A SER A 1 125 ? 45.024 -19.356 55.592 0.50 26.28 ? 148 SER A CB 1 ATOM 1109 C CB B SER A 1 125 ? 44.858 -19.095 55.781 0.50 25.81 ? 148 SER A CB 1 ATOM 1110 O OG A SER A 1 125 ? 45.102 -19.004 54.219 0.50 26.32 ? 148 SER A OG 1 ATOM 1111 O OG B SER A 1 125 ? 45.846 -20.100 55.773 0.50 24.90 ? 148 SER A OG 1 ATOM 1112 N N . CYS A 1 126 ? 41.695 -18.229 55.486 1.00 22.84 ? 149 CYS A N 1 ATOM 1113 C CA . CYS A 1 126 ? 40.763 -17.125 55.645 1.00 21.28 ? 149 CYS A CA 1 ATOM 1114 C C . CYS A 1 126 ? 39.506 -17.556 56.437 1.00 22.54 ? 149 CYS A C 1 ATOM 1115 O O . CYS A 1 126 ? 38.498 -16.804 56.520 1.00 23.43 ? 149 CYS A O 1 ATOM 1116 C CB . CYS A 1 126 ? 40.384 -16.564 54.259 1.00 22.31 ? 149 CYS A CB 1 ATOM 1117 S SG . CYS A 1 126 ? 41.766 -15.967 53.292 1.00 22.82 ? 149 CYS A SG 1 ATOM 1118 N N . TYR A 1 127 ? 39.547 -18.777 56.995 1.00 21.16 ? 150 TYR A N 1 ATOM 1119 C CA . TYR A 1 127 ? 38.419 -19.309 57.760 1.00 22.56 ? 150 TYR A CA 1 ATOM 1120 C C . TYR A 1 127 ? 38.750 -19.371 59.268 1.00 24.48 ? 150 TYR A C 1 ATOM 1121 O O . TYR A 1 127 ? 39.845 -19.732 59.641 1.00 25.07 ? 150 TYR A O 1 ATOM 1122 C CB . TYR A 1 127 ? 38.083 -20.712 57.285 1.00 22.42 ? 150 TYR A CB 1 ATOM 1123 C CG . TYR A 1 127 ? 37.286 -20.681 56.008 1.00 21.51 ? 150 TYR A CG 1 ATOM 1124 C CD1 . TYR A 1 127 ? 37.888 -20.427 54.761 1.00 20.70 ? 150 TYR A CD1 1 ATOM 1125 C CD2 . TYR A 1 127 ? 35.913 -20.763 56.045 1.00 19.45 ? 150 TYR A CD2 1 ATOM 1126 C CE1 . TYR A 1 127 ? 37.141 -20.302 53.618 1.00 20.82 ? 150 TYR A CE1 1 ATOM 1127 C CE2 . TYR A 1 127 ? 35.160 -20.667 54.862 1.00 22.10 ? 150 TYR A CE2 1 ATOM 1128 C CZ . TYR A 1 127 ? 35.772 -20.412 53.658 1.00 17.38 ? 150 TYR A CZ 1 ATOM 1129 O OH . TYR A 1 127 ? 34.936 -20.356 52.513 1.00 19.96 ? 150 TYR A OH 1 ATOM 1130 N N . THR A 1 128 ? 37.741 -19.142 60.087 1.00 23.36 ? 151 THR A N 1 ATOM 1131 C CA . THR A 1 128 ? 37.702 -19.674 61.425 1.00 23.96 ? 151 THR A CA 1 ATOM 1132 C C . THR A 1 128 ? 37.051 -21.026 61.507 1.00 22.97 ? 151 THR A C 1 ATOM 1133 O O . THR A 1 128 ? 36.005 -21.266 60.884 1.00 23.48 ? 151 THR A O 1 ATOM 1134 C CB . THR A 1 128 ? 36.949 -18.701 62.345 1.00 25.47 ? 151 THR A CB 1 ATOM 1135 O OG1 . THR A 1 128 ? 37.639 -17.446 62.277 1.00 27.96 ? 151 THR A OG1 1 ATOM 1136 C CG2 . THR A 1 128 ? 37.021 -19.215 63.864 1.00 24.15 ? 151 THR A CG2 1 ATOM 1137 N N . ASP A 1 129 ? 37.647 -21.921 62.280 1.00 23.12 ? 152 ASP A N 1 ATOM 1138 C CA . ASP A 1 129 ? 37.139 -23.265 62.416 1.00 23.19 ? 152 ASP A CA 1 ATOM 1139 C C . ASP A 1 129 ? 36.889 -23.922 61.029 1.00 23.27 ? 152 ASP A C 1 ATOM 1140 O O . ASP A 1 129 ? 35.864 -24.479 60.771 1.00 21.88 ? 152 ASP A O 1 ATOM 1141 C CB . ASP A 1 129 ? 35.858 -23.291 63.296 1.00 24.20 ? 152 ASP A CB 1 ATOM 1142 C CG . ASP A 1 129 ? 36.149 -22.939 64.746 1.00 23.35 ? 152 ASP A CG 1 ATOM 1143 O OD1 . ASP A 1 129 ? 37.344 -22.718 65.080 1.00 25.32 ? 152 ASP A OD1 1 ATOM 1144 O OD2 . ASP A 1 129 ? 35.173 -22.781 65.470 1.00 26.27 ? 152 ASP A OD2 1 ATOM 1145 N N . TYR A 1 130 ? 37.886 -23.784 60.149 1.00 24.16 ? 153 TYR A N 1 ATOM 1146 C CA . TYR A 1 130 ? 37.842 -24.355 58.803 1.00 23.36 ? 153 TYR A CA 1 ATOM 1147 C C . TYR A 1 130 ? 37.569 -25.845 58.930 1.00 23.18 ? 153 TYR A C 1 ATOM 1148 O O . TYR A 1 130 ? 38.201 -26.564 59.728 1.00 22.42 ? 153 TYR A O 1 ATOM 1149 C CB . TYR A 1 130 ? 39.162 -24.131 58.090 1.00 23.82 ? 153 TYR A CB 1 ATOM 1150 C CG . TYR A 1 130 ? 39.195 -24.791 56.712 1.00 22.09 ? 153 TYR A CG 1 ATOM 1151 C CD1 . TYR A 1 130 ? 38.559 -24.191 55.618 1.00 22.03 ? 153 TYR A CD1 1 ATOM 1152 C CD2 . TYR A 1 130 ? 39.925 -25.944 56.476 1.00 25.04 ? 153 TYR A CD2 1 ATOM 1153 C CE1 . TYR A 1 130 ? 38.663 -24.765 54.385 1.00 19.64 ? 153 TYR A CE1 1 ATOM 1154 C CE2 . TYR A 1 130 ? 40.041 -26.502 55.205 1.00 21.84 ? 153 TYR A CE2 1 ATOM 1155 C CZ . TYR A 1 130 ? 39.412 -25.893 54.187 1.00 22.81 ? 153 TYR A CZ 1 ATOM 1156 O OH . TYR A 1 130 ? 39.396 -26.509 52.950 1.00 21.09 ? 153 TYR A OH 1 ATOM 1157 N N . TYR A 1 131 ? 36.738 -26.367 58.058 1.00 21.51 ? 154 TYR A N 1 ATOM 1158 C CA . TYR A 1 131 ? 36.668 -27.831 57.878 1.00 23.08 ? 154 TYR A CA 1 ATOM 1159 C C . TYR A 1 131 ? 36.986 -28.193 56.402 1.00 23.72 ? 154 TYR A C 1 ATOM 1160 O O . TYR A 1 131 ? 36.760 -27.351 55.529 1.00 20.37 ? 154 TYR A O 1 ATOM 1161 C CB . TYR A 1 131 ? 35.276 -28.369 58.295 1.00 24.62 ? 154 TYR A CB 1 ATOM 1162 C CG . TYR A 1 131 ? 34.136 -27.906 57.432 1.00 23.65 ? 154 TYR A CG 1 ATOM 1163 C CD1 . TYR A 1 131 ? 33.849 -28.537 56.244 1.00 25.64 ? 154 TYR A CD1 1 ATOM 1164 C CD2 . TYR A 1 131 ? 33.234 -26.968 57.869 1.00 19.97 ? 154 TYR A CD2 1 ATOM 1165 C CE1 . TYR A 1 131 ? 32.802 -28.159 55.466 1.00 24.92 ? 154 TYR A CE1 1 ATOM 1166 C CE2 . TYR A 1 131 ? 32.211 -26.559 57.084 1.00 22.28 ? 154 TYR A CE2 1 ATOM 1167 C CZ . TYR A 1 131 ? 31.986 -27.158 55.877 1.00 22.81 ? 154 TYR A CZ 1 ATOM 1168 O OH . TYR A 1 131 ? 30.918 -26.761 55.108 1.00 23.87 ? 154 TYR A OH 1 ATOM 1169 N N . ALA A 1 132 ? 37.524 -29.387 56.151 1.00 22.92 ? 155 ALA A N 1 ATOM 1170 C CA . ALA A 1 132 ? 38.035 -29.736 54.784 1.00 22.31 ? 155 ALA A CA 1 ATOM 1171 C C . ALA A 1 132 ? 36.999 -29.427 53.678 1.00 20.11 ? 155 ALA A C 1 ATOM 1172 O O . ALA A 1 132 ? 35.809 -29.873 53.734 1.00 20.01 ? 155 ALA A O 1 ATOM 1173 C CB . ALA A 1 132 ? 38.488 -31.239 54.665 1.00 23.42 ? 155 ALA A CB 1 ATOM 1174 N N . GLN A 1 133 ? 37.454 -28.679 52.680 1.00 20.32 ? 156 GLN A N 1 ATOM 1175 C CA . GLN A 1 133 ? 36.696 -28.246 51.494 1.00 20.07 ? 156 GLN A CA 1 ATOM 1176 C C . GLN A 1 133 ? 35.529 -27.325 51.761 1.00 19.36 ? 156 GLN A C 1 ATOM 1177 O O . GLN A 1 133 ? 34.673 -27.080 50.885 1.00 20.23 ? 156 GLN A O 1 ATOM 1178 C CB . GLN A 1 133 ? 36.231 -29.481 50.669 1.00 17.75 ? 156 GLN A CB 1 ATOM 1179 C CG . GLN A 1 133 ? 37.369 -30.253 50.011 1.00 21.03 ? 156 GLN A CG 1 ATOM 1180 C CD . GLN A 1 133 ? 38.065 -31.249 50.942 1.00 23.68 ? 156 GLN A CD 1 ATOM 1181 O OE1 . GLN A 1 133 ? 37.395 -32.018 51.679 1.00 26.95 ? 156 GLN A OE1 1 ATOM 1182 N NE2 . GLN A 1 133 ? 39.372 -31.213 50.952 1.00 23.66 ? 156 GLN A NE2 1 ATOM 1183 N N . GLU A 1 134 ? 35.528 -26.683 52.928 1.00 19.36 ? 157 GLU A N 1 ATOM 1184 C CA . GLU A 1 134 ? 34.451 -25.722 53.236 1.00 17.41 ? 157 GLU A CA 1 ATOM 1185 C C . GLU A 1 134 ? 34.377 -24.640 52.183 1.00 16.10 ? 157 GLU A C 1 ATOM 1186 O O . GLU A 1 134 ? 33.289 -24.248 51.778 1.00 18.06 ? 157 GLU A O 1 ATOM 1187 C CB . GLU A 1 134 ? 34.618 -25.075 54.618 1.00 18.74 ? 157 GLU A CB 1 ATOM 1188 C CG . GLU A 1 134 ? 33.544 -24.118 54.992 1.00 18.31 ? 157 GLU A CG 1 ATOM 1189 C CD . GLU A 1 134 ? 33.650 -23.520 56.419 1.00 19.36 ? 157 GLU A CD 1 ATOM 1190 O OE1 . GLU A 1 134 ? 34.653 -23.830 57.139 1.00 20.47 ? 157 GLU A OE1 1 ATOM 1191 O OE2 . GLU A 1 134 ? 32.697 -22.726 56.745 1.00 20.35 ? 157 GLU A OE2 1 ATOM 1192 N N . GLU A 1 135 ? 35.530 -24.146 51.760 1.00 17.06 ? 158 GLU A N 1 ATOM 1193 C CA . GLU A 1 135 ? 35.575 -23.059 50.763 1.00 16.00 ? 158 GLU A CA 1 ATOM 1194 C C . GLU A 1 135 ? 35.033 -23.451 49.371 1.00 17.99 ? 158 GLU A C 1 ATOM 1195 O O . GLU A 1 135 ? 34.497 -22.579 48.657 1.00 18.99 ? 158 GLU A O 1 ATOM 1196 C CB . GLU A 1 135 ? 36.970 -22.461 50.670 1.00 17.98 ? 158 GLU A CB 1 ATOM 1197 C CG . GLU A 1 135 ? 38.027 -23.122 49.747 1.00 18.41 ? 158 GLU A CG 1 ATOM 1198 C CD . GLU A 1 135 ? 38.639 -24.422 50.210 1.00 20.56 ? 158 GLU A CD 1 ATOM 1199 O OE1 . GLU A 1 135 ? 38.134 -25.045 51.185 1.00 21.40 ? 158 GLU A OE1 1 ATOM 1200 O OE2 . GLU A 1 135 ? 39.661 -24.897 49.588 1.00 21.50 ? 158 GLU A OE2 1 ATOM 1201 N N . VAL A 1 136 ? 35.141 -24.746 49.020 1.00 19.42 ? 159 VAL A N 1 ATOM 1202 C CA . VAL A 1 136 ? 34.564 -25.246 47.793 1.00 18.67 ? 159 VAL A CA 1 ATOM 1203 C C . VAL A 1 136 ? 33.043 -25.047 47.812 1.00 19.88 ? 159 VAL A C 1 ATOM 1204 O O . VAL A 1 136 ? 32.488 -24.417 46.916 1.00 21.01 ? 159 VAL A O 1 ATOM 1205 C CB . VAL A 1 136 ? 34.916 -26.726 47.569 1.00 20.55 ? 159 VAL A CB 1 ATOM 1206 C CG1 . VAL A 1 136 ? 34.256 -27.234 46.274 1.00 19.48 ? 159 VAL A CG1 1 ATOM 1207 C CG2 . VAL A 1 136 ? 36.425 -26.840 47.539 1.00 20.42 ? 159 VAL A CG2 1 ATOM 1208 N N . GLY A 1 137 ? 32.354 -25.548 48.850 1.00 19.63 ? 160 GLY A N 1 ATOM 1209 C CA . GLY A 1 137 ? 30.930 -25.328 49.001 1.00 19.31 ? 160 GLY A CA 1 ATOM 1210 C C . GLY A 1 137 ? 30.494 -23.858 49.099 1.00 20.51 ? 160 GLY A C 1 ATOM 1211 O O . GLY A 1 137 ? 29.485 -23.367 48.451 1.00 18.08 ? 160 GLY A O 1 ATOM 1212 N N . ASP A 1 138 ? 31.280 -23.093 49.848 1.00 18.87 ? 161 ASP A N 1 ATOM 1213 C CA . ASP A 1 138 ? 31.062 -21.655 49.959 1.00 17.63 ? 161 ASP A CA 1 ATOM 1214 C C . ASP A 1 138 ? 31.154 -20.946 48.603 1.00 17.75 ? 161 ASP A C 1 ATOM 1215 O O . ASP A 1 138 ? 30.395 -20.016 48.332 1.00 17.93 ? 161 ASP A O 1 ATOM 1216 C CB . ASP A 1 138 ? 32.058 -21.037 50.943 1.00 20.10 ? 161 ASP A CB 1 ATOM 1217 C CG . ASP A 1 138 ? 31.659 -21.254 52.389 1.00 22.50 ? 161 ASP A CG 1 ATOM 1218 O OD1 . ASP A 1 138 ? 30.604 -21.878 52.629 1.00 23.11 ? 161 ASP A OD1 1 ATOM 1219 O OD2 . ASP A 1 138 ? 32.401 -20.801 53.286 1.00 24.17 ? 161 ASP A OD2 1 ATOM 1220 N N . PHE A 1 139 ? 32.084 -21.386 47.758 1.00 18.81 ? 162 PHE A N 1 ATOM 1221 C CA . PHE A 1 139 ? 32.290 -20.770 46.462 1.00 19.25 ? 162 PHE A CA 1 ATOM 1222 C C . PHE A 1 139 ? 31.030 -21.026 45.591 1.00 18.07 ? 162 PHE A C 1 ATOM 1223 O O . PHE A 1 139 ? 30.435 -20.079 45.045 1.00 16.92 ? 162 PHE A O 1 ATOM 1224 C CB . PHE A 1 139 ? 33.541 -21.346 45.777 1.00 20.45 ? 162 PHE A CB 1 ATOM 1225 C CG . PHE A 1 139 ? 33.566 -21.169 44.253 1.00 19.68 ? 162 PHE A CG 1 ATOM 1226 C CD1 . PHE A 1 139 ? 34.021 -20.019 43.720 1.00 20.85 ? 162 PHE A CD1 1 ATOM 1227 C CD2 . PHE A 1 139 ? 33.094 -22.143 43.402 1.00 19.16 ? 162 PHE A CD2 1 ATOM 1228 C CE1 . PHE A 1 139 ? 34.082 -19.848 42.342 1.00 19.91 ? 162 PHE A CE1 1 ATOM 1229 C CE2 . PHE A 1 139 ? 33.169 -21.993 42.046 1.00 20.31 ? 162 PHE A CE2 1 ATOM 1230 C CZ . PHE A 1 139 ? 33.673 -20.853 41.510 1.00 20.04 ? 162 PHE A CZ 1 ATOM 1231 N N . PHE A 1 140 ? 30.559 -22.231 45.570 1.00 16.64 ? 163 PHE A N 1 ATOM 1232 C CA . PHE A 1 140 ? 29.363 -22.546 44.751 1.00 17.05 ? 163 PHE A CA 1 ATOM 1233 C C . PHE A 1 140 ? 28.143 -21.801 45.195 1.00 18.50 ? 163 PHE A C 1 ATOM 1234 O O . PHE A 1 140 ? 27.452 -21.152 44.369 1.00 17.48 ? 163 PHE A O 1 ATOM 1235 C CB . PHE A 1 140 ? 29.141 -24.041 44.713 1.00 16.78 ? 163 PHE A CB 1 ATOM 1236 C CG . PHE A 1 140 ? 30.064 -24.735 43.770 1.00 14.63 ? 163 PHE A CG 1 ATOM 1237 C CD1 . PHE A 1 140 ? 29.808 -24.692 42.420 1.00 17.73 ? 163 PHE A CD1 1 ATOM 1238 C CD2 . PHE A 1 140 ? 31.263 -25.380 44.217 1.00 14.15 ? 163 PHE A CD2 1 ATOM 1239 C CE1 . PHE A 1 140 ? 30.673 -25.225 41.518 1.00 17.75 ? 163 PHE A CE1 1 ATOM 1240 C CE2 . PHE A 1 140 ? 32.141 -25.909 43.294 1.00 17.31 ? 163 PHE A CE2 1 ATOM 1241 C CZ . PHE A 1 140 ? 31.824 -25.839 41.933 1.00 19.53 ? 163 PHE A CZ 1 ATOM 1242 N N . GLN A 1 141 ? 27.989 -21.694 46.505 1.00 18.28 ? 164 GLN A N 1 ATOM 1243 C CA . GLN A 1 141 ? 26.887 -20.839 47.074 1.00 18.18 ? 164 GLN A CA 1 ATOM 1244 C C . GLN A 1 141 ? 27.048 -19.366 46.683 1.00 19.11 ? 164 GLN A C 1 ATOM 1245 O O . GLN A 1 141 ? 26.079 -18.761 46.278 1.00 18.33 ? 164 GLN A O 1 ATOM 1246 C CB . GLN A 1 141 ? 26.794 -20.970 48.613 1.00 19.83 ? 164 GLN A CB 1 ATOM 1247 C CG . GLN A 1 141 ? 25.566 -20.237 49.200 1.00 20.23 ? 164 GLN A CG 1 ATOM 1248 C CD . GLN A 1 141 ? 24.255 -20.830 48.694 1.00 21.97 ? 164 GLN A CD 1 ATOM 1249 O OE1 . GLN A 1 141 ? 23.452 -20.126 48.048 1.00 24.04 ? 164 GLN A OE1 1 ATOM 1250 N NE2 . GLN A 1 141 ? 24.010 -22.043 48.999 1.00 19.79 ? 164 GLN A NE2 1 ATOM 1251 N N . GLN A 1 142 ? 28.252 -18.813 46.745 1.00 18.53 ? 165 GLN A N 1 ATOM 1252 C CA . GLN A 1 142 ? 28.482 -17.383 46.384 1.00 20.39 ? 165 GLN A CA 1 ATOM 1253 C C . GLN A 1 142 ? 28.158 -17.122 44.900 1.00 19.19 ? 165 GLN A C 1 ATOM 1254 O O . GLN A 1 142 ? 27.569 -16.146 44.571 1.00 20.19 ? 165 GLN A O 1 ATOM 1255 C CB . GLN A 1 142 ? 29.917 -17.026 46.702 1.00 22.52 ? 165 GLN A CB 1 ATOM 1256 C CG . GLN A 1 142 ? 30.351 -15.620 46.361 1.00 20.84 ? 165 GLN A CG 1 ATOM 1257 C CD . GLN A 1 142 ? 29.684 -14.587 47.244 1.00 27.31 ? 165 GLN A CD 1 ATOM 1258 O OE1 . GLN A 1 142 ? 29.471 -14.818 48.423 1.00 27.29 ? 165 GLN A OE1 1 ATOM 1259 N NE2 . GLN A 1 142 ? 29.288 -13.494 46.651 1.00 30.57 ? 165 GLN A NE2 1 ATOM 1260 N N . VAL A 1 143 ? 28.577 -18.032 44.002 1.00 19.03 ? 166 VAL A N 1 ATOM 1261 C CA . VAL A 1 143 ? 28.248 -17.877 42.579 1.00 19.96 ? 166 VAL A CA 1 ATOM 1262 C C . VAL A 1 143 ? 26.747 -17.771 42.393 1.00 19.18 ? 166 VAL A C 1 ATOM 1263 O O . VAL A 1 143 ? 26.260 -16.868 41.710 1.00 19.41 ? 166 VAL A O 1 ATOM 1264 C CB . VAL A 1 143 ? 28.791 -18.999 41.695 1.00 17.16 ? 166 VAL A CB 1 ATOM 1265 C CG1 . VAL A 1 143 ? 28.467 -18.638 40.187 1.00 16.91 ? 166 VAL A CG1 1 ATOM 1266 C CG2 . VAL A 1 143 ? 30.268 -19.071 41.935 1.00 16.24 ? 166 VAL A CG2 1 ATOM 1267 N N . VAL A 1 144 ? 26.054 -18.675 43.047 1.00 19.81 ? 167 VAL A N 1 ATOM 1268 C CA . VAL A 1 144 ? 24.607 -18.737 42.922 1.00 19.55 ? 167 VAL A CA 1 ATOM 1269 C C . VAL A 1 144 ? 24.012 -17.450 43.462 1.00 21.13 ? 167 VAL A C 1 ATOM 1270 O O . VAL A 1 144 ? 23.089 -16.866 42.870 1.00 20.66 ? 167 VAL A O 1 ATOM 1271 C CB . VAL A 1 144 ? 24.071 -19.974 43.656 1.00 20.30 ? 167 VAL A CB 1 ATOM 1272 C CG1 . VAL A 1 144 ? 22.500 -19.838 43.996 1.00 18.46 ? 167 VAL A CG1 1 ATOM 1273 C CG2 . VAL A 1 144 ? 24.328 -21.259 42.742 1.00 17.90 ? 167 VAL A CG2 1 ATOM 1274 N N . ASP A 1 145 ? 24.515 -17.004 44.615 1.00 20.34 ? 168 ASP A N 1 ATOM 1275 C CA . ASP A 1 145 ? 23.974 -15.796 45.219 1.00 20.50 ? 168 ASP A CA 1 ATOM 1276 C C . ASP A 1 145 ? 24.138 -14.599 44.312 1.00 20.75 ? 168 ASP A C 1 ATOM 1277 O O . ASP A 1 145 ? 23.236 -13.804 44.207 1.00 19.85 ? 168 ASP A O 1 ATOM 1278 C CB . ASP A 1 145 ? 24.677 -15.471 46.593 1.00 20.36 ? 168 ASP A CB 1 ATOM 1279 C CG . ASP A 1 145 ? 24.334 -16.491 47.692 1.00 19.89 ? 168 ASP A CG 1 ATOM 1280 O OD1 . ASP A 1 145 ? 23.374 -17.275 47.586 1.00 24.38 ? 168 ASP A OD1 1 ATOM 1281 O OD2 . ASP A 1 145 ? 25.008 -16.391 48.722 1.00 24.70 ? 168 ASP A OD2 1 ATOM 1282 N N A LEU A 1 146 ? 25.281 -14.483 43.658 0.50 19.57 ? 169 LEU A N 1 ATOM 1283 N N B LEU A 1 146 ? 25.299 -14.469 43.663 0.50 20.51 ? 169 LEU A N 1 ATOM 1284 C CA A LEU A 1 146 ? 25.501 -13.351 42.756 0.50 19.91 ? 169 LEU A CA 1 ATOM 1285 C CA B LEU A 1 146 ? 25.540 -13.343 42.720 0.50 21.46 ? 169 LEU A CA 1 ATOM 1286 C C A LEU A 1 146 ? 24.643 -13.472 41.491 0.50 20.27 ? 169 LEU A C 1 ATOM 1287 C C B LEU A 1 146 ? 24.679 -13.457 41.464 0.50 21.15 ? 169 LEU A C 1 ATOM 1288 O O A LEU A 1 146 ? 23.970 -12.501 41.059 0.50 21.35 ? 169 LEU A O 1 ATOM 1289 O O B LEU A 1 146 ? 24.074 -12.455 40.988 0.50 22.03 ? 169 LEU A O 1 ATOM 1290 C CB A LEU A 1 146 ? 26.951 -13.262 42.408 0.50 18.42 ? 169 LEU A CB 1 ATOM 1291 C CB B LEU A 1 146 ? 26.987 -13.268 42.294 0.50 21.12 ? 169 LEU A CB 1 ATOM 1292 C CG A LEU A 1 146 ? 27.397 -11.999 41.709 0.50 17.92 ? 169 LEU A CG 1 ATOM 1293 C CG B LEU A 1 146 ? 28.005 -12.658 43.244 0.50 23.52 ? 169 LEU A CG 1 ATOM 1294 C CD1 A LEU A 1 146 ? 27.054 -10.784 42.508 0.50 14.23 ? 169 LEU A CD1 1 ATOM 1295 C CD1 B LEU A 1 146 ? 29.387 -12.897 42.626 0.50 26.05 ? 169 LEU A CD1 1 ATOM 1296 C CD2 A LEU A 1 146 ? 28.844 -12.191 41.476 0.50 13.24 ? 169 LEU A CD2 1 ATOM 1297 C CD2 B LEU A 1 146 ? 27.724 -11.151 43.504 0.50 23.87 ? 169 LEU A CD2 1 ATOM 1298 N N . PHE A 1 147 ? 24.659 -14.665 40.914 1.00 19.50 ? 170 PHE A N 1 ATOM 1299 C CA . PHE A 1 147 ? 23.811 -14.975 39.750 1.00 18.84 ? 170 PHE A CA 1 ATOM 1300 C C . PHE A 1 147 ? 22.395 -14.550 39.980 1.00 19.88 ? 170 PHE A C 1 ATOM 1301 O O . PHE A 1 147 ? 21.783 -13.962 39.072 1.00 23.85 ? 170 PHE A O 1 ATOM 1302 C CB . PHE A 1 147 ? 23.827 -16.467 39.505 1.00 17.87 ? 170 PHE A CB 1 ATOM 1303 C CG . PHE A 1 147 ? 22.919 -16.913 38.390 1.00 16.24 ? 170 PHE A CG 1 ATOM 1304 C CD1 . PHE A 1 147 ? 23.181 -16.560 37.081 1.00 20.65 ? 170 PHE A CD1 1 ATOM 1305 C CD2 . PHE A 1 147 ? 21.853 -17.692 38.632 1.00 19.49 ? 170 PHE A CD2 1 ATOM 1306 C CE1 . PHE A 1 147 ? 22.356 -17.018 36.003 1.00 20.60 ? 170 PHE A CE1 1 ATOM 1307 C CE2 . PHE A 1 147 ? 21.013 -18.161 37.587 1.00 22.54 ? 170 PHE A CE2 1 ATOM 1308 C CZ . PHE A 1 147 ? 21.279 -17.838 36.268 1.00 19.63 ? 170 PHE A CZ 1 ATOM 1309 N N . LYS A 1 148 ? 21.853 -14.864 41.153 1.00 19.78 ? 171 LYS A N 1 ATOM 1310 C CA . LYS A 1 148 ? 20.442 -14.507 41.450 1.00 21.71 ? 171 LYS A CA 1 ATOM 1311 C C . LYS A 1 148 ? 20.163 -13.005 41.324 1.00 23.13 ? 171 LYS A C 1 ATOM 1312 O O . LYS A 1 148 ? 19.028 -12.621 41.070 1.00 24.64 ? 171 LYS A O 1 ATOM 1313 C CB . LYS A 1 148 ? 19.977 -14.970 42.785 1.00 22.39 ? 171 LYS A CB 1 ATOM 1314 C CG . LYS A 1 148 ? 19.836 -16.519 42.898 1.00 21.38 ? 171 LYS A CG 1 ATOM 1315 C CD . LYS A 1 148 ? 19.493 -16.876 44.303 1.00 25.13 ? 171 LYS A CD 1 ATOM 1316 C CE . LYS A 1 148 ? 19.284 -18.320 44.444 1.00 26.72 ? 171 LYS A CE 1 ATOM 1317 N NZ . LYS A 1 148 ? 18.876 -18.679 45.896 1.00 25.49 ? 171 LYS A NZ 1 ATOM 1318 N N . THR A 1 149 ? 21.180 -12.195 41.470 1.00 24.13 ? 172 THR A N 1 ATOM 1319 C CA . THR A 1 149 ? 20.985 -10.780 41.395 1.00 25.83 ? 172 THR A CA 1 ATOM 1320 C C . THR A 1 149 ? 21.094 -10.249 39.954 1.00 25.88 ? 172 THR A C 1 ATOM 1321 O O . THR A 1 149 ? 20.990 -9.022 39.730 1.00 24.24 ? 172 THR A O 1 ATOM 1322 C CB . THR A 1 149 ? 21.991 -9.968 42.290 1.00 26.88 ? 172 THR A CB 1 ATOM 1323 O OG1 . THR A 1 149 ? 23.286 -10.111 41.742 1.00 25.73 ? 172 THR A OG1 1 ATOM 1324 C CG2 . THR A 1 149 ? 21.978 -10.343 43.875 1.00 27.37 ? 172 THR A CG2 1 ATOM 1325 N N . LEU A 1 150 ? 21.386 -11.133 38.992 1.00 22.96 ? 173 LEU A N 1 ATOM 1326 C CA . LEU A 1 150 ? 21.762 -10.713 37.622 1.00 23.39 ? 173 LEU A CA 1 ATOM 1327 C C . LEU A 1 150 ? 20.846 -11.468 36.630 1.00 23.21 ? 173 LEU A C 1 ATOM 1328 O O . LEU A 1 150 ? 21.313 -12.311 35.838 1.00 21.83 ? 173 LEU A O 1 ATOM 1329 C CB . LEU A 1 150 ? 23.237 -11.068 37.372 1.00 21.95 ? 173 LEU A CB 1 ATOM 1330 C CG . LEU A 1 150 ? 24.233 -10.214 38.159 1.00 25.87 ? 173 LEU A CG 1 ATOM 1331 C CD1 . LEU A 1 150 ? 25.584 -10.829 38.086 1.00 22.01 ? 173 LEU A CD1 1 ATOM 1332 C CD2 . LEU A 1 150 ? 24.271 -8.763 37.709 1.00 23.19 ? 173 LEU A CD2 1 ATOM 1333 N N . ASP A 1 151 ? 19.539 -11.194 36.736 1.00 24.41 ? 174 ASP A N 1 ATOM 1334 C CA . ASP A 1 151 ? 18.518 -11.879 35.902 1.00 24.66 ? 174 ASP A CA 1 ATOM 1335 C C . ASP A 1 151 ? 18.518 -11.172 34.521 1.00 25.66 ? 174 ASP A C 1 ATOM 1336 O O . ASP A 1 151 ? 17.732 -10.272 34.255 1.00 23.65 ? 174 ASP A O 1 ATOM 1337 C CB . ASP A 1 151 ? 17.151 -11.789 36.564 1.00 26.33 ? 174 ASP A CB 1 ATOM 1338 C CG . ASP A 1 151 ? 16.098 -12.545 35.808 1.00 27.81 ? 174 ASP A CG 1 ATOM 1339 O OD1 . ASP A 1 151 ? 16.374 -12.986 34.699 1.00 25.27 ? 174 ASP A OD1 1 ATOM 1340 O OD2 . ASP A 1 151 ? 14.943 -12.630 36.290 1.00 28.98 ? 174 ASP A OD2 1 ATOM 1341 N N . SER A 1 152 ? 19.409 -11.658 33.663 1.00 24.24 ? 175 SER A N 1 ATOM 1342 C CA . SER A 1 152 ? 19.613 -11.178 32.324 1.00 23.26 ? 175 SER A CA 1 ATOM 1343 C C . SER A 1 152 ? 18.323 -11.310 31.487 1.00 24.93 ? 175 SER A C 1 ATOM 1344 O O . SER A 1 152 ? 17.988 -10.404 30.742 1.00 24.44 ? 175 SER A O 1 ATOM 1345 C CB . SER A 1 152 ? 20.772 -12.014 31.694 1.00 22.95 ? 175 SER A CB 1 ATOM 1346 O OG . SER A 1 152 ? 21.905 -11.846 32.469 1.00 21.62 ? 175 SER A OG 1 ATOM 1347 N N . TYR A 1 153 ? 17.639 -12.445 31.569 1.00 24.62 ? 176 TYR A N 1 ATOM 1348 C CA . TYR A 1 153 ? 16.457 -12.609 30.747 1.00 24.55 ? 176 TYR A CA 1 ATOM 1349 C C . TYR A 1 153 ? 15.401 -11.507 31.082 1.00 26.47 ? 176 TYR A C 1 ATOM 1350 O O . TYR A 1 153 ? 14.827 -10.888 30.122 1.00 25.51 ? 176 TYR A O 1 ATOM 1351 C CB . TYR A 1 153 ? 15.829 -13.978 30.958 1.00 24.23 ? 176 TYR A CB 1 ATOM 1352 C CG . TYR A 1 153 ? 14.646 -14.173 30.039 1.00 23.61 ? 176 TYR A CG 1 ATOM 1353 C CD1 . TYR A 1 153 ? 14.794 -14.894 28.896 1.00 26.47 ? 176 TYR A CD1 1 ATOM 1354 C CD2 . TYR A 1 153 ? 13.371 -13.623 30.317 1.00 28.42 ? 176 TYR A CD2 1 ATOM 1355 C CE1 . TYR A 1 153 ? 13.731 -15.076 28.042 1.00 25.29 ? 176 TYR A CE1 1 ATOM 1356 C CE2 . TYR A 1 153 ? 12.290 -13.830 29.416 1.00 29.42 ? 176 TYR A CE2 1 ATOM 1357 C CZ . TYR A 1 153 ? 12.516 -14.545 28.283 1.00 28.56 ? 176 TYR A CZ 1 ATOM 1358 O OH . TYR A 1 153 ? 11.588 -14.831 27.296 1.00 31.42 ? 176 TYR A OH 1 ATOM 1359 N N . THR A 1 154 ? 15.164 -11.236 32.376 1.00 26.24 ? 177 THR A N 1 ATOM 1360 C CA . THR A 1 154 ? 14.170 -10.225 32.741 1.00 27.66 ? 177 THR A CA 1 ATOM 1361 C C . THR A 1 154 ? 14.657 -8.847 32.313 1.00 29.72 ? 177 THR A C 1 ATOM 1362 O O . THR A 1 154 ? 13.879 -8.006 31.798 1.00 30.36 ? 177 THR A O 1 ATOM 1363 C CB . THR A 1 154 ? 13.833 -10.324 34.194 1.00 28.34 ? 177 THR A CB 1 ATOM 1364 O OG1 . THR A 1 154 ? 13.239 -11.617 34.358 1.00 29.36 ? 177 THR A OG1 1 ATOM 1365 C CG2 . THR A 1 154 ? 12.808 -9.197 34.662 1.00 31.36 ? 177 THR A CG2 1 ATOM 1366 N N . ALA A 1 155 ? 15.932 -8.564 32.535 1.00 29.49 ? 178 ALA A N 1 ATOM 1367 C CA . ALA A 1 155 ? 16.440 -7.238 32.165 1.00 30.33 ? 178 ALA A CA 1 ATOM 1368 C C . ALA A 1 155 ? 16.263 -6.987 30.662 1.00 29.89 ? 178 ALA A C 1 ATOM 1369 O O . ALA A 1 155 ? 15.947 -5.882 30.238 1.00 30.80 ? 178 ALA A O 1 ATOM 1370 C CB . ALA A 1 155 ? 17.879 -7.087 32.568 1.00 28.78 ? 178 ALA A CB 1 ATOM 1371 N N . LEU A 1 156 ? 16.502 -7.998 29.850 1.00 27.93 ? 179 LEU A N 1 ATOM 1372 C CA . LEU A 1 156 ? 16.323 -7.910 28.442 1.00 29.73 ? 179 LEU A CA 1 ATOM 1373 C C . LEU A 1 156 ? 14.856 -7.785 28.047 1.00 31.04 ? 179 LEU A C 1 ATOM 1374 O O . LEU A 1 156 ? 14.481 -6.901 27.242 1.00 31.87 ? 179 LEU A O 1 ATOM 1375 C CB . LEU A 1 156 ? 16.983 -9.078 27.705 1.00 29.06 ? 179 LEU A CB 1 ATOM 1376 C CG . LEU A 1 156 ? 18.539 -9.070 27.641 1.00 27.39 ? 179 LEU A CG 1 ATOM 1377 C CD1 . LEU A 1 156 ? 19.067 -10.487 27.342 1.00 21.92 ? 179 LEU A CD1 1 ATOM 1378 C CD2 . LEU A 1 156 ? 19.079 -8.091 26.622 1.00 26.13 ? 179 LEU A CD2 1 ATOM 1379 N N . SER A 1 157 ? 14.039 -8.590 28.662 1.00 30.78 ? 180 SER A N 1 ATOM 1380 C CA . SER A 1 157 ? 12.647 -8.589 28.390 1.00 32.98 ? 180 SER A CA 1 ATOM 1381 C C . SER A 1 157 ? 11.991 -7.240 28.683 1.00 35.51 ? 180 SER A C 1 ATOM 1382 O O . SER A 1 157 ? 11.090 -6.792 27.929 1.00 35.55 ? 180 SER A O 1 ATOM 1383 C CB . SER A 1 157 ? 11.958 -9.599 29.283 1.00 33.67 ? 180 SER A CB 1 ATOM 1384 O OG . SER A 1 157 ? 10.625 -9.750 28.845 1.00 35.91 ? 180 SER A OG 1 ATOM 1385 N N . ASP A 1 158 ? 12.432 -6.623 29.762 1.00 34.31 ? 181 ASP A N 1 ATOM 1386 C CA . ASP A 1 158 ? 11.888 -5.355 30.191 1.00 36.87 ? 181 ASP A CA 1 ATOM 1387 C C . ASP A 1 158 ? 12.192 -4.250 29.211 1.00 38.42 ? 181 ASP A C 1 ATOM 1388 O O . ASP A 1 158 ? 11.553 -3.193 29.291 1.00 38.10 ? 181 ASP A O 1 ATOM 1389 C CB . ASP A 1 158 ? 12.441 -4.926 31.546 1.00 37.01 ? 181 ASP A CB 1 ATOM 1390 C CG . ASP A 1 158 ? 11.858 -5.701 32.702 1.00 37.69 ? 181 ASP A CG 1 ATOM 1391 O OD1 . ASP A 1 158 ? 10.867 -6.455 32.537 1.00 37.75 ? 181 ASP A OD1 1 ATOM 1392 O OD2 . ASP A 1 158 ? 12.439 -5.569 33.788 1.00 40.38 ? 181 ASP A OD2 1 ATOM 1393 N N . ALA A 1 159 ? 13.216 -4.471 28.385 1.00 36.81 ? 182 ALA A N 1 ATOM 1394 C CA . ALA A 1 159 ? 13.649 -3.563 27.350 1.00 36.28 ? 182 ALA A CA 1 ATOM 1395 C C . ALA A 1 159 ? 13.139 -3.998 25.994 1.00 36.50 ? 182 ALA A C 1 ATOM 1396 O O . ALA A 1 159 ? 13.611 -3.489 25.003 1.00 37.26 ? 182 ALA A O 1 ATOM 1397 C CB . ALA A 1 159 ? 15.160 -3.458 27.328 1.00 35.13 ? 182 ALA A CB 1 ATOM 1398 N N . GLY A 1 160 ? 12.140 -4.876 25.954 1.00 34.78 ? 183 GLY A N 1 ATOM 1399 C CA . GLY A 1 160 ? 11.544 -5.316 24.694 1.00 35.90 ? 183 GLY A CA 1 ATOM 1400 C C . GLY A 1 160 ? 12.407 -6.343 23.927 1.00 36.00 ? 183 GLY A C 1 ATOM 1401 O O . GLY A 1 160 ? 12.194 -6.597 22.728 1.00 35.39 ? 183 GLY A O 1 ATOM 1402 N N . ILE A 1 161 ? 13.380 -6.990 24.612 1.00 33.53 ? 184 ILE A N 1 ATOM 1403 C CA . ILE A 1 161 ? 14.303 -7.916 23.890 1.00 30.28 ? 184 ILE A CA 1 ATOM 1404 C C . ILE A 1 161 ? 14.043 -9.366 24.417 1.00 30.90 ? 184 ILE A C 1 ATOM 1405 O O . ILE A 1 161 ? 14.347 -9.702 25.574 1.00 28.70 ? 184 ILE A O 1 ATOM 1406 C CB . ILE A 1 161 ? 15.784 -7.503 24.098 1.00 30.79 ? 184 ILE A CB 1 ATOM 1407 C CG1 . ILE A 1 161 ? 16.072 -6.092 23.555 1.00 32.19 ? 184 ILE A CG1 1 ATOM 1408 C CG2 . ILE A 1 161 ? 16.739 -8.485 23.469 1.00 26.29 ? 184 ILE A CG2 1 ATOM 1409 C CD1 . ILE A 1 161 ? 17.422 -5.469 24.091 1.00 32.38 ? 184 ILE A CD1 1 ATOM 1410 N N . THR A 1 162 ? 13.392 -10.166 23.581 1.00 31.99 ? 185 THR A N 1 ATOM 1411 C CA . THR A 1 162 ? 12.946 -11.491 23.957 1.00 31.37 ? 185 THR A CA 1 ATOM 1412 C C . THR A 1 162 ? 13.337 -12.441 22.858 1.00 31.09 ? 185 THR A C 1 ATOM 1413 O O . THR A 1 162 ? 13.533 -12.055 21.674 1.00 29.95 ? 185 THR A O 1 ATOM 1414 C CB . THR A 1 162 ? 11.449 -11.548 24.220 1.00 33.10 ? 185 THR A CB 1 ATOM 1415 O OG1 . THR A 1 162 ? 10.697 -11.112 23.067 1.00 34.87 ? 185 THR A OG1 1 ATOM 1416 C CG2 . THR A 1 162 ? 11.082 -10.710 25.443 1.00 33.68 ? 185 THR A CG2 1 ATOM 1417 N N . PRO A 1 163 ? 13.605 -13.715 23.221 1.00 28.79 ? 186 PRO A N 1 ATOM 1418 C CA . PRO A 1 163 ? 14.008 -14.627 22.184 1.00 27.62 ? 186 PRO A CA 1 ATOM 1419 C C . PRO A 1 163 ? 12.956 -14.708 21.081 1.00 29.42 ? 186 PRO A C 1 ATOM 1420 O O . PRO A 1 163 ? 11.740 -14.658 21.378 1.00 30.46 ? 186 PRO A O 1 ATOM 1421 C CB . PRO A 1 163 ? 14.036 -16.031 22.910 1.00 27.11 ? 186 PRO A CB 1 ATOM 1422 C CG . PRO A 1 163 ? 14.349 -15.668 24.333 1.00 28.32 ? 186 PRO A CG 1 ATOM 1423 C CD . PRO A 1 163 ? 13.572 -14.352 24.560 1.00 28.89 ? 186 PRO A CD 1 ATOM 1424 N N A SER A 1 164 ? 13.424 -14.812 19.846 0.60 30.20 ? 187 SER A N 1 ATOM 1425 N N B SER A 1 164 ? 13.410 -14.926 19.867 0.40 30.66 ? 187 SER A N 1 ATOM 1426 C CA A SER A 1 164 ? 12.554 -14.813 18.611 0.60 30.43 ? 187 SER A CA 1 ATOM 1427 C CA B SER A 1 164 ? 12.498 -15.004 18.722 0.40 31.89 ? 187 SER A CA 1 ATOM 1428 C C A SER A 1 164 ? 13.198 -15.577 17.469 0.60 30.29 ? 187 SER A C 1 ATOM 1429 C C B SER A 1 164 ? 13.174 -15.600 17.503 0.40 31.56 ? 187 SER A C 1 ATOM 1430 O O A SER A 1 164 ? 14.407 -15.511 17.258 0.60 27.66 ? 187 SER A O 1 ATOM 1431 O O B SER A 1 164 ? 14.376 -15.453 17.288 0.40 29.98 ? 187 SER A O 1 ATOM 1432 C CB A SER A 1 164 ? 12.204 -13.370 18.161 0.60 31.73 ? 187 SER A CB 1 ATOM 1433 C CB B SER A 1 164 ? 11.913 -13.624 18.416 0.40 32.73 ? 187 SER A CB 1 ATOM 1434 O OG A SER A 1 164 ? 11.454 -13.287 16.934 0.60 28.02 ? 187 SER A OG 1 ATOM 1435 O OG B SER A 1 164 ? 12.900 -12.615 18.579 0.40 34.79 ? 187 SER A OG 1 ATOM 1436 N N . GLU A 1 165 ? 12.356 -16.294 16.719 1.00 33.49 ? 188 GLU A N 1 ATOM 1437 C CA . GLU A 1 165 ? 12.803 -16.995 15.513 1.00 36.04 ? 188 GLU A CA 1 ATOM 1438 C C . GLU A 1 165 ? 13.150 -15.971 14.432 1.00 39.12 ? 188 GLU A C 1 ATOM 1439 O O . GLU A 1 165 ? 14.129 -16.182 13.690 1.00 41.39 ? 188 GLU A O 1 ATOM 1440 C CB . GLU A 1 165 ? 11.706 -17.946 14.988 1.00 38.62 ? 188 GLU A CB 1 ATOM 1441 C CG . GLU A 1 165 ? 11.102 -18.952 15.988 1.00 42.98 ? 188 GLU A CG 1 ATOM 1442 C CD . GLU A 1 165 ? 12.108 -19.991 16.427 1.00 49.15 ? 188 GLU A CD 1 ATOM 1443 O OE1 . GLU A 1 165 ? 13.259 -19.965 15.884 1.00 49.18 ? 188 GLU A OE1 1 ATOM 1444 O OE2 . GLU A 1 165 ? 11.744 -20.816 17.330 1.00 52.80 ? 188 GLU A OE2 1 ATOM 1445 N N . ASP A 1 166 ? 12.467 -14.825 14.420 1.00 39.66 ? 189 ASP A N 1 ATOM 1446 C CA . ASP A 1 166 ? 12.655 -13.809 13.324 1.00 42.93 ? 189 ASP A CA 1 ATOM 1447 C C . ASP A 1 166 ? 13.210 -12.454 13.668 1.00 40.98 ? 189 ASP A C 1 ATOM 1448 O O . ASP A 1 166 ? 13.843 -11.828 12.823 1.00 41.77 ? 189 ASP A O 1 ATOM 1449 C CB . ASP A 1 166 ? 11.307 -13.500 12.643 1.00 44.91 ? 189 ASP A CB 1 ATOM 1450 C CG . ASP A 1 166 ? 10.578 -14.712 12.311 1.00 53.21 ? 189 ASP A CG 1 ATOM 1451 O OD1 . ASP A 1 166 ? 11.129 -15.531 11.515 1.00 61.54 ? 189 ASP A OD1 1 ATOM 1452 O OD2 . ASP A 1 166 ? 9.503 -14.907 12.927 1.00 64.65 ? 189 ASP A OD2 1 ATOM 1453 N N . ALA A 1 167 ? 12.861 -11.928 14.821 1.00 39.28 ? 190 ALA A N 1 ATOM 1454 C CA . ALA A 1 167 ? 13.407 -10.629 15.253 1.00 38.47 ? 190 ALA A CA 1 ATOM 1455 C C . ALA A 1 167 ? 14.923 -10.683 15.416 1.00 37.88 ? 190 ALA A C 1 ATOM 1456 O O . ALA A 1 167 ? 15.513 -11.737 15.786 1.00 34.83 ? 190 ALA A O 1 ATOM 1457 C CB . ALA A 1 167 ? 12.698 -10.126 16.542 1.00 38.89 ? 190 ALA A CB 1 ATOM 1458 N N . THR A 1 168 ? 15.576 -9.571 15.112 1.00 35.87 ? 191 THR A N 1 ATOM 1459 C CA . THR A 1 168 ? 16.990 -9.457 15.425 1.00 36.61 ? 191 THR A CA 1 ATOM 1460 C C . THR A 1 168 ? 17.240 -8.179 16.152 1.00 35.48 ? 191 THR A C 1 ATOM 1461 O O . THR A 1 168 ? 16.372 -7.284 16.184 1.00 37.78 ? 191 THR A O 1 ATOM 1462 C CB . THR A 1 168 ? 17.924 -9.560 14.210 1.00 37.05 ? 191 THR A CB 1 ATOM 1463 O OG1 . THR A 1 168 ? 17.732 -8.383 13.416 1.00 40.45 ? 191 THR A OG1 1 ATOM 1464 C CG2 . THR A 1 168 ? 17.627 -10.838 13.393 1.00 38.29 ? 191 THR A CG2 1 ATOM 1465 N N . TYR A 1 169 ? 18.409 -8.075 16.775 1.00 33.96 ? 192 TYR A N 1 ATOM 1466 C CA . TYR A 1 169 ? 18.628 -7.037 17.784 1.00 32.97 ? 192 TYR A CA 1 ATOM 1467 C C . TYR A 1 169 ? 19.929 -6.274 17.645 1.00 32.66 ? 192 TYR A C 1 ATOM 1468 O O . TYR A 1 169 ? 20.924 -6.731 17.036 1.00 32.82 ? 192 TYR A O 1 ATOM 1469 C CB . TYR A 1 169 ? 18.543 -7.663 19.213 1.00 33.07 ? 192 TYR A CB 1 ATOM 1470 C CG . TYR A 1 169 ? 17.201 -8.211 19.544 1.00 30.49 ? 192 TYR A CG 1 ATOM 1471 C CD1 . TYR A 1 169 ? 16.135 -7.358 19.901 1.00 33.96 ? 192 TYR A CD1 1 ATOM 1472 C CD2 . TYR A 1 169 ? 16.979 -9.568 19.523 1.00 29.41 ? 192 TYR A CD2 1 ATOM 1473 C CE1 . TYR A 1 169 ? 14.892 -7.864 20.203 1.00 33.46 ? 192 TYR A CE1 1 ATOM 1474 C CE2 . TYR A 1 169 ? 15.742 -10.091 19.786 1.00 27.29 ? 192 TYR A CE2 1 ATOM 1475 C CZ . TYR A 1 169 ? 14.700 -9.234 20.166 1.00 32.87 ? 192 TYR A CZ 1 ATOM 1476 O OH . TYR A 1 169 ? 13.461 -9.752 20.486 1.00 28.61 ? 192 TYR A OH 1 ATOM 1477 N N . LYS A 1 170 ? 19.913 -5.088 18.230 1.00 33.35 ? 193 LYS A N 1 ATOM 1478 C CA . LYS A 1 170 ? 21.080 -4.233 18.212 1.00 34.58 ? 193 LYS A CA 1 ATOM 1479 C C . LYS A 1 170 ? 21.936 -4.431 19.470 1.00 32.78 ? 193 LYS A C 1 ATOM 1480 O O . LYS A 1 170 ? 21.427 -4.410 20.569 1.00 33.78 ? 193 LYS A O 1 ATOM 1481 C CB . LYS A 1 170 ? 20.664 -2.746 18.072 1.00 37.20 ? 193 LYS A CB 1 ATOM 1482 C CG . LYS A 1 170 ? 20.174 -2.436 16.582 1.00 41.75 ? 193 LYS A CG 1 ATOM 1483 C CD . LYS A 1 170 ? 18.989 -1.463 16.442 1.00 49.59 ? 193 LYS A CD 1 ATOM 1484 C CE . LYS A 1 170 ? 18.052 -1.685 15.148 1.00 47.25 ? 193 LYS A CE 1 ATOM 1485 N NZ . LYS A 1 170 ? 16.839 -0.661 15.172 1.00 50.36 ? 193 LYS A NZ 1 ATOM 1486 N N . LEU A 1 171 ? 23.246 -4.489 19.300 1.00 32.06 ? 194 LEU A N 1 ATOM 1487 C CA . LEU A 1 171 ? 24.123 -4.609 20.402 1.00 31.75 ? 194 LEU A CA 1 ATOM 1488 C C . LEU A 1 171 ? 23.899 -3.599 21.467 1.00 32.70 ? 194 LEU A C 1 ATOM 1489 O O . LEU A 1 171 ? 23.944 -3.921 22.685 1.00 29.04 ? 194 LEU A O 1 ATOM 1490 C CB . LEU A 1 171 ? 25.566 -4.664 19.935 1.00 32.44 ? 194 LEU A CB 1 ATOM 1491 C CG . LEU A 1 171 ? 26.633 -4.876 20.996 1.00 30.04 ? 194 LEU A CG 1 ATOM 1492 C CD1 . LEU A 1 171 ? 26.389 -6.227 21.789 1.00 25.79 ? 194 LEU A CD1 1 ATOM 1493 C CD2 . LEU A 1 171 ? 28.074 -4.796 20.423 1.00 33.84 ? 194 LEU A CD2 1 ATOM 1494 N N . SER A 1 172 ? 23.753 -2.337 21.052 1.00 31.41 ? 195 SER A N 1 ATOM 1495 C CA . SER A 1 172 ? 23.723 -1.271 22.049 1.00 32.24 ? 195 SER A CA 1 ATOM 1496 C C . SER A 1 172 ? 22.455 -1.368 22.849 1.00 30.22 ? 195 SER A C 1 ATOM 1497 O O . SER A 1 172 ? 22.437 -0.946 24.004 1.00 31.81 ? 195 SER A O 1 ATOM 1498 C CB . SER A 1 172 ? 23.850 0.155 21.379 1.00 33.72 ? 195 SER A CB 1 ATOM 1499 O OG . SER A 1 172 ? 22.622 0.485 20.789 1.00 36.92 ? 195 SER A OG 1 ATOM 1500 N N . ASP A 1 173 ? 21.374 -1.910 22.265 1.00 30.62 ? 196 ASP A N 1 ATOM 1501 C CA . ASP A 1 173 ? 20.127 -2.072 23.024 1.00 30.40 ? 196 ASP A CA 1 ATOM 1502 C C . ASP A 1 173 ? 20.323 -3.183 24.095 1.00 30.74 ? 196 ASP A C 1 ATOM 1503 O O . ASP A 1 173 ? 19.816 -3.063 25.219 1.00 30.82 ? 196 ASP A O 1 ATOM 1504 C CB . ASP A 1 173 ? 18.950 -2.428 22.136 1.00 31.02 ? 196 ASP A CB 1 ATOM 1505 C CG . ASP A 1 173 ? 18.470 -1.215 21.270 1.00 35.51 ? 196 ASP A CG 1 ATOM 1506 O OD1 . ASP A 1 173 ? 18.748 -0.098 21.675 1.00 33.91 ? 196 ASP A OD1 1 ATOM 1507 O OD2 . ASP A 1 173 ? 17.860 -1.451 20.231 1.00 34.54 ? 196 ASP A OD2 1 ATOM 1508 N N . ILE A 1 174 ? 21.038 -4.220 23.685 1.00 30.79 ? 197 ILE A N 1 ATOM 1509 C CA . ILE A 1 174 ? 21.325 -5.417 24.565 1.00 30.15 ? 197 ILE A CA 1 ATOM 1510 C C . ILE A 1 174 ? 22.170 -4.938 25.723 1.00 30.01 ? 197 ILE A C 1 ATOM 1511 O O . ILE A 1 174 ? 21.849 -5.172 26.895 1.00 30.32 ? 197 ILE A O 1 ATOM 1512 C CB . ILE A 1 174 ? 22.041 -6.536 23.831 1.00 29.57 ? 197 ILE A CB 1 ATOM 1513 C CG1 . ILE A 1 174 ? 21.096 -7.204 22.832 1.00 29.59 ? 197 ILE A CG1 1 ATOM 1514 C CG2 . ILE A 1 174 ? 22.621 -7.569 24.900 1.00 25.12 ? 197 ILE A CG2 1 ATOM 1515 C CD1 . ILE A 1 174 ? 21.831 -8.072 21.812 1.00 25.90 ? 197 ILE A CD1 1 ATOM 1516 N N . GLU A 1 175 ? 23.224 -4.196 25.397 1.00 30.92 ? 198 GLU A N 1 ATOM 1517 C CA . GLU A 1 175 ? 24.105 -3.619 26.377 1.00 31.39 ? 198 GLU A CA 1 ATOM 1518 C C . GLU A 1 175 ? 23.377 -2.655 27.383 1.00 32.42 ? 198 GLU A C 1 ATOM 1519 O O . GLU A 1 175 ? 23.611 -2.679 28.604 1.00 32.12 ? 198 GLU A O 1 ATOM 1520 C CB . GLU A 1 175 ? 25.263 -2.915 25.663 1.00 32.99 ? 198 GLU A CB 1 ATOM 1521 C CG . GLU A 1 175 ? 26.259 -3.838 25.006 1.00 30.86 ? 198 GLU A CG 1 ATOM 1522 C CD . GLU A 1 175 ? 27.339 -3.136 24.224 1.00 35.66 ? 198 GLU A CD 1 ATOM 1523 O OE1 . GLU A 1 175 ? 27.058 -2.024 23.742 1.00 36.10 ? 198 GLU A OE1 1 ATOM 1524 O OE2 . GLU A 1 175 ? 28.441 -3.731 24.052 1.00 34.11 ? 198 GLU A OE2 1 ATOM 1525 N N . ASP A 1 176 ? 22.480 -1.809 26.886 1.00 32.55 ? 199 ASP A N 1 ATOM 1526 C CA . ASP A 1 176 ? 21.872 -0.811 27.732 1.00 32.90 ? 199 ASP A CA 1 ATOM 1527 C C . ASP A 1 176 ? 20.936 -1.535 28.681 1.00 31.27 ? 199 ASP A C 1 ATOM 1528 O O . ASP A 1 176 ? 20.897 -1.208 29.850 1.00 29.83 ? 199 ASP A O 1 ATOM 1529 C CB . ASP A 1 176 ? 21.067 0.220 26.916 1.00 33.58 ? 199 ASP A CB 1 ATOM 1530 C CG . ASP A 1 176 ? 21.931 1.179 26.088 1.00 37.28 ? 199 ASP A CG 1 ATOM 1531 O OD1 . ASP A 1 176 ? 23.140 1.350 26.297 1.00 37.68 ? 199 ASP A OD1 1 ATOM 1532 O OD2 . ASP A 1 176 ? 21.322 1.844 25.215 1.00 39.86 ? 199 ASP A OD2 1 ATOM 1533 N N . ALA A 1 177 ? 20.206 -2.529 28.152 1.00 31.77 ? 200 ALA A N 1 ATOM 1534 C CA . ALA A 1 177 ? 19.200 -3.296 28.901 1.00 30.32 ? 200 ALA A CA 1 ATOM 1535 C C . ALA A 1 177 ? 19.858 -3.986 30.105 1.00 30.79 ? 200 ALA A C 1 ATOM 1536 O O . ALA A 1 177 ? 19.241 -4.043 31.202 1.00 31.76 ? 200 ALA A O 1 ATOM 1537 C CB . ALA A 1 177 ? 18.535 -4.347 28.019 1.00 29.18 ? 200 ALA A CB 1 ATOM 1538 N N . LEU A 1 178 ? 21.084 -4.456 29.902 1.00 29.29 ? 201 LEU A N 1 ATOM 1539 C CA . LEU A 1 178 ? 21.787 -5.288 30.908 1.00 29.30 ? 201 LEU A CA 1 ATOM 1540 C C . LEU A 1 178 ? 22.549 -4.385 31.849 1.00 29.78 ? 201 LEU A C 1 ATOM 1541 O O . LEU A 1 178 ? 22.649 -4.645 33.028 1.00 29.78 ? 201 LEU A O 1 ATOM 1542 C CB . LEU A 1 178 ? 22.702 -6.267 30.225 1.00 27.02 ? 201 LEU A CB 1 ATOM 1543 C CG . LEU A 1 178 ? 21.970 -7.370 29.421 1.00 27.25 ? 201 LEU A CG 1 ATOM 1544 C CD1 . LEU A 1 178 ? 22.934 -8.252 28.587 1.00 26.78 ? 201 LEU A CD1 1 ATOM 1545 C CD2 . LEU A 1 178 ? 20.915 -8.149 30.296 1.00 25.03 ? 201 LEU A CD2 1 ATOM 1546 N N . ALA A 1 179 ? 23.023 -3.255 31.329 1.00 30.54 ? 202 ALA A N 1 ATOM 1547 C CA . ALA A 1 179 ? 23.641 -2.251 32.160 1.00 30.42 ? 202 ALA A CA 1 ATOM 1548 C C . ALA A 1 179 ? 22.707 -1.764 33.269 1.00 31.86 ? 202 ALA A C 1 ATOM 1549 O O . ALA A 1 179 ? 23.199 -1.364 34.347 1.00 31.11 ? 202 ALA A O 1 ATOM 1550 C CB . ALA A 1 179 ? 24.136 -1.048 31.279 1.00 32.11 ? 202 ALA A CB 1 ATOM 1551 N N . ALA A 1 180 ? 21.386 -1.764 32.995 1.00 32.28 ? 203 ALA A N 1 ATOM 1552 C CA . ALA A 1 180 ? 20.337 -1.292 33.920 1.00 33.11 ? 203 ALA A CA 1 ATOM 1553 C C . ALA A 1 180 ? 20.287 -2.147 35.181 1.00 32.36 ? 203 ALA A C 1 ATOM 1554 O O . ALA A 1 180 ? 19.826 -1.690 36.225 1.00 33.60 ? 203 ALA A O 1 ATOM 1555 C CB . ALA A 1 180 ? 18.908 -1.341 33.215 1.00 32.73 ? 203 ALA A CB 1 ATOM 1556 N N . ILE A 1 181 ? 20.752 -3.387 35.094 1.00 30.48 ? 204 ILE A N 1 ATOM 1557 C CA . ILE A 1 181 ? 20.813 -4.239 36.324 1.00 28.48 ? 204 ILE A CA 1 ATOM 1558 C C . ILE A 1 181 ? 22.222 -4.316 36.939 1.00 28.75 ? 204 ILE A C 1 ATOM 1559 O O . ILE A 1 181 ? 22.493 -5.155 37.867 1.00 27.55 ? 204 ILE A O 1 ATOM 1560 C CB . ILE A 1 181 ? 20.191 -5.621 36.137 1.00 27.84 ? 204 ILE A CB 1 ATOM 1561 C CG1 . ILE A 1 181 ? 20.941 -6.450 35.087 1.00 27.67 ? 204 ILE A CG1 1 ATOM 1562 C CG2 . ILE A 1 181 ? 18.736 -5.485 35.830 1.00 28.84 ? 204 ILE A CG2 1 ATOM 1563 C CD1 . ILE A 1 181 ? 20.541 -7.962 35.139 1.00 27.85 ? 204 ILE A CD1 1 ATOM 1564 N N . HIS A 1 182 ? 23.117 -3.445 36.480 1.00 28.61 ? 205 HIS A N 1 ATOM 1565 C CA . HIS A 1 182 ? 24.539 -3.531 36.803 1.00 28.60 ? 205 HIS A CA 1 ATOM 1566 C C . HIS A 1 182 ? 25.106 -2.136 36.936 1.00 30.93 ? 205 HIS A C 1 ATOM 1567 O O . HIS A 1 182 ? 26.238 -1.860 36.504 1.00 30.05 ? 205 HIS A O 1 ATOM 1568 C CB . HIS A 1 182 ? 25.265 -4.344 35.728 1.00 27.40 ? 205 HIS A CB 1 ATOM 1569 C CG . HIS A 1 182 ? 26.663 -4.784 36.093 1.00 28.05 ? 205 HIS A CG 1 ATOM 1570 N ND1 . HIS A 1 182 ? 26.958 -5.606 37.196 1.00 29.62 ? 205 HIS A ND1 1 ATOM 1571 C CD2 . HIS A 1 182 ? 27.853 -4.541 35.492 1.00 26.17 ? 205 HIS A CD2 1 ATOM 1572 C CE1 . HIS A 1 182 ? 28.266 -5.785 37.267 1.00 24.91 ? 205 HIS A CE1 1 ATOM 1573 N NE2 . HIS A 1 182 ? 28.833 -5.174 36.245 1.00 29.18 ? 205 HIS A NE2 1 ATOM 1574 N N A ASP A 1 183 ? 24.306 -1.243 37.518 0.50 32.54 ? 206 ASP A N 1 ATOM 1575 N N B ASP A 1 183 ? 24.304 -1.252 37.530 0.50 32.59 ? 206 ASP A N 1 ATOM 1576 C CA A ASP A 1 183 ? 24.730 0.112 37.840 0.50 34.90 ? 206 ASP A CA 1 ATOM 1577 C CA B ASP A 1 183 ? 24.711 0.111 37.834 0.50 35.00 ? 206 ASP A CA 1 ATOM 1578 C C A ASP A 1 183 ? 25.148 0.966 36.657 0.50 36.00 ? 206 ASP A C 1 ATOM 1579 C C B ASP A 1 183 ? 25.216 0.901 36.643 0.50 35.99 ? 206 ASP A C 1 ATOM 1580 O O A ASP A 1 183 ? 25.913 1.914 36.813 0.50 37.52 ? 206 ASP A O 1 ATOM 1581 O O B ASP A 1 183 ? 26.124 1.719 36.773 0.50 37.37 ? 206 ASP A O 1 ATOM 1582 C CB A ASP A 1 183 ? 25.866 0.087 38.876 0.50 35.15 ? 206 ASP A CB 1 ATOM 1583 C CB B ASP A 1 183 ? 25.772 0.118 38.949 0.50 35.36 ? 206 ASP A CB 1 ATOM 1584 C CG A ASP A 1 183 ? 25.897 1.342 39.732 0.50 38.49 ? 206 ASP A CG 1 ATOM 1585 C CG B ASP A 1 183 ? 25.187 -0.173 40.316 0.50 37.92 ? 206 ASP A CG 1 ATOM 1586 O OD1 A ASP A 1 183 ? 24.798 1.848 40.050 0.50 42.49 ? 206 ASP A OD1 1 ATOM 1587 O OD1 B ASP A 1 183 ? 23.946 -0.297 40.427 0.50 41.31 ? 206 ASP A OD1 1 ATOM 1588 O OD2 A ASP A 1 183 ? 26.996 1.824 40.095 0.50 41.15 ? 206 ASP A OD2 1 ATOM 1589 O OD2 B ASP A 1 183 ? 25.962 -0.285 41.302 0.50 44.18 ? 206 ASP A OD2 1 ATOM 1590 N N . GLY A 1 184 ? 24.652 0.672 35.472 1.00 35.98 ? 207 GLY A N 1 ATOM 1591 C CA . GLY A 1 184 ? 25.052 1.447 34.293 1.00 36.68 ? 207 GLY A CA 1 ATOM 1592 C C . GLY A 1 184 ? 26.297 0.932 33.572 1.00 35.97 ? 207 GLY A C 1 ATOM 1593 O O . GLY A 1 184 ? 26.631 1.441 32.500 1.00 34.34 ? 207 GLY A O 1 ATOM 1594 N N . TYR A 1 185 ? 26.942 -0.120 34.124 1.00 35.25 ? 208 TYR A N 1 ATOM 1595 C CA . TYR A 1 185 ? 28.027 -0.807 33.437 1.00 33.39 ? 208 TYR A CA 1 ATOM 1596 C C . TYR A 1 185 ? 27.514 -2.039 32.670 1.00 33.15 ? 208 TYR A C 1 ATOM 1597 O O . TYR A 1 185 ? 27.020 -3.033 33.270 1.00 31.30 ? 208 TYR A O 1 ATOM 1598 C CB . TYR A 1 185 ? 29.073 -1.238 34.437 1.00 34.31 ? 208 TYR A CB 1 ATOM 1599 C CG . TYR A 1 185 ? 29.794 -0.144 35.108 1.00 36.65 ? 208 TYR A CG 1 ATOM 1600 C CD1 . TYR A 1 185 ? 30.776 0.589 34.441 1.00 41.26 ? 208 TYR A CD1 1 ATOM 1601 C CD2 . TYR A 1 185 ? 29.527 0.185 36.439 1.00 38.29 ? 208 TYR A CD2 1 ATOM 1602 C CE1 . TYR A 1 185 ? 31.498 1.638 35.099 1.00 44.97 ? 208 TYR A CE1 1 ATOM 1603 C CE2 . TYR A 1 185 ? 30.234 1.230 37.098 1.00 42.75 ? 208 TYR A CE2 1 ATOM 1604 C CZ . TYR A 1 185 ? 31.207 1.955 36.399 1.00 45.06 ? 208 TYR A CZ 1 ATOM 1605 O OH . TYR A 1 185 ? 31.878 2.971 37.002 1.00 46.22 ? 208 TYR A OH 1 ATOM 1606 N N . PRO A 1 186 ? 27.604 -2.016 31.347 1.00 32.31 ? 209 PRO A N 1 ATOM 1607 C CA . PRO A 1 186 ? 27.242 -3.169 30.592 1.00 31.38 ? 209 PRO A CA 1 ATOM 1608 C C . PRO A 1 186 ? 28.157 -4.360 30.839 1.00 29.00 ? 209 PRO A C 1 ATOM 1609 O O . PRO A 1 186 ? 29.313 -4.193 31.180 1.00 28.03 ? 209 PRO A O 1 ATOM 1610 C CB . PRO A 1 186 ? 27.439 -2.727 29.122 1.00 32.46 ? 209 PRO A CB 1 ATOM 1611 C CG . PRO A 1 186 ? 28.063 -1.471 29.178 1.00 34.37 ? 209 PRO A CG 1 ATOM 1612 C CD . PRO A 1 186 ? 28.066 -0.897 30.496 1.00 33.49 ? 209 PRO A CD 1 ATOM 1613 N N . PRO A 1 187 ? 27.618 -5.576 30.720 1.00 28.05 ? 210 PRO A N 1 ATOM 1614 C CA . PRO A 1 187 ? 28.519 -6.749 30.729 1.00 25.98 ? 210 PRO A CA 1 ATOM 1615 C C . PRO A 1 187 ? 29.303 -6.850 29.418 1.00 26.53 ? 210 PRO A C 1 ATOM 1616 O O . PRO A 1 187 ? 28.949 -6.202 28.442 1.00 25.90 ? 210 PRO A O 1 ATOM 1617 C CB . PRO A 1 187 ? 27.547 -7.920 30.870 1.00 25.68 ? 210 PRO A CB 1 ATOM 1618 C CG . PRO A 1 187 ? 26.300 -7.465 30.116 1.00 25.36 ? 210 PRO A CG 1 ATOM 1619 C CD . PRO A 1 187 ? 26.233 -5.925 30.371 1.00 27.42 ? 210 PRO A CD 1 ATOM 1620 N N . TYR A 1 188 ? 30.353 -7.671 29.384 1.00 26.47 ? 211 TYR A N 1 ATOM 1621 C CA . TYR A 1 188 ? 30.743 -8.309 28.110 1.00 27.50 ? 211 TYR A CA 1 ATOM 1622 C C . TYR A 1 188 ? 29.551 -9.076 27.516 1.00 26.65 ? 211 TYR A C 1 ATOM 1623 O O . TYR A 1 188 ? 28.896 -9.800 28.205 1.00 26.10 ? 211 TYR A O 1 ATOM 1624 C CB . TYR A 1 188 ? 31.956 -9.227 28.259 1.00 25.97 ? 211 TYR A CB 1 ATOM 1625 C CG . TYR A 1 188 ? 32.235 -10.029 27.046 1.00 26.72 ? 211 TYR A CG 1 ATOM 1626 C CD1 . TYR A 1 188 ? 32.944 -9.508 25.947 1.00 29.49 ? 211 TYR A CD1 1 ATOM 1627 C CD2 . TYR A 1 188 ? 31.800 -11.360 26.966 1.00 22.03 ? 211 TYR A CD2 1 ATOM 1628 C CE1 . TYR A 1 188 ? 33.198 -10.327 24.828 1.00 30.32 ? 211 TYR A CE1 1 ATOM 1629 C CE2 . TYR A 1 188 ? 32.011 -12.134 25.852 1.00 24.00 ? 211 TYR A CE2 1 ATOM 1630 C CZ . TYR A 1 188 ? 32.722 -11.609 24.787 1.00 28.08 ? 211 TYR A CZ 1 ATOM 1631 O OH . TYR A 1 188 ? 32.926 -12.481 23.717 1.00 28.42 ? 211 TYR A OH 1 ATOM 1632 N N . VAL A 1 189 ? 29.289 -8.860 26.235 1.00 25.33 ? 212 VAL A N 1 ATOM 1633 C CA . VAL A 1 189 ? 28.253 -9.522 25.450 1.00 25.00 ? 212 VAL A CA 1 ATOM 1634 C C . VAL A 1 189 ? 28.933 -10.379 24.370 1.00 26.26 ? 212 VAL A C 1 ATOM 1635 O O . VAL A 1 189 ? 29.607 -9.855 23.454 1.00 26.60 ? 212 VAL A O 1 ATOM 1636 C CB . VAL A 1 189 ? 27.292 -8.562 24.797 1.00 26.63 ? 212 VAL A CB 1 ATOM 1637 C CG1 . VAL A 1 189 ? 26.233 -9.407 23.994 1.00 24.26 ? 212 VAL A CG1 1 ATOM 1638 C CG2 . VAL A 1 189 ? 26.574 -7.674 25.862 1.00 24.42 ? 212 VAL A CG2 1 ATOM 1639 N N . GLY A 1 190 ? 28.766 -11.685 24.507 1.00 24.20 ? 213 GLY A N 1 ATOM 1640 C CA . GLY A 1 190 ? 29.350 -12.697 23.593 1.00 24.21 ? 213 GLY A CA 1 ATOM 1641 C C . GLY A 1 190 ? 28.299 -13.341 22.721 1.00 25.16 ? 213 GLY A C 1 ATOM 1642 O O . GLY A 1 190 ? 27.219 -13.694 23.168 1.00 23.68 ? 213 GLY A O 1 ATOM 1643 N N . CYS A 1 191 ? 28.601 -13.393 21.410 1.00 26.52 ? 214 CYS A N 1 ATOM 1644 C CA . CYS A 1 191 ? 27.739 -14.021 20.417 1.00 25.14 ? 214 CYS A CA 1 ATOM 1645 C C . CYS A 1 191 ? 28.442 -15.252 19.853 1.00 26.27 ? 214 CYS A C 1 ATOM 1646 O O . CYS A 1 191 ? 29.689 -15.310 19.795 1.00 25.98 ? 214 CYS A O 1 ATOM 1647 C CB . CYS A 1 191 ? 27.513 -13.022 19.223 1.00 26.34 ? 214 CYS A CB 1 ATOM 1648 S SG . CYS A 1 191 ? 26.321 -11.764 19.682 1.00 28.88 ? 214 CYS A SG 1 ATOM 1649 N N . GLU A 1 192 ? 27.633 -16.177 19.342 1.00 27.28 ? 215 GLU A N 1 ATOM 1650 C CA . GLU A 1 192 ? 28.132 -17.362 18.624 1.00 28.77 ? 215 GLU A CA 1 ATOM 1651 C C . GLU A 1 192 ? 27.252 -17.513 17.397 1.00 29.21 ? 215 GLU A C 1 ATOM 1652 O O . GLU A 1 192 ? 26.057 -17.575 17.518 1.00 28.67 ? 215 GLU A O 1 ATOM 1653 C CB . GLU A 1 192 ? 28.007 -18.651 19.469 1.00 28.30 ? 215 GLU A CB 1 ATOM 1654 C CG . GLU A 1 192 ? 28.749 -19.847 18.892 1.00 33.78 ? 215 GLU A CG 1 ATOM 1655 C CD . GLU A 1 192 ? 30.228 -19.706 19.042 1.00 35.46 ? 215 GLU A CD 1 ATOM 1656 O OE1 . GLU A 1 192 ? 30.588 -19.099 20.043 1.00 46.39 ? 215 GLU A OE1 1 ATOM 1657 O OE2 . GLU A 1 192 ? 31.021 -20.191 18.201 1.00 39.24 ? 215 GLU A OE2 1 ATOM 1658 N N . ASP A 1 193 ? 27.880 -17.554 16.257 1.00 30.60 ? 216 ASP A N 1 ATOM 1659 C CA . ASP A 1 193 ? 27.211 -17.799 14.996 1.00 33.16 ? 216 ASP A CA 1 ATOM 1660 C C . ASP A 1 193 ? 26.126 -16.674 14.858 1.00 32.86 ? 216 ASP A C 1 ATOM 1661 O O . ASP A 1 193 ? 24.975 -16.984 14.521 1.00 31.54 ? 216 ASP A O 1 ATOM 1662 C CB . ASP A 1 193 ? 26.551 -19.204 14.985 1.00 32.77 ? 216 ASP A CB 1 ATOM 1663 C CG . ASP A 1 193 ? 27.603 -20.404 14.984 1.00 38.16 ? 216 ASP A CG 1 ATOM 1664 O OD1 . ASP A 1 193 ? 28.445 -20.352 14.092 1.00 46.78 ? 216 ASP A OD1 1 ATOM 1665 O OD2 . ASP A 1 193 ? 27.598 -21.314 15.867 1.00 38.16 ? 216 ASP A OD2 1 ATOM 1666 N N . GLY A 1 194 ? 26.477 -15.438 15.234 1.00 32.53 ? 217 GLY A N 1 ATOM 1667 C CA . GLY A 1 194 ? 25.498 -14.348 15.228 1.00 32.42 ? 217 GLY A CA 1 ATOM 1668 C C . GLY A 1 194 ? 24.329 -14.411 16.206 1.00 29.93 ? 217 GLY A C 1 ATOM 1669 O O . GLY A 1 194 ? 23.398 -13.626 16.090 1.00 28.86 ? 217 GLY A O 1 ATOM 1670 N N . ALA A 1 195 ? 24.398 -15.323 17.183 1.00 26.17 ? 218 ALA A N 1 ATOM 1671 C CA . ALA A 1 195 ? 23.406 -15.514 18.214 1.00 25.93 ? 218 ALA A CA 1 ATOM 1672 C C . ALA A 1 195 ? 23.967 -15.129 19.617 1.00 24.23 ? 218 ALA A C 1 ATOM 1673 O O . ALA A 1 195 ? 25.111 -15.418 19.981 1.00 23.36 ? 218 ALA A O 1 ATOM 1674 C CB . ALA A 1 195 ? 22.903 -16.946 18.273 1.00 24.26 ? 218 ALA A CB 1 ATOM 1675 N N . LEU A 1 196 ? 23.124 -14.456 20.373 1.00 25.15 ? 219 LEU A N 1 ATOM 1676 C CA . LEU A 1 196 ? 23.470 -14.069 21.688 1.00 25.47 ? 219 LEU A CA 1 ATOM 1677 C C . LEU A 1 196 ? 23.679 -15.382 22.521 1.00 23.91 ? 219 LEU A C 1 ATOM 1678 O O . LEU A 1 196 ? 22.876 -16.319 22.492 1.00 25.10 ? 219 LEU A O 1 ATOM 1679 C CB . LEU A 1 196 ? 22.364 -13.119 22.194 1.00 28.60 ? 219 LEU A CB 1 ATOM 1680 C CG . LEU A 1 196 ? 22.450 -12.303 23.453 1.00 31.63 ? 219 LEU A CG 1 ATOM 1681 C CD1 . LEU A 1 196 ? 23.574 -11.271 23.437 1.00 27.05 ? 219 LEU A CD1 1 ATOM 1682 C CD2 . LEU A 1 196 ? 21.008 -11.733 23.674 1.00 25.22 ? 219 LEU A CD2 1 ATOM 1683 N N . SER A 1 197 ? 24.784 -15.429 23.223 1.00 23.43 ? 220 SER A N 1 ATOM 1684 C CA . SER A 1 197 ? 25.325 -16.654 23.803 1.00 23.37 ? 220 SER A CA 1 ATOM 1685 C C . SER A 1 197 ? 25.939 -16.563 25.206 1.00 22.59 ? 220 SER A C 1 ATOM 1686 O O . SER A 1 197 ? 25.767 -17.492 26.001 1.00 22.46 ? 220 SER A O 1 ATOM 1687 C CB . SER A 1 197 ? 26.399 -17.160 22.868 1.00 25.02 ? 220 SER A CB 1 ATOM 1688 O OG . SER A 1 197 ? 26.942 -18.341 23.365 1.00 29.83 ? 220 SER A OG 1 ATOM 1689 N N . GLN A 1 198 ? 26.692 -15.511 25.493 1.00 22.77 ? 221 GLN A N 1 ATOM 1690 C CA . GLN A 1 198 ? 27.450 -15.430 26.773 1.00 21.98 ? 221 GLN A CA 1 ATOM 1691 C C . GLN A 1 198 ? 27.377 -13.992 27.287 1.00 22.22 ? 221 GLN A C 1 ATOM 1692 O O . GLN A 1 198 ? 27.362 -13.064 26.468 1.00 22.93 ? 221 GLN A O 1 ATOM 1693 C CB . GLN A 1 198 ? 28.896 -15.797 26.527 1.00 22.56 ? 221 GLN A CB 1 ATOM 1694 C CG . GLN A 1 198 ? 29.092 -17.262 26.177 1.00 23.59 ? 221 GLN A CG 1 ATOM 1695 C CD . GLN A 1 198 ? 30.466 -17.770 26.337 1.00 26.61 ? 221 GLN A CD 1 ATOM 1696 O OE1 . GLN A 1 198 ? 31.062 -17.608 27.395 1.00 23.84 ? 221 GLN A OE1 1 ATOM 1697 N NE2 . GLN A 1 198 ? 30.987 -18.475 25.270 1.00 26.07 ? 221 GLN A NE2 1 ATOM 1698 N N . LEU A 1 199 ? 27.422 -13.847 28.600 1.00 20.40 ? 222 LEU A N 1 ATOM 1699 C CA . LEU A 1 199 ? 27.540 -12.555 29.294 1.00 20.75 ? 222 LEU A CA 1 ATOM 1700 C C . LEU A 1 199 ? 28.562 -12.648 30.398 1.00 21.93 ? 222 LEU A C 1 ATOM 1701 O O . LEU A 1 199 ? 28.629 -13.686 31.131 1.00 19.97 ? 222 LEU A O 1 ATOM 1702 C CB . LEU A 1 199 ? 26.203 -12.081 29.867 1.00 19.94 ? 222 LEU A CB 1 ATOM 1703 C CG . LEU A 1 199 ? 25.014 -11.934 28.921 1.00 21.24 ? 222 LEU A CG 1 ATOM 1704 C CD1 . LEU A 1 199 ? 23.738 -11.714 29.756 1.00 21.77 ? 222 LEU A CD1 1 ATOM 1705 C CD2 . LEU A 1 199 ? 25.285 -10.713 27.941 1.00 20.82 ? 222 LEU A CD2 1 ATOM 1706 N N . TYR A 1 200 ? 29.431 -11.620 30.504 1.00 22.98 ? 223 TYR A N 1 ATOM 1707 C CA . TYR A 1 200 ? 30.310 -11.481 31.700 1.00 22.66 ? 223 TYR A CA 1 ATOM 1708 C C . TYR A 1 200 ? 30.014 -10.177 32.404 1.00 23.90 ? 223 TYR A C 1 ATOM 1709 O O . TYR A 1 200 ? 30.182 -9.052 31.837 1.00 25.30 ? 223 TYR A O 1 ATOM 1710 C CB . TYR A 1 200 ? 31.797 -11.483 31.413 1.00 22.01 ? 223 TYR A CB 1 ATOM 1711 C CG . TYR A 1 200 ? 32.385 -12.419 30.429 1.00 20.84 ? 223 TYR A CG 1 ATOM 1712 C CD1 . TYR A 1 200 ? 31.792 -13.653 30.073 1.00 21.19 ? 223 TYR A CD1 1 ATOM 1713 C CD2 . TYR A 1 200 ? 33.644 -12.081 29.838 1.00 22.51 ? 223 TYR A CD2 1 ATOM 1714 C CE1 . TYR A 1 200 ? 32.400 -14.494 29.210 1.00 21.59 ? 223 TYR A CE1 1 ATOM 1715 C CE2 . TYR A 1 200 ? 34.262 -12.931 28.945 1.00 25.55 ? 223 TYR A CE2 1 ATOM 1716 C CZ . TYR A 1 200 ? 33.641 -14.133 28.631 1.00 24.22 ? 223 TYR A CZ 1 ATOM 1717 O OH . TYR A 1 200 ? 34.252 -14.980 27.745 1.00 25.33 ? 223 TYR A OH 1 ATOM 1718 N N . TYR A 1 201 ? 29.489 -10.303 33.622 1.00 23.13 ? 224 TYR A N 1 ATOM 1719 C CA . TYR A 1 201 ? 29.304 -9.125 34.474 1.00 22.40 ? 224 TYR A CA 1 ATOM 1720 C C . TYR A 1 201 ? 30.475 -8.907 35.386 1.00 22.75 ? 224 TYR A C 1 ATOM 1721 O O . TYR A 1 201 ? 30.711 -9.711 36.266 1.00 22.33 ? 224 TYR A O 1 ATOM 1722 C CB . TYR A 1 201 ? 28.034 -9.199 35.302 1.00 22.14 ? 224 TYR A CB 1 ATOM 1723 C CG . TYR A 1 201 ? 26.709 -9.259 34.548 1.00 23.19 ? 224 TYR A CG 1 ATOM 1724 C CD1 . TYR A 1 201 ? 25.986 -8.108 34.269 1.00 20.89 ? 224 TYR A CD1 1 ATOM 1725 C CD2 . TYR A 1 201 ? 26.168 -10.468 34.144 1.00 21.59 ? 224 TYR A CD2 1 ATOM 1726 C CE1 . TYR A 1 201 ? 24.761 -8.163 33.671 1.00 24.20 ? 224 TYR A CE1 1 ATOM 1727 C CE2 . TYR A 1 201 ? 24.983 -10.514 33.488 1.00 23.72 ? 224 TYR A CE2 1 ATOM 1728 C CZ . TYR A 1 201 ? 24.287 -9.367 33.251 1.00 21.68 ? 224 TYR A CZ 1 ATOM 1729 O OH . TYR A 1 201 ? 23.108 -9.413 32.608 1.00 26.07 ? 224 TYR A OH 1 ATOM 1730 N N . TYR A 1 202 ? 31.123 -7.727 35.278 1.00 24.21 ? 225 TYR A N 1 ATOM 1731 C CA . TYR A 1 202 ? 32.367 -7.463 36.033 1.00 24.22 ? 225 TYR A CA 1 ATOM 1732 C C . TYR A 1 202 ? 32.062 -6.739 37.329 1.00 25.34 ? 225 TYR A C 1 ATOM 1733 O O . TYR A 1 202 ? 31.197 -5.796 37.405 1.00 26.30 ? 225 TYR A O 1 ATOM 1734 C CB . TYR A 1 202 ? 33.402 -6.654 35.232 1.00 25.94 ? 225 TYR A CB 1 ATOM 1735 C CG . TYR A 1 202 ? 33.974 -7.321 33.978 1.00 25.71 ? 225 TYR A CG 1 ATOM 1736 C CD1 . TYR A 1 202 ? 35.287 -7.689 33.897 1.00 27.49 ? 225 TYR A CD1 1 ATOM 1737 C CD2 . TYR A 1 202 ? 33.173 -7.546 32.861 1.00 30.23 ? 225 TYR A CD2 1 ATOM 1738 C CE1 . TYR A 1 202 ? 35.807 -8.328 32.763 1.00 26.64 ? 225 TYR A CE1 1 ATOM 1739 C CE2 . TYR A 1 202 ? 33.679 -8.145 31.716 1.00 26.29 ? 225 TYR A CE2 1 ATOM 1740 C CZ . TYR A 1 202 ? 34.993 -8.504 31.668 1.00 27.77 ? 225 TYR A CZ 1 ATOM 1741 O OH . TYR A 1 202 ? 35.496 -9.115 30.536 1.00 26.41 ? 225 TYR A OH 1 ATOM 1742 N N . PHE A 1 203 ? 32.812 -7.110 38.362 1.00 24.88 ? 226 PHE A N 1 ATOM 1743 C CA . PHE A 1 203 ? 32.726 -6.476 39.681 1.00 24.52 ? 226 PHE A CA 1 ATOM 1744 C C . PHE A 1 203 ? 34.092 -6.278 40.287 1.00 23.77 ? 226 PHE A C 1 ATOM 1745 O O . PHE A 1 203 ? 35.085 -7.005 40.022 1.00 23.68 ? 226 PHE A O 1 ATOM 1746 C CB . PHE A 1 203 ? 31.991 -7.416 40.638 1.00 24.65 ? 226 PHE A CB 1 ATOM 1747 C CG . PHE A 1 203 ? 30.565 -7.662 40.320 1.00 24.19 ? 226 PHE A CG 1 ATOM 1748 C CD1 . PHE A 1 203 ? 29.585 -6.810 40.800 1.00 22.76 ? 226 PHE A CD1 1 ATOM 1749 C CD2 . PHE A 1 203 ? 30.205 -8.698 39.491 1.00 22.51 ? 226 PHE A CD2 1 ATOM 1750 C CE1 . PHE A 1 203 ? 28.284 -7.054 40.530 1.00 22.35 ? 226 PHE A CE1 1 ATOM 1751 C CE2 . PHE A 1 203 ? 28.899 -8.943 39.199 1.00 24.21 ? 226 PHE A CE2 1 ATOM 1752 C CZ . PHE A 1 203 ? 27.927 -8.100 39.721 1.00 24.90 ? 226 PHE A CZ 1 ATOM 1753 N N . ASN A 1 204 ? 34.154 -5.291 41.133 1.00 24.88 ? 227 ASN A N 1 ATOM 1754 C CA . ASN A 1 204 ? 35.224 -5.212 42.123 1.00 24.61 ? 227 ASN A CA 1 ATOM 1755 C C . ASN A 1 204 ? 34.555 -5.480 43.483 1.00 24.21 ? 227 ASN A C 1 ATOM 1756 O O . ASN A 1 204 ? 33.302 -5.438 43.607 1.00 25.79 ? 227 ASN A O 1 ATOM 1757 C CB . ASN A 1 204 ? 35.900 -3.876 42.068 1.00 27.29 ? 227 ASN A CB 1 ATOM 1758 C CG . ASN A 1 204 ? 36.617 -3.610 40.714 1.00 29.23 ? 227 ASN A CG 1 ATOM 1759 O OD1 . ASN A 1 204 ? 37.201 -4.494 40.063 1.00 30.89 ? 227 ASN A OD1 1 ATOM 1760 N ND2 . ASN A 1 204 ? 36.530 -2.407 40.300 1.00 25.94 ? 227 ASN A ND2 1 ATOM 1761 N N . VAL A 1 205 ? 35.386 -5.790 44.475 1.00 24.50 ? 228 VAL A N 1 ATOM 1762 C CA . VAL A 1 205 ? 34.964 -6.440 45.778 1.00 23.70 ? 228 VAL A CA 1 ATOM 1763 C C . VAL A 1 205 ? 35.607 -5.674 46.948 1.00 24.54 ? 228 VAL A C 1 ATOM 1764 O O . VAL A 1 205 ? 36.786 -5.407 46.977 1.00 24.57 ? 228 VAL A O 1 ATOM 1765 C CB . VAL A 1 205 ? 35.279 -7.940 45.892 1.00 21.67 ? 228 VAL A CB 1 ATOM 1766 C CG1 . VAL A 1 205 ? 34.775 -8.502 47.206 1.00 21.43 ? 228 VAL A CG1 1 ATOM 1767 C CG2 . VAL A 1 205 ? 34.548 -8.745 44.712 1.00 21.33 ? 228 VAL A CG2 1 ATOM 1768 N N . LYS A 1 206 ? 34.732 -5.317 47.881 1.00 26.55 ? 229 LYS A N 1 ATOM 1769 C CA . LYS A 1 206 ? 35.107 -4.811 49.186 1.00 27.84 ? 229 LYS A CA 1 ATOM 1770 C C . LYS A 1 206 ? 35.057 -6.015 50.144 1.00 25.72 ? 229 LYS A C 1 ATOM 1771 O O . LYS A 1 206 ? 33.984 -6.534 50.429 1.00 25.93 ? 229 LYS A O 1 ATOM 1772 C CB . LYS A 1 206 ? 34.103 -3.764 49.617 1.00 28.71 ? 229 LYS A CB 1 ATOM 1773 C CG . LYS A 1 206 ? 34.087 -2.476 48.693 1.00 34.09 ? 229 LYS A CG 1 ATOM 1774 C CD . LYS A 1 206 ? 32.964 -1.431 49.022 1.00 40.41 ? 229 LYS A CD 1 ATOM 1775 C CE . LYS A 1 206 ? 33.334 -0.478 50.152 1.00 45.87 ? 229 LYS A CE 1 ATOM 1776 N NZ . LYS A 1 206 ? 34.513 0.439 49.948 1.00 49.75 ? 229 LYS A NZ 1 ATOM 1777 N N . GLY A 1 207 ? 36.207 -6.397 50.676 1.00 25.49 ? 230 GLY A N 1 ATOM 1778 C CA . GLY A 1 207 ? 36.310 -7.505 51.572 1.00 25.06 ? 230 GLY A CA 1 ATOM 1779 C C . GLY A 1 207 ? 36.543 -8.856 50.874 1.00 25.46 ? 230 GLY A C 1 ATOM 1780 O O . GLY A 1 207 ? 37.296 -8.956 49.900 1.00 25.51 ? 230 GLY A O 1 ATOM 1781 N N . SER A 1 208 ? 35.954 -9.910 51.425 1.00 23.93 ? 231 SER A N 1 ATOM 1782 C CA . SER A 1 208 ? 36.211 -11.247 50.926 1.00 23.86 ? 231 SER A CA 1 ATOM 1783 C C . SER A 1 208 ? 35.329 -11.541 49.717 1.00 22.21 ? 231 SER A C 1 ATOM 1784 O O . SER A 1 208 ? 34.220 -10.977 49.617 1.00 23.03 ? 231 SER A O 1 ATOM 1785 C CB . SER A 1 208 ? 35.872 -12.346 51.993 1.00 24.69 ? 231 SER A CB 1 ATOM 1786 O OG . SER A 1 208 ? 36.146 -13.643 51.436 1.00 24.31 ? 231 SER A OG 1 ATOM 1787 N N . ALA A 1 209 ? 35.836 -12.358 48.815 1.00 22.90 ? 232 ALA A N 1 ATOM 1788 C CA . ALA A 1 209 ? 34.977 -12.844 47.687 1.00 22.84 ? 232 ALA A CA 1 ATOM 1789 C C . ALA A 1 209 ? 33.793 -13.618 48.235 1.00 23.15 ? 232 ALA A C 1 ATOM 1790 O O . ALA A 1 209 ? 32.761 -13.730 47.547 1.00 24.93 ? 232 ALA A O 1 ATOM 1791 C CB . ALA A 1 209 ? 35.729 -13.679 46.676 1.00 22.51 ? 232 ALA A CB 1 ATOM 1792 N N . ILE A 1 210 ? 33.893 -14.247 49.408 1.00 23.46 ? 233 ILE A N 1 ATOM 1793 C CA . ILE A 1 210 ? 32.671 -14.836 50.053 1.00 25.07 ? 233 ILE A CA 1 ATOM 1794 C C . ILE A 1 210 ? 32.103 -13.853 51.050 1.00 25.41 ? 233 ILE A C 1 ATOM 1795 O O . ILE A 1 210 ? 32.692 -13.589 52.123 1.00 24.52 ? 233 ILE A O 1 ATOM 1796 C CB . ILE A 1 210 ? 32.936 -16.199 50.816 1.00 26.61 ? 233 ILE A CB 1 ATOM 1797 C CG1 . ILE A 1 210 ? 33.788 -17.115 49.964 1.00 32.76 ? 233 ILE A CG1 1 ATOM 1798 C CG2 . ILE A 1 210 ? 31.624 -16.751 51.423 1.00 27.89 ? 233 ILE A CG2 1 ATOM 1799 C CD1 . ILE A 1 210 ? 33.154 -17.838 48.857 1.00 26.16 ? 233 ILE A CD1 1 ATOM 1800 N N . GLY A 1 211 ? 30.942 -13.331 50.757 1.00 25.29 ? 234 GLY A N 1 ATOM 1801 C CA . GLY A 1 211 ? 30.321 -12.423 51.685 1.00 26.93 ? 234 GLY A CA 1 ATOM 1802 C C . GLY A 1 211 ? 30.675 -10.971 51.581 1.00 28.03 ? 234 GLY A C 1 ATOM 1803 O O . GLY A 1 211 ? 30.056 -10.169 52.279 1.00 29.04 ? 234 GLY A O 1 ATOM 1804 N N . GLY A 1 212 ? 31.681 -10.595 50.767 1.00 26.52 ? 235 GLY A N 1 ATOM 1805 C CA . GLY A 1 212 ? 31.971 -9.186 50.634 1.00 26.50 ? 235 GLY A CA 1 ATOM 1806 C C . GLY A 1 212 ? 31.017 -8.443 49.721 1.00 26.78 ? 235 GLY A C 1 ATOM 1807 O O . GLY A 1 212 ? 30.068 -8.978 49.207 1.00 28.06 ? 235 GLY A O 1 ATOM 1808 N N . THR A 1 213 ? 31.232 -7.138 49.574 1.00 27.46 ? 236 THR A N 1 ATOM 1809 C CA . THR A 1 213 ? 30.348 -6.313 48.738 1.00 29.05 ? 236 THR A CA 1 ATOM 1810 C C . THR A 1 213 ? 30.865 -6.268 47.348 1.00 28.35 ? 236 THR A C 1 ATOM 1811 O O . THR A 1 213 ? 32.040 -5.853 47.069 1.00 28.65 ? 236 THR A O 1 ATOM 1812 C CB . THR A 1 213 ? 30.252 -4.857 49.292 1.00 31.40 ? 236 THR A CB 1 ATOM 1813 O OG1 . THR A 1 213 ? 29.836 -4.945 50.638 1.00 29.89 ? 236 THR A OG1 1 ATOM 1814 C CG2 . THR A 1 213 ? 29.275 -3.988 48.470 1.00 33.25 ? 236 THR A CG2 1 ATOM 1815 N N . TYR A 1 214 ? 30.012 -6.741 46.448 1.00 28.11 ? 237 TYR A N 1 ATOM 1816 C CA . TYR A 1 214 ? 30.342 -6.799 45.036 1.00 27.13 ? 237 TYR A CA 1 ATOM 1817 C C . TYR A 1 214 ? 29.839 -5.520 44.391 1.00 28.63 ? 237 TYR A C 1 ATOM 1818 O O . TYR A 1 214 ? 28.615 -5.298 44.372 1.00 31.34 ? 237 TYR A O 1 ATOM 1819 C CB . TYR A 1 214 ? 29.735 -8.017 44.353 1.00 26.84 ? 237 TYR A CB 1 ATOM 1820 C CG . TYR A 1 214 ? 30.545 -9.271 44.541 1.00 25.56 ? 237 TYR A CG 1 ATOM 1821 C CD1 . TYR A 1 214 ? 30.627 -9.910 45.804 1.00 24.59 ? 237 TYR A CD1 1 ATOM 1822 C CD2 . TYR A 1 214 ? 31.229 -9.824 43.493 1.00 23.42 ? 237 TYR A CD2 1 ATOM 1823 C CE1 . TYR A 1 214 ? 31.314 -11.047 45.959 1.00 23.91 ? 237 TYR A CE1 1 ATOM 1824 C CE2 . TYR A 1 214 ? 31.969 -10.983 43.674 1.00 24.75 ? 237 TYR A CE2 1 ATOM 1825 C CZ . TYR A 1 214 ? 31.999 -11.572 44.904 1.00 23.87 ? 237 TYR A CZ 1 ATOM 1826 O OH . TYR A 1 214 ? 32.719 -12.720 45.036 1.00 21.83 ? 237 TYR A OH 1 ATOM 1827 N N . VAL A 1 215 ? 30.767 -4.719 43.863 1.00 28.09 ? 238 VAL A N 1 ATOM 1828 C CA . VAL A 1 215 ? 30.493 -3.384 43.252 1.00 27.77 ? 238 VAL A CA 1 ATOM 1829 C C . VAL A 1 215 ? 30.610 -3.491 41.751 1.00 28.37 ? 238 VAL A C 1 ATOM 1830 O O . VAL A 1 215 ? 31.685 -3.841 41.245 1.00 26.76 ? 238 VAL A O 1 ATOM 1831 C CB . VAL A 1 215 ? 31.436 -2.308 43.873 1.00 28.72 ? 238 VAL A CB 1 ATOM 1832 C CG1 . VAL A 1 215 ? 31.275 -0.851 43.207 1.00 28.77 ? 238 VAL A CG1 1 ATOM 1833 C CG2 . VAL A 1 215 ? 31.166 -2.234 45.360 1.00 28.27 ? 238 VAL A CG2 1 ATOM 1834 N N . ALA A 1 216 ? 29.512 -3.182 41.032 1.00 29.16 ? 239 ALA A N 1 ATOM 1835 C CA . ALA A 1 216 ? 29.457 -3.280 39.592 1.00 29.59 ? 239 ALA A CA 1 ATOM 1836 C C . ALA A 1 216 ? 30.581 -2.490 39.012 1.00 30.61 ? 239 ALA A C 1 ATOM 1837 O O . ALA A 1 216 ? 30.857 -1.381 39.457 1.00 31.47 ? 239 ALA A O 1 ATOM 1838 C CB . ALA A 1 216 ? 28.074 -2.848 39.052 1.00 29.78 ? 239 ALA A CB 1 ATOM 1839 N N . SER A 1 217 ? 31.371 -3.091 38.129 1.00 29.36 ? 240 SER A N 1 ATOM 1840 C CA . SER A 1 217 ? 32.492 -2.353 37.521 1.00 30.38 ? 240 SER A CA 1 ATOM 1841 C C . SER A 1 217 ? 32.572 -2.453 36.009 1.00 30.72 ? 240 SER A C 1 ATOM 1842 O O . SER A 1 217 ? 31.839 -3.200 35.336 1.00 27.75 ? 240 SER A O 1 ATOM 1843 C CB . SER A 1 217 ? 33.836 -2.819 38.120 1.00 32.17 ? 240 SER A CB 1 ATOM 1844 O OG . SER A 1 217 ? 34.046 -4.178 37.842 1.00 28.27 ? 240 SER A OG 1 ATOM 1845 N N . GLU A 1 218 ? 33.477 -1.673 35.460 1.00 31.45 ? 241 GLU A N 1 ATOM 1846 C CA . GLU A 1 218 ? 33.587 -1.602 34.012 1.00 34.09 ? 241 GLU A CA 1 ATOM 1847 C C . GLU A 1 218 ? 34.123 -2.915 33.370 1.00 31.59 ? 241 GLU A C 1 ATOM 1848 O O . GLU A 1 218 ? 35.107 -3.534 33.819 1.00 32.20 ? 241 GLU A O 1 ATOM 1849 C CB . GLU A 1 218 ? 34.482 -0.418 33.602 1.00 34.49 ? 241 GLU A CB 1 ATOM 1850 C CG . GLU A 1 218 ? 34.206 -0.003 32.188 1.00 41.02 ? 241 GLU A CG 1 ATOM 1851 C CD . GLU A 1 218 ? 34.886 1.294 31.844 1.00 51.23 ? 241 GLU A CD 1 ATOM 1852 O OE1 . GLU A 1 218 ? 34.743 2.267 32.638 1.00 58.28 ? 241 GLU A OE1 1 ATOM 1853 O OE2 . GLU A 1 218 ? 35.524 1.351 30.764 1.00 57.65 ? 241 GLU A OE2 1 ATOM 1854 N N . ARG A 1 219 ? 33.479 -3.339 32.285 1.00 31.43 ? 242 ARG A N 1 ATOM 1855 C CA . ARG A 1 219 ? 33.974 -4.496 31.559 1.00 29.18 ? 242 ARG A CA 1 ATOM 1856 C C . ARG A 1 219 ? 35.386 -4.331 31.016 1.00 31.01 ? 242 ARG A C 1 ATOM 1857 O O . ARG A 1 219 ? 35.791 -3.240 30.488 1.00 30.69 ? 242 ARG A O 1 ATOM 1858 C CB . ARG A 1 219 ? 32.995 -4.884 30.444 1.00 29.48 ? 242 ARG A CB 1 ATOM 1859 C CG . ARG A 1 219 ? 32.909 -3.821 29.266 1.00 28.69 ? 242 ARG A CG 1 ATOM 1860 C CD . ARG A 1 219 ? 31.691 -4.172 28.424 1.00 34.47 ? 242 ARG A CD 1 ATOM 1861 N NE . ARG A 1 219 ? 31.518 -3.142 27.389 1.00 36.95 ? 242 ARG A NE 1 ATOM 1862 C CZ . ARG A 1 219 ? 30.574 -3.165 26.460 1.00 44.08 ? 242 ARG A CZ 1 ATOM 1863 N NH1 . ARG A 1 219 ? 29.736 -4.229 26.358 1.00 42.20 ? 242 ARG A NH1 1 ATOM 1864 N NH2 . ARG A 1 219 ? 30.522 -2.139 25.565 1.00 41.99 ? 242 ARG A NH2 1 ATOM 1865 N N . LEU A 1 220 ? 36.174 -5.389 31.117 1.00 31.41 ? 243 LEU A N 1 ATOM 1866 C CA . LEU A 1 220 ? 37.549 -5.364 30.598 1.00 34.22 ? 243 LEU A CA 1 ATOM 1867 C C . LEU A 1 220 ? 37.660 -5.961 29.151 1.00 37.87 ? 243 LEU A C 1 ATOM 1868 O O . LEU A 1 220 ? 38.770 -5.996 28.568 1.00 38.46 ? 243 LEU A O 1 ATOM 1869 C CB . LEU A 1 220 ? 38.483 -6.113 31.562 1.00 34.73 ? 243 LEU A CB 1 ATOM 1870 C CG . LEU A 1 220 ? 38.468 -5.694 33.078 1.00 35.35 ? 243 LEU A CG 1 ATOM 1871 C CD1 . LEU A 1 220 ? 39.407 -6.630 33.954 1.00 35.03 ? 243 LEU A CD1 1 ATOM 1872 C CD2 . LEU A 1 220 ? 38.807 -4.240 33.223 1.00 36.20 ? 243 LEU A CD2 1 ATOM 1873 N N . GLU A 1 221 ? 36.534 -6.429 28.612 1.00 36.87 ? 244 GLU A N 1 ATOM 1874 C CA . GLU A 1 221 ? 36.426 -6.935 27.230 1.00 38.69 ? 244 GLU A CA 1 ATOM 1875 C C . GLU A 1 221 ? 35.032 -6.480 26.790 1.00 37.60 ? 244 GLU A C 1 ATOM 1876 O O . GLU A 1 221 ? 34.140 -6.506 27.594 1.00 37.40 ? 244 GLU A O 1 ATOM 1877 C CB . GLU A 1 221 ? 36.659 -8.464 27.276 1.00 38.32 ? 244 GLU A CB 1 ATOM 1878 C CG . GLU A 1 221 ? 37.162 -9.042 25.994 1.00 46.93 ? 244 GLU A CG 1 ATOM 1879 C CD . GLU A 1 221 ? 36.987 -10.580 25.828 1.00 51.29 ? 244 GLU A CD 1 ATOM 1880 O OE1 . GLU A 1 221 ? 36.977 -11.329 26.842 1.00 52.08 ? 244 GLU A OE1 1 ATOM 1881 O OE2 . GLU A 1 221 ? 36.849 -11.016 24.637 1.00 53.86 ? 244 GLU A OE2 1 ATOM 1882 N N A ASP A 1 222 ? 34.824 -5.987 25.549 0.60 39.98 ? 245 ASP A N 1 ATOM 1883 N N B ASP A 1 222 ? 34.848 -6.063 25.535 0.40 39.15 ? 245 ASP A N 1 ATOM 1884 C CA A ASP A 1 222 ? 33.500 -5.360 25.199 0.60 39.89 ? 245 ASP A CA 1 ATOM 1885 C CA B ASP A 1 222 ? 33.608 -5.368 25.137 0.40 38.90 ? 245 ASP A CA 1 ATOM 1886 C C A ASP A 1 222 ? 32.441 -6.335 24.610 0.60 38.79 ? 245 ASP A C 1 ATOM 1887 C C B ASP A 1 222 ? 32.480 -6.278 24.594 0.40 37.96 ? 245 ASP A C 1 ATOM 1888 O O A ASP A 1 222 ? 31.323 -6.578 25.194 0.60 39.20 ? 245 ASP A O 1 ATOM 1889 O O B ASP A 1 222 ? 31.369 -6.420 25.195 0.40 38.62 ? 245 ASP A O 1 ATOM 1890 C CB A ASP A 1 222 ? 33.662 -4.138 24.234 0.60 42.41 ? 245 ASP A CB 1 ATOM 1891 C CB B ASP A 1 222 ? 33.985 -4.300 24.099 0.40 40.90 ? 245 ASP A CB 1 ATOM 1892 C CG A ASP A 1 222 ? 34.283 -2.894 24.912 0.60 44.54 ? 245 ASP A CG 1 ATOM 1893 C CG B ASP A 1 222 ? 35.207 -4.697 23.303 0.40 40.71 ? 245 ASP A CG 1 ATOM 1894 O OD1 A ASP A 1 222 ? 34.405 -2.861 26.165 0.60 45.97 ? 245 ASP A OD1 1 ATOM 1895 O OD1 B ASP A 1 222 ? 35.052 -5.531 22.390 0.40 40.22 ? 245 ASP A OD1 1 ATOM 1896 O OD2 A ASP A 1 222 ? 34.613 -1.945 24.163 0.60 45.55 ? 245 ASP A OD2 1 ATOM 1897 O OD2 B ASP A 1 222 ? 36.312 -4.203 23.611 0.40 43.38 ? 245 ASP A OD2 1 ATOM 1898 N N . SER A 1 223 ? 32.763 -6.883 23.457 1.00 35.73 ? 246 SER A N 1 ATOM 1899 C CA . SER A 1 223 ? 31.836 -7.745 22.813 1.00 32.00 ? 246 SER A CA 1 ATOM 1900 C C . SER A 1 223 ? 32.502 -8.284 21.602 1.00 32.52 ? 246 SER A C 1 ATOM 1901 O O . SER A 1 223 ? 33.275 -7.538 20.918 1.00 31.24 ? 246 SER A O 1 ATOM 1902 C CB . SER A 1 223 ? 30.560 -6.998 22.396 1.00 32.02 ? 246 SER A CB 1 ATOM 1903 O OG . SER A 1 223 ? 29.665 -7.902 21.775 1.00 27.66 ? 246 SER A OG 1 ATOM 1904 N N . ASN A 1 224 ? 32.113 -9.475 21.202 1.00 30.89 ? 247 ASN A N 1 ATOM 1905 C CA . ASN A 1 224 ? 32.522 -9.959 19.882 1.00 32.18 ? 247 ASN A CA 1 ATOM 1906 C C . ASN A 1 224 ? 31.336 -10.057 18.953 1.00 31.95 ? 247 ASN A C 1 ATOM 1907 O O . ASN A 1 224 ? 31.413 -10.767 17.933 1.00 31.49 ? 247 ASN A O 1 ATOM 1908 C CB . ASN A 1 224 ? 33.202 -11.357 20.015 1.00 31.76 ? 247 ASN A CB 1 ATOM 1909 C CG . ASN A 1 224 ? 32.171 -12.459 20.445 1.00 32.92 ? 247 ASN A CG 1 ATOM 1910 O OD1 . ASN A 1 224 ? 31.066 -12.136 20.807 1.00 28.47 ? 247 ASN A OD1 1 ATOM 1911 N ND2 . ASN A 1 224 ? 32.572 -13.702 20.438 1.00 27.53 ? 247 ASN A ND2 1 ATOM 1912 N N . CYS A 1 225 ? 30.208 -9.415 19.283 1.00 30.54 ? 248 CYS A N 1 ATOM 1913 C CA . CYS A 1 225 ? 29.068 -9.425 18.417 1.00 30.83 ? 248 CYS A CA 1 ATOM 1914 C C . CYS A 1 225 ? 29.175 -8.291 17.334 1.00 32.76 ? 248 CYS A C 1 ATOM 1915 O O . CYS A 1 225 ? 29.890 -7.278 17.542 1.00 33.92 ? 248 CYS A O 1 ATOM 1916 C CB . CYS A 1 225 ? 27.789 -9.146 19.176 1.00 30.14 ? 248 CYS A CB 1 ATOM 1917 S SG . CYS A 1 225 ? 27.460 -10.349 20.540 1.00 28.93 ? 248 CYS A SG 1 ATOM 1918 N N . LYS A 1 226 ? 28.427 -8.475 16.254 1.00 35.45 ? 249 LYS A N 1 ATOM 1919 C CA . LYS A 1 226 ? 28.168 -7.366 15.285 1.00 38.96 ? 249 LYS A CA 1 ATOM 1920 C C . LYS A 1 226 ? 27.220 -6.396 15.939 1.00 39.18 ? 249 LYS A C 1 ATOM 1921 O O . LYS A 1 226 ? 26.523 -6.725 16.925 1.00 36.18 ? 249 LYS A O 1 ATOM 1922 C CB . LYS A 1 226 ? 27.510 -7.836 13.979 1.00 41.05 ? 249 LYS A CB 1 ATOM 1923 C CG . LYS A 1 226 ? 28.214 -8.983 13.195 1.00 47.31 ? 249 LYS A CG 1 ATOM 1924 C CD . LYS A 1 226 ? 29.745 -8.820 13.160 1.00 56.35 ? 249 LYS A CD 1 ATOM 1925 C CE . LYS A 1 226 ? 30.351 -9.780 12.079 1.00 62.30 ? 249 LYS A CE 1 ATOM 1926 N NZ . LYS A 1 226 ? 31.286 -9.058 11.139 1.00 65.30 ? 249 LYS A NZ 1 ATOM 1927 N N . ASP A 1 227 ? 27.132 -5.193 15.340 1.00 38.39 ? 250 ASP A N 1 ATOM 1928 C CA . ASP A 1 227 ? 26.439 -4.116 15.953 1.00 37.87 ? 250 ASP A CA 1 ATOM 1929 C C . ASP A 1 227 ? 24.977 -4.306 15.861 1.00 34.70 ? 250 ASP A C 1 ATOM 1930 O O . ASP A 1 227 ? 24.230 -3.694 16.657 1.00 37.41 ? 250 ASP A O 1 ATOM 1931 C CB . ASP A 1 227 ? 26.863 -2.765 15.298 1.00 42.09 ? 250 ASP A CB 1 ATOM 1932 C CG . ASP A 1 227 ? 28.228 -2.388 15.680 1.00 46.23 ? 250 ASP A CG 1 ATOM 1933 O OD1 . ASP A 1 227 ? 28.581 -2.633 16.859 1.00 53.96 ? 250 ASP A OD1 1 ATOM 1934 O OD2 . ASP A 1 227 ? 28.967 -1.860 14.825 1.00 58.00 ? 250 ASP A OD2 1 ATOM 1935 N N . SER A 1 228 ? 24.539 -5.115 14.914 1.00 33.25 ? 251 SER A N 1 ATOM 1936 C CA . SER A 1 228 ? 23.148 -5.311 14.679 1.00 32.93 ? 251 SER A CA 1 ATOM 1937 C C . SER A 1 228 ? 23.002 -6.681 14.014 1.00 32.41 ? 251 SER A C 1 ATOM 1938 O O . SER A 1 228 ? 23.992 -7.309 13.681 1.00 35.32 ? 251 SER A O 1 ATOM 1939 C CB . SER A 1 228 ? 22.611 -4.156 13.764 1.00 36.55 ? 251 SER A CB 1 ATOM 1940 O OG . SER A 1 228 ? 23.170 -4.292 12.476 1.00 38.50 ? 251 SER A OG 1 ATOM 1941 N N . GLY A 1 229 ? 21.769 -7.144 13.852 1.00 31.14 ? 252 GLY A N 1 ATOM 1942 C CA . GLY A 1 229 ? 21.482 -8.404 13.224 1.00 31.78 ? 252 GLY A CA 1 ATOM 1943 C C . GLY A 1 229 ? 21.574 -9.568 14.221 1.00 29.84 ? 252 GLY A C 1 ATOM 1944 O O . GLY A 1 229 ? 21.474 -10.702 13.823 1.00 30.68 ? 252 GLY A O 1 ATOM 1945 N N . ILE A 1 230 ? 21.685 -9.252 15.503 1.00 29.35 ? 253 ILE A N 1 ATOM 1946 C CA . ILE A 1 230 ? 21.938 -10.312 16.555 1.00 29.33 ? 253 ILE A CA 1 ATOM 1947 C C . ILE A 1 230 ? 20.685 -11.126 16.807 1.00 28.55 ? 253 ILE A C 1 ATOM 1948 O O . ILE A 1 230 ? 19.602 -10.603 17.035 1.00 29.87 ? 253 ILE A O 1 ATOM 1949 C CB . ILE A 1 230 ? 22.456 -9.684 17.856 1.00 28.89 ? 253 ILE A CB 1 ATOM 1950 C CG1 . ILE A 1 230 ? 23.806 -9.045 17.650 1.00 26.21 ? 253 ILE A CG1 1 ATOM 1951 C CG2 . ILE A 1 230 ? 22.621 -10.773 18.967 1.00 28.92 ? 253 ILE A CG2 1 ATOM 1952 C CD1 . ILE A 1 230 ? 24.263 -8.039 18.824 1.00 24.48 ? 253 ILE A CD1 1 ATOM 1953 N N . LYS A 1 231 ? 20.811 -12.444 16.726 1.00 28.76 ? 254 LYS A N 1 ATOM 1954 C CA . LYS A 1 231 ? 19.717 -13.332 16.993 1.00 29.22 ? 254 LYS A CA 1 ATOM 1955 C C . LYS A 1 231 ? 19.675 -13.744 18.471 1.00 27.59 ? 254 LYS A C 1 ATOM 1956 O O . LYS A 1 231 ? 20.709 -13.854 19.069 1.00 26.57 ? 254 LYS A O 1 ATOM 1957 C CB . LYS A 1 231 ? 19.893 -14.638 16.188 1.00 29.95 ? 254 LYS A CB 1 ATOM 1958 C CG . LYS A 1 231 ? 19.985 -14.446 14.700 1.00 35.55 ? 254 LYS A CG 1 ATOM 1959 C CD . LYS A 1 231 ? 19.929 -15.752 13.896 1.00 44.78 ? 254 LYS A CD 1 ATOM 1960 C CE . LYS A 1 231 ? 21.206 -16.630 14.056 1.00 47.65 ? 254 LYS A CE 1 ATOM 1961 N NZ . LYS A 1 231 ? 20.844 -18.137 13.707 1.00 50.14 ? 254 LYS A NZ 1 ATOM 1962 N N . TYR A 1 232 ? 18.490 -13.948 19.015 1.00 27.62 ? 255 TYR A N 1 ATOM 1963 C CA . TYR A 1 232 ? 18.280 -14.354 20.392 1.00 27.68 ? 255 TYR A CA 1 ATOM 1964 C C . TYR A 1 232 ? 17.434 -15.596 20.277 1.00 26.80 ? 255 TYR A C 1 ATOM 1965 O O . TYR A 1 232 ? 16.184 -15.504 20.259 1.00 27.15 ? 255 TYR A O 1 ATOM 1966 C CB . TYR A 1 232 ? 17.589 -13.245 21.144 1.00 28.98 ? 255 TYR A CB 1 ATOM 1967 C CG . TYR A 1 232 ? 17.441 -13.351 22.662 1.00 23.70 ? 255 TYR A CG 1 ATOM 1968 C CD1 . TYR A 1 232 ? 18.040 -14.409 23.442 1.00 26.83 ? 255 TYR A CD1 1 ATOM 1969 C CD2 . TYR A 1 232 ? 16.821 -12.352 23.335 1.00 26.23 ? 255 TYR A CD2 1 ATOM 1970 C CE1 . TYR A 1 232 ? 17.915 -14.378 24.821 1.00 25.29 ? 255 TYR A CE1 1 ATOM 1971 C CE2 . TYR A 1 232 ? 16.677 -12.332 24.667 1.00 27.08 ? 255 TYR A CE2 1 ATOM 1972 C CZ . TYR A 1 232 ? 17.250 -13.353 25.432 1.00 25.88 ? 255 TYR A CZ 1 ATOM 1973 O OH . TYR A 1 232 ? 17.032 -13.353 26.780 1.00 22.45 ? 255 TYR A OH 1 ATOM 1974 N N . PRO A 1 233 ? 18.085 -16.744 20.034 1.00 23.97 ? 256 PRO A N 1 ATOM 1975 C CA . PRO A 1 233 ? 17.244 -17.901 19.626 1.00 25.48 ? 256 PRO A CA 1 ATOM 1976 C C . PRO A 1 233 ? 16.360 -18.482 20.741 1.00 26.00 ? 256 PRO A C 1 ATOM 1977 O O . PRO A 1 233 ? 16.817 -18.556 21.906 1.00 26.16 ? 256 PRO A O 1 ATOM 1978 C CB . PRO A 1 233 ? 18.268 -18.924 19.105 1.00 25.72 ? 256 PRO A CB 1 ATOM 1979 C CG . PRO A 1 233 ? 19.568 -18.163 18.903 1.00 25.08 ? 256 PRO A CG 1 ATOM 1980 C CD . PRO A 1 233 ? 19.529 -16.995 19.820 1.00 24.86 ? 256 PRO A CD 1 ATOM 1981 N N . PRO A 1 234 ? 15.081 -18.823 20.437 1.00 26.96 ? 257 PRO A N 1 ATOM 1982 C CA . PRO A 1 234 ? 14.248 -19.355 21.478 1.00 27.03 ? 257 PRO A CA 1 ATOM 1983 C C . PRO A 1 234 ? 14.757 -20.732 21.928 1.00 25.20 ? 257 PRO A C 1 ATOM 1984 O O . PRO A 1 234 ? 15.270 -21.468 21.121 1.00 25.06 ? 257 PRO A O 1 ATOM 1985 C CB . PRO A 1 234 ? 12.852 -19.537 20.808 1.00 29.22 ? 257 PRO A CB 1 ATOM 1986 C CG . PRO A 1 234 ? 12.820 -18.523 19.705 1.00 29.18 ? 257 PRO A CG 1 ATOM 1987 C CD . PRO A 1 234 ? 14.291 -18.524 19.214 1.00 26.98 ? 257 PRO A CD 1 ATOM 1988 N N . LYS A 1 235 ? 14.721 -20.980 23.226 1.00 24.38 ? 258 LYS A N 1 ATOM 1989 C CA . LYS A 1 235 ? 15.050 -22.317 23.724 1.00 21.90 ? 258 LYS A CA 1 ATOM 1990 C C . LYS A 1 235 ? 13.932 -23.318 23.375 1.00 22.11 ? 258 LYS A C 1 ATOM 1991 O O . LYS A 1 235 ? 12.785 -22.904 23.335 1.00 25.15 ? 258 LYS A O 1 ATOM 1992 C CB . LYS A 1 235 ? 15.335 -22.289 25.206 1.00 20.44 ? 258 LYS A CB 1 ATOM 1993 C CG . LYS A 1 235 ? 16.554 -21.522 25.640 1.00 19.05 ? 258 LYS A CG 1 ATOM 1994 C CD . LYS A 1 235 ? 16.773 -21.658 27.143 1.00 19.07 ? 258 LYS A CD 1 ATOM 1995 C CE . LYS A 1 235 ? 18.105 -21.184 27.649 1.00 20.42 ? 258 LYS A CE 1 ATOM 1996 N NZ . LYS A 1 235 ? 18.323 -21.307 29.101 1.00 16.82 ? 258 LYS A NZ 1 ATOM 1997 N N . TYR A 1 236 ? 14.291 -24.599 23.205 1.00 23.63 ? 259 TYR A N 1 ATOM 1998 C CA . TYR A 1 236 ? 13.333 -25.696 22.999 1.00 25.99 ? 259 TYR A CA 1 ATOM 1999 C C . TYR A 1 236 ? 12.430 -25.404 21.792 1.00 30.40 ? 259 TYR A C 1 ATOM 2000 O O . TYR A 1 236 ? 11.229 -25.650 21.832 1.00 27.13 ? 259 TYR A O 1 ATOM 2001 C CB . TYR A 1 236 ? 12.448 -25.876 24.291 1.00 25.03 ? 259 TYR A CB 1 ATOM 2002 C CG . TYR A 1 236 ? 13.320 -26.064 25.550 1.00 22.31 ? 259 TYR A CG 1 ATOM 2003 C CD1 . TYR A 1 236 ? 14.142 -27.170 25.715 1.00 20.84 ? 259 TYR A CD1 1 ATOM 2004 C CD2 . TYR A 1 236 ? 13.311 -25.098 26.556 1.00 21.75 ? 259 TYR A CD2 1 ATOM 2005 C CE1 . TYR A 1 236 ? 14.955 -27.282 26.834 1.00 19.46 ? 259 TYR A CE1 1 ATOM 2006 C CE2 . TYR A 1 236 ? 14.106 -25.208 27.683 1.00 18.59 ? 259 TYR A CE2 1 ATOM 2007 C CZ . TYR A 1 236 ? 14.930 -26.302 27.824 1.00 16.22 ? 259 TYR A CZ 1 ATOM 2008 O OH . TYR A 1 236 ? 15.750 -26.453 28.924 1.00 19.91 ? 259 TYR A OH 1 ATOM 2009 N N A SER A 1 237 ? 13.009 -24.853 20.736 0.50 32.95 ? 260 SER A N 1 ATOM 2010 N N B SER A 1 237 ? 13.011 -24.837 20.753 0.50 33.03 ? 260 SER A N 1 ATOM 2011 C CA A SER A 1 237 ? 12.181 -24.154 19.739 0.50 37.45 ? 260 SER A CA 1 ATOM 2012 C CA B SER A 1 237 ? 12.222 -24.178 19.708 0.50 37.66 ? 260 SER A CA 1 ATOM 2013 C C A SER A 1 237 ? 11.289 -25.017 18.856 0.50 42.26 ? 260 SER A C 1 ATOM 2014 C C B SER A 1 237 ? 11.269 -25.085 18.953 0.50 42.26 ? 260 SER A C 1 ATOM 2015 O O A SER A 1 237 ? 10.097 -24.671 18.631 0.50 44.95 ? 260 SER A O 1 ATOM 2016 O O B SER A 1 237 ? 10.032 -24.848 18.914 0.50 45.10 ? 260 SER A O 1 ATOM 2017 C CB A SER A 1 237 ? 13.037 -23.328 18.810 0.50 37.06 ? 260 SER A CB 1 ATOM 2018 C CB B SER A 1 237 ? 13.172 -23.702 18.666 0.50 37.12 ? 260 SER A CB 1 ATOM 2019 O OG A SER A 1 237 ? 12.363 -23.203 17.575 0.50 35.02 ? 260 SER A OG 1 ATOM 2020 O OG B SER A 1 237 ? 13.782 -24.869 18.178 0.50 35.93 ? 260 SER A OG 1 HETATM 2021 C C1 . NAG B 2 . ? 36.677 -35.259 47.809 1.00 22.50 ? 301 NAG A C1 1 HETATM 2022 C C2 . NAG B 2 . ? 36.412 -35.841 49.219 1.00 21.71 ? 301 NAG A C2 1 HETATM 2023 C C3 . NAG B 2 . ? 37.492 -35.377 50.224 1.00 26.44 ? 301 NAG A C3 1 HETATM 2024 C C4 . NAG B 2 . ? 38.819 -35.692 49.667 1.00 25.16 ? 301 NAG A C4 1 HETATM 2025 C C5 . NAG B 2 . ? 39.037 -35.088 48.248 1.00 27.33 ? 301 NAG A C5 1 HETATM 2026 C C6 . NAG B 2 . ? 40.374 -35.230 47.542 1.00 31.39 ? 301 NAG A C6 1 HETATM 2027 C C7 . NAG B 2 . ? 34.077 -36.215 49.827 1.00 21.86 ? 301 NAG A C7 1 HETATM 2028 C C8 . NAG B 2 . ? 32.842 -35.816 50.550 1.00 24.28 ? 301 NAG A C8 1 HETATM 2029 N N2 . NAG B 2 . ? 35.156 -35.450 49.827 1.00 21.29 ? 301 NAG A N2 1 HETATM 2030 O O3 . NAG B 2 . ? 37.233 -36.050 51.451 1.00 26.42 ? 301 NAG A O3 1 HETATM 2031 O O4 . NAG B 2 . ? 39.698 -35.098 50.569 1.00 33.23 ? 301 NAG A O4 1 HETATM 2032 O O5 . NAG B 2 . ? 37.990 -35.587 47.400 1.00 26.44 ? 301 NAG A O5 1 HETATM 2033 O O6 . NAG B 2 . ? 40.685 -36.594 47.594 1.00 35.47 ? 301 NAG A O6 1 HETATM 2034 O O7 . NAG B 2 . ? 34.063 -37.288 49.279 1.00 32.63 ? 301 NAG A O7 1 HETATM 2035 C C1 . NAG C 2 . ? 40.757 -36.019 50.947 1.00 36.92 ? 302 NAG A C1 1 HETATM 2036 C C2 . NAG C 2 . ? 41.813 -35.315 51.742 1.00 37.73 ? 302 NAG A C2 1 HETATM 2037 C C3 . NAG C 2 . ? 42.813 -36.352 52.336 1.00 48.62 ? 302 NAG A C3 1 HETATM 2038 C C4 . NAG C 2 . ? 42.076 -37.482 53.035 1.00 49.76 ? 302 NAG A C4 1 HETATM 2039 C C5 . NAG C 2 . ? 41.237 -38.077 51.915 1.00 49.06 ? 302 NAG A C5 1 HETATM 2040 C C6 . NAG C 2 . ? 40.579 -39.445 52.167 1.00 48.71 ? 302 NAG A C6 1 HETATM 2041 C C7 . NAG C 2 . ? 42.295 -33.030 51.182 1.00 34.24 ? 302 NAG A C7 1 HETATM 2042 C C8 . NAG C 2 . ? 43.034 -32.093 50.317 1.00 39.02 ? 302 NAG A C8 1 HETATM 2043 N N2 . NAG C 2 . ? 42.472 -34.348 50.913 1.00 37.07 ? 302 NAG A N2 1 HETATM 2044 O O3 . NAG C 2 . ? 43.576 -35.713 53.305 1.00 50.80 ? 302 NAG A O3 1 HETATM 2045 O O4 . NAG C 2 . ? 42.950 -38.387 53.682 1.00 57.03 ? 302 NAG A O4 1 HETATM 2046 O O5 . NAG C 2 . ? 40.256 -37.038 51.780 1.00 40.08 ? 302 NAG A O5 1 HETATM 2047 O O6 . NAG C 2 . ? 39.726 -39.248 53.265 1.00 51.50 ? 302 NAG A O6 1 HETATM 2048 O O7 . NAG C 2 . ? 41.527 -32.624 52.085 1.00 34.58 ? 302 NAG A O7 1 HETATM 2049 C C1 . NAG D 2 . ? 26.026 -32.246 57.677 0.60 32.87 ? 303 NAG A C1 1 HETATM 2050 C C2 . NAG D 2 . ? 27.059 -31.513 58.553 0.60 32.61 ? 303 NAG A C2 1 HETATM 2051 C C3 . NAG D 2 . ? 27.873 -32.567 59.311 0.60 33.40 ? 303 NAG A C3 1 HETATM 2052 C C4 . NAG D 2 . ? 26.966 -33.535 60.087 0.60 36.62 ? 303 NAG A C4 1 HETATM 2053 C C5 . NAG D 2 . ? 25.966 -34.124 59.084 0.60 35.24 ? 303 NAG A C5 1 HETATM 2054 C C6 . NAG D 2 . ? 25.056 -35.158 59.754 0.60 36.36 ? 303 NAG A C6 1 HETATM 2055 C C7 . NAG D 2 . ? 27.685 -29.275 57.663 0.60 29.31 ? 303 NAG A C7 1 HETATM 2056 C C8 . NAG D 2 . ? 28.719 -28.488 56.955 0.60 21.51 ? 303 NAG A C8 1 HETATM 2057 N N2 . NAG D 2 . ? 27.945 -30.559 57.845 0.60 30.06 ? 303 NAG A N2 1 HETATM 2058 O O3 . NAG D 2 . ? 28.722 -31.885 60.177 0.60 33.51 ? 303 NAG A O3 1 HETATM 2059 O O4 . NAG D 2 . ? 27.731 -34.564 60.698 0.60 38.59 ? 303 NAG A O4 1 HETATM 2060 O O5 . NAG D 2 . ? 25.199 -33.036 58.554 0.60 28.90 ? 303 NAG A O5 1 HETATM 2061 O O6 . NAG D 2 . ? 24.120 -34.387 60.468 0.60 36.15 ? 303 NAG A O6 1 HETATM 2062 O O7 . NAG D 2 . ? 26.636 -28.731 57.936 0.60 30.30 ? 303 NAG A O7 1 HETATM 2063 P P . PO4 E 3 . ? 36.102 -21.121 31.449 1.00 22.84 ? 304 PO4 A P 1 HETATM 2064 O O1 . PO4 E 3 . ? 37.388 -20.329 31.653 1.00 22.52 ? 304 PO4 A O1 1 HETATM 2065 O O2 . PO4 E 3 . ? 35.294 -20.320 30.379 1.00 23.93 ? 304 PO4 A O2 1 HETATM 2066 O O3 . PO4 E 3 . ? 35.221 -21.212 32.725 1.00 22.38 ? 304 PO4 A O3 1 HETATM 2067 O O4 . PO4 E 3 . ? 36.468 -22.513 31.022 1.00 19.62 ? 304 PO4 A O4 1 HETATM 2068 P P . PO4 F 3 . ? 19.962 -22.010 46.962 0.50 39.13 ? 305 PO4 A P 1 HETATM 2069 O O1 . PO4 F 3 . ? 20.656 -22.834 46.021 0.50 36.40 ? 305 PO4 A O1 1 HETATM 2070 O O2 . PO4 F 3 . ? 18.776 -21.678 46.087 0.50 19.55 ? 305 PO4 A O2 1 HETATM 2071 O O3 . PO4 F 3 . ? 19.776 -22.987 48.055 0.50 37.38 ? 305 PO4 A O3 1 HETATM 2072 O O4 . PO4 F 3 . ? 20.699 -20.803 47.569 0.50 21.62 ? 305 PO4 A O4 1 HETATM 2073 C C1 . EDO G 4 . ? 17.812 -29.283 32.410 1.00 30.85 ? 306 EDO A C1 1 HETATM 2074 O O1 . EDO G 4 . ? 18.341 -28.818 31.151 1.00 32.01 ? 306 EDO A O1 1 HETATM 2075 C C2 . EDO G 4 . ? 18.550 -28.574 33.497 1.00 28.78 ? 306 EDO A C2 1 HETATM 2076 O O2 . EDO G 4 . ? 18.577 -27.141 33.418 1.00 27.31 ? 306 EDO A O2 1 HETATM 2077 C C1 . EDO H 4 . ? 25.950 -24.404 23.634 1.00 48.94 ? 307 EDO A C1 1 HETATM 2078 O O1 . EDO H 4 . ? 24.609 -24.863 23.776 1.00 49.24 ? 307 EDO A O1 1 HETATM 2079 C C2 . EDO H 4 . ? 26.840 -25.541 23.105 1.00 47.74 ? 307 EDO A C2 1 HETATM 2080 O O2 . EDO H 4 . ? 26.441 -25.820 21.745 1.00 49.32 ? 307 EDO A O2 1 HETATM 2081 C C1 . EDO I 4 . ? 29.030 -18.861 55.318 1.00 46.12 ? 308 EDO A C1 1 HETATM 2082 O O1 . EDO I 4 . ? 28.813 -20.128 56.034 1.00 53.84 ? 308 EDO A O1 1 HETATM 2083 C C2 . EDO I 4 . ? 30.526 -18.390 55.295 1.00 42.35 ? 308 EDO A C2 1 HETATM 2084 O O2 . EDO I 4 . ? 31.707 -19.334 55.401 1.00 26.52 ? 308 EDO A O2 1 HETATM 2085 O O . HOH J 5 . ? 18.102 -14.819 33.170 1.00 10.68 ? 401 HOH A O 1 HETATM 2086 O O . HOH J 5 . ? 30.523 -22.418 55.288 1.00 13.95 ? 402 HOH A O 1 HETATM 2087 O O . HOH J 5 . ? 32.013 -15.014 23.997 1.00 20.29 ? 403 HOH A O 1 HETATM 2088 O O . HOH J 5 . ? 29.925 -17.192 29.725 1.00 17.02 ? 404 HOH A O 1 HETATM 2089 O O . HOH J 5 . ? 22.040 -25.753 50.217 1.00 16.93 ? 405 HOH A O 1 HETATM 2090 O O . HOH J 5 . ? 40.656 -20.476 46.285 1.00 16.79 ? 406 HOH A O 1 HETATM 2091 O O . HOH J 5 . ? 21.108 -21.432 29.160 1.00 12.82 ? 407 HOH A O 1 HETATM 2092 O O . HOH J 5 . ? 40.105 -27.405 50.030 1.00 14.35 ? 408 HOH A O 1 HETATM 2093 O O . HOH J 5 . ? 24.981 -5.763 39.535 1.00 20.56 ? 409 HOH A O 1 HETATM 2094 O O . HOH J 5 . ? 38.255 -18.133 30.916 1.00 32.73 ? 410 HOH A O 1 HETATM 2095 O O . HOH J 5 . ? 38.451 -3.477 37.453 1.00 28.96 ? 411 HOH A O 1 HETATM 2096 O O . HOH J 5 . ? 21.453 -6.479 39.803 1.00 29.41 ? 412 HOH A O 1 HETATM 2097 O O . HOH J 5 . ? 43.232 -30.058 36.521 1.00 46.15 ? 413 HOH A O 1 HETATM 2098 O O . HOH J 5 . ? 27.915 -37.704 37.105 1.00 31.61 ? 414 HOH A O 1 HETATM 2099 O O . HOH J 5 . ? 15.537 -3.636 33.845 1.00 36.75 ? 415 HOH A O 1 HETATM 2100 O O . HOH J 5 . ? 11.062 -20.995 24.053 1.00 30.71 ? 416 HOH A O 1 HETATM 2101 O O . HOH J 5 . ? 44.387 -28.993 50.299 1.00 30.63 ? 417 HOH A O 1 HETATM 2102 O O . HOH J 5 . ? 8.929 -7.849 26.383 1.00 33.00 ? 418 HOH A O 1 HETATM 2103 O O . HOH J 5 . ? 10.277 -15.601 23.378 1.00 44.04 ? 419 HOH A O 1 HETATM 2104 O O . HOH J 5 . ? 33.396 -17.915 62.057 1.00 38.78 ? 420 HOH A O 1 HETATM 2105 O O . HOH J 5 . ? 32.698 -22.231 27.321 1.00 46.41 ? 421 HOH A O 1 HETATM 2106 O O . HOH J 5 . ? 46.173 -3.694 36.342 1.00 45.18 ? 422 HOH A O 1 HETATM 2107 O O . HOH J 5 . ? 30.481 -3.140 22.382 1.00 34.70 ? 423 HOH A O 1 HETATM 2108 O O . HOH J 5 . ? 13.593 -6.370 17.281 1.00 45.64 ? 424 HOH A O 1 HETATM 2109 O O . HOH J 5 . ? 25.774 -37.040 26.367 1.00 47.46 ? 425 HOH A O 1 HETATM 2110 O O . HOH J 5 . ? 24.872 -26.932 54.711 1.00 37.63 ? 426 HOH A O 1 HETATM 2111 O O . HOH J 5 . ? 44.449 -13.123 28.827 1.00 37.73 ? 427 HOH A O 1 HETATM 2112 O O . HOH J 5 . ? 34.466 -37.357 38.549 1.00 39.68 ? 428 HOH A O 1 HETATM 2113 O O . HOH J 5 . ? 46.936 -24.743 49.536 1.00 39.13 ? 429 HOH A O 1 HETATM 2114 O O . HOH J 5 . ? 9.599 -8.351 23.903 1.00 48.76 ? 430 HOH A O 1 HETATM 2115 O O . HOH J 5 . ? 27.611 -38.651 45.416 1.00 42.99 ? 431 HOH A O 1 HETATM 2116 O O . HOH J 5 . ? 15.037 -24.198 15.256 1.00 47.33 ? 432 HOH A O 1 HETATM 2117 O O . HOH J 5 . ? 19.943 -5.829 10.749 1.00 35.50 ? 433 HOH A O 1 HETATM 2118 O O . HOH J 5 . ? 23.941 -33.620 38.490 1.00 39.74 ? 434 HOH A O 1 HETATM 2119 O O . HOH J 5 . ? 32.229 -32.171 54.886 1.00 33.62 ? 435 HOH A O 1 HETATM 2120 O O . HOH J 5 . ? 30.507 -36.445 26.997 1.00 55.69 ? 436 HOH A O 1 HETATM 2121 O O . HOH J 5 . ? 47.054 -2.789 51.937 1.00 25.94 ? 437 HOH A O 1 HETATM 2122 O O . HOH J 5 . ? 9.753 -12.643 21.417 1.00 33.62 ? 438 HOH A O 1 HETATM 2123 O O . HOH J 5 . ? 31.939 -39.200 49.803 0.50 24.50 ? 439 HOH A O 1 HETATM 2124 O O . HOH J 5 . ? 37.497 -38.813 51.166 1.00 52.53 ? 440 HOH A O 1 HETATM 2125 O O . HOH J 5 . ? 25.301 -7.427 10.765 0.50 30.72 ? 441 HOH A O 1 HETATM 2126 O O . HOH J 5 . ? 11.201 -17.081 25.777 1.00 31.58 ? 442 HOH A O 1 HETATM 2127 O O . HOH J 5 . ? 27.352 -8.307 51.418 1.00 44.13 ? 443 HOH A O 1 HETATM 2128 O O . HOH J 5 . ? 7.587 -26.167 20.032 1.00 44.42 ? 444 HOH A O 1 HETATM 2129 O O . HOH J 5 . ? 44.264 -25.551 40.452 1.00 23.90 ? 445 HOH A O 1 HETATM 2130 O O . HOH J 5 . ? 9.311 -23.233 25.145 1.00 38.42 ? 446 HOH A O 1 HETATM 2131 O O . HOH J 5 . ? 25.896 -35.559 55.644 1.00 49.18 ? 447 HOH A O 1 HETATM 2132 O O . HOH J 5 . ? 23.544 -35.557 42.306 1.00 43.76 ? 448 HOH A O 1 HETATM 2133 O O . HOH J 5 . ? 13.041 -0.891 30.379 1.00 45.27 ? 449 HOH A O 1 HETATM 2134 O O . HOH J 5 . ? 54.976 -5.237 48.814 1.00 42.28 ? 450 HOH A O 1 HETATM 2135 O O . HOH J 5 . ? 10.915 -8.817 19.303 1.00 39.71 ? 451 HOH A O 1 HETATM 2136 O O . HOH J 5 . ? 8.704 -22.781 27.958 1.00 40.34 ? 452 HOH A O 1 HETATM 2137 O O . HOH J 5 . ? 15.863 -1.958 23.943 1.00 29.64 ? 453 HOH A O 1 HETATM 2138 O O A HOH J 5 . ? 37.396 -6.215 23.891 0.60 33.60 ? 454 HOH A O 1 HETATM 2139 O O B HOH J 5 . ? 39.131 -5.964 24.321 0.40 25.10 ? 454 HOH A O 1 HETATM 2140 O O . HOH J 5 . ? 13.823 -10.382 37.962 1.00 41.36 ? 455 HOH A O 1 HETATM 2141 O O . HOH J 5 . ? 40.992 -4.941 53.291 1.00 18.46 ? 456 HOH A O 1 HETATM 2142 O O . HOH J 5 . ? 45.955 -3.075 44.503 1.00 23.69 ? 457 HOH A O 1 HETATM 2143 O O . HOH J 5 . ? 33.871 -20.361 38.093 1.00 14.66 ? 458 HOH A O 1 HETATM 2144 O O . HOH J 5 . ? 23.468 -23.166 22.116 1.00 19.15 ? 459 HOH A O 1 HETATM 2145 O O . HOH J 5 . ? 45.345 1.393 41.986 1.00 44.81 ? 460 HOH A O 1 HETATM 2146 O O . HOH J 5 . ? 37.808 -9.844 30.572 1.00 28.21 ? 461 HOH A O 1 HETATM 2147 O O . HOH J 5 . ? 43.814 -35.553 49.048 1.00 53.06 ? 462 HOH A O 1 HETATM 2148 O O . HOH J 5 . ? 8.963 -11.641 28.534 1.00 36.45 ? 463 HOH A O 1 HETATM 2149 O O . HOH J 5 . ? 36.976 -38.403 43.771 1.00 37.16 ? 464 HOH A O 1 HETATM 2150 O O . HOH J 5 . ? 15.722 -19.807 15.805 1.00 56.38 ? 465 HOH A O 1 HETATM 2151 O O . HOH J 5 . ? 31.591 -3.225 58.746 1.00 39.41 ? 466 HOH A O 1 HETATM 2152 O O . HOH J 5 . ? 35.362 -12.731 22.788 1.00 41.28 ? 467 HOH A O 1 HETATM 2153 O O . HOH J 5 . ? 21.848 -5.985 42.424 1.00 39.15 ? 468 HOH A O 1 HETATM 2154 O O . HOH J 5 . ? 38.162 -5.505 57.846 1.00 20.23 ? 469 HOH A O 1 HETATM 2155 O O . HOH J 5 . ? 22.562 -32.894 24.859 1.00 27.87 ? 470 HOH A O 1 HETATM 2156 O O . HOH J 5 . ? 17.214 -29.819 50.467 1.00 24.87 ? 471 HOH A O 1 HETATM 2157 O O . HOH J 5 . ? 19.066 -30.084 20.259 1.00 33.11 ? 472 HOH A O 1 HETATM 2158 O O . HOH J 5 . ? 38.465 -13.793 31.961 0.50 33.28 ? 473 HOH A O 1 HETATM 2159 O O . HOH J 5 . ? 22.348 -33.420 53.938 1.00 48.31 ? 474 HOH A O 1 HETATM 2160 O O . HOH J 5 . ? 10.069 -23.526 14.720 1.00 48.49 ? 475 HOH A O 1 HETATM 2161 O O . HOH J 5 . ? 44.403 -39.199 55.131 1.00 60.17 ? 476 HOH A O 1 HETATM 2162 O O . HOH J 5 . ? 24.552 2.244 30.001 1.00 39.82 ? 477 HOH A O 1 HETATM 2163 O O . HOH J 5 . ? 15.996 -4.349 16.710 1.00 40.14 ? 478 HOH A O 1 HETATM 2164 O O . HOH J 5 . ? 33.007 -21.336 64.543 0.50 19.01 ? 479 HOH A O 1 HETATM 2165 O O . HOH J 5 . ? 39.209 -37.773 44.942 1.00 47.52 ? 480 HOH A O 1 HETATM 2166 O O . HOH J 5 . ? 29.725 -38.225 31.530 1.00 38.57 ? 481 HOH A O 1 HETATM 2167 O O . HOH J 5 . ? 44.328 3.403 46.936 1.00 36.96 ? 482 HOH A O 1 HETATM 2168 O O . HOH J 5 . ? 16.397 -16.692 46.504 1.00 44.06 ? 483 HOH A O 1 HETATM 2169 O O . HOH J 5 . ? 48.595 -20.247 37.941 1.00 43.58 ? 484 HOH A O 1 HETATM 2170 O O . HOH J 5 . ? 37.926 -17.782 28.658 1.00 41.88 ? 485 HOH A O 1 HETATM 2171 O O . HOH J 5 . ? 32.615 -5.610 52.961 1.00 39.36 ? 486 HOH A O 1 HETATM 2172 O O . HOH J 5 . ? 19.734 -14.819 37.159 1.00 14.88 ? 487 HOH A O 1 HETATM 2173 O O . HOH J 5 . ? 16.849 -16.348 36.302 1.00 34.79 ? 488 HOH A O 1 HETATM 2174 O O . HOH J 5 . ? 14.912 -21.888 16.339 1.00 48.95 ? 489 HOH A O 1 HETATM 2175 O O . HOH J 5 . ? 34.947 -38.532 46.869 1.00 32.85 ? 490 HOH A O 1 HETATM 2176 O O . HOH J 5 . ? 36.934 1.579 48.061 1.00 32.14 ? 491 HOH A O 1 HETATM 2177 O O . HOH J 5 . ? 18.146 -15.971 38.157 1.00 37.29 ? 492 HOH A O 1 HETATM 2178 O O . HOH J 5 . ? 39.498 -35.435 37.050 1.00 53.72 ? 493 HOH A O 1 HETATM 2179 O O . HOH J 5 . ? 13.881 -3.812 21.104 1.00 36.14 ? 494 HOH A O 1 HETATM 2180 O O . HOH J 5 . ? 41.250 -33.410 39.289 1.00 40.91 ? 495 HOH A O 1 HETATM 2181 O O . HOH J 5 . ? 28.607 -13.876 15.918 1.00 34.10 ? 496 HOH A O 1 HETATM 2182 O O . HOH J 5 . ? 32.616 -37.179 41.369 1.00 30.88 ? 497 HOH A O 1 HETATM 2183 O O . HOH J 5 . ? 44.162 -18.378 45.180 1.00 33.97 ? 498 HOH A O 1 HETATM 2184 O O . HOH J 5 . ? 9.472 -13.969 27.760 1.00 38.56 ? 499 HOH A O 1 HETATM 2185 O O . HOH J 5 . ? 20.639 -27.348 52.025 0.50 22.36 ? 500 HOH A O 1 HETATM 2186 O O . HOH J 5 . ? 30.310 -4.592 17.195 1.00 32.76 ? 501 HOH A O 1 HETATM 2187 O O . HOH J 5 . ? 39.985 -12.265 56.956 0.50 20.54 ? 502 HOH A O 1 HETATM 2188 O O . HOH J 5 . ? 45.457 -16.794 48.732 0.50 18.45 ? 503 HOH A O 1 HETATM 2189 O O . HOH J 5 . ? 45.617 -22.317 50.333 1.00 38.88 ? 504 HOH A O 1 HETATM 2190 O O . HOH J 5 . ? 36.219 -13.666 26.250 1.00 44.03 ? 505 HOH A O 1 HETATM 2191 O O . HOH J 5 . ? 36.019 -19.386 28.212 1.00 40.03 ? 506 HOH A O 1 HETATM 2192 O O . HOH J 5 . ? 21.019 1.639 22.586 1.00 33.04 ? 507 HOH A O 1 HETATM 2193 O O . HOH J 5 . ? 47.983 -19.059 35.508 1.00 38.28 ? 508 HOH A O 1 HETATM 2194 O O . HOH J 5 . ? 50.342 -2.568 47.805 1.00 44.11 ? 509 HOH A O 1 HETATM 2195 O O . HOH J 5 . ? 37.591 -2.823 26.398 1.00 47.43 ? 510 HOH A O 1 HETATM 2196 O O . HOH J 5 . ? 35.986 -8.822 22.162 1.00 39.57 ? 511 HOH A O 1 HETATM 2197 O O . HOH J 5 . ? 18.638 1.439 25.068 1.00 30.60 ? 512 HOH A O 1 HETATM 2198 O O . HOH J 5 . ? 36.368 -16.233 60.582 0.50 30.58 ? 513 HOH A O 1 HETATM 2199 O O . HOH J 5 . ? 26.938 0.397 25.557 1.00 38.29 ? 514 HOH A O 1 HETATM 2200 O O . HOH J 5 . ? 42.507 -15.460 58.513 1.00 37.97 ? 515 HOH A O 1 HETATM 2201 O O . HOH J 5 . ? 49.069 -9.290 44.806 1.00 37.11 ? 516 HOH A O 1 HETATM 2202 O O . HOH J 5 . ? 29.650 -38.218 38.734 1.00 37.75 ? 517 HOH A O 1 HETATM 2203 O O . HOH J 5 . ? 49.375 -11.436 38.174 1.00 39.22 ? 518 HOH A O 1 HETATM 2204 O O . HOH J 5 . ? 33.607 -31.465 27.026 1.00 48.40 ? 519 HOH A O 1 HETATM 2205 O O . HOH J 5 . ? 39.278 -0.397 34.044 1.00 39.89 ? 520 HOH A O 1 HETATM 2206 O O . HOH J 5 . ? 32.064 -21.475 62.303 1.00 41.83 ? 521 HOH A O 1 HETATM 2207 O O . HOH J 5 . ? 49.073 -24.314 40.224 1.00 44.54 ? 522 HOH A O 1 HETATM 2208 O O . HOH J 5 . ? 48.314 -26.669 39.010 0.50 43.21 ? 523 HOH A O 1 HETATM 2209 O O . HOH J 5 . ? 19.769 -35.758 40.981 1.00 48.15 ? 524 HOH A O 1 HETATM 2210 O O . HOH J 5 . ? 35.413 -13.817 19.649 1.00 44.12 ? 525 HOH A O 1 HETATM 2211 O O . HOH J 5 . ? 26.213 -25.193 29.819 0.50 10.76 ? 526 HOH A O 1 HETATM 2212 O O . HOH J 5 . ? 29.799 -25.535 29.468 0.50 23.03 ? 527 HOH A O 1 HETATM 2213 O O . HOH J 5 . ? 20.760 -17.481 47.706 1.00 25.85 ? 528 HOH A O 1 HETATM 2214 O O . HOH J 5 . ? 24.875 -23.318 32.451 1.00 13.72 ? 529 HOH A O 1 HETATM 2215 O O . HOH J 5 . ? 31.193 -36.386 43.367 1.00 16.47 ? 530 HOH A O 1 HETATM 2216 O O . HOH J 5 . ? 29.305 -25.015 55.999 1.00 19.42 ? 531 HOH A O 1 HETATM 2217 O O . HOH J 5 . ? 34.083 -9.777 53.638 1.00 26.02 ? 532 HOH A O 1 HETATM 2218 O O . HOH J 5 . ? 40.783 -17.265 36.921 1.00 19.60 ? 533 HOH A O 1 HETATM 2219 O O . HOH J 5 . ? 22.274 -30.648 32.320 1.00 20.14 ? 534 HOH A O 1 HETATM 2220 O O . HOH J 5 . ? 15.933 -29.469 46.585 1.00 24.70 ? 535 HOH A O 1 HETATM 2221 O O . HOH J 5 . ? 38.396 -7.409 47.868 1.00 13.94 ? 536 HOH A O 1 HETATM 2222 O O . HOH J 5 . ? 20.386 -14.674 34.452 1.00 14.65 ? 537 HOH A O 1 HETATM 2223 O O . HOH J 5 . ? 34.952 -33.042 51.551 1.00 16.92 ? 538 HOH A O 1 HETATM 2224 O O . HOH J 5 . ? 16.700 -3.538 31.483 1.00 20.59 ? 539 HOH A O 1 HETATM 2225 O O . HOH J 5 . ? 14.872 -11.845 27.318 1.00 16.20 ? 540 HOH A O 1 HETATM 2226 O O . HOH J 5 . ? 18.353 -9.001 38.197 1.00 24.77 ? 541 HOH A O 1 HETATM 2227 O O . HOH J 5 . ? 38.660 -5.293 50.235 1.00 18.51 ? 542 HOH A O 1 HETATM 2228 O O . HOH J 5 . ? 27.041 -34.949 36.858 1.00 18.76 ? 543 HOH A O 1 HETATM 2229 O O . HOH J 5 . ? 31.024 -2.066 31.437 1.00 21.56 ? 544 HOH A O 1 HETATM 2230 O O . HOH J 5 . ? 30.520 -5.083 33.591 1.00 14.57 ? 545 HOH A O 1 HETATM 2231 O O . HOH J 5 . ? 25.029 -20.427 23.429 1.00 22.97 ? 546 HOH A O 1 HETATM 2232 O O . HOH J 5 . ? 21.714 -30.507 35.093 1.00 15.58 ? 547 HOH A O 1 HETATM 2233 O O . HOH J 5 . ? 33.689 -23.325 59.629 1.00 18.41 ? 548 HOH A O 1 HETATM 2234 O O . HOH J 5 . ? 25.968 -34.501 39.857 1.00 24.35 ? 549 HOH A O 1 HETATM 2235 O O . HOH J 5 . ? 28.899 -18.790 50.407 1.00 23.43 ? 550 HOH A O 1 HETATM 2236 O O . HOH J 5 . ? 30.496 -35.366 34.819 1.00 13.65 ? 551 HOH A O 1 HETATM 2237 O O . HOH J 5 . ? 42.787 -5.824 43.289 1.00 19.54 ? 552 HOH A O 1 HETATM 2238 O O . HOH J 5 . ? 29.869 -22.187 16.728 1.00 20.31 ? 553 HOH A O 1 HETATM 2239 O O . HOH J 5 . ? 40.572 -13.089 43.842 1.00 22.13 ? 554 HOH A O 1 HETATM 2240 O O . HOH J 5 . ? 17.438 -3.958 19.426 1.00 21.45 ? 555 HOH A O 1 HETATM 2241 O O . HOH J 5 . ? 43.494 -14.295 37.941 1.00 29.31 ? 556 HOH A O 1 HETATM 2242 O O . HOH J 5 . ? 21.310 -13.128 45.931 1.00 21.70 ? 557 HOH A O 1 HETATM 2243 O O . HOH J 5 . ? 25.423 -23.344 51.044 1.00 25.30 ? 558 HOH A O 1 HETATM 2244 O O . HOH J 5 . ? 45.223 -21.477 53.221 1.00 26.96 ? 559 HOH A O 1 HETATM 2245 O O . HOH J 5 . ? 39.248 -29.921 36.237 1.00 20.57 ? 560 HOH A O 1 HETATM 2246 O O . HOH J 5 . ? 17.942 -1.183 25.573 1.00 22.16 ? 561 HOH A O 1 HETATM 2247 O O . HOH J 5 . ? 40.527 -22.709 60.835 1.00 21.62 ? 562 HOH A O 1 HETATM 2248 O O . HOH J 5 . ? 34.962 0.284 37.062 1.00 20.21 ? 563 HOH A O 1 HETATM 2249 O O . HOH J 5 . ? 16.436 -21.916 18.642 1.00 26.48 ? 564 HOH A O 1 HETATM 2250 O O . HOH J 5 . ? 45.673 -7.478 39.043 1.00 21.13 ? 565 HOH A O 1 HETATM 2251 O O . HOH J 5 . ? 27.660 -16.490 49.695 1.00 29.74 ? 566 HOH A O 1 HETATM 2252 O O . HOH J 5 . ? 13.918 -19.214 36.442 1.00 20.92 ? 567 HOH A O 1 HETATM 2253 O O . HOH J 5 . ? 38.156 -14.032 52.995 1.00 27.34 ? 568 HOH A O 1 HETATM 2254 O O . HOH J 5 . ? 33.663 -17.773 27.753 1.00 24.03 ? 569 HOH A O 1 HETATM 2255 O O . HOH J 5 . ? 27.083 -11.026 15.931 1.00 29.74 ? 570 HOH A O 1 HETATM 2256 O O . HOH J 5 . ? 23.879 -17.575 50.882 1.00 26.89 ? 571 HOH A O 1 HETATM 2257 O O . HOH J 5 . ? 13.417 -19.052 25.006 1.00 15.35 ? 572 HOH A O 1 HETATM 2258 O O . HOH J 5 . ? 43.889 -14.750 40.640 1.00 27.76 ? 573 HOH A O 1 HETATM 2259 O O . HOH J 5 . ? 24.783 -7.683 41.468 1.00 21.41 ? 574 HOH A O 1 HETATM 2260 O O . HOH J 5 . ? 33.476 -31.298 52.860 1.00 32.68 ? 575 HOH A O 1 HETATM 2261 O O . HOH J 5 . ? 39.266 -28.702 33.840 1.00 22.27 ? 576 HOH A O 1 HETATM 2262 O O . HOH J 5 . ? 34.311 -26.755 61.618 1.00 36.02 ? 577 HOH A O 1 HETATM 2263 O O . HOH J 5 . ? 37.756 -22.273 28.627 1.00 19.50 ? 578 HOH A O 1 HETATM 2264 O O . HOH J 5 . ? 11.166 -12.689 33.166 1.00 36.45 ? 579 HOH A O 1 HETATM 2265 O O . HOH J 5 . ? 21.969 -23.154 50.146 1.00 32.72 ? 580 HOH A O 1 HETATM 2266 O O . HOH J 5 . ? 26.968 -2.291 42.202 1.00 30.87 ? 581 HOH A O 1 HETATM 2267 O O . HOH J 5 . ? 40.645 -2.888 36.328 1.00 26.13 ? 582 HOH A O 1 HETATM 2268 O O . HOH J 5 . ? 43.365 -13.336 43.492 1.00 22.22 ? 583 HOH A O 1 HETATM 2269 O O . HOH J 5 . ? 31.866 -29.858 26.577 1.00 29.70 ? 584 HOH A O 1 HETATM 2270 O O . HOH J 5 . ? 28.649 -11.433 48.910 1.00 29.74 ? 585 HOH A O 1 HETATM 2271 O O . HOH J 5 . ? 36.896 2.862 51.864 1.00 36.68 ? 586 HOH A O 1 HETATM 2272 O O . HOH J 5 . ? 42.067 -28.105 51.915 1.00 24.40 ? 587 HOH A O 1 HETATM 2273 O O . HOH J 5 . ? 16.009 -13.417 17.767 1.00 20.97 ? 588 HOH A O 1 HETATM 2274 O O . HOH J 5 . ? 47.983 -18.217 50.720 1.00 37.30 ? 589 HOH A O 1 HETATM 2275 O O . HOH J 5 . ? 19.390 -31.930 35.682 1.00 27.27 ? 590 HOH A O 1 HETATM 2276 O O . HOH J 5 . ? 27.804 -20.444 52.298 1.00 30.58 ? 591 HOH A O 1 HETATM 2277 O O . HOH J 5 . ? 18.991 -5.791 14.159 1.00 27.83 ? 592 HOH A O 1 HETATM 2278 O O . HOH J 5 . ? 29.150 -4.653 13.192 1.00 32.23 ? 593 HOH A O 1 HETATM 2279 O O . HOH J 5 . ? 47.304 -13.132 46.140 1.00 20.53 ? 594 HOH A O 1 HETATM 2280 O O . HOH J 5 . ? 27.424 -7.367 47.250 1.00 24.86 ? 595 HOH A O 1 HETATM 2281 O O . HOH J 5 . ? 30.382 -31.891 56.749 1.00 39.74 ? 596 HOH A O 1 HETATM 2282 O O . HOH J 5 . ? 16.642 -8.428 35.958 1.00 26.33 ? 597 HOH A O 1 HETATM 2283 O O . HOH J 5 . ? 20.413 -35.695 30.695 1.00 36.71 ? 598 HOH A O 1 HETATM 2284 O O . HOH J 5 . ? 20.400 -32.491 45.916 1.00 39.35 ? 599 HOH A O 1 HETATM 2285 O O . HOH J 5 . ? 9.958 -18.577 27.363 1.00 32.65 ? 600 HOH A O 1 HETATM 2286 O O . HOH J 5 . ? 42.308 -22.324 58.545 1.00 31.03 ? 601 HOH A O 1 HETATM 2287 O O . HOH J 5 . ? 19.790 -30.050 53.734 1.00 23.65 ? 602 HOH A O 1 HETATM 2288 O O . HOH J 5 . ? 33.248 -12.477 54.440 1.00 19.83 ? 603 HOH A O 1 HETATM 2289 O O . HOH J 5 . ? 49.668 -25.520 42.207 1.00 30.63 ? 604 HOH A O 1 HETATM 2290 O O . HOH J 5 . ? 43.162 -21.997 29.336 1.00 36.94 ? 605 HOH A O 1 HETATM 2291 O O . HOH J 5 . ? 22.671 -19.195 15.407 1.00 34.18 ? 606 HOH A O 1 HETATM 2292 O O . HOH J 5 . ? 44.897 -12.368 55.550 1.00 16.66 ? 607 HOH A O 1 HETATM 2293 O O . HOH J 5 . ? 36.261 -4.574 36.202 1.00 24.30 ? 608 HOH A O 1 HETATM 2294 O O . HOH J 5 . ? 31.535 -16.016 58.632 1.00 27.35 ? 609 HOH A O 1 HETATM 2295 O O . HOH J 5 . ? 38.231 -34.130 53.297 1.00 19.98 ? 610 HOH A O 1 HETATM 2296 O O . HOH J 5 . ? 29.730 -18.774 22.804 1.00 24.47 ? 611 HOH A O 1 HETATM 2297 O O . HOH J 5 . ? 33.842 -23.420 30.432 0.50 6.28 ? 612 HOH A O 1 HETATM 2298 O O . HOH J 5 . ? 17.406 -17.984 40.123 1.00 28.97 ? 613 HOH A O 1 HETATM 2299 O O . HOH J 5 . ? 46.989 -6.589 36.348 1.00 27.95 ? 614 HOH A O 1 HETATM 2300 O O . HOH J 5 . ? 31.167 -16.427 22.026 1.00 38.09 ? 615 HOH A O 1 HETATM 2301 O O . HOH J 5 . ? 24.513 -37.019 29.288 1.00 32.49 ? 616 HOH A O 1 HETATM 2302 O O . HOH J 5 . ? 38.690 -35.242 44.544 1.00 18.12 ? 617 HOH A O 1 HETATM 2303 O O . HOH J 5 . ? 13.059 -26.266 48.644 1.00 30.51 ? 618 HOH A O 1 HETATM 2304 O O . HOH J 5 . ? 20.519 -30.695 30.513 1.00 30.73 ? 619 HOH A O 1 HETATM 2305 O O . HOH J 5 . ? 39.255 -4.680 55.450 1.00 19.11 ? 620 HOH A O 1 HETATM 2306 O O . HOH J 5 . ? 17.104 -29.540 40.211 1.00 22.97 ? 621 HOH A O 1 HETATM 2307 O O . HOH J 5 . ? 31.442 -24.304 60.255 1.00 28.40 ? 622 HOH A O 1 HETATM 2308 O O . HOH J 5 . ? 46.483 -5.242 40.551 1.00 27.40 ? 623 HOH A O 1 HETATM 2309 O O . HOH J 5 . ? 45.837 -21.291 47.044 1.00 29.29 ? 624 HOH A O 1 HETATM 2310 O O . HOH J 5 . ? 20.700 -29.885 27.711 1.00 28.17 ? 625 HOH A O 1 HETATM 2311 O O . HOH J 5 . ? 29.301 -24.669 58.738 1.00 23.80 ? 626 HOH A O 1 HETATM 2312 O O . HOH J 5 . ? 16.448 -13.904 14.307 1.00 33.00 ? 627 HOH A O 1 HETATM 2313 O O . HOH J 5 . ? 45.520 -5.409 43.169 1.00 22.60 ? 628 HOH A O 1 HETATM 2314 O O . HOH J 5 . ? 9.566 -16.403 17.514 1.00 32.12 ? 629 HOH A O 1 HETATM 2315 O O . HOH J 5 . ? 20.195 -14.976 47.666 1.00 30.67 ? 630 HOH A O 1 HETATM 2316 O O . HOH J 5 . ? 34.222 -15.933 61.023 1.00 31.41 ? 631 HOH A O 1 HETATM 2317 O O . HOH J 5 . ? 34.717 -31.819 55.316 1.00 32.69 ? 632 HOH A O 1 HETATM 2318 O O . HOH J 5 . ? 19.671 -33.250 31.749 1.00 29.98 ? 633 HOH A O 1 HETATM 2319 O O . HOH J 5 . ? 20.888 1.413 30.736 1.00 30.09 ? 634 HOH A O 1 HETATM 2320 O O . HOH J 5 . ? 27.317 -23.641 27.044 1.00 32.24 ? 635 HOH A O 1 HETATM 2321 O O . HOH J 5 . ? 9.640 -8.074 31.007 1.00 32.12 ? 636 HOH A O 1 HETATM 2322 O O . HOH J 5 . ? 24.749 -3.202 40.525 1.00 37.33 ? 637 HOH A O 1 HETATM 2323 O O . HOH J 5 . ? 32.516 -7.626 53.991 1.00 38.93 ? 638 HOH A O 1 HETATM 2324 O O . HOH J 5 . ? 29.066 0.361 40.679 1.00 31.30 ? 639 HOH A O 1 HETATM 2325 O O . HOH J 5 . ? 39.031 -16.344 32.554 1.00 30.54 ? 640 HOH A O 1 HETATM 2326 O O . HOH J 5 . ? 21.609 -1.347 38.543 1.00 27.99 ? 641 HOH A O 1 HETATM 2327 O O . HOH J 5 . ? 32.860 0.554 39.685 1.00 31.42 ? 642 HOH A O 1 HETATM 2328 O O . HOH J 5 . ? 22.673 -36.894 31.383 1.00 32.03 ? 643 HOH A O 1 HETATM 2329 O O . HOH J 5 . ? 42.611 -1.150 37.657 1.00 38.45 ? 644 HOH A O 1 HETATM 2330 O O . HOH J 5 . ? 36.971 -1.073 37.804 1.00 34.42 ? 645 HOH A O 1 HETATM 2331 O O . HOH J 5 . ? 17.519 -0.365 28.344 1.00 24.95 ? 646 HOH A O 1 HETATM 2332 O O . HOH J 5 . ? 33.334 -20.071 24.913 1.00 26.81 ? 647 HOH A O 1 HETATM 2333 O O . HOH J 5 . ? 41.673 -30.001 53.602 1.00 37.92 ? 648 HOH A O 1 HETATM 2334 O O . HOH J 5 . ? 16.881 -14.147 40.343 1.00 39.34 ? 649 HOH A O 1 HETATM 2335 O O . HOH J 5 . ? 45.806 -14.076 30.668 1.00 33.43 ? 650 HOH A O 1 HETATM 2336 O O . HOH J 5 . ? 26.929 -22.145 24.947 1.00 39.68 ? 651 HOH A O 1 HETATM 2337 O O . HOH J 5 . ? 22.930 -37.460 36.710 1.00 38.78 ? 652 HOH A O 1 HETATM 2338 O O . HOH J 5 . ? 43.273 -32.298 46.120 1.00 34.19 ? 653 HOH A O 1 HETATM 2339 O O . HOH J 5 . ? 33.921 2.082 51.933 1.00 36.38 ? 654 HOH A O 1 HETATM 2340 O O . HOH J 5 . ? 46.378 -27.352 50.395 1.00 41.09 ? 655 HOH A O 1 HETATM 2341 O O . HOH J 5 . ? 41.368 -20.182 29.247 1.00 26.32 ? 656 HOH A O 1 HETATM 2342 O O . HOH J 5 . ? 32.194 -37.025 36.216 1.00 31.14 ? 657 HOH A O 1 HETATM 2343 O O . HOH J 5 . ? 30.244 -30.890 28.145 1.00 38.51 ? 658 HOH A O 1 HETATM 2344 O O . HOH J 5 . ? 30.916 -12.918 55.641 1.00 38.34 ? 659 HOH A O 1 HETATM 2345 O O . HOH J 5 . ? 25.307 0.340 27.735 1.00 31.50 ? 660 HOH A O 1 HETATM 2346 O O . HOH J 5 . ? 13.852 -7.378 14.002 1.00 31.15 ? 661 HOH A O 1 HETATM 2347 O O . HOH J 5 . ? 36.437 -31.092 34.346 1.00 31.52 ? 662 HOH A O 1 HETATM 2348 O O . HOH J 5 . ? 25.197 -10.799 13.982 1.00 33.13 ? 663 HOH A O 1 HETATM 2349 O O . HOH J 5 . ? 14.550 -15.163 34.505 1.00 30.47 ? 664 HOH A O 1 HETATM 2350 O O . HOH J 5 . ? 48.026 -8.309 37.881 1.00 25.49 ? 665 HOH A O 1 HETATM 2351 O O . HOH J 5 . ? 24.738 -1.539 18.228 1.00 33.78 ? 666 HOH A O 1 HETATM 2352 O O . HOH J 5 . ? 46.458 -28.016 37.763 1.00 41.84 ? 667 HOH A O 1 HETATM 2353 O O . HOH J 5 . ? 16.763 -16.246 16.004 1.00 37.03 ? 668 HOH A O 1 HETATM 2354 O O . HOH J 5 . ? 15.224 -12.933 10.561 1.00 33.30 ? 669 HOH A O 1 HETATM 2355 O O . HOH J 5 . ? 25.642 -21.088 21.023 1.00 27.49 ? 670 HOH A O 1 HETATM 2356 O O . HOH J 5 . ? 17.459 -10.631 40.251 1.00 28.97 ? 671 HOH A O 1 HETATM 2357 O O . HOH J 5 . ? 16.838 -8.705 10.802 0.50 24.50 ? 672 HOH A O 1 HETATM 2358 O O . HOH J 5 . ? 15.744 -1.329 30.467 1.00 28.21 ? 673 HOH A O 1 HETATM 2359 O O . HOH J 5 . ? 37.946 -31.092 58.311 1.00 25.51 ? 674 HOH A O 1 HETATM 2360 O O . HOH J 5 . ? 15.101 -6.274 35.396 1.00 35.23 ? 675 HOH A O 1 HETATM 2361 O O . HOH J 5 . ? 15.249 -0.421 17.787 0.50 23.40 ? 676 HOH A O 1 HETATM 2362 O O . HOH J 5 . ? 49.516 -7.803 47.054 1.00 27.72 ? 677 HOH A O 1 HETATM 2363 O O . HOH J 5 . ? 40.096 -1.745 55.757 1.00 30.90 ? 678 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . THR A 1 ? 0.3687 0.3079 0.2251 -0.0361 -0.0036 0.0248 24 THR A N 2 C CA . THR A 1 ? 0.3661 0.3003 0.2265 -0.0318 -0.0014 0.0226 24 THR A CA 3 C C . THR A 1 ? 0.3541 0.2862 0.2126 -0.0320 0.0006 0.0183 24 THR A C 4 O O . THR A 1 ? 0.3766 0.3119 0.2320 -0.0352 -0.0002 0.0172 24 THR A O 5 C CB . THR A 1 ? 0.3781 0.3112 0.2374 -0.0307 0.0028 0.0217 24 THR A CB 6 O OG1 . THR A 1 ? 0.3955 0.3304 0.2486 -0.0335 0.0064 0.0188 24 THR A OG1 7 C CG2 . THR A 1 ? 0.3905 0.3269 0.2515 -0.0317 0.0006 0.0262 24 THR A CG2 8 N N A ILE A 2 ? 0.3675 0.2947 0.2277 -0.0291 0.0028 0.0161 25 ILE A N 9 N N B ILE A 2 ? 0.3674 0.2943 0.2271 -0.0292 0.0032 0.0159 25 ILE A N 10 C CA A ILE A 2 ? 0.3553 0.2802 0.2134 -0.0302 0.0041 0.0127 25 ILE A CA 11 C CA B ILE A 2 ? 0.3556 0.2794 0.2132 -0.0299 0.0047 0.0124 25 ILE A CA 12 C C A ILE A 2 ? 0.3607 0.2835 0.2109 -0.0338 0.0077 0.0095 25 ILE A C 13 C C B ILE A 2 ? 0.3677 0.2900 0.2174 -0.0339 0.0079 0.0092 25 ILE A C 14 O O A ILE A 2 ? 0.3442 0.2654 0.1911 -0.0336 0.0103 0.0088 25 ILE A O 15 O O B ILE A 2 ? 0.3571 0.2778 0.2032 -0.0340 0.0106 0.0083 25 ILE A O 16 C CB A ILE A 2 ? 0.3536 0.2729 0.2142 -0.0269 0.0054 0.0115 25 ILE A CB 17 C CB B ILE A 2 ? 0.3529 0.2701 0.2121 -0.0264 0.0069 0.0111 25 ILE A CB 18 C CG1 A ILE A 2 ? 0.3648 0.2852 0.2256 -0.0286 0.0044 0.0094 25 ILE A CG1 19 C CG1 B ILE A 2 ? 0.3307 0.2448 0.1877 -0.0279 0.0076 0.0084 25 ILE A CG1 20 C CG2 A ILE A 2 ? 0.3607 0.2730 0.2169 -0.0256 0.0096 0.0095 25 ILE A CG2 21 C CG2 B ILE A 2 ? 0.3614 0.2737 0.2167 -0.0249 0.0107 0.0097 25 ILE A CG2 22 C CD1 A ILE A 2 ? 0.3404 0.2581 0.2050 -0.0258 0.0043 0.0089 25 ILE A CD1 23 C CD1 B ILE A 2 ? 0.3053 0.2260 0.1678 -0.0281 0.0039 0.0088 25 ILE A CD1 24 N N A ASP A 3 ? 0.3813 0.3051 0.2284 -0.0372 0.0076 0.0073 26 ASP A N 25 N N B ASP A 3 ? 0.3945 0.3180 0.2415 -0.0373 0.0076 0.0071 26 ASP A N 26 C CA A ASP A 3 ? 0.4169 0.3370 0.2560 -0.0410 0.0109 0.0038 26 ASP A CA 27 C CA B ASP A 3 ? 0.4337 0.3540 0.2725 -0.0414 0.0108 0.0035 26 ASP A CA 28 C C A ASP A 3 ? 0.4308 0.3402 0.2662 -0.0389 0.0145 0.0012 26 ASP A C 29 C C B ASP A 3 ? 0.4372 0.3463 0.2715 -0.0399 0.0145 0.0007 26 ASP A C 30 O O A ASP A 3 ? 0.4179 0.3234 0.2569 -0.0350 0.0143 0.0022 26 ASP A O 31 O O B ASP A 3 ? 0.4321 0.3366 0.2687 -0.0374 0.0144 0.0009 26 ASP A O 32 C CB A ASP A 3 ? 0.4309 0.3548 0.2678 -0.0455 0.0098 0.0020 26 ASP A CB 33 C CB B ASP A 3 ? 0.4558 0.3820 0.2924 -0.0465 0.0092 0.0021 26 ASP A CB 34 C CG A ASP A 3 ? 0.4081 0.3428 0.2471 -0.0476 0.0061 0.0040 26 ASP A CG 35 C CG B ASP A 3 ? 0.4668 0.3923 0.3045 -0.0474 0.0088 0.0005 26 ASP A CG 36 O OD1 A ASP A 3 ? 0.4622 0.4001 0.3017 -0.0471 0.0050 0.0066 26 ASP A OD1 37 O OD1 B ASP A 3 ? 0.5697 0.4878 0.4080 -0.0449 0.0102 0.0002 26 ASP A OD1 38 O OD2 A ASP A 3 ? 0.4540 0.3944 0.2940 -0.0498 0.0042 0.0030 26 ASP A OD2 39 O OD2 B ASP A 3 ? 0.4746 0.4082 0.3124 -0.0510 0.0069 -0.0005 26 ASP A OD2 40 N N . THR A 4 ? 0.4355 0.3402 0.2634 -0.0409 0.0176 -0.0020 27 THR A N 41 C CA . THR A 4 ? 0.4407 0.3343 0.2640 -0.0384 0.0206 -0.0049 27 THR A CA 42 C C . THR A 4 ? 0.4562 0.3421 0.2710 -0.0433 0.0219 -0.0083 27 THR A C 43 O O . THR A 4 ? 0.4996 0.3903 0.3112 -0.0490 0.0214 -0.0093 27 THR A O 44 C CB . THR A 4 ? 0.4638 0.3573 0.2848 -0.0360 0.0231 -0.0068 27 THR A CB 45 O OG1 . THR A 4 ? 0.4756 0.3746 0.2924 -0.0409 0.0237 -0.0083 27 THR A OG1 46 C CG2 . THR A 4 ? 0.4778 0.3791 0.3067 -0.0319 0.0219 -0.0032 27 THR A CG2 47 N N . CYS A 5 ? 0.4557 0.3296 0.2666 -0.0417 0.0230 -0.0098 28 CYS A N 48 C CA . CYS A 5 ? 0.4569 0.3207 0.2583 -0.0468 0.0241 -0.0128 28 CYS A CA 49 C C . CYS A 5 ? 0.5110 0.3603 0.3050 -0.0435 0.0264 -0.0161 28 CYS A C 50 O O . CYS A 5 ? 0.4880 0.3350 0.2855 -0.0363 0.0269 -0.0158 28 CYS A O 51 C CB . CYS A 5 ? 0.4580 0.3193 0.2606 -0.0483 0.0225 -0.0110 28 CYS A CB 52 S SG . CYS A 5 ? 0.4497 0.3282 0.2630 -0.0493 0.0193 -0.0076 28 CYS A SG 53 N N . SER A 6 ? 0.5251 0.3642 0.3086 -0.0486 0.0277 -0.0197 29 SER A N 54 C CA . SER A 6 ? 0.5669 0.3900 0.3422 -0.0452 0.0294 -0.0236 29 SER A CA 55 C C . SER A 6 ? 0.5871 0.3984 0.3625 -0.0395 0.0284 -0.0220 29 SER A C 56 O O . SER A 6 ? 0.5713 0.3817 0.3479 -0.0417 0.0267 -0.0188 29 SER A O 57 C CB . SER A 6 ? 0.5874 0.3994 0.3503 -0.0526 0.0303 -0.0274 29 SER A CB 58 O OG . SER A 6 ? 0.6561 0.4482 0.4103 -0.0489 0.0308 -0.0304 29 SER A OG 59 N N . SER A 7 ? 0.6056 0.4091 0.3798 -0.0318 0.0293 -0.0243 30 SER A N 60 C CA . SER A 7 ? 0.6425 0.4340 0.4160 -0.0257 0.0279 -0.0229 30 SER A CA 61 C C . SER A 7 ? 0.6412 0.4123 0.4018 -0.0301 0.0270 -0.0239 30 SER A C 62 O O . SER A 7 ? 0.6525 0.4129 0.4112 -0.0271 0.0251 -0.0216 30 SER A O 63 C CB . SER A 7 ? 0.6651 0.4554 0.4414 -0.0156 0.0288 -0.0255 30 SER A CB 64 O OG . SER A 7 ? 0.7465 0.5269 0.5142 -0.0146 0.0303 -0.0313 30 SER A OG 65 N N A ASP A 8 ? 0.6398 0.4054 0.3913 -0.0378 0.0278 -0.0269 31 ASP A N 66 N N B ASP A 8 ? 0.6358 0.4016 0.3872 -0.0378 0.0279 -0.0271 31 ASP A N 67 C CA A ASP A 8 ? 0.6525 0.4004 0.3916 -0.0444 0.0267 -0.0269 31 ASP A CA 68 C CA B ASP A 8 ? 0.6471 0.3957 0.3855 -0.0455 0.0270 -0.0275 31 ASP A CA 69 C C A ASP A 8 ? 0.6252 0.3832 0.3647 -0.0553 0.0262 -0.0243 31 ASP A C 70 C C B ASP A 8 ? 0.6174 0.3742 0.3570 -0.0548 0.0259 -0.0238 31 ASP A C 71 O O A ASP A 8 ? 0.6443 0.3933 0.3729 -0.0644 0.0262 -0.0257 31 ASP A O 72 O O B ASP A 8 ? 0.6272 0.3716 0.3558 -0.0625 0.0251 -0.0238 31 ASP A O 73 C CB A ASP A 8 ? 0.6779 0.4080 0.4044 -0.0449 0.0275 -0.0326 31 ASP A CB 74 C CB B ASP A 8 ? 0.6668 0.4043 0.3933 -0.0503 0.0284 -0.0331 31 ASP A CB 75 C CG A ASP A 8 ? 0.6958 0.4149 0.4220 -0.0328 0.0272 -0.0353 31 ASP A CG 76 C CG B ASP A 8 ? 0.6811 0.4331 0.4080 -0.0601 0.0297 -0.0340 31 ASP A CG 77 O OD1 A ASP A 8 ? 0.6640 0.3664 0.3847 -0.0294 0.0249 -0.0338 31 ASP A OD1 78 O OD1 B ASP A 8 ? 0.6386 0.4104 0.3760 -0.0616 0.0295 -0.0308 31 ASP A OD1 79 O OD2 A ASP A 8 ? 0.6881 0.4161 0.4196 -0.0267 0.0290 -0.0388 31 ASP A OD2 80 O OD2 B ASP A 8 ? 0.7095 0.4521 0.4254 -0.0659 0.0308 -0.0385 31 ASP A OD2 81 N N . SER A 9 ? 0.5721 0.3494 0.3243 -0.0541 0.0257 -0.0208 32 SER A N 82 C CA . SER A 9 ? 0.5467 0.3348 0.3010 -0.0621 0.0249 -0.0184 32 SER A CA 83 C C . SER A 9 ? 0.5411 0.3170 0.2886 -0.0657 0.0234 -0.0163 32 SER A C 84 O O . SER A 9 ? 0.5563 0.3209 0.3030 -0.0592 0.0224 -0.0148 32 SER A O 85 C CB . SER A 9 ? 0.5396 0.3479 0.3088 -0.0580 0.0241 -0.0154 32 SER A CB 86 O OG . SER A 9 ? 0.4867 0.3073 0.2614 -0.0567 0.0249 -0.0166 32 SER A OG 87 N N . PRO A 10 ? 0.5270 0.3064 0.2698 -0.0760 0.0231 -0.0161 33 PRO A N 88 C CA . PRO A 10 ? 0.5540 0.3220 0.2889 -0.0807 0.0217 -0.0139 33 PRO A CA 89 C C . PRO A 10 ? 0.5401 0.3172 0.2849 -0.0762 0.0203 -0.0100 33 PRO A C 90 O O . PRO A 10 ? 0.5065 0.3039 0.2644 -0.0739 0.0202 -0.0090 33 PRO A O 91 C CB . PRO A 10 ? 0.5351 0.3096 0.2637 -0.0938 0.0221 -0.0152 33 PRO A CB 92 C CG . PRO A 10 ? 0.5680 0.3654 0.3084 -0.0927 0.0228 -0.0163 33 PRO A CG 93 C CD . PRO A 10 ? 0.5230 0.3182 0.2675 -0.0840 0.0237 -0.0175 33 PRO A CD 94 N N . LEU A 11 ? 0.5603 0.3214 0.2982 -0.0751 0.0189 -0.0078 34 LEU A N 95 C CA . LEU A 11 ? 0.5404 0.3069 0.2856 -0.0708 0.0175 -0.0043 34 LEU A CA 96 C C . LEU A 11 ? 0.5096 0.2918 0.2583 -0.0788 0.0172 -0.0032 34 LEU A C 97 O O . LEU A 11 ? 0.5209 0.2997 0.2596 -0.0897 0.0172 -0.0037 34 LEU A O 98 C CB . LEU A 11 ? 0.5740 0.3179 0.3085 -0.0690 0.0157 -0.0022 34 LEU A CB 99 C CG . LEU A 11 ? 0.6240 0.3653 0.3637 -0.0604 0.0141 0.0010 34 LEU A CG 100 C CD1 . LEU A 11 ? 0.5593 0.3149 0.3140 -0.0500 0.0149 0.0008 34 LEU A CD1 101 C CD2 . LEU A 11 ? 0.7428 0.4563 0.4682 -0.0579 0.0123 0.0014 34 LEU A CD2 102 N N . SER A 12 ? 0.4765 0.2761 0.2392 -0.0734 0.0169 -0.0019 35 SER A N 103 C CA . SER A 12 ? 0.4708 0.2870 0.2383 -0.0793 0.0164 -0.0016 35 SER A CA 104 C C . SER A 12 ? 0.4908 0.2962 0.2487 -0.0849 0.0153 0.0009 35 SER A C 105 O O . SER A 12 ? 0.4884 0.2770 0.2409 -0.0806 0.0143 0.0032 35 SER A O 106 C CB . SER A 12 ? 0.4290 0.2629 0.2126 -0.0716 0.0158 -0.0009 35 SER A CB 107 O OG . SER A 12 ? 0.4391 0.2664 0.2264 -0.0632 0.0150 0.0017 35 SER A OG 108 N N . CYS A 13 ? 0.4872 0.3039 0.2434 -0.0944 0.0154 0.0002 36 CYS A N 109 C CA . CYS A 13 ? 0.5347 0.3452 0.2809 -0.1029 0.0146 0.0022 36 CYS A CA 110 C C . CYS A 13 ? 0.5707 0.3561 0.2978 -0.1105 0.0141 0.0033 36 CYS A C 111 O O . CYS A 13 ? 0.5977 0.3825 0.3149 -0.1223 0.0139 0.0037 36 CYS A O 112 C CB . CYS A 13 ? 0.5410 0.3517 0.2927 -0.0965 0.0132 0.0054 36 CYS A CB 113 S SG . CYS A 13 ? 0.5142 0.3534 0.2844 -0.0921 0.0133 0.0039 36 CYS A SG 114 N N . GLN A 14 ? 0.5921 0.3580 0.3146 -0.1034 0.0136 0.0038 37 GLN A N 115 C CA . GLN A 14 ? 0.6408 0.3800 0.3458 -0.1078 0.0125 0.0048 37 GLN A CA 116 C C . GLN A 14 ? 0.6583 0.3946 0.3550 -0.1164 0.0138 0.0013 37 GLN A C 117 O O . GLN A 14 ? 0.6824 0.3973 0.3625 -0.1235 0.0128 0.0018 37 GLN A O 118 C CB . GLN A 14 ? 0.6645 0.3853 0.3691 -0.0951 0.0111 0.0060 37 GLN A CB 119 C CG . GLN A 14 ? 0.7134 0.4356 0.4241 -0.0880 0.0093 0.0098 37 GLN A CG 120 C CD . GLN A 14 ? 0.8194 0.5223 0.5277 -0.0761 0.0073 0.0113 37 GLN A CD 121 O OE1 . GLN A 14 ? 0.8623 0.5404 0.5559 -0.0772 0.0054 0.0119 37 GLN A OE1 122 N NE2 . GLN A 14 ? 0.7566 0.4713 0.4792 -0.0649 0.0073 0.0122 37 GLN A NE2 123 N N . THR A 15 ? 0.6326 0.3895 0.3397 -0.1163 0.0158 -0.0020 38 THR A N 124 C CA . THR A 15 ? 0.6283 0.3856 0.3280 -0.1255 0.0172 -0.0054 38 THR A CA 125 C C . THR A 15 ? 0.6091 0.3939 0.3163 -0.1332 0.0183 -0.0073 38 THR A C 126 O O . THR A 15 ? 0.5867 0.3903 0.3066 -0.1293 0.0181 -0.0067 38 THR A O 127 C CB . THR A 15 ? 0.6480 0.4012 0.3510 -0.1174 0.0184 -0.0083 38 THR A CB 128 O OG1 . THR A 15 ? 0.5572 0.3328 0.2779 -0.1090 0.0192 -0.0090 38 THR A OG1 129 C CG2 . THR A 15 ? 0.6555 0.3830 0.3523 -0.1079 0.0172 -0.0073 38 THR A CG2 130 N N A ASP A 16 ? 0.6144 0.4015 0.3139 -0.1437 0.0194 -0.0101 39 ASP A N 131 N N B ASP A 16 ? 0.6194 0.4057 0.3178 -0.1447 0.0193 -0.0099 39 ASP A N 132 C CA A ASP A 16 ? 0.6226 0.4357 0.3281 -0.1515 0.0202 -0.0125 39 ASP A CA 133 C CA B ASP A 16 ? 0.6167 0.4298 0.3217 -0.1520 0.0202 -0.0126 39 ASP A CA 134 C C A ASP A 16 ? 0.6092 0.4355 0.3235 -0.1472 0.0213 -0.0158 39 ASP A C 135 C C B ASP A 16 ? 0.6010 0.4247 0.3152 -0.1457 0.0212 -0.0155 39 ASP A C 136 O O A ASP A 16 ? 0.6264 0.4461 0.3318 -0.1532 0.0222 -0.0182 39 ASP A O 137 O O B ASP A 16 ? 0.6045 0.4156 0.3100 -0.1483 0.0220 -0.0174 39 ASP A O 138 C CB A ASP A 16 ? 0.6567 0.4653 0.3459 -0.1686 0.0205 -0.0134 39 ASP A CB 139 C CB B ASP A 16 ? 0.6430 0.4526 0.3321 -0.1691 0.0207 -0.0140 39 ASP A CB 140 C CG A ASP A 16 ? 0.6602 0.4986 0.3561 -0.1766 0.0214 -0.0165 39 ASP A CG 141 C CG B ASP A 16 ? 0.6711 0.4777 0.3520 -0.1781 0.0198 -0.0112 39 ASP A CG 142 O OD1 A ASP A 16 ? 0.7005 0.5610 0.4126 -0.1692 0.0213 -0.0172 39 ASP A OD1 143 O OD1 B ASP A 16 ? 0.7121 0.5381 0.4037 -0.1762 0.0196 -0.0106 39 ASP A OD1 144 O OD2 A ASP A 16 ? 0.7609 0.6006 0.4460 -0.1900 0.0222 -0.0185 39 ASP A OD2 145 O OD2 B ASP A 16 ? 0.7314 0.5158 0.3942 -0.1878 0.0191 -0.0097 39 ASP A OD2 146 N N . ASN A 17 ? 0.5764 0.4213 0.3076 -0.1373 0.0209 -0.0158 40 ASN A N 147 C CA . ASN A 17 ? 0.5626 0.4203 0.3022 -0.1329 0.0213 -0.0182 40 ASN A CA 148 C C . ASN A 17 ? 0.5463 0.4313 0.3016 -0.1292 0.0203 -0.0190 40 ASN A C 149 O O . ASN A 17 ? 0.5328 0.4264 0.2939 -0.1281 0.0195 -0.0179 40 ASN A O 150 C CB . ASN A 17 ? 0.5593 0.4037 0.3019 -0.1215 0.0214 -0.0170 40 ASN A CB 151 C CG . ASN A 17 ? 0.5896 0.4092 0.3172 -0.1244 0.0224 -0.0179 40 ASN A CG 152 O OD1 . ASN A 17 ? 0.6212 0.4206 0.3423 -0.1212 0.0219 -0.0159 40 ASN A OD1 153 N ND2 . ASN A 17 ? 0.5463 0.3669 0.2683 -0.1303 0.0235 -0.0211 40 ASN A ND2 154 N N . GLU A 18 ? 0.5255 0.4237 0.2870 -0.1275 0.0201 -0.0210 41 GLU A N 155 C CA . GLU A 18 ? 0.5182 0.4422 0.2937 -0.1241 0.0185 -0.0223 41 GLU A CA 156 C C . GLU A 18 ? 0.4729 0.3997 0.2615 -0.1107 0.0170 -0.0201 41 GLU A C 157 O O . GLU A 18 ? 0.4776 0.3947 0.2663 -0.1050 0.0173 -0.0189 41 GLU A O 158 C CB . GLU A 18 ? 0.5392 0.4770 0.3140 -0.1298 0.0185 -0.0255 41 GLU A CB 159 C CG . GLU A 18 ? 0.6600 0.6089 0.4279 -0.1429 0.0191 -0.0285 41 GLU A CG 160 C CD . GLU A 18 ? 0.7012 0.6763 0.4809 -0.1419 0.0174 -0.0303 41 GLU A CD 161 O OE1 . GLU A 18 ? 0.8022 0.7803 0.5919 -0.1328 0.0161 -0.0287 41 GLU A OE1 162 O OE2 . GLU A 18 ? 0.7989 0.7923 0.5779 -0.1500 0.0174 -0.0338 41 GLU A OE2 163 N N . ALA A 19 ? 0.4352 0.3758 0.2345 -0.1063 0.0153 -0.0199 42 ALA A N 164 C CA . ALA A 19 ? 0.4132 0.3581 0.2252 -0.0944 0.0133 -0.0179 42 ALA A CA 165 C C . ALA A 19 ? 0.3988 0.3488 0.2156 -0.0899 0.0121 -0.0178 42 ALA A C 166 O O . ALA A 19 ? 0.3963 0.3603 0.2142 -0.0938 0.0112 -0.0202 42 ALA A O 167 C CB . ALA A 19 ? 0.4063 0.3700 0.2293 -0.0917 0.0112 -0.0193 42 ALA A CB 168 N N . SER A 20 ? 0.3917 0.3320 0.2116 -0.0820 0.0119 -0.0151 43 SER A N 169 C CA . SER A 20 ? 0.3758 0.3186 0.1989 -0.0780 0.0108 -0.0142 43 SER A CA 170 C C . SER A 20 ? 0.3735 0.3084 0.2022 -0.0688 0.0103 -0.0110 43 SER A C 171 O O . SER A 20 ? 0.3862 0.3135 0.2156 -0.0660 0.0109 -0.0097 43 SER A O 172 C CB . SER A 20 ? 0.3817 0.3155 0.1942 -0.0835 0.0131 -0.0154 43 SER A CB 173 O OG . SER A 20 ? 0.3750 0.2891 0.1808 -0.0814 0.0155 -0.0143 43 SER A OG 174 N N . CYS A 21 ? 0.3883 0.3252 0.2203 -0.0649 0.0092 -0.0096 44 CYS A N 175 C CA . CYS A 21 ? 0.3730 0.3022 0.2086 -0.0577 0.0091 -0.0066 44 CYS A CA 176 C C . CYS A 21 ? 0.3961 0.3083 0.2242 -0.0572 0.0124 -0.0064 44 CYS A C 177 O O . CYS A 21 ? 0.4082 0.3150 0.2399 -0.0512 0.0125 -0.0043 44 CYS A O 178 C CB . CYS A 21 ? 0.3927 0.3275 0.2315 -0.0552 0.0073 -0.0050 44 CYS A CB 179 S SG . CYS A 21 ? 0.3819 0.3332 0.2310 -0.0521 0.0022 -0.0040 44 CYS A SG 180 N N . CYS A 22 ? 0.3993 0.3029 0.2169 -0.0634 0.0148 -0.0088 45 CYS A N 181 C CA . CYS A 22 ? 0.3940 0.2805 0.2040 -0.0624 0.0172 -0.0091 45 CYS A CA 182 C C . CYS A 22 ? 0.4030 0.2801 0.2061 -0.0666 0.0179 -0.0096 45 CYS A C 183 O O . CYS A 22 ? 0.4220 0.2828 0.2153 -0.0681 0.0196 -0.0105 45 CYS A O 184 C CB . CYS A 22 ? 0.4143 0.2941 0.2154 -0.0659 0.0192 -0.0115 45 CYS A CB 185 S SG . CYS A 22 ? 0.4266 0.3130 0.2339 -0.0598 0.0190 -0.0103 45 CYS A SG 186 N N . PHE A 23 ? 0.3957 0.2829 0.2034 -0.0689 0.0165 -0.0093 46 PHE A N 187 C CA . PHE A 23 ? 0.3961 0.2764 0.1974 -0.0738 0.0169 -0.0094 46 PHE A CA 188 C C . PHE A 23 ? 0.4044 0.2965 0.2151 -0.0712 0.0152 -0.0082 46 PHE A C 189 O O . PHE A 23 ? 0.4130 0.3213 0.2298 -0.0732 0.0138 -0.0097 46 PHE A O 190 C CB . PHE A 23 ? 0.3975 0.2777 0.1886 -0.0848 0.0179 -0.0120 46 PHE A CB 191 C CG . PHE A 23 ? 0.4234 0.2912 0.2044 -0.0908 0.0185 -0.0116 46 PHE A CG 192 C CD1 . PHE A 23 ? 0.4587 0.3046 0.2309 -0.0885 0.0193 -0.0103 46 PHE A CD1 193 C CD2 . PHE A 23 ? 0.4394 0.3176 0.2202 -0.0976 0.0180 -0.0123 46 PHE A CD2 194 C CE1 . PHE A 23 ? 0.4686 0.3009 0.2302 -0.0940 0.0192 -0.0093 46 PHE A CE1 195 C CE2 . PHE A 23 ? 0.4597 0.3256 0.2298 -0.1042 0.0183 -0.0112 46 PHE A CE2 196 C CZ . PHE A 23 ? 0.4588 0.3014 0.2195 -0.1020 0.0187 -0.0094 46 PHE A CZ 197 N N . ASN A 24 ? 0.4059 0.2901 0.2182 -0.0663 0.0150 -0.0060 47 ASN A N 198 C CA . ASN A 24 ? 0.3955 0.2897 0.2156 -0.0644 0.0136 -0.0053 47 ASN A CA 199 C C . ASN A 24 ? 0.3962 0.2939 0.2106 -0.0730 0.0138 -0.0067 47 ASN A C 200 O O . ASN A 24 ? 0.4064 0.2904 0.2104 -0.0776 0.0148 -0.0057 47 ASN A O 201 C CB . ASN A 24 ? 0.3742 0.2591 0.1971 -0.0570 0.0133 -0.0025 47 ASN A CB 202 C CG . ASN A 24 ? 0.3506 0.2384 0.1821 -0.0487 0.0126 -0.0012 47 ASN A CG 203 O OD1 . ASN A 24 ? 0.3832 0.2834 0.2249 -0.0452 0.0107 -0.0011 47 ASN A OD1 204 N ND2 . ASN A 24 ? 0.3868 0.2629 0.2139 -0.0457 0.0139 -0.0006 47 ASN A ND2 205 N N . SER A 25 ? 0.4194 0.3361 0.2405 -0.0755 0.0127 -0.0091 48 SER A N 206 C CA . SER A 25 ? 0.4025 0.3279 0.2189 -0.0851 0.0132 -0.0114 48 SER A CA 207 C C . SER A 25 ? 0.4173 0.3653 0.2457 -0.0827 0.0113 -0.0142 48 SER A C 208 O O . SER A 25 ? 0.4196 0.3757 0.2552 -0.0780 0.0099 -0.0150 48 SER A O 209 C CB . SER A 25 ? 0.4525 0.3744 0.2577 -0.0949 0.0146 -0.0132 48 SER A CB 210 O OG . SER A 25 ? 0.4425 0.3726 0.2422 -0.1051 0.0152 -0.0151 48 SER A OG 211 N N . PRO A 26 ? 0.3955 0.3545 0.2261 -0.0858 0.0111 -0.0159 49 PRO A N 212 C CA . PRO A 26 ? 0.4166 0.3679 0.2383 -0.0925 0.0124 -0.0147 49 PRO A CA 213 C C . PRO A 26 ? 0.4145 0.3519 0.2370 -0.0859 0.0122 -0.0109 49 PRO A C 214 O O . PRO A 26 ? 0.4350 0.3609 0.2481 -0.0908 0.0130 -0.0088 49 PRO A O 215 C CB . PRO A 26 ? 0.4318 0.4059 0.2591 -0.0966 0.0119 -0.0187 49 PRO A CB 216 C CG . PRO A 26 ? 0.4106 0.3994 0.2530 -0.0866 0.0096 -0.0209 49 PRO A CG 217 C CD . PRO A 26 ? 0.3941 0.3760 0.2368 -0.0827 0.0090 -0.0196 49 PRO A CD 218 N N . GLY A 27 ? 0.3927 0.3309 0.2255 -0.0754 0.0108 -0.0099 50 GLY A N 219 C CA . GLY A 27 ? 0.4022 0.3298 0.2378 -0.0680 0.0104 -0.0066 50 GLY A CA 220 C C . GLY A 27 ? 0.3930 0.2997 0.2205 -0.0660 0.0114 -0.0034 50 GLY A C 221 O O . GLY A 27 ? 0.3960 0.2984 0.2284 -0.0584 0.0111 -0.0020 50 GLY A O 222 N N . GLY A 28 ? 0.4181 0.3118 0.2328 -0.0729 0.0126 -0.0024 51 GLY A N 223 C CA . GLY A 28 ? 0.4232 0.2959 0.2283 -0.0717 0.0133 -0.0002 51 GLY A CA 224 C C . GLY A 28 ? 0.4269 0.2859 0.2297 -0.0665 0.0127 0.0032 51 GLY A C 225 O O . GLY A 28 ? 0.4427 0.2844 0.2387 -0.0635 0.0130 0.0046 51 GLY A O 226 N N . SER A 29 ? 0.3953 0.2617 0.2026 -0.0660 0.0119 0.0041 52 SER A N 227 C CA . SER A 29 ? 0.4212 0.2767 0.2270 -0.0610 0.0110 0.0074 52 SER A CA 228 C C . SER A 29 ? 0.3943 0.2603 0.2140 -0.0519 0.0103 0.0074 52 SER A C 229 O O . SER A 29 ? 0.4230 0.3052 0.2514 -0.0521 0.0098 0.0057 52 SER A O 230 C CB . SER A 29 ? 0.4204 0.2766 0.2204 -0.0678 0.0103 0.0086 52 SER A CB 231 O OG . SER A 29 ? 0.4826 0.3276 0.2809 -0.0624 0.0092 0.0121 52 SER A OG 232 N N . LEU A 30 ? 0.3925 0.2506 0.2146 -0.0441 0.0103 0.0088 53 LEU A N 233 C CA . LEU A 30 ? 0.3802 0.2477 0.2149 -0.0360 0.0096 0.0091 53 LEU A CA 234 C C . LEU A 30 ? 0.3753 0.2376 0.2110 -0.0310 0.0087 0.0118 53 LEU A C 235 O O . LEU A 30 ? 0.4180 0.2665 0.2469 -0.0286 0.0087 0.0136 53 LEU A O 236 C CB . LEU A 30 ? 0.3816 0.2467 0.2190 -0.0311 0.0103 0.0087 53 LEU A CB 237 C CG . LEU A 30 ? 0.4043 0.2790 0.2455 -0.0330 0.0106 0.0064 53 LEU A CG 238 C CD1 . LEU A 30 ? 0.3781 0.2682 0.2313 -0.0302 0.0089 0.0058 53 LEU A CD1 239 C CD2 . LEU A 30 ? 0.3984 0.2734 0.2324 -0.0412 0.0112 0.0046 53 LEU A CD2 240 N N . LEU A 31 ? 0.3532 0.2270 0.1976 -0.0291 0.0078 0.0117 54 LEU A N 241 C CA . LEU A 31 ? 0.3522 0.2242 0.1980 -0.0256 0.0068 0.0140 54 LEU A CA 242 C C . LEU A 31 ? 0.3481 0.2257 0.2045 -0.0178 0.0063 0.0143 54 LEU A C 243 O O . LEU A 31 ? 0.3532 0.2421 0.2182 -0.0167 0.0058 0.0127 54 LEU A O 244 C CB . LEU A 31 ? 0.3576 0.2395 0.2051 -0.0302 0.0061 0.0131 54 LEU A CB 245 C CG . LEU A 31 ? 0.3685 0.2460 0.2048 -0.0391 0.0063 0.0135 54 LEU A CG 246 C CD1 . LEU A 31 ? 0.3722 0.2482 0.2027 -0.0452 0.0075 0.0115 54 LEU A CD1 247 C CD2 . LEU A 31 ? 0.3828 0.2743 0.2235 -0.0424 0.0059 0.0120 54 LEU A CD2 248 N N . GLN A 32 ? 0.3618 0.2309 0.2166 -0.0124 0.0063 0.0164 55 GLN A N 249 C CA . GLN A 32 ? 0.3400 0.2150 0.2038 -0.0060 0.0058 0.0171 55 GLN A CA 250 C C . GLN A 32 ? 0.3368 0.2143 0.2023 -0.0050 0.0046 0.0186 55 GLN A C 251 O O . GLN A 32 ? 0.3372 0.2060 0.1962 -0.0042 0.0041 0.0207 55 GLN A O 252 C CB . GLN A 32 ? 0.3491 0.2172 0.2116 -0.0006 0.0065 0.0178 55 GLN A CB 253 C CG . GLN A 32 ? 0.3192 0.1958 0.1911 0.0043 0.0065 0.0179 55 GLN A CG 254 C CD . GLN A 32 ? 0.3473 0.2302 0.2255 0.0074 0.0052 0.0192 55 GLN A CD 255 O OE1 . GLN A 32 ? 0.3442 0.2232 0.2205 0.0112 0.0049 0.0207 55 GLN A OE1 256 N NE2 . GLN A 32 ? 0.3087 0.2016 0.1945 0.0061 0.0043 0.0185 55 GLN A NE2 257 N N . THR A 33 ? 0.3314 0.2208 0.2056 -0.0049 0.0038 0.0174 56 THR A N 258 C CA . THR A 33 ? 0.3318 0.2258 0.2080 -0.0051 0.0027 0.0181 56 THR A CA 259 C C . THR A 33 ? 0.3175 0.2167 0.2018 0.0005 0.0019 0.0189 56 THR A C 260 O O . THR A 33 ? 0.2973 0.2008 0.1879 0.0029 0.0019 0.0181 56 THR A O 261 C CB . THR A 33 ? 0.3300 0.2348 0.2096 -0.0100 0.0023 0.0152 56 THR A CB 262 O OG1 . THR A 33 ? 0.3065 0.2194 0.1946 -0.0081 0.0018 0.0128 56 THR A OG1 263 C CG2 . THR A 33 ? 0.3181 0.2192 0.1891 -0.0165 0.0032 0.0143 56 THR A CG2 264 N N . GLN A 34 ? 0.3173 0.2165 0.2009 0.0018 0.0011 0.0206 57 GLN A N 265 C CA . GLN A 34 ? 0.3126 0.2163 0.2024 0.0066 0.0004 0.0217 57 GLN A CA 266 C C . GLN A 34 ? 0.3006 0.2114 0.1930 0.0053 -0.0008 0.0216 57 GLN A C 267 O O . GLN A 34 ? 0.3161 0.2264 0.2036 0.0011 -0.0011 0.0216 57 GLN A O 268 C CB . GLN A 34 ? 0.3487 0.2442 0.2340 0.0114 0.0004 0.0243 57 GLN A CB 269 C CG . GLN A 34 ? 0.3461 0.2350 0.2285 0.0131 0.0017 0.0238 57 GLN A CG 270 C CD . GLN A 34 ? 0.3506 0.2324 0.2293 0.0190 0.0016 0.0253 57 GLN A CD 271 O OE1 . GLN A 34 ? 0.3437 0.2275 0.2237 0.0226 0.0004 0.0269 57 GLN A OE1 272 N NE2 . GLN A 34 ? 0.3267 0.2017 0.2016 0.0206 0.0028 0.0243 57 GLN A NE2 273 N N . PHE A 35 ? 0.2688 0.1865 0.1685 0.0082 -0.0015 0.0215 58 PHE A N 274 C CA . PHE A 35 ? 0.2825 0.2074 0.1851 0.0073 -0.0026 0.0212 58 PHE A CA 275 C C . PHE A 35 ? 0.3106 0.2365 0.2146 0.0116 -0.0033 0.0236 58 PHE A C 276 O O . PHE A 35 ? 0.2884 0.2135 0.1948 0.0154 -0.0030 0.0245 58 PHE A O 277 C CB . PHE A 35 ? 0.2771 0.2109 0.1887 0.0071 -0.0033 0.0181 58 PHE A CB 278 C CG . PHE A 35 ? 0.3118 0.2495 0.2248 0.0036 -0.0034 0.0145 58 PHE A CG 279 C CD1 . PHE A 35 ? 0.3245 0.2650 0.2339 -0.0004 -0.0032 0.0132 58 PHE A CD1 280 C CD2 . PHE A 35 ? 0.3111 0.2508 0.2294 0.0044 -0.0039 0.0123 58 PHE A CD2 281 C CE1 . PHE A 35 ? 0.3690 0.3162 0.2812 -0.0032 -0.0034 0.0090 58 PHE A CE1 282 C CE2 . PHE A 35 ? 0.3307 0.2755 0.2514 0.0022 -0.0046 0.0085 58 PHE A CE2 283 C CZ . PHE A 35 ? 0.3535 0.3026 0.2714 -0.0014 -0.0041 0.0066 58 PHE A CZ 284 N N . TRP A 36 ? 0.3095 0.2388 0.2124 0.0107 -0.0044 0.0245 59 TRP A N 285 C CA . TRP A 36 ? 0.2920 0.2258 0.1976 0.0141 -0.0054 0.0263 59 TRP A CA 286 C C . TRP A 36 ? 0.2976 0.2419 0.2094 0.0113 -0.0061 0.0237 59 TRP A C 287 O O . TRP A 36 ? 0.2913 0.2388 0.2006 0.0079 -0.0067 0.0232 59 TRP A O 288 C CB . TRP A 36 ? 0.3151 0.2424 0.2126 0.0154 -0.0066 0.0298 59 TRP A CB 289 C CG . TRP A 36 ? 0.3250 0.2583 0.2256 0.0193 -0.0080 0.0315 59 TRP A CG 290 C CD1 . TRP A 36 ? 0.3589 0.2981 0.2591 0.0178 -0.0095 0.0325 59 TRP A CD1 291 C CD2 . TRP A 36 ? 0.3221 0.2576 0.2265 0.0251 -0.0080 0.0323 59 TRP A CD2 292 N NE1 . TRP A 36 ? 0.3265 0.2714 0.2304 0.0224 -0.0105 0.0338 59 TRP A NE1 293 C CE2 . TRP A 36 ? 0.3242 0.2672 0.2306 0.0271 -0.0096 0.0337 59 TRP A CE2 294 C CE3 . TRP A 36 ? 0.3505 0.2832 0.2563 0.0288 -0.0068 0.0318 59 TRP A CE3 295 C CZ2 . TRP A 36 ? 0.2988 0.2475 0.2091 0.0323 -0.0101 0.0343 59 TRP A CZ2 296 C CZ3 . TRP A 36 ? 0.3186 0.2576 0.2285 0.0341 -0.0071 0.0323 59 TRP A CZ3 297 C CH2 . TRP A 36 ? 0.2943 0.2418 0.2067 0.0358 -0.0087 0.0335 59 TRP A CH2 298 N N . ASP A 37 ? 0.2830 0.2329 0.2023 0.0124 -0.0062 0.0219 60 ASP A N 299 C CA . ASP A 37 ? 0.2802 0.2382 0.2053 0.0100 -0.0070 0.0186 60 ASP A CA 300 C C . ASP A 37 ? 0.2902 0.2546 0.2182 0.0115 -0.0079 0.0199 60 ASP A C 301 O O . ASP A 37 ? 0.2864 0.2522 0.2175 0.0140 -0.0079 0.0211 60 ASP A O 302 C CB . ASP A 37 ? 0.2824 0.2406 0.2129 0.0100 -0.0072 0.0162 60 ASP A CB 303 C CG . ASP A 37 ? 0.3551 0.3099 0.2845 0.0083 -0.0068 0.0139 60 ASP A CG 304 O OD1 . ASP A 37 ? 0.3752 0.3293 0.3002 0.0060 -0.0062 0.0133 60 ASP A OD1 305 O OD2 . ASP A 37 ? 0.3332 0.2859 0.2657 0.0090 -0.0071 0.0130 60 ASP A OD2 306 N N . TYR A 38 ? 0.2950 0.2643 0.2215 0.0097 -0.0087 0.0198 61 TYR A N 307 C CA . TYR A 38 ? 0.2929 0.2693 0.2215 0.0108 -0.0097 0.0211 61 TYR A CA 308 C C . TYR A 38 ? 0.2953 0.2802 0.2290 0.0079 -0.0105 0.0174 61 TYR A C 309 O O . TYR A 38 ? 0.3145 0.3059 0.2520 0.0083 -0.0113 0.0176 61 TYR A O 310 C CB . TYR A 38 ? 0.3165 0.2909 0.2382 0.0119 -0.0105 0.0249 61 TYR A CB 311 C CG . TYR A 38 ? 0.3061 0.2797 0.2227 0.0074 -0.0105 0.0241 61 TYR A CG 312 C CD1 . TYR A 38 ? 0.3274 0.2919 0.2375 0.0059 -0.0098 0.0250 61 TYR A CD1 313 C CD2 . TYR A 38 ? 0.3480 0.3307 0.2665 0.0037 -0.0111 0.0216 61 TYR A CD2 314 C CE1 . TYR A 38 ? 0.3301 0.2953 0.2352 0.0005 -0.0096 0.0239 61 TYR A CE1 315 C CE2 . TYR A 38 ? 0.3665 0.3504 0.2803 -0.0013 -0.0109 0.0202 61 TYR A CE2 316 C CZ . TYR A 38 ? 0.3165 0.2918 0.2235 -0.0030 -0.0101 0.0216 61 TYR A CZ 317 O OH . TYR A 38 ? 0.3921 0.3699 0.2942 -0.0088 -0.0097 0.0201 61 TYR A OH 318 N N . ASP A 39 ? 0.3158 0.3020 0.2503 0.0047 -0.0104 0.0134 62 ASP A N 319 C CA . ASP A 39 ? 0.3087 0.3026 0.2482 0.0025 -0.0113 0.0091 62 ASP A CA 320 C C . ASP A 39 ? 0.3256 0.3185 0.2682 0.0013 -0.0115 0.0039 62 ASP A C 321 O O . ASP A 39 ? 0.3105 0.3062 0.2513 -0.0008 -0.0110 0.0012 62 ASP A O 322 C CB . ASP A 39 ? 0.3366 0.3379 0.2734 -0.0002 -0.0117 0.0087 62 ASP A CB 323 C CG . ASP A 39 ? 0.3127 0.3229 0.2547 -0.0027 -0.0126 0.0032 62 ASP A CG 324 O OD1 . ASP A 39 ? 0.3155 0.3249 0.2628 -0.0021 -0.0133 -0.0001 62 ASP A OD1 325 O OD2 . ASP A 39 ? 0.3346 0.3523 0.2745 -0.0056 -0.0128 0.0020 62 ASP A OD2 326 N N . PRO A 40 ? 0.3090 0.2986 0.2560 0.0027 -0.0123 0.0025 63 PRO A N 327 C CA . PRO A 40 ? 0.3085 0.2959 0.2573 0.0041 -0.0127 0.0056 63 PRO A CA 328 C C . PRO A 40 ? 0.3105 0.2920 0.2559 0.0065 -0.0114 0.0103 63 PRO A C 329 O O . PRO A 40 ? 0.3061 0.2822 0.2485 0.0071 -0.0105 0.0107 63 PRO A O 330 C CB . PRO A 40 ? 0.3248 0.3089 0.2778 0.0038 -0.0143 0.0023 63 PRO A CB 331 C CG . PRO A 40 ? 0.3528 0.3341 0.3055 0.0042 -0.0143 -0.0007 63 PRO A CG 332 C CD . PRO A 40 ? 0.3096 0.2968 0.2595 0.0028 -0.0131 -0.0020 63 PRO A CD 333 N N . SER A 41 ? 0.2839 0.2672 0.2298 0.0079 -0.0113 0.0134 64 SER A N 334 C CA . SER A 41 ? 0.2844 0.2639 0.2281 0.0107 -0.0101 0.0170 64 SER A CA 335 C C . SER A 41 ? 0.2954 0.2701 0.2410 0.0104 -0.0101 0.0168 64 SER A C 336 O O . SER A 41 ? 0.3017 0.2774 0.2508 0.0082 -0.0115 0.0150 64 SER A O 337 C CB . SER A 41 ? 0.2759 0.2620 0.2204 0.0124 -0.0102 0.0196 64 SER A CB 338 O OG . SER A 41 ? 0.2892 0.2785 0.2307 0.0134 -0.0105 0.0210 64 SER A OG 339 N N . ASP A 42 ? 0.2918 0.2610 0.2344 0.0124 -0.0088 0.0187 65 ASP A N 340 C CA . ASP A 42 ? 0.2924 0.2580 0.2358 0.0121 -0.0086 0.0192 65 ASP A CA 341 C C . ASP A 42 ? 0.2827 0.2471 0.2231 0.0152 -0.0068 0.0220 65 ASP A C 342 O O . ASP A 42 ? 0.2787 0.2431 0.2161 0.0180 -0.0061 0.0232 65 ASP A O 343 C CB . ASP A 42 ? 0.2862 0.2457 0.2294 0.0109 -0.0093 0.0171 65 ASP A CB 344 C CG . ASP A 42 ? 0.2232 0.1788 0.1621 0.0119 -0.0080 0.0170 65 ASP A CG 345 O OD1 . ASP A 42 ? 0.3333 0.2869 0.2683 0.0140 -0.0065 0.0195 65 ASP A OD1 346 O OD2 . ASP A 42 ? 0.3271 0.2820 0.2664 0.0105 -0.0087 0.0142 65 ASP A OD2 347 N N . GLY A 43 ? 0.2708 0.2344 0.2119 0.0147 -0.0064 0.0227 66 GLY A N 348 C CA . GLY A 43 ? 0.2549 0.2180 0.1935 0.0176 -0.0046 0.0243 66 GLY A CA 349 C C . GLY A 43 ? 0.2704 0.2416 0.2102 0.0204 -0.0042 0.0254 66 GLY A C 350 O O . GLY A 43 ? 0.2560 0.2340 0.1987 0.0192 -0.0052 0.0253 66 GLY A O 351 N N . PRO A 44 ? 0.2640 0.2356 0.2018 0.0243 -0.0027 0.0262 67 PRO A N 352 C CA . PRO A 44 ? 0.2599 0.2406 0.1992 0.0280 -0.0025 0.0268 67 PRO A CA 353 C C . PRO A 44 ? 0.2964 0.2759 0.2339 0.0311 -0.0037 0.0275 67 PRO A C 354 O O . PRO A 44 ? 0.2854 0.2551 0.2185 0.0312 -0.0040 0.0277 67 PRO A O 355 C CB . PRO A 44 ? 0.2809 0.2599 0.2176 0.0324 -0.0008 0.0266 67 PRO A CB 356 C CG . PRO A 44 ? 0.2819 0.2532 0.2165 0.0294 0.0002 0.0261 67 PRO A CG 357 C CD . PRO A 44 ? 0.2447 0.2093 0.1790 0.0253 -0.0012 0.0260 67 PRO A CD 358 N N A SER A 45 ? 0.2840 0.2736 0.2242 0.0333 -0.0045 0.0280 68 SER A N 359 N N B SER A 45 ? 0.2880 0.2775 0.2282 0.0331 -0.0045 0.0280 68 SER A N 360 C CA A SER A 45 ? 0.3040 0.2932 0.2421 0.0361 -0.0060 0.0291 68 SER A CA 361 C CA B SER A 45 ? 0.2996 0.2889 0.2376 0.0363 -0.0060 0.0292 68 SER A CA 362 C C A SER A 45 ? 0.3179 0.2978 0.2500 0.0419 -0.0062 0.0302 68 SER A C 363 C C B SER A 45 ? 0.3143 0.2928 0.2459 0.0414 -0.0061 0.0302 68 SER A C 364 O O A SER A 45 ? 0.3312 0.3063 0.2592 0.0430 -0.0078 0.0317 68 SER A O 365 O O B SER A 45 ? 0.3200 0.2914 0.2470 0.0414 -0.0074 0.0315 68 SER A O 366 C CB A SER A 45 ? 0.3058 0.3092 0.2483 0.0375 -0.0070 0.0294 68 SER A CB 367 C CB B SER A 45 ? 0.3009 0.3039 0.2428 0.0392 -0.0068 0.0295 68 SER A CB 368 O OG A SER A 45 ? 0.3301 0.3392 0.2733 0.0434 -0.0064 0.0293 68 SER A OG 369 O OG B SER A 45 ? 0.2921 0.3042 0.2389 0.0336 -0.0070 0.0286 68 SER A OG 370 N N . ASP A 46 ? 0.3195 0.2963 0.2503 0.0451 -0.0048 0.0295 69 ASP A N 371 C CA . ASP A 46 ? 0.3408 0.3075 0.2655 0.0509 -0.0052 0.0300 69 ASP A CA 372 C C . ASP A 46 ? 0.3362 0.2918 0.2568 0.0491 -0.0035 0.0290 69 ASP A C 373 O O . ASP A 46 ? 0.3453 0.2963 0.2630 0.0538 -0.0029 0.0282 69 ASP A O 374 C CB . ASP A 46 ? 0.3624 0.3376 0.2893 0.0584 -0.0052 0.0290 69 ASP A CB 375 C CG . ASP A 46 ? 0.3883 0.3733 0.3201 0.0571 -0.0029 0.0268 69 ASP A CG 376 O OD1 . ASP A 46 ? 0.3494 0.3363 0.2838 0.0502 -0.0016 0.0265 69 ASP A OD1 377 O OD2 . ASP A 46 ? 0.4569 0.4489 0.3902 0.0633 -0.0026 0.0253 69 ASP A OD2 378 N N . SER A 47 ? 0.3177 0.2697 0.2385 0.0426 -0.0029 0.0288 70 SER A N 379 C CA . SER A 47 ? 0.2930 0.2343 0.2093 0.0404 -0.0017 0.0281 70 SER A CA 380 C C . SER A 47 ? 0.3056 0.2424 0.2204 0.0348 -0.0023 0.0282 70 SER A C 381 O O . SER A 47 ? 0.3038 0.2472 0.2231 0.0314 -0.0029 0.0279 70 SER A O 382 C CB . SER A 47 ? 0.2863 0.2317 0.2059 0.0388 0.0001 0.0266 70 SER A CB 383 O OG . SER A 47 ? 0.3035 0.2393 0.2189 0.0364 0.0012 0.0258 70 SER A OG 384 N N . TRP A 48 ? 0.2946 0.2202 0.2028 0.0336 -0.0020 0.0283 71 TRP A N 385 C CA . TRP A 48 ? 0.2920 0.2147 0.1989 0.0280 -0.0020 0.0276 71 TRP A CA 386 C C . TRP A 48 ? 0.2908 0.2161 0.2018 0.0255 -0.0009 0.0258 71 TRP A C 387 O O . TRP A 48 ? 0.3129 0.2415 0.2265 0.0277 0.0000 0.0256 71 TRP A O 388 C CB . TRP A 48 ? 0.3097 0.2204 0.2078 0.0271 -0.0019 0.0282 71 TRP A CB 389 C CG . TRP A 48 ? 0.3255 0.2313 0.2176 0.0284 -0.0038 0.0306 71 TRP A CG 390 C CD1 . TRP A 48 ? 0.3313 0.2368 0.2223 0.0342 -0.0052 0.0324 71 TRP A CD1 391 C CD2 . TRP A 48 ? 0.3525 0.2540 0.2389 0.0234 -0.0046 0.0315 71 TRP A CD2 392 N NE1 . TRP A 48 ? 0.3661 0.2656 0.2504 0.0330 -0.0072 0.0349 71 TRP A NE1 393 C CE2 . TRP A 48 ? 0.3645 0.2618 0.2457 0.0259 -0.0067 0.0344 71 TRP A CE2 394 C CE3 . TRP A 48 ? 0.3257 0.2271 0.2106 0.0169 -0.0039 0.0299 71 TRP A CE3 395 C CZ2 . TRP A 48 ? 0.3891 0.2818 0.2632 0.0214 -0.0080 0.0361 71 TRP A CZ2 396 C CZ3 . TRP A 48 ? 0.3598 0.2584 0.2383 0.0123 -0.0049 0.0312 71 TRP A CZ3 397 C CH2 . TRP A 48 ? 0.3608 0.2551 0.2339 0.0142 -0.0069 0.0344 71 TRP A CH2 398 N N . THR A 49 ? 0.2638 0.1892 0.1758 0.0210 -0.0012 0.0245 72 THR A N 399 C CA . THR A 49 ? 0.2768 0.2038 0.1922 0.0186 -0.0009 0.0230 72 THR A CA 400 C C . THR A 49 ? 0.2597 0.1812 0.1712 0.0156 -0.0005 0.0217 72 THR A C 401 O O . THR A 49 ? 0.3002 0.2171 0.2062 0.0142 -0.0003 0.0219 72 THR A O 402 C CB . THR A 49 ? 0.2437 0.1781 0.1656 0.0168 -0.0024 0.0220 72 THR A CB 403 O OG1 . THR A 49 ? 0.2649 0.2006 0.1865 0.0148 -0.0032 0.0208 72 THR A OG1 404 C CG2 . THR A 49 ? 0.2371 0.1780 0.1630 0.0186 -0.0028 0.0231 72 THR A CG2 405 N N . ILE A 50 ? 0.2795 0.2014 0.1929 0.0141 -0.0004 0.0207 73 ILE A N 406 C CA . ILE A 50 ? 0.2438 0.1619 0.1540 0.0114 0.0000 0.0193 73 ILE A CA 407 C C . ILE A 50 ? 0.2608 0.1833 0.1736 0.0086 -0.0013 0.0170 73 ILE A C 408 O O . ILE A 50 ? 0.2772 0.2052 0.1959 0.0088 -0.0030 0.0158 73 ILE A O 409 C CB . ILE A 50 ? 0.2567 0.1746 0.1682 0.0111 0.0001 0.0191 73 ILE A CB 410 C CG1 . ILE A 50 ? 0.2696 0.1845 0.1783 0.0136 0.0018 0.0206 73 ILE A CG1 411 C CG2 . ILE A 50 ? 0.2473 0.1635 0.1564 0.0080 0.0000 0.0173 73 ILE A CG2 412 C CD1 . ILE A 50 ? 0.2733 0.1907 0.1843 0.0130 0.0018 0.0209 73 ILE A CD1 413 N N . HIS A 51 ? 0.2727 0.1930 0.1806 0.0058 -0.0007 0.0160 74 HIS A N 414 C CA . HIS A 51 ? 0.2633 0.1896 0.1737 0.0028 -0.0017 0.0128 74 HIS A CA 415 C C . HIS A 51 ? 0.2880 0.2136 0.1980 0.0016 -0.0017 0.0115 74 HIS A C 416 O O . HIS A 51 ? 0.2713 0.2019 0.1869 0.0022 -0.0034 0.0095 74 HIS A O 417 C CB . HIS A 51 ? 0.2759 0.2024 0.1810 -0.0006 -0.0010 0.0124 74 HIS A CB 418 C CG . HIS A 51 ? 0.2685 0.2039 0.1764 -0.0037 -0.0018 0.0085 74 HIS A CG 419 N ND1 . HIS A 51 ? 0.2928 0.2309 0.1962 -0.0079 -0.0012 0.0078 74 HIS A ND1 420 C CD2 . HIS A 51 ? 0.3198 0.2627 0.2345 -0.0030 -0.0032 0.0049 74 HIS A CD2 421 C CE1 . HIS A 51 ? 0.2860 0.2347 0.1940 -0.0096 -0.0019 0.0033 74 HIS A CE1 422 N NE2 . HIS A 51 ? 0.2995 0.2507 0.2145 -0.0061 -0.0033 0.0014 74 HIS A NE2 423 N N . GLY A 52 ? 0.2911 0.2105 0.1943 -0.0001 0.0000 0.0124 75 GLY A N 424 C CA . GLY A 52 ? 0.2915 0.2105 0.1938 -0.0016 0.0001 0.0113 75 GLY A CA 425 C C . GLY A 52 ? 0.3111 0.2222 0.2048 -0.0039 0.0021 0.0122 75 GLY A C 426 O O . GLY A 52 ? 0.3112 0.2148 0.1995 -0.0031 0.0032 0.0141 75 GLY A O 427 N N . LEU A 53 ? 0.3170 0.2302 0.2094 -0.0068 0.0021 0.0104 76 LEU A N 428 C CA . LEU A 53 ? 0.3267 0.2338 0.2111 -0.0104 0.0037 0.0102 76 LEU A CA 429 C C . LEU A 53 ? 0.3237 0.2380 0.2077 -0.0152 0.0033 0.0073 76 LEU A C 430 O O . LEU A 53 ? 0.3087 0.2315 0.1989 -0.0144 0.0017 0.0053 76 LEU A O 431 C CB . LEU A 53 ? 0.3414 0.2447 0.2251 -0.0085 0.0043 0.0111 76 LEU A CB 432 C CG . LEU A 53 ? 0.3365 0.2326 0.2112 -0.0123 0.0061 0.0105 76 LEU A CG 433 C CD1 . LEU A 53 ? 0.3221 0.2064 0.1883 -0.0123 0.0074 0.0119 76 LEU A CD1 434 C CD2 . LEU A 53 ? 0.3629 0.2586 0.2381 -0.0109 0.0065 0.0107 76 LEU A CD2 435 N N . TRP A 54 ? 0.3215 0.2333 0.1984 -0.0201 0.0044 0.0068 77 TRP A N 436 C CA . TRP A 54 ? 0.3288 0.2500 0.2053 -0.0256 0.0043 0.0037 77 TRP A CA 437 C C . TRP A 54 ? 0.3466 0.2624 0.2134 -0.0319 0.0058 0.0034 77 TRP A C 438 O O . TRP A 54 ? 0.3564 0.2599 0.2138 -0.0343 0.0070 0.0056 77 TRP A O 439 C CB . TRP A 54 ? 0.3457 0.2714 0.2215 -0.0283 0.0042 0.0030 77 TRP A CB 440 C CG . TRP A 54 ? 0.3248 0.2545 0.2083 -0.0232 0.0029 0.0033 77 TRP A CG 441 C CD1 . TRP A 54 ? 0.3199 0.2531 0.2126 -0.0170 0.0013 0.0031 77 TRP A CD1 442 C CD2 . TRP A 54 ? 0.3367 0.2681 0.2193 -0.0243 0.0028 0.0039 77 TRP A CD2 443 N NE1 . TRP A 54 ? 0.3379 0.2741 0.2351 -0.0144 0.0004 0.0032 77 TRP A NE1 444 C CE2 . TRP A 54 ? 0.3062 0.2420 0.1978 -0.0185 0.0013 0.0036 77 TRP A CE2 445 C CE3 . TRP A 54 ? 0.3545 0.2832 0.2289 -0.0300 0.0036 0.0049 77 TRP A CE3 446 C CZ2 . TRP A 54 ? 0.3419 0.2806 0.2351 -0.0180 0.0009 0.0039 77 TRP A CZ2 447 C CZ3 . TRP A 54 ? 0.3751 0.3071 0.2510 -0.0295 0.0030 0.0055 77 TRP A CZ3 448 C CH2 . TRP A 54 ? 0.3517 0.2890 0.2371 -0.0235 0.0018 0.0048 77 TRP A CH2 449 N N . PRO A 55 ? 0.3677 0.2924 0.2359 -0.0350 0.0056 0.0005 78 PRO A N 450 C CA . PRO A 55 ? 0.4121 0.3338 0.2709 -0.0425 0.0071 -0.0004 78 PRO A CA 451 C C . PRO A 55 ? 0.4224 0.3511 0.2773 -0.0498 0.0075 -0.0022 78 PRO A C 452 O O . PRO A 55 ? 0.4661 0.4106 0.3281 -0.0501 0.0065 -0.0056 78 PRO A O 453 C CB . PRO A 55 ? 0.4031 0.3346 0.2666 -0.0423 0.0062 -0.0030 78 PRO A CB 454 C CG . PRO A 55 ? 0.3863 0.3304 0.2627 -0.0359 0.0036 -0.0046 78 PRO A CG 455 C CD . PRO A 55 ? 0.3631 0.2999 0.2417 -0.0310 0.0035 -0.0019 78 PRO A CD 456 N N . ASP A 56 ? 0.4134 0.3309 0.2573 -0.0552 0.0086 -0.0001 79 ASP A N 457 C CA . ASP A 56 ? 0.4156 0.3397 0.2537 -0.0642 0.0091 -0.0016 79 ASP A CA 458 C C . ASP A 56 ? 0.4217 0.3430 0.2503 -0.0726 0.0103 -0.0027 79 ASP A C 459 O O . ASP A 56 ? 0.4038 0.3111 0.2265 -0.0718 0.0109 -0.0011 79 ASP A O 460 C CB . ASP A 56 ? 0.4391 0.3500 0.2681 -0.0667 0.0092 0.0022 79 ASP A CB 461 C CG . ASP A 56 ? 0.4959 0.4137 0.3321 -0.0624 0.0082 0.0026 79 ASP A CG 462 O OD1 . ASP A 56 ? 0.4956 0.4241 0.3442 -0.0553 0.0073 0.0006 79 ASP A OD1 463 O OD2 . ASP A 56 ? 0.5253 0.4349 0.3525 -0.0669 0.0081 0.0055 79 ASP A OD2 464 N N . ASN A 57 ? 0.3990 0.3338 0.2256 -0.0811 0.0108 -0.0057 80 ASN A N 465 C CA . ASN A 57 ? 0.4305 0.3618 0.2451 -0.0919 0.0120 -0.0063 80 ASN A CA 466 C C . ASN A 57 ? 0.4438 0.3523 0.2432 -0.0970 0.0123 -0.0018 80 ASN A C 467 O O . ASN A 57 ? 0.4534 0.3527 0.2517 -0.0932 0.0115 0.0015 80 ASN A O 468 C CB . ASN A 57 ? 0.4364 0.3891 0.2525 -0.1002 0.0124 -0.0106 80 ASN A CB 469 C CG . ASN A 57 ? 0.4587 0.4323 0.2889 -0.0945 0.0115 -0.0153 80 ASN A CG 470 O OD1 . ASN A 57 ? 0.4747 0.4453 0.3092 -0.0887 0.0110 -0.0152 80 ASN A OD1 471 N ND2 . ASN A 57 ? 0.4854 0.4797 0.3239 -0.0945 0.0110 -0.0194 80 ASN A ND2 472 N N . CYS A 58 ? 0.4586 0.3567 0.2460 -0.1049 0.0132 -0.0015 81 CYS A N 473 C CA . CYS A 58 ? 0.4881 0.3616 0.2598 -0.1093 0.0129 0.0026 81 CYS A CA 474 C C . CYS A 58 ? 0.5098 0.3825 0.2735 -0.1172 0.0122 0.0048 81 CYS A C 475 O O . CYS A 58 ? 0.5150 0.3671 0.2681 -0.1177 0.0110 0.0091 81 CYS A O 476 C CB . CYS A 58 ? 0.5319 0.3944 0.2922 -0.1164 0.0137 0.0017 81 CYS A CB 477 S SG . CYS A 58 ? 0.5470 0.4101 0.3166 -0.1063 0.0143 -0.0003 81 CYS A SG 478 N N . ASP A 59 ? 0.5157 0.4110 0.2844 -0.1231 0.0128 0.0016 82 ASP A N 479 C CA . ASP A 59 ? 0.5499 0.4482 0.3117 -0.1315 0.0125 0.0032 82 ASP A CA 480 C C . ASP A 59 ? 0.5391 0.4441 0.3112 -0.1230 0.0115 0.0041 82 ASP A C 481 O O . ASP A 59 ? 0.5610 0.4706 0.3289 -0.1289 0.0112 0.0052 82 ASP A O 482 C CB . ASP A 59 ? 0.5479 0.4683 0.3080 -0.1441 0.0138 -0.0012 82 ASP A CB 483 C CG . ASP A 59 ? 0.5801 0.5292 0.3576 -0.1388 0.0145 -0.0072 82 ASP A CG 484 O OD1 . ASP A 59 ? 0.5676 0.5182 0.3580 -0.1257 0.0137 -0.0076 82 ASP A OD1 485 O OD2 . ASP A 59 ? 0.6564 0.6274 0.4349 -0.1475 0.0155 -0.0117 82 ASP A OD2 486 N N . GLY A 60 ? 0.5102 0.4159 0.2949 -0.1099 0.0111 0.0037 83 GLY A N 487 C CA . GLY A 60 ? 0.5140 0.4272 0.3089 -0.1021 0.0102 0.0041 83 GLY A CA 488 C C . GLY A 60 ? 0.4895 0.4294 0.2990 -0.0996 0.0105 -0.0015 83 GLY A C 489 O O . GLY A 60 ? 0.4849 0.4303 0.3037 -0.0922 0.0097 -0.0016 83 GLY A O 490 N N . THR A 61 ? 0.4799 0.4366 0.2917 -0.1053 0.0115 -0.0063 84 THR A N 491 C CA . THR A 61 ? 0.4719 0.4527 0.2986 -0.1004 0.0113 -0.0121 84 THR A CA 492 C C . THR A 61 ? 0.4694 0.4469 0.3070 -0.0883 0.0102 -0.0124 84 THR A C 493 O O . THR A 61 ? 0.4345 0.3931 0.2675 -0.0849 0.0101 -0.0084 84 THR A O 494 C CB . THR A 61 ? 0.4913 0.4927 0.3175 -0.1097 0.0123 -0.0176 84 THR A CB 495 O OG1 . THR A 61 ? 0.4840 0.4773 0.3042 -0.1129 0.0129 -0.0170 84 THR A OG1 496 C CG2 . THR A 61 ? 0.4662 0.4738 0.2816 -0.1231 0.0134 -0.0175 84 THR A CG2 497 N N . TYR A 62 ? 0.4659 0.4605 0.3171 -0.0816 0.0091 -0.0170 85 TYR A N 498 C CA . TYR A 62 ? 0.4819 0.4716 0.3414 -0.0714 0.0078 -0.0165 85 TYR A CA 499 C C . TYR A 62 ? 0.4731 0.4828 0.3443 -0.0676 0.0064 -0.0222 85 TYR A C 500 O O . TYR A 62 ? 0.4650 0.4922 0.3396 -0.0706 0.0064 -0.0268 85 TYR A O 501 C CB . TYR A 62 ? 0.5000 0.4791 0.3643 -0.0626 0.0068 -0.0131 85 TYR A CB 502 C CG . TYR A 62 ? 0.5015 0.4921 0.3728 -0.0602 0.0060 -0.0155 85 TYR A CG 503 C CD1 . TYR A 62 ? 0.5577 0.5596 0.4421 -0.0520 0.0040 -0.0192 85 TYR A CD1 504 C CD2 . TYR A 62 ? 0.5351 0.5239 0.3993 -0.0662 0.0069 -0.0138 85 TYR A CD2 505 C CE1 . TYR A 62 ? 0.5805 0.5922 0.4716 -0.0492 0.0032 -0.0219 85 TYR A CE1 506 C CE2 . TYR A 62 ? 0.5884 0.5880 0.4591 -0.0640 0.0063 -0.0161 85 TYR A CE2 507 C CZ . TYR A 62 ? 0.6301 0.6417 0.5145 -0.0555 0.0045 -0.0206 85 TYR A CZ 508 O OH . TYR A 62 ? 0.6539 0.6759 0.5453 -0.0526 0.0037 -0.0237 85 TYR A OH 509 N N A GLN A 63 ? 0.4711 0.4788 0.3470 -0.0619 0.0051 -0.0222 86 GLN A N 510 N N B GLN A 63 ? 0.4714 0.4790 0.3480 -0.0612 0.0050 -0.0221 86 GLN A N 511 C CA A GLN A 63 ? 0.4576 0.4815 0.3455 -0.0555 0.0026 -0.0270 86 GLN A CA 512 C CA B GLN A 63 ? 0.4588 0.4833 0.3471 -0.0555 0.0026 -0.0272 86 GLN A CA 513 C C A GLN A 63 ? 0.4175 0.4363 0.3145 -0.0450 0.0004 -0.0257 86 GLN A C 514 C C B GLN A 63 ? 0.4177 0.4364 0.3148 -0.0449 0.0003 -0.0257 86 GLN A C 515 O O A GLN A 63 ? 0.3912 0.3947 0.2850 -0.0430 0.0010 -0.0211 86 GLN A O 516 O O B GLN A 63 ? 0.3929 0.3961 0.2869 -0.0427 0.0010 -0.0210 86 GLN A O 517 C CB A GLN A 63 ? 0.4709 0.4952 0.3589 -0.0549 0.0018 -0.0272 86 GLN A CB 518 C CB B GLN A 63 ? 0.4709 0.4976 0.3588 -0.0559 0.0020 -0.0278 86 GLN A CB 519 C CG A GLN A 63 ? 0.5148 0.5337 0.3907 -0.0649 0.0042 -0.0259 86 GLN A CG 520 C CG B GLN A 63 ? 0.5119 0.5389 0.3885 -0.0673 0.0045 -0.0280 86 GLN A CG 521 C CD A GLN A 63 ? 0.5143 0.5405 0.3929 -0.0639 0.0029 -0.0278 86 GLN A CD 522 C CD B GLN A 63 ? 0.5456 0.5927 0.4223 -0.0745 0.0052 -0.0332 86 GLN A CD 523 O OE1 A GLN A 63 ? 0.5511 0.5650 0.4269 -0.0618 0.0028 -0.0245 86 GLN A OE1 524 O OE1 B GLN A 63 ? 0.5937 0.6607 0.4802 -0.0710 0.0033 -0.0388 86 GLN A OE1 525 N NE2 A GLN A 63 ? 0.4796 0.5272 0.3641 -0.0651 0.0016 -0.0334 86 GLN A NE2 526 N NE2 B GLN A 63 ? 0.5146 0.5572 0.3802 -0.0847 0.0077 -0.0317 86 GLN A NE2 527 N N . GLU A 64 ? 0.3995 0.4314 0.3074 -0.0385 -0.0025 -0.0302 87 GLU A N 528 C CA . GLU A 64 ? 0.3751 0.4027 0.2914 -0.0291 -0.0052 -0.0296 87 GLU A CA 529 C C . GLU A 64 ? 0.3691 0.4062 0.2947 -0.0222 -0.0091 -0.0333 87 GLU A C 530 O O . GLU A 64 ? 0.3993 0.4531 0.3277 -0.0237 -0.0098 -0.0387 87 GLU A O 531 C CB . GLU A 64 ? 0.3602 0.3936 0.2794 -0.0288 -0.0048 -0.0320 87 GLU A CB 532 C CG . GLU A 64 ? 0.4270 0.4813 0.3496 -0.0320 -0.0047 -0.0389 87 GLU A CG 533 C CD . GLU A 64 ? 0.4872 0.5446 0.4119 -0.0316 -0.0041 -0.0404 87 GLU A CD 534 O OE1 . GLU A 64 ? 0.6339 0.6876 0.5503 -0.0389 -0.0014 -0.0378 87 GLU A OE1 535 O OE2 . GLU A 64 ? 0.5196 0.5789 0.4526 -0.0241 -0.0066 -0.0427 87 GLU A OE2 536 N N . TYR A 65 ? 0.3537 0.3809 0.2836 -0.0147 -0.0118 -0.0306 88 TYR A N 537 C CA . TYR A 65 ? 0.3343 0.3685 0.2727 -0.0074 -0.0165 -0.0338 88 TYR A CA 538 C C . TYR A 65 ? 0.3439 0.3860 0.2810 -0.0095 -0.0173 -0.0352 88 TYR A C 539 O O . TYR A 65 ? 0.3218 0.3809 0.2647 -0.0076 -0.0195 -0.0413 88 TYR A O 540 C CB . TYR A 65 ? 0.3536 0.4017 0.3006 -0.0029 -0.0189 -0.0406 88 TYR A CB 541 C CG . TYR A 65 ? 0.3343 0.3741 0.2832 0.0000 -0.0188 -0.0393 88 TYR A CG 542 C CD1 . TYR A 65 ? 0.2758 0.3021 0.2272 0.0060 -0.0216 -0.0356 88 TYR A CD1 543 C CD2 . TYR A 65 ? 0.3327 0.3782 0.2799 -0.0043 -0.0158 -0.0412 88 TYR A CD2 544 C CE1 . TYR A 65 ? 0.3019 0.3219 0.2551 0.0083 -0.0217 -0.0348 88 TYR A CE1 545 C CE2 . TYR A 65 ? 0.3107 0.3490 0.2593 -0.0021 -0.0157 -0.0398 88 TYR A CE2 546 C CZ . TYR A 65 ? 0.2945 0.3210 0.2466 0.0044 -0.0187 -0.0371 88 TYR A CZ 547 O OH . TYR A 65 ? 0.2798 0.2995 0.2331 0.0062 -0.0187 -0.0357 88 TYR A OH 548 N N . CYS A 66 ? 0.3519 0.3831 0.2816 -0.0134 -0.0154 -0.0301 89 CYS A N 549 C CA . CYS A 66 ? 0.3641 0.4030 0.2903 -0.0181 -0.0149 -0.0314 89 CYS A CA 550 C C . CYS A 66 ? 0.3552 0.3971 0.2865 -0.0120 -0.0196 -0.0316 89 CYS A C 551 O O . CYS A 66 ? 0.3664 0.4185 0.2969 -0.0146 -0.0202 -0.0338 89 CYS A O 552 C CB . CYS A 66 ? 0.3784 0.4048 0.2937 -0.0254 -0.0108 -0.0267 89 CYS A CB 553 S SG . CYS A 66 ? 0.4345 0.4571 0.3410 -0.0344 -0.0058 -0.0262 89 CYS A SG 554 N N . ASP A 67 ? 0.3440 0.3773 0.2802 -0.0043 -0.0233 -0.0294 90 ASP A N 555 C CA . ASP A 67 ? 0.3570 0.3910 0.2967 0.0012 -0.0283 -0.0287 90 ASP A CA 556 C C . ASP A 67 ? 0.3470 0.3771 0.2941 0.0103 -0.0337 -0.0291 90 ASP A C 557 O O . ASP A 67 ? 0.3293 0.3442 0.2745 0.0121 -0.0346 -0.0238 90 ASP A O 558 C CB . ASP A 67 ? 0.3445 0.3657 0.2770 -0.0019 -0.0272 -0.0224 90 ASP A CB 559 C CG . ASP A 67 ? 0.3957 0.4205 0.3301 0.0016 -0.0321 -0.0218 90 ASP A CG 560 O OD1 . ASP A 67 ? 0.3759 0.4106 0.3178 0.0081 -0.0372 -0.0257 90 ASP A OD1 561 O OD2 . ASP A 67 ? 0.3915 0.4091 0.3197 -0.0020 -0.0309 -0.0175 90 ASP A OD2 562 N N A GLU A 68 ? 0.3532 0.3969 0.3082 0.0158 -0.0374 -0.0355 91 GLU A N 563 N N B GLU A 68 ? 0.3573 0.4014 0.3121 0.0157 -0.0374 -0.0356 91 GLU A N 564 C CA A GLU A 68 ? 0.3697 0.4093 0.3315 0.0250 -0.0431 -0.0369 91 GLU A CA 565 C CA B GLU A 68 ? 0.3768 0.4183 0.3391 0.0251 -0.0433 -0.0376 91 GLU A CA 566 C C A GLU A 68 ? 0.3785 0.4059 0.3392 0.0292 -0.0484 -0.0317 91 GLU A C 567 C C B GLU A 68 ? 0.3824 0.4106 0.3433 0.0293 -0.0483 -0.0320 91 GLU A C 568 O O A GLU A 68 ? 0.3875 0.4029 0.3501 0.0345 -0.0523 -0.0295 91 GLU A O 569 O O B GLU A 68 ? 0.3930 0.4092 0.3558 0.0344 -0.0521 -0.0298 91 GLU A O 570 C CB A GLU A 68 ? 0.3848 0.4428 0.3554 0.0309 -0.0466 -0.0458 91 GLU A CB 571 C CB B GLU A 68 ? 0.3964 0.4579 0.3672 0.0307 -0.0469 -0.0465 91 GLU A CB 572 C CG A GLU A 68 ? 0.4219 0.4746 0.3994 0.0412 -0.0532 -0.0481 91 GLU A CG 573 C CG B GLU A 68 ? 0.4458 0.5234 0.4181 0.0261 -0.0422 -0.0528 91 GLU A CG 574 C CD A GLU A 68 ? 0.4770 0.5481 0.4631 0.0467 -0.0552 -0.0580 91 GLU A CD 575 C CD B GLU A 68 ? 0.5281 0.6300 0.5080 0.0298 -0.0448 -0.0621 91 GLU A CD 576 O OE1 A GLU A 68 ? 0.4782 0.5679 0.4650 0.0419 -0.0514 -0.0630 91 GLU A OE1 577 O OE1 B GLU A 68 ? 0.5152 0.6209 0.5010 0.0385 -0.0512 -0.0646 91 GLU A OE1 578 O OE2 A GLU A 68 ? 0.5396 0.6066 0.5315 0.0555 -0.0607 -0.0610 91 GLU A OE2 579 O OE2 B GLU A 68 ? 0.5821 0.6996 0.5617 0.0237 -0.0403 -0.0668 91 GLU A OE2 580 N N . SER A 69 ? 0.3726 0.4026 0.3295 0.0263 -0.0485 -0.0294 92 SER A N 581 C CA . SER A 69 ? 0.3950 0.4141 0.3499 0.0294 -0.0535 -0.0240 92 SER A CA 582 C C . SER A 69 ? 0.3767 0.3771 0.3251 0.0257 -0.0510 -0.0163 92 SER A C 583 O O . SER A 69 ? 0.3849 0.3743 0.3314 0.0279 -0.0552 -0.0115 92 SER A O 584 C CB . SER A 69 ? 0.3904 0.4189 0.3428 0.0268 -0.0542 -0.0239 92 SER A CB 585 O OG . SER A 69 ? 0.3915 0.4151 0.3356 0.0179 -0.0482 -0.0196 92 SER A OG 586 N N . ARG A 70 ? 0.3498 0.3472 0.2946 0.0199 -0.0445 -0.0154 93 ARG A N 587 C CA . ARG A 70 ? 0.3291 0.3111 0.2685 0.0169 -0.0419 -0.0090 93 ARG A CA 588 C C . ARG A 70 ? 0.3471 0.3246 0.2887 0.0177 -0.0397 -0.0099 93 ARG A C 589 O O . ARG A 70 ? 0.3254 0.2952 0.2626 0.0138 -0.0354 -0.0065 93 ARG A O 590 C CB . ARG A 70 ? 0.3357 0.3155 0.2674 0.0095 -0.0363 -0.0060 93 ARG A CB 591 C CG . ARG A 70 ? 0.3525 0.3352 0.2809 0.0079 -0.0381 -0.0043 93 ARG A CG 592 C CD . ARG A 70 ? 0.3631 0.3425 0.2835 0.0006 -0.0326 -0.0018 93 ARG A CD 593 N NE . ARG A 70 ? 0.3287 0.3138 0.2472 -0.0039 -0.0275 -0.0054 93 ARG A NE 594 C CZ . ARG A 70 ? 0.3254 0.3034 0.2390 -0.0079 -0.0222 -0.0042 93 ARG A CZ 595 N NH1 . ARG A 70 ? 0.3005 0.2667 0.2110 -0.0080 -0.0206 0.0001 93 ARG A NH1 596 N NH2 . ARG A 70 ? 0.3238 0.3073 0.2350 -0.0124 -0.0186 -0.0075 93 ARG A NH2 597 N N . GLU A 71 ? 0.3415 0.3242 0.2899 0.0231 -0.0430 -0.0147 94 GLU A N 598 C CA . GLU A 71 ? 0.3438 0.3216 0.2947 0.0247 -0.0422 -0.0155 94 GLU A CA 599 C C . GLU A 71 ? 0.3394 0.3051 0.2918 0.0294 -0.0478 -0.0125 94 GLU A C 600 O O . GLU A 71 ? 0.3378 0.3023 0.2922 0.0342 -0.0539 -0.0128 94 GLU A O 601 C CB . GLU A 71 ? 0.3372 0.3286 0.2943 0.0273 -0.0424 -0.0231 94 GLU A CB 602 C CG . GLU A 71 ? 0.3787 0.3800 0.3327 0.0207 -0.0363 -0.0252 94 GLU A CG 603 C CD . GLU A 71 ? 0.4613 0.4784 0.4214 0.0225 -0.0363 -0.0332 94 GLU A CD 604 O OE1 . GLU A 71 ? 0.5843 0.6022 0.5505 0.0287 -0.0401 -0.0367 94 GLU A OE1 605 O OE2 . GLU A 71 ? 0.5009 0.5301 0.4596 0.0178 -0.0330 -0.0364 94 GLU A OE2 606 N N . TYR A 72 ? 0.3077 0.2637 0.2583 0.0278 -0.0459 -0.0092 95 TYR A N 607 C CA . TYR A 72 ? 0.3139 0.2567 0.2638 0.0299 -0.0503 -0.0053 95 TYR A CA 608 C C . TYR A 72 ? 0.3237 0.2623 0.2766 0.0317 -0.0507 -0.0069 95 TYR A C 609 O O . TYR A 72 ? 0.3196 0.2641 0.2738 0.0298 -0.0460 -0.0095 95 TYR A O 610 C CB . TYR A 72 ? 0.3237 0.2578 0.2665 0.0243 -0.0474 0.0021 95 TYR A CB 611 C CG . TYR A 72 ? 0.2974 0.2349 0.2369 0.0226 -0.0479 0.0039 95 TYR A CG 612 C CD1 . TYR A 72 ? 0.3295 0.2652 0.2697 0.0264 -0.0546 0.0044 95 TYR A CD1 613 C CD2 . TYR A 72 ? 0.3500 0.2917 0.2852 0.0175 -0.0421 0.0048 95 TYR A CD2 614 C CE1 . TYR A 72 ? 0.3639 0.3042 0.3013 0.0249 -0.0552 0.0056 95 TYR A CE1 615 C CE2 . TYR A 72 ? 0.3312 0.2765 0.2633 0.0157 -0.0425 0.0058 95 TYR A CE2 616 C CZ . TYR A 72 ? 0.3506 0.2958 0.2838 0.0190 -0.0487 0.0063 95 TYR A CZ 617 O OH . TYR A 72 ? 0.3377 0.2879 0.2677 0.0169 -0.0490 0.0072 95 TYR A OH 618 N N A SER A 73 ? 0.3169 0.2450 0.2705 0.0351 -0.0566 -0.0055 96 SER A N 619 N N B SER A 73 ? 0.3239 0.2519 0.2773 0.0349 -0.0565 -0.0052 96 SER A N 620 C CA A SER A 73 ? 0.3239 0.2460 0.2795 0.0363 -0.0575 -0.0066 96 SER A CA 621 C CA B SER A 73 ? 0.3377 0.2600 0.2934 0.0364 -0.0577 -0.0066 96 SER A CA 622 C C A SER A 73 ? 0.3309 0.2392 0.2812 0.0326 -0.0587 0.0005 96 SER A C 623 C C B SER A 73 ? 0.3372 0.2455 0.2875 0.0328 -0.0589 0.0004 96 SER A C 624 O O A SER A 73 ? 0.3267 0.2266 0.2775 0.0337 -0.0618 0.0006 96 SER A O 625 O O B SER A 73 ? 0.3352 0.2351 0.2861 0.0339 -0.0621 0.0004 96 SER A O 626 C CB A SER A 73 ? 0.3460 0.2675 0.3072 0.0438 -0.0642 -0.0125 96 SER A CB 627 C CB B SER A 73 ? 0.3607 0.2836 0.3221 0.0441 -0.0642 -0.0129 96 SER A CB 628 O OG A SER A 73 ? 0.3418 0.2567 0.3017 0.0473 -0.0707 -0.0107 96 SER A OG 629 O OG B SER A 73 ? 0.3895 0.3286 0.3558 0.0465 -0.0622 -0.0198 96 SER A OG 630 N N . ASN A 74 ? 0.3199 0.2268 0.2649 0.0277 -0.0557 0.0061 97 ASN A N 631 C CA . ASN A 74 ? 0.3455 0.2411 0.2850 0.0235 -0.0569 0.0128 97 ASN A CA 632 C C . ASN A 74 ? 0.3378 0.2362 0.2728 0.0177 -0.0508 0.0170 97 ASN A C 633 O O . ASN A 74 ? 0.3240 0.2177 0.2539 0.0142 -0.0516 0.0221 97 ASN A O 634 C CB . ASN A 74 ? 0.3469 0.2336 0.2834 0.0249 -0.0640 0.0160 97 ASN A CB 635 C CG . ASN A 74 ? 0.3719 0.2650 0.3068 0.0249 -0.0637 0.0167 97 ASN A CG 636 O OD1 . ASN A 74 ? 0.3153 0.2194 0.2519 0.0245 -0.0587 0.0137 97 ASN A OD1 637 N ND2 . ASN A 74 ? 0.4309 0.3168 0.3620 0.0251 -0.0693 0.0207 97 ASN A ND2 638 N N . ILE A 75 ? 0.3245 0.2300 0.2610 0.0165 -0.0448 0.0148 98 ILE A N 639 C CA . ILE A 75 ? 0.2991 0.2071 0.2316 0.0120 -0.0389 0.0179 98 ILE A CA 640 C C . ILE A 75 ? 0.3110 0.2130 0.2398 0.0081 -0.0387 0.0230 98 ILE A C 641 O O . ILE A 75 ? 0.2994 0.2014 0.2238 0.0046 -0.0366 0.0266 98 ILE A O 642 C CB . ILE A 75 ? 0.2749 0.1898 0.2093 0.0119 -0.0333 0.0147 98 ILE A CB 643 C CG1 . ILE A 75 ? 0.2955 0.2183 0.2322 0.0138 -0.0323 0.0098 98 ILE A CG1 644 C CG2 . ILE A 75 ? 0.2768 0.1922 0.2066 0.0081 -0.0278 0.0180 98 ILE A CG2 645 C CD1 . ILE A 75 ? 0.2561 0.1816 0.1896 0.0124 -0.0317 0.0104 98 ILE A CD1 646 N N . THR A 76 ? 0.3117 0.2092 0.2421 0.0082 -0.0408 0.0233 99 THR A N 647 C CA . THR A 76 ? 0.3251 0.2185 0.2520 0.0036 -0.0404 0.0280 99 THR A CA 648 C C . THR A 76 ? 0.3405 0.2271 0.2623 0.0008 -0.0447 0.0326 99 THR A C 649 O O . THR A 76 ? 0.3326 0.2197 0.2497 -0.0041 -0.0427 0.0368 99 THR A O 650 C CB . THR A 76 ? 0.3430 0.2318 0.2722 0.0038 -0.0432 0.0270 99 THR A CB 651 O OG1 . THR A 76 ? 0.3464 0.2422 0.2796 0.0057 -0.0391 0.0233 99 THR A OG1 652 C CG2 . THR A 76 ? 0.3657 0.2506 0.2908 -0.0020 -0.0434 0.0320 99 THR A CG2 653 N N . SER A 77 ? 0.3458 0.2267 0.2682 0.0040 -0.0507 0.0318 100 SER A N 654 C CA . SER A 77 ? 0.3501 0.2238 0.2670 0.0015 -0.0555 0.0366 100 SER A CA 655 C C . SER A 77 ? 0.3591 0.2389 0.2730 -0.0004 -0.0524 0.0383 100 SER A C 656 O O . SER A 77 ? 0.3269 0.2040 0.2347 -0.0053 -0.0533 0.0433 100 SER A O 657 C CB . SER A 77 ? 0.3854 0.2513 0.3038 0.0068 -0.0634 0.0350 100 SER A CB 658 O OG . SER A 77 ? 0.4290 0.2873 0.3491 0.0079 -0.0667 0.0337 100 SER A OG 659 N N . ILE A 78 ? 0.3301 0.2183 0.2474 0.0028 -0.0488 0.0339 101 ILE A N 660 C CA . ILE A 78 ? 0.3158 0.2099 0.2299 0.0008 -0.0454 0.0347 101 ILE A CA 661 C C . ILE A 78 ? 0.3008 0.1978 0.2114 -0.0042 -0.0396 0.0372 101 ILE A C 662 O O . ILE A 78 ? 0.3321 0.2294 0.2375 -0.0082 -0.0392 0.0407 101 ILE A O 663 C CB . ILE A 78 ? 0.3095 0.2115 0.2275 0.0042 -0.0425 0.0294 101 ILE A CB 664 C CG1 . ILE A 78 ? 0.3276 0.2299 0.2489 0.0091 -0.0481 0.0266 101 ILE A CG1 665 C CG2 . ILE A 78 ? 0.3135 0.2212 0.2276 0.0010 -0.0371 0.0298 101 ILE A CG2 666 C CD1 . ILE A 78 ? 0.3127 0.2241 0.2388 0.0123 -0.0455 0.0204 101 ILE A CD1 667 N N . LEU A 79 ? 0.2961 0.1956 0.2092 -0.0040 -0.0357 0.0356 102 LEU A N 668 C CA . LEU A 79 ? 0.3197 0.2230 0.2300 -0.0077 -0.0306 0.0374 102 LEU A CA 669 C C . LEU A 79 ? 0.3087 0.2089 0.2147 -0.0130 -0.0327 0.0425 102 LEU A C 670 O O . LEU A 79 ? 0.3198 0.2241 0.2216 -0.0170 -0.0297 0.0446 102 LEU A O 671 C CB . LEU A 79 ? 0.3200 0.2270 0.2338 -0.0059 -0.0264 0.0348 102 LEU A CB 672 C CG . LEU A 79 ? 0.3435 0.2539 0.2603 -0.0020 -0.0238 0.0302 102 LEU A CG 673 C CD1 . LEU A 79 ? 0.3371 0.2502 0.2569 -0.0004 -0.0206 0.0282 102 LEU A CD1 674 C CD2 . LEU A 79 ? 0.3153 0.2287 0.2287 -0.0028 -0.0202 0.0294 102 LEU A CD2 675 N N . GLU A 80 ? 0.3518 0.2452 0.2581 -0.0136 -0.0376 0.0442 103 GLU A N 676 C CA . GLU A 80 ? 0.3695 0.2587 0.2705 -0.0199 -0.0404 0.0495 103 GLU A CA 677 C C . GLU A 80 ? 0.4032 0.2898 0.2983 -0.0231 -0.0434 0.0533 103 GLU A C 678 O O . GLU A 80 ? 0.3834 0.2729 0.2733 -0.0291 -0.0418 0.0568 103 GLU A O 679 C CB . GLU A 80 ? 0.3980 0.2774 0.2996 -0.0198 -0.0463 0.0505 103 GLU A CB 680 C CG . GLU A 80 ? 0.4244 0.3072 0.3305 -0.0188 -0.0432 0.0478 103 GLU A CG 681 C CD . GLU A 80 ? 0.4818 0.3551 0.3901 -0.0169 -0.0487 0.0466 103 GLU A CD 682 O OE1 . GLU A 80 ? 0.5174 0.3822 0.4257 -0.0135 -0.0545 0.0461 103 GLU A OE1 683 O OE2 . GLU A 80 ? 0.5269 0.4027 0.4375 -0.0181 -0.0467 0.0455 103 GLU A OE2 684 N N . ALA A 81 ? 0.4066 0.2891 0.3024 -0.0190 -0.0475 0.0524 104 ALA A N 685 C CA . ALA A 81 ? 0.4094 0.2897 0.2997 -0.0215 -0.0508 0.0559 104 ALA A CA 686 C C . ALA A 81 ? 0.4041 0.2945 0.2919 -0.0243 -0.0445 0.0554 104 ALA A C 687 O O . ALA A 81 ? 0.4070 0.2982 0.2890 -0.0289 -0.0454 0.0590 104 ALA A O 688 C CB . ALA A 81 ? 0.4199 0.2962 0.3129 -0.0154 -0.0561 0.0538 104 ALA A CB 689 N N . GLN A 82 ? 0.3615 0.2592 0.2534 -0.0215 -0.0383 0.0509 105 GLN A N 690 C CA . GLN A 82 ? 0.3568 0.2627 0.2465 -0.0232 -0.0324 0.0495 105 GLN A CA 691 C C . GLN A 82 ? 0.3728 0.2839 0.2605 -0.0273 -0.0279 0.0506 105 GLN A C 692 O O . GLN A 82 ? 0.3520 0.2700 0.2383 -0.0280 -0.0226 0.0486 105 GLN A O 693 C CB . GLN A 82 ? 0.3555 0.2650 0.2493 -0.0182 -0.0286 0.0441 105 GLN A CB 694 C CG . GLN A 82 ? 0.3212 0.2288 0.2164 -0.0150 -0.0327 0.0427 105 GLN A CG 695 C CD . GLN A 82 ? 0.3400 0.2515 0.2388 -0.0111 -0.0296 0.0375 105 GLN A CD 696 O OE1 . GLN A 82 ? 0.3396 0.2543 0.2386 -0.0110 -0.0240 0.0350 105 GLN A OE1 697 N NE2 . GLN A 82 ? 0.3264 0.2379 0.2276 -0.0081 -0.0334 0.0357 105 GLN A NE2 698 N N . ASN A 83 ? 0.3439 0.2522 0.2319 -0.0297 -0.0301 0.0531 106 ASN A N 699 C CA . ASN A 83 ? 0.3869 0.3021 0.2737 -0.0339 -0.0261 0.0540 106 ASN A CA 700 C C . ASN A 83 ? 0.3842 0.3064 0.2754 -0.0297 -0.0200 0.0493 106 ASN A C 701 O O . ASN A 83 ? 0.3781 0.3089 0.2683 -0.0317 -0.0156 0.0486 106 ASN A O 702 C CB . ASN A 83 ? 0.4169 0.3374 0.2972 -0.0405 -0.0250 0.0569 106 ASN A CB 703 C CG . ASN A 83 ? 0.4721 0.3845 0.3469 -0.0444 -0.0317 0.0620 106 ASN A CG 704 O OD1 . ASN A 83 ? 0.4469 0.3501 0.3209 -0.0457 -0.0373 0.0652 106 ASN A OD1 705 N ND2 . ASN A 83 ? 0.4904 0.4050 0.3613 -0.0456 -0.0315 0.0625 106 ASN A ND2 706 N N . ARG A 84 ? 0.3444 0.2635 0.2406 -0.0238 -0.0200 0.0460 107 ARG A N 707 C CA . ARG A 84 ? 0.3384 0.2626 0.2379 -0.0198 -0.0147 0.0420 107 ARG A CA 708 C C . ARG A 84 ? 0.3564 0.2816 0.2599 -0.0191 -0.0148 0.0419 107 ARG A C 709 O O . ARG A 84 ? 0.3333 0.2567 0.2410 -0.0147 -0.0146 0.0393 107 ARG A O 710 C CB . ARG A 84 ? 0.3282 0.2496 0.2300 -0.0148 -0.0141 0.0385 107 ARG A CB 711 C CG . ARG A 84 ? 0.3397 0.2608 0.2376 -0.0159 -0.0141 0.0383 107 ARG A CG 712 C CD . ARG A 84 ? 0.3448 0.2648 0.2442 -0.0120 -0.0126 0.0345 107 ARG A CD 713 N NE . ARG A 84 ? 0.3567 0.2761 0.2534 -0.0129 -0.0138 0.0341 107 ARG A NE 714 C CZ . ARG A 84 ? 0.3874 0.3085 0.2811 -0.0131 -0.0106 0.0318 107 ARG A CZ 715 N NH1 . ARG A 84 ? 0.3640 0.2864 0.2562 -0.0123 -0.0059 0.0296 107 ARG A NH1 716 N NH2 . ARG A 84 ? 0.4002 0.3212 0.2918 -0.0142 -0.0126 0.0316 107 ARG A NH2 717 N N . THR A 85 ? 0.3512 0.2797 0.2529 -0.0241 -0.0154 0.0448 108 THR A N 718 C CA . THR A 85 ? 0.3577 0.2868 0.2619 -0.0254 -0.0165 0.0456 108 THR A CA 719 C C . THR A 85 ? 0.3374 0.2749 0.2456 -0.0215 -0.0116 0.0422 108 THR A C 720 O O . THR A 85 ? 0.3448 0.2814 0.2570 -0.0192 -0.0123 0.0410 108 THR A O 721 C CB . THR A 85 ? 0.3773 0.3079 0.2769 -0.0336 -0.0187 0.0501 108 THR A CB 722 O OG1 . THR A 85 ? 0.4398 0.3809 0.3365 -0.0364 -0.0145 0.0500 108 THR A OG1 723 C CG2 . THR A 85 ? 0.3783 0.2980 0.2738 -0.0367 -0.0247 0.0537 108 THR A CG2 724 N N A GLU A 86 ? 0.3265 0.2715 0.2336 -0.0202 -0.0071 0.0404 109 GLU A N 725 N N B GLU A 86 ? 0.3297 0.2748 0.2366 -0.0205 -0.0072 0.0406 109 GLU A N 726 C CA A GLU A 86 ? 0.3364 0.2878 0.2470 -0.0154 -0.0033 0.0372 109 GLU A CA 727 C CA B GLU A 86 ? 0.3324 0.2840 0.2424 -0.0156 -0.0031 0.0372 109 GLU A CA 728 C C A GLU A 86 ? 0.3247 0.2700 0.2377 -0.0093 -0.0029 0.0345 109 GLU A C 729 C C B GLU A 86 ? 0.3252 0.2701 0.2381 -0.0098 -0.0033 0.0348 109 GLU A C 730 O O A GLU A 86 ? 0.3034 0.2507 0.2195 -0.0057 -0.0017 0.0328 109 GLU A O 731 O O B GLU A 86 ? 0.3059 0.2520 0.2224 -0.0073 -0.0032 0.0338 109 GLU A O 732 C CB A GLU A 86 ? 0.3449 0.3051 0.2536 -0.0144 0.0012 0.0352 109 GLU A CB 733 C CB B GLU A 86 ? 0.3395 0.2977 0.2469 -0.0144 0.0012 0.0351 109 GLU A CB 734 C CG A GLU A 86 ? 0.3928 0.3627 0.2996 -0.0204 0.0017 0.0371 109 GLU A CG 735 C CG B GLU A 86 ? 0.3647 0.3328 0.2692 -0.0202 0.0024 0.0366 109 GLU A CG 736 C CD A GLU A 86 ? 0.3918 0.3721 0.3018 -0.0205 0.0032 0.0364 109 GLU A CD 737 C CD B GLU A 86 ? 0.3908 0.3554 0.2899 -0.0259 0.0003 0.0395 109 GLU A CD 738 O OE1 A GLU A 86 ? 0.4055 0.3836 0.3194 -0.0183 0.0019 0.0363 109 GLU A OE1 739 O OE1 B GLU A 86 ? 0.3178 0.2724 0.2158 -0.0252 -0.0024 0.0404 109 GLU A OE1 740 O OE2 A GLU A 86 ? 0.4556 0.4480 0.3642 -0.0234 0.0058 0.0357 109 GLU A OE2 741 O OE2 B GLU A 86 ? 0.4277 0.4012 0.3237 -0.0312 0.0016 0.0406 109 GLU A OE2 742 N N . LEU A 87 ? 0.3205 0.2591 0.2313 -0.0086 -0.0039 0.0341 110 LEU A N 743 C CA . LEU A 87 ? 0.3248 0.2581 0.2371 -0.0044 -0.0039 0.0317 110 LEU A CA 744 C C . LEU A 87 ? 0.3056 0.2357 0.2219 -0.0040 -0.0072 0.0320 110 LEU A C 745 O O . LEU A 87 ? 0.2761 0.2062 0.1949 -0.0007 -0.0063 0.0300 110 LEU A O 746 C CB . LEU A 87 ? 0.3150 0.2435 0.2244 -0.0048 -0.0046 0.0312 110 LEU A CB 747 C CG . LEU A 87 ? 0.3287 0.2527 0.2392 -0.0018 -0.0051 0.0287 110 LEU A CG 748 C CD1 . LEU A 87 ? 0.2890 0.2135 0.1988 0.0016 -0.0013 0.0263 110 LEU A CD1 749 C CD2 . LEU A 87 ? 0.3005 0.2219 0.2083 -0.0032 -0.0063 0.0285 110 LEU A CD2 750 N N . LEU A 88 ? 0.2964 0.2232 0.2127 -0.0073 -0.0113 0.0343 111 LEU A N 751 C CA . LEU A 88 ? 0.3145 0.2376 0.2342 -0.0066 -0.0147 0.0339 111 LEU A CA 752 C C . LEU A 88 ? 0.3244 0.2525 0.2470 -0.0063 -0.0133 0.0335 111 LEU A C 753 O O . LEU A 88 ? 0.2956 0.2232 0.2216 -0.0036 -0.0137 0.0314 111 LEU A O 754 C CB . LEU A 88 ? 0.3185 0.2352 0.2368 -0.0096 -0.0199 0.0363 111 LEU A CB 755 C CG . LEU A 88 ? 0.3857 0.2970 0.3067 -0.0092 -0.0242 0.0358 111 LEU A CG 756 C CD1 . LEU A 88 ? 0.3691 0.2794 0.2939 -0.0039 -0.0246 0.0316 111 LEU A CD1 757 C CD2 . LEU A 88 ? 0.4015 0.3039 0.3190 -0.0127 -0.0303 0.0392 111 LEU A CD2 758 N N A SER A 89 ? 0.3132 0.2475 0.2346 -0.0093 -0.0116 0.0353 112 SER A N 759 N N B SER A 89 ? 0.3221 0.2562 0.2436 -0.0093 -0.0117 0.0353 112 SER A N 760 C CA A SER A 89 ? 0.3095 0.2506 0.2337 -0.0094 -0.0102 0.0350 112 SER A CA 761 C CA B SER A 89 ? 0.3269 0.2670 0.2512 -0.0093 -0.0106 0.0349 112 SER A CA 762 C C A SER A 89 ? 0.3024 0.2468 0.2286 -0.0037 -0.0070 0.0322 112 SER A C 763 C C B SER A 89 ? 0.3112 0.2553 0.2375 -0.0037 -0.0071 0.0322 112 SER A C 764 O O A SER A 89 ? 0.3035 0.2498 0.2328 -0.0020 -0.0071 0.0312 112 SER A O 765 O O B SER A 89 ? 0.3110 0.2566 0.2403 -0.0018 -0.0073 0.0310 112 SER A O 766 C CB A SER A 89 ? 0.3173 0.2671 0.2397 -0.0137 -0.0086 0.0370 112 SER A CB 767 C CB B SER A 89 ? 0.3407 0.2884 0.2634 -0.0144 -0.0098 0.0373 112 SER A CB 768 O OG A SER A 89 ? 0.2885 0.2345 0.2075 -0.0201 -0.0119 0.0402 112 SER A OG 769 O OG B SER A 89 ? 0.3740 0.3270 0.2943 -0.0138 -0.0065 0.0370 112 SER A OG 770 N N . TYR A 90 ? 0.2986 0.2429 0.2225 -0.0011 -0.0043 0.0312 113 TYR A N 771 C CA . TYR A 90 ? 0.2871 0.2322 0.2114 0.0039 -0.0017 0.0290 113 TYR A CA 772 C C . TYR A 90 ? 0.2665 0.2055 0.1923 0.0057 -0.0034 0.0276 113 TYR A C 773 O O . TYR A 90 ? 0.2670 0.2074 0.1943 0.0084 -0.0028 0.0265 113 TYR A O 774 C CB . TYR A 90 ? 0.2947 0.2389 0.2152 0.0057 0.0010 0.0279 113 TYR A CB 775 C CG . TYR A 90 ? 0.2885 0.2311 0.2079 0.0109 0.0032 0.0259 113 TYR A CG 776 C CD1 . TYR A 90 ? 0.2788 0.2270 0.1982 0.0143 0.0055 0.0249 113 TYR A CD1 777 C CD2 . TYR A 90 ? 0.2951 0.2302 0.2129 0.0122 0.0027 0.0249 113 TYR A CD2 778 C CE1 . TYR A 90 ? 0.3214 0.2659 0.2388 0.0195 0.0067 0.0234 113 TYR A CE1 779 C CE2 . TYR A 90 ? 0.2480 0.1800 0.1634 0.0161 0.0043 0.0236 113 TYR A CE2 780 C CZ . TYR A 90 ? 0.3096 0.2453 0.2247 0.0198 0.0060 0.0230 113 TYR A CZ 781 O OH . TYR A 90 ? 0.3287 0.2589 0.2405 0.0238 0.0067 0.0221 113 TYR A OH 782 N N . MET A 91 ? 0.2698 0.2034 0.1951 0.0041 -0.0057 0.0275 114 MET A N 783 C CA . MET A 91 ? 0.2451 0.1751 0.1720 0.0055 -0.0073 0.0255 114 MET A CA 784 C C . MET A 91 ? 0.2542 0.1861 0.1849 0.0055 -0.0090 0.0250 114 MET A C 785 O O . MET A 91 ? 0.2682 0.2006 0.2004 0.0074 -0.0089 0.0230 114 MET A O 786 C CB . MET A 91 ? 0.2484 0.1738 0.1742 0.0044 -0.0095 0.0250 114 MET A CB 787 C CG . MET A 91 ? 0.2548 0.1788 0.1766 0.0046 -0.0073 0.0248 114 MET A CG 788 S SD . MET A 91 ? 0.3074 0.2279 0.2283 0.0031 -0.0104 0.0246 114 MET A SD 789 C CE . MET A 91 ? 0.2576 0.1777 0.1834 0.0049 -0.0141 0.0217 114 MET A CE 790 N N . LYS A 92 ? 0.2679 0.2007 0.1998 0.0027 -0.0110 0.0267 115 LYS A N 791 C CA . LYS A 92 ? 0.2755 0.2096 0.2107 0.0020 -0.0130 0.0261 115 LYS A CA 792 C C . LYS A 92 ? 0.2893 0.2300 0.2259 0.0039 -0.0104 0.0256 115 LYS A C 793 O O . LYS A 92 ? 0.2759 0.2178 0.2149 0.0049 -0.0111 0.0238 115 LYS A O 794 C CB . LYS A 92 ? 0.2842 0.2178 0.2190 -0.0025 -0.0154 0.0285 115 LYS A CB 795 C CG . LYS A 92 ? 0.3283 0.2534 0.2618 -0.0040 -0.0194 0.0290 115 LYS A CG 796 C CD . LYS A 92 ? 0.4290 0.3515 0.3598 -0.0095 -0.0220 0.0324 115 LYS A CD 797 C CE . LYS A 92 ? 0.4877 0.3996 0.4166 -0.0107 -0.0273 0.0332 115 LYS A CE 798 N NZ . LYS A 92 ? 0.5087 0.4180 0.4326 -0.0171 -0.0292 0.0379 115 LYS A NZ 799 N N . GLU A 93 ? 0.2686 0.2136 0.2035 0.0051 -0.0074 0.0267 116 GLU A N 800 C CA . GLU A 93 ? 0.2518 0.2034 0.1878 0.0078 -0.0054 0.0264 116 GLU A CA 801 C C . GLU A 93 ? 0.2631 0.2118 0.1973 0.0118 -0.0039 0.0251 116 GLU A C 802 O O . GLU A 93 ? 0.2618 0.2125 0.1972 0.0133 -0.0041 0.0245 116 GLU A O 803 C CB . GLU A 93 ? 0.2532 0.2115 0.1883 0.0078 -0.0032 0.0277 116 GLU A CB 804 C CG . GLU A 93 ? 0.2691 0.2333 0.2048 0.0125 -0.0012 0.0270 116 GLU A CG 805 C CD . GLU A 93 ? 0.3306 0.3012 0.2697 0.0121 -0.0023 0.0270 116 GLU A CD 806 O OE1 . GLU A 93 ? 0.3451 0.3157 0.2860 0.0077 -0.0043 0.0274 116 GLU A OE1 807 O OE2 . GLU A 93 ? 0.2727 0.2479 0.2125 0.0160 -0.0014 0.0266 116 GLU A OE2 808 N N . TYR A 94 ? 0.2638 0.2070 0.1945 0.0127 -0.0029 0.0248 117 TYR A N 809 C CA . TYR A 94 ? 0.2775 0.2166 0.2047 0.0155 -0.0014 0.0239 117 TYR A CA 810 C C . TYR A 94 ? 0.2627 0.1965 0.1886 0.0141 -0.0023 0.0225 117 TYR A C 811 O O . TYR A 94 ? 0.2529 0.1835 0.1754 0.0152 -0.0014 0.0219 117 TYR A O 812 C CB . TYR A 94 ? 0.2783 0.2157 0.2016 0.0178 0.0009 0.0242 117 TYR A CB 813 C CG . TYR A 94 ? 0.2814 0.2253 0.2058 0.0207 0.0021 0.0247 117 TYR A CG 814 C CD1 . TYR A 94 ? 0.2787 0.2232 0.2022 0.0249 0.0024 0.0246 117 TYR A CD1 815 C CD2 . TYR A 94 ? 0.2657 0.2162 0.1917 0.0192 0.0027 0.0252 117 TYR A CD2 816 C CE1 . TYR A 94 ? 0.2894 0.2415 0.2145 0.0285 0.0033 0.0246 117 TYR A CE1 817 C CE2 . TYR A 94 ? 0.2490 0.2083 0.1767 0.0218 0.0039 0.0250 117 TYR A CE2 818 C CZ . TYR A 94 ? 0.2662 0.2264 0.1937 0.0271 0.0042 0.0245 117 TYR A CZ 819 O OH . TYR A 94 ? 0.2654 0.2358 0.1951 0.0305 0.0051 0.0239 117 TYR A OH 820 N N . TRP A 95 ? 0.2479 0.1809 0.1759 0.0117 -0.0043 0.0218 118 TRP A N 821 C CA . TRP A 95 ? 0.2678 0.1987 0.1960 0.0107 -0.0055 0.0195 118 TRP A CA 822 C C . TRP A 95 ? 0.2580 0.1915 0.1912 0.0099 -0.0084 0.0179 118 TRP A C 823 O O . TRP A 95 ? 0.2869 0.2192 0.2219 0.0093 -0.0107 0.0161 118 TRP A O 824 C CB . TRP A 95 ? 0.2440 0.1715 0.1700 0.0096 -0.0056 0.0194 118 TRP A CB 825 C CG . TRP A 95 ? 0.2438 0.1701 0.1682 0.0088 -0.0058 0.0171 118 TRP A CG 826 C CD1 . TRP A 95 ? 0.2664 0.1954 0.1927 0.0085 -0.0067 0.0145 118 TRP A CD1 827 C CD2 . TRP A 95 ? 0.2826 0.2063 0.2036 0.0076 -0.0051 0.0167 118 TRP A CD2 828 N NE1 . TRP A 95 ? 0.2438 0.1729 0.1681 0.0071 -0.0065 0.0125 118 TRP A NE1 829 C CE2 . TRP A 95 ? 0.2614 0.1869 0.1823 0.0065 -0.0056 0.0139 118 TRP A CE2 830 C CE3 . TRP A 95 ? 0.3123 0.2332 0.2300 0.0071 -0.0040 0.0181 118 TRP A CE3 831 C CZ2 . TRP A 95 ? 0.2838 0.2085 0.2016 0.0048 -0.0051 0.0127 118 TRP A CZ2 832 C CZ3 . TRP A 95 ? 0.2914 0.2106 0.2056 0.0054 -0.0035 0.0169 118 TRP A CZ3 833 C CH2 . TRP A 95 ? 0.3228 0.2440 0.2373 0.0043 -0.0041 0.0143 118 TRP A CH2 834 N N . PRO A 96 ? 0.2510 0.1882 0.1864 0.0103 -0.0085 0.0182 119 PRO A N 835 C CA . PRO A 96 ? 0.2594 0.1984 0.1989 0.0095 -0.0111 0.0161 119 PRO A CA 836 C C . PRO A 96 ? 0.2648 0.2054 0.2055 0.0098 -0.0118 0.0124 119 PRO A C 837 O O . PRO A 96 ? 0.2661 0.2079 0.2040 0.0099 -0.0099 0.0120 119 PRO A O 838 C CB . PRO A 96 ? 0.2600 0.2036 0.2009 0.0095 -0.0106 0.0173 119 PRO A CB 839 C CG . PRO A 96 ? 0.2732 0.2181 0.2109 0.0113 -0.0079 0.0184 119 PRO A CG 840 C CD . PRO A 96 ? 0.2796 0.2197 0.2137 0.0118 -0.0066 0.0195 119 PRO A CD 841 N N . ASP A 97 ? 0.2795 0.2201 0.2238 0.0097 -0.0147 0.0096 120 ASP A N 842 C CA . ASP A 97 ? 0.2817 0.2267 0.2284 0.0100 -0.0155 0.0053 120 ASP A CA 843 C C . ASP A 97 ? 0.3065 0.2556 0.2549 0.0094 -0.0154 0.0053 120 ASP A C 844 O O . ASP A 97 ? 0.3105 0.2582 0.2606 0.0088 -0.0169 0.0064 120 ASP A O 845 C CB . ASP A 97 ? 0.2812 0.2247 0.2313 0.0113 -0.0191 0.0016 120 ASP A CB 846 C CG . ASP A 97 ? 0.3248 0.2748 0.2779 0.0121 -0.0198 -0.0040 120 ASP A CG 847 O OD1 . ASP A 97 ? 0.3533 0.3067 0.3085 0.0117 -0.0201 -0.0059 120 ASP A OD1 848 O OD2 . ASP A 97 ? 0.3457 0.2984 0.2989 0.0127 -0.0198 -0.0067 120 ASP A OD2 849 N N . TYR A 98 ? 0.3238 0.2780 0.2711 0.0090 -0.0137 0.0042 121 TYR A N 850 C CA . TYR A 98 ? 0.3284 0.2873 0.2768 0.0083 -0.0136 0.0044 121 TYR A CA 851 C C . TYR A 98 ? 0.3411 0.3013 0.2940 0.0079 -0.0163 0.0012 121 TYR A C 852 O O . TYR A 98 ? 0.3461 0.3091 0.3000 0.0068 -0.0165 0.0022 121 TYR A O 853 C CB . TYR A 98 ? 0.3390 0.3031 0.2849 0.0073 -0.0120 0.0036 121 TYR A CB 854 C CG . TYR A 98 ? 0.3660 0.3345 0.3138 0.0065 -0.0128 -0.0017 121 TYR A CG 855 C CD1 . TYR A 98 ? 0.3806 0.3543 0.3326 0.0063 -0.0145 -0.0062 121 TYR A CD1 856 C CD2 . TYR A 98 ? 0.3723 0.3407 0.3175 0.0058 -0.0118 -0.0028 121 TYR A CD2 857 C CE1 . TYR A 98 ? 0.3716 0.3512 0.3260 0.0061 -0.0153 -0.0122 121 TYR A CE1 858 C CE2 . TYR A 98 ? 0.3823 0.3573 0.3301 0.0052 -0.0126 -0.0086 121 TYR A CE2 859 C CZ . TYR A 98 ? 0.4165 0.3974 0.3690 0.0057 -0.0143 -0.0134 121 TYR A CZ 860 O OH . TYR A 98 ? 0.4361 0.4245 0.3915 0.0058 -0.0151 -0.0198 121 TYR A OH 861 N N . GLU A 99 ? 0.3553 0.3140 0.3107 0.0088 -0.0185 -0.0030 122 GLU A N 862 C CA . GLU A 99 ? 0.3811 0.3396 0.3403 0.0090 -0.0216 -0.0070 122 GLU A CA 863 C C . GLU A 99 ? 0.3996 0.3508 0.3590 0.0081 -0.0238 -0.0044 122 GLU A C 864 O O . GLU A 99 ? 0.4184 0.3690 0.3795 0.0068 -0.0259 -0.0061 122 GLU A O 865 C CB . GLU A 99 ? 0.3906 0.3501 0.3526 0.0111 -0.0236 -0.0129 122 GLU A CB 866 C CG . GLU A 99 ? 0.4250 0.3856 0.3905 0.0117 -0.0263 -0.0180 122 GLU A CG 867 C CD . GLU A 99 ? 0.4564 0.4195 0.4255 0.0151 -0.0286 -0.0250 122 GLU A CD 868 O OE1 . GLU A 99 ? 0.4522 0.4183 0.4209 0.0162 -0.0277 -0.0257 122 GLU A OE1 869 O OE2 . GLU A 99 ? 0.5283 0.4900 0.5004 0.0165 -0.0317 -0.0298 122 GLU A OE2 870 N N . GLY A 100 ? 0.3689 0.3149 0.3259 0.0080 -0.0235 -0.0003 123 GLY A N 871 C CA . GLY A 100 ? 0.3790 0.3194 0.3350 0.0058 -0.0251 0.0032 123 GLY A CA 872 C C . GLY A 100 ? 0.3852 0.3187 0.3392 0.0063 -0.0262 0.0055 123 GLY A C 873 O O . GLY A 100 ? 0.3559 0.2888 0.3101 0.0087 -0.0264 0.0037 123 GLY A O 874 N N . ALA A 101 ? 0.3617 0.2912 0.3134 0.0035 -0.0269 0.0096 124 ALA A N 875 C CA . ALA A 101 ? 0.3860 0.3097 0.3350 0.0030 -0.0279 0.0127 124 ALA A CA 876 C C . ALA A 101 ? 0.3758 0.2918 0.3254 0.0051 -0.0323 0.0101 124 ALA A C 877 O O . ALA A 101 ? 0.3577 0.2710 0.3058 0.0063 -0.0327 0.0113 124 ALA A O 878 C CB . ALA A 101 ? 0.3864 0.3080 0.3326 -0.0015 -0.0283 0.0171 124 ALA A CB 879 N N . ASP A 102 ? 0.3996 0.3123 0.3515 0.0060 -0.0358 0.0064 125 ASP A N 880 C CA . ASP A 102 ? 0.4002 0.3052 0.3530 0.0091 -0.0407 0.0034 125 ASP A CA 881 C C . ASP A 102 ? 0.3660 0.2770 0.3215 0.0136 -0.0396 -0.0006 125 ASP A C 882 O O . ASP A 102 ? 0.3634 0.2702 0.3198 0.0168 -0.0433 -0.0027 125 ASP A O 883 C CB . ASP A 102 ? 0.4366 0.3359 0.3911 0.0097 -0.0452 -0.0006 125 ASP A CB 884 C CG . ASP A 102 ? 0.5104 0.4004 0.4608 0.0044 -0.0479 0.0035 125 ASP A CG 885 O OD1 . ASP A 102 ? 0.5337 0.4219 0.4801 0.0004 -0.0468 0.0095 125 ASP A OD1 886 O OD2 . ASP A 102 ? 0.6273 0.5128 0.5785 0.0040 -0.0509 0.0003 125 ASP A OD2 887 N N . GLU A 103 ? 0.3290 0.2501 0.2857 0.0135 -0.0348 -0.0017 126 GLU A N 888 C CA . GLU A 103 ? 0.3313 0.2590 0.2894 0.0161 -0.0332 -0.0050 126 GLU A CA 889 C C . GLU A 103 ? 0.2914 0.2202 0.2459 0.0149 -0.0299 -0.0010 126 GLU A C 890 O O . GLU A 103 ? 0.2558 0.1894 0.2104 0.0161 -0.0286 -0.0031 126 GLU A O 891 C CB . GLU A 103 ? 0.3299 0.2671 0.2902 0.0161 -0.0305 -0.0089 126 GLU A CB 892 C CG . GLU A 103 ? 0.3634 0.3015 0.3279 0.0182 -0.0339 -0.0152 126 GLU A CG 893 C CD . GLU A 103 ? 0.4985 0.4294 0.4625 0.0162 -0.0362 -0.0134 126 GLU A CD 894 O OE1 . GLU A 103 ? 0.4791 0.4123 0.4414 0.0127 -0.0335 -0.0098 126 GLU A OE1 895 O OE2 . GLU A 103 ? 0.5782 0.5006 0.5430 0.0180 -0.0412 -0.0156 126 GLU A OE2 896 N N . ASP A 104 ? 0.2969 0.2215 0.2481 0.0123 -0.0288 0.0045 127 ASP A N 897 C CA . ASP A 104 ? 0.2703 0.1954 0.2179 0.0113 -0.0258 0.0079 127 ASP A CA 898 C C . ASP A 104 ? 0.2718 0.1948 0.2192 0.0130 -0.0281 0.0067 127 ASP A C 899 O O . ASP A 104 ? 0.2676 0.1945 0.2135 0.0132 -0.0255 0.0060 127 ASP A O 900 C CB . ASP A 104 ? 0.2717 0.1934 0.2162 0.0085 -0.0250 0.0131 127 ASP A CB 901 C CG . ASP A 104 ? 0.2992 0.2250 0.2437 0.0071 -0.0223 0.0144 127 ASP A CG 902 O OD1 . ASP A 104 ? 0.2984 0.2294 0.2445 0.0082 -0.0205 0.0120 127 ASP A OD1 903 O OD2 . ASP A 104 ? 0.3205 0.2456 0.2631 0.0046 -0.0217 0.0181 127 ASP A OD2 904 N N . GLU A 105 ? 0.2516 0.1682 0.1997 0.0142 -0.0330 0.0065 128 GLU A N 905 C CA . GLU A 105 ? 0.2601 0.1745 0.2077 0.0161 -0.0358 0.0061 128 GLU A CA 906 C C . GLU A 105 ? 0.2784 0.2012 0.2293 0.0190 -0.0350 0.0005 128 GLU A C 907 O O . GLU A 105 ? 0.2663 0.1927 0.2156 0.0187 -0.0334 0.0006 128 GLU A O 908 C CB . GLU A 105 ? 0.2549 0.1603 0.2031 0.0176 -0.0422 0.0063 128 GLU A CB 909 C CG . GLU A 105 ? 0.3071 0.2106 0.2558 0.0212 -0.0464 0.0047 128 GLU A CG 910 C CD . GLU A 105 ? 0.3205 0.2248 0.2652 0.0190 -0.0447 0.0087 128 GLU A CD 911 O OE1 . GLU A 105 ? 0.3227 0.2248 0.2632 0.0147 -0.0419 0.0137 128 GLU A OE1 912 O OE2 . GLU A 105 ? 0.3162 0.2245 0.2621 0.0217 -0.0459 0.0062 128 GLU A OE2 913 N N A SER A 106 ? 0.2954 0.2226 0.2505 0.0211 -0.0358 -0.0046 129 SER A N 914 N N B SER A 106 ? 0.2757 0.2028 0.2307 0.0211 -0.0358 -0.0045 129 SER A N 915 C CA A SER A 106 ? 0.2841 0.2212 0.2423 0.0233 -0.0352 -0.0104 129 SER A CA 916 C CA B SER A 106 ? 0.2625 0.1996 0.2208 0.0233 -0.0352 -0.0105 129 SER A CA 917 C C A SER A 106 ? 0.2634 0.2069 0.2184 0.0198 -0.0295 -0.0091 129 SER A C 918 C C B SER A 106 ? 0.2579 0.2020 0.2132 0.0199 -0.0295 -0.0096 129 SER A C 919 O O A SER A 106 ? 0.2569 0.2064 0.2115 0.0196 -0.0285 -0.0111 129 SER A O 920 O O B SER A 106 ? 0.2533 0.2049 0.2089 0.0198 -0.0284 -0.0126 129 SER A O 921 C CB A SER A 106 ? 0.3098 0.2519 0.2729 0.0259 -0.0368 -0.0167 129 SER A CB 922 C CB B SER A 106 ? 0.2726 0.2140 0.2358 0.0260 -0.0371 -0.0167 129 SER A CB 923 O OG A SER A 106 ? 0.3348 0.2772 0.2971 0.0231 -0.0339 -0.0152 129 SER A OG 924 O OG B SER A 106 ? 0.2328 0.1648 0.1973 0.0281 -0.0419 -0.0166 129 SER A OG 925 N N . PHE A 107 ? 0.2662 0.2081 0.2185 0.0169 -0.0261 -0.0056 130 PHE A N 926 C CA . PHE A 107 ? 0.2721 0.2175 0.2202 0.0139 -0.0213 -0.0040 130 PHE A CA 927 C C . PHE A 107 ? 0.2704 0.2127 0.2143 0.0126 -0.0201 -0.0010 130 PHE A C 928 O O . PHE A 107 ? 0.2601 0.2064 0.2013 0.0107 -0.0177 -0.0021 130 PHE A O 929 C CB . PHE A 107 ? 0.2517 0.1947 0.1978 0.0122 -0.0188 -0.0005 130 PHE A CB 930 C CG . PHE A 107 ? 0.2564 0.2012 0.1979 0.0099 -0.0146 0.0012 130 PHE A CG 931 C CD1 . PHE A 107 ? 0.2795 0.2288 0.2188 0.0082 -0.0130 -0.0010 130 PHE A CD1 932 C CD2 . PHE A 107 ? 0.2559 0.1972 0.1947 0.0093 -0.0127 0.0053 130 PHE A CD2 933 C CE1 . PHE A 107 ? 0.2825 0.2308 0.2162 0.0058 -0.0098 0.0012 130 PHE A CE1 934 C CE2 . PHE A 107 ? 0.2591 0.2002 0.1934 0.0081 -0.0097 0.0069 130 PHE A CE2 935 C CZ . PHE A 107 ? 0.2714 0.2147 0.2026 0.0062 -0.0084 0.0053 130 PHE A CZ 936 N N . TRP A 108 ? 0.2703 0.2057 0.2130 0.0128 -0.0216 0.0028 131 TRP A N 937 C CA . TRP A 108 ? 0.2627 0.1956 0.2012 0.0113 -0.0204 0.0055 131 TRP A CA 938 C C . TRP A 108 ? 0.2546 0.1909 0.1944 0.0124 -0.0227 0.0027 131 TRP A C 939 O O . TRP A 108 ? 0.2660 0.2045 0.2025 0.0106 -0.0206 0.0027 131 TRP A O 940 C CB . TRP A 108 ? 0.2758 0.2021 0.2127 0.0106 -0.0215 0.0101 131 TRP A CB 941 C CG . TRP A 108 ? 0.2363 0.1613 0.1723 0.0095 -0.0192 0.0126 131 TRP A CG 942 C CD1 . TRP A 108 ? 0.2895 0.2171 0.2240 0.0090 -0.0154 0.0127 131 TRP A CD1 943 C CD2 . TRP A 108 ? 0.2570 0.1782 0.1928 0.0084 -0.0205 0.0159 131 TRP A CD2 944 N NE1 . TRP A 108 ? 0.2631 0.1898 0.1976 0.0086 -0.0146 0.0152 131 TRP A NE1 945 C CE2 . TRP A 108 ? 0.2721 0.1957 0.2073 0.0077 -0.0173 0.0172 131 TRP A CE2 946 C CE3 . TRP A 108 ? 0.3244 0.2407 0.2599 0.0075 -0.0242 0.0181 131 TRP A CE3 947 C CZ2 . TRP A 108 ? 0.2655 0.1884 0.2008 0.0062 -0.0175 0.0199 131 TRP A CZ2 948 C CZ3 . TRP A 108 ? 0.2654 0.1798 0.2001 0.0051 -0.0244 0.0213 131 TRP A CZ3 949 C CH2 . TRP A 108 ? 0.2970 0.2156 0.2318 0.0044 -0.0208 0.0219 131 TRP A CH2 950 N N . GLU A 109 ? 0.2721 0.2092 0.2166 0.0157 -0.0272 -0.0002 132 GLU A N 951 C CA . GLU A 109 ? 0.2831 0.2259 0.2300 0.0179 -0.0298 -0.0041 132 GLU A CA 952 C C . GLU A 109 ? 0.2662 0.2191 0.2127 0.0159 -0.0262 -0.0080 132 GLU A C 953 O O . GLU A 109 ? 0.2631 0.2212 0.2080 0.0145 -0.0254 -0.0092 132 GLU A O 954 C CB . GLU A 109 ? 0.2963 0.2393 0.2489 0.0228 -0.0352 -0.0081 132 GLU A CB 955 C CG . GLU A 109 ? 0.3123 0.2443 0.2640 0.0242 -0.0397 -0.0042 132 GLU A CG 956 C CD . GLU A 109 ? 0.3649 0.2940 0.3215 0.0291 -0.0453 -0.0082 132 GLU A CD 957 O OE1 . GLU A 109 ? 0.3249 0.2627 0.2861 0.0322 -0.0457 -0.0146 132 GLU A OE1 958 O OE2 . GLU A 109 ? 0.2973 0.2155 0.2525 0.0296 -0.0493 -0.0050 132 GLU A OE2 959 N N . HIS A 110 ? 0.2773 0.2339 0.2253 0.0154 -0.0244 -0.0102 133 HIS A N 960 C CA . HIS A 110 ? 0.2382 0.2048 0.1852 0.0124 -0.0212 -0.0138 133 HIS A CA 961 C C . HIS A 110 ? 0.2440 0.2082 0.1839 0.0077 -0.0173 -0.0105 133 HIS A C 962 O O . HIS A 110 ? 0.2694 0.2401 0.2072 0.0051 -0.0161 -0.0126 133 HIS A O 963 C CB . HIS A 110 ? 0.2521 0.2217 0.2006 0.0119 -0.0199 -0.0156 133 HIS A CB 964 C CG . HIS A 110 ? 0.2632 0.2416 0.2090 0.0076 -0.0165 -0.0180 133 HIS A CG 965 N ND1 . HIS A 110 ? 0.2698 0.2609 0.2186 0.0074 -0.0172 -0.0241 133 HIS A ND1 966 C CD2 . HIS A 110 ? 0.2864 0.2626 0.2261 0.0032 -0.0128 -0.0151 133 HIS A CD2 967 C CE1 . HIS A 110 ? 0.3335 0.3301 0.2775 0.0019 -0.0137 -0.0245 133 HIS A CE1 968 N NE2 . HIS A 110 ? 0.2846 0.2712 0.2228 -0.0007 -0.0113 -0.0188 133 HIS A NE2 969 N N . GLU A 111 ? 0.2412 0.1962 0.1769 0.0065 -0.0152 -0.0053 134 GLU A N 970 C CA . GLU A 111 ? 0.2520 0.2030 0.1807 0.0028 -0.0118 -0.0025 134 GLU A CA 971 C C . GLU A 111 ? 0.2712 0.2220 0.1977 0.0018 -0.0123 -0.0021 134 GLU A C 972 O O . GLU A 111 ? 0.2797 0.2331 0.2018 -0.0019 -0.0102 -0.0032 134 GLU A O 973 C CB . GLU A 111 ? 0.2547 0.1968 0.1801 0.0029 -0.0099 0.0022 134 GLU A CB 974 C CG . GLU A 111 ? 0.2588 0.2023 0.1845 0.0026 -0.0086 0.0019 134 GLU A CG 975 C CD . GLU A 111 ? 0.2732 0.2206 0.1945 -0.0014 -0.0064 0.0001 134 GLU A CD 976 O OE1 . GLU A 111 ? 0.2828 0.2265 0.1976 -0.0045 -0.0043 0.0013 134 GLU A OE1 977 O OE2 . GLU A 111 ? 0.2718 0.2261 0.1956 -0.0020 -0.0067 -0.0027 134 GLU A OE2 978 N N . TRP A 112 ? 0.2916 0.2393 0.2206 0.0046 -0.0153 -0.0006 135 TRP A N 979 C CA . TRP A 112 ? 0.2699 0.2183 0.1971 0.0038 -0.0163 -0.0002 135 TRP A CA 980 C C . TRP A 112 ? 0.2672 0.2267 0.1973 0.0039 -0.0179 -0.0054 135 TRP A C 981 O O . TRP A 112 ? 0.2789 0.2421 0.2054 0.0005 -0.0163 -0.0063 135 TRP A O 982 C CB . TRP A 112 ? 0.2670 0.2099 0.1960 0.0066 -0.0201 0.0027 135 TRP A CB 983 C CG . TRP A 112 ? 0.2731 0.2188 0.2012 0.0063 -0.0221 0.0024 135 TRP A CG 984 C CD1 . TRP A 112 ? 0.2759 0.2267 0.2085 0.0095 -0.0266 -0.0003 135 TRP A CD1 985 C CD2 . TRP A 112 ? 0.2957 0.2408 0.2179 0.0025 -0.0193 0.0038 135 TRP A CD2 986 N NE1 . TRP A 112 ? 0.2807 0.2345 0.2107 0.0080 -0.0271 0.0000 135 TRP A NE1 987 C CE2 . TRP A 112 ? 0.2677 0.2185 0.1911 0.0031 -0.0224 0.0022 135 TRP A CE2 988 C CE3 . TRP A 112 ? 0.2761 0.2165 0.1921 -0.0010 -0.0148 0.0059 135 TRP A CE3 989 C CZ2 . TRP A 112 ? 0.2499 0.2019 0.1682 -0.0004 -0.0208 0.0029 135 TRP A CZ2 990 C CZ3 . TRP A 112 ? 0.3258 0.2665 0.2365 -0.0044 -0.0131 0.0061 135 TRP A CZ3 991 C CH2 . TRP A 112 ? 0.3052 0.2521 0.2171 -0.0045 -0.0160 0.0046 135 TRP A CH2 992 N N . ASN A 113 ? 0.2563 0.2212 0.1932 0.0080 -0.0213 -0.0090 136 ASN A N 993 C CA . ASN A 113 ? 0.2576 0.2349 0.1985 0.0092 -0.0233 -0.0147 136 ASN A CA 994 C C . ASN A 113 ? 0.2856 0.2720 0.2234 0.0038 -0.0194 -0.0176 136 ASN A C 995 O O . ASN A 113 ? 0.2646 0.2592 0.2011 0.0013 -0.0190 -0.0200 136 ASN A O 996 C CB . ASN A 113 ? 0.2694 0.2502 0.2181 0.0152 -0.0277 -0.0186 136 ASN A CB 997 C CG . ASN A 113 ? 0.2500 0.2213 0.2004 0.0196 -0.0324 -0.0156 136 ASN A CG 998 O OD1 . ASN A 113 ? 0.2770 0.2427 0.2235 0.0183 -0.0329 -0.0114 136 ASN A OD1 999 N ND2 . ASN A 113 ? 0.2704 0.2395 0.2261 0.0247 -0.0364 -0.0179 136 ASN A ND2 1000 N N . LYS A 114 ? 0.2995 0.2840 0.2352 0.0014 -0.0164 -0.0171 137 LYS A N 1001 C CA . LYS A 114 ? 0.2954 0.2874 0.2273 -0.0043 -0.0131 -0.0194 137 LYS A CA 1002 C C . LYS A 114 ? 0.2817 0.2674 0.2046 -0.0102 -0.0097 -0.0161 137 LYS A C 1003 O O . LYS A 114 ? 0.2776 0.2707 0.1970 -0.0153 -0.0082 -0.0184 137 LYS A O 1004 C CB . LYS A 114 ? 0.2760 0.2666 0.2078 -0.0050 -0.0115 -0.0193 137 LYS A CB 1005 C CG . LYS A 114 ? 0.2688 0.2682 0.1958 -0.0119 -0.0084 -0.0218 137 LYS A CG 1006 C CD . LYS A 114 ? 0.2520 0.2529 0.1800 -0.0122 -0.0076 -0.0225 137 LYS A CD 1007 C CE . LYS A 114 ? 0.3103 0.3194 0.2321 -0.0203 -0.0048 -0.0243 137 LYS A CE 1008 N NZ . LYS A 114 ? 0.3258 0.3377 0.2481 -0.0211 -0.0042 -0.0250 137 LYS A NZ 1009 N N . HIS A 115 ? 0.2900 0.2623 0.2087 -0.0099 -0.0085 -0.0108 138 HIS A N 1010 C CA . HIS A 115 ? 0.2845 0.2492 0.1941 -0.0150 -0.0052 -0.0080 138 HIS A CA 1011 C C . HIS A 115 ? 0.3104 0.2684 0.2168 -0.0149 -0.0052 -0.0054 138 HIS A C 1012 O O . HIS A 115 ? 0.3317 0.2881 0.2314 -0.0198 -0.0032 -0.0053 138 HIS A O 1013 C CB . HIS A 115 ? 0.3060 0.2605 0.2116 -0.0151 -0.0031 -0.0046 138 HIS A CB 1014 C CG . HIS A 115 ? 0.3162 0.2756 0.2213 -0.0176 -0.0023 -0.0063 138 HIS A CG 1015 N ND1 . HIS A 115 ? 0.3164 0.2804 0.2156 -0.0242 -0.0005 -0.0081 138 HIS A ND1 1016 C CD2 . HIS A 115 ? 0.3097 0.2703 0.2188 -0.0149 -0.0029 -0.0063 138 HIS A CD2 1017 C CE1 . HIS A 115 ? 0.3647 0.3321 0.2640 -0.0256 -0.0001 -0.0088 138 HIS A CE1 1018 N NE2 . HIS A 115 ? 0.3502 0.3162 0.2559 -0.0197 -0.0016 -0.0080 138 HIS A NE2 1019 N N . GLY A 116 ? 0.3035 0.2569 0.2138 -0.0101 -0.0072 -0.0030 139 GLY A N 1020 C CA . GLY A 116 ? 0.3158 0.2638 0.2233 -0.0100 -0.0073 -0.0004 139 GLY A CA 1021 C C . GLY A 116 ? 0.3168 0.2730 0.2244 -0.0119 -0.0087 -0.0030 139 GLY A C 1022 O O . GLY A 116 ? 0.3289 0.2822 0.2310 -0.0151 -0.0073 -0.0019 139 GLY A O 1023 N N . THR A 117 ? 0.3049 0.2718 0.2191 -0.0096 -0.0118 -0.0067 140 THR A N 1024 C CA . THR A 117 ? 0.3093 0.2864 0.2246 -0.0107 -0.0136 -0.0096 140 THR A CA 1025 C C . THR A 117 ? 0.3451 0.3272 0.2543 -0.0177 -0.0103 -0.0118 140 THR A C 1026 O O . THR A 117 ? 0.3471 0.3371 0.2558 -0.0197 -0.0112 -0.0137 140 THR A O 1027 C CB . THR A 117 ? 0.3064 0.2950 0.2306 -0.0058 -0.0177 -0.0140 140 THR A CB 1028 O OG1 . THR A 117 ? 0.2821 0.2771 0.2078 -0.0072 -0.0161 -0.0174 140 THR A OG1 1029 C CG2 . THR A 117 ? 0.2932 0.2755 0.2227 0.0010 -0.0219 -0.0119 140 THR A CG2 1030 N N . CYS A 118 ? 0.3382 0.3152 0.2419 -0.0219 -0.0067 -0.0112 141 CYS A N 1031 C CA . CYS A 118 ? 0.3511 0.3313 0.2475 -0.0297 -0.0038 -0.0130 141 CYS A CA 1032 C C . CYS A 118 ? 0.3429 0.3095 0.2293 -0.0340 -0.0008 -0.0096 141 CYS A C 1033 O O . CYS A 118 ? 0.3631 0.3283 0.2414 -0.0412 0.0017 -0.0105 141 CYS A O 1034 C CB . CYS A 118 ? 0.3323 0.3162 0.2285 -0.0321 -0.0024 -0.0147 141 CYS A CB 1035 S SG . CYS A 118 ? 0.3575 0.3603 0.2644 -0.0285 -0.0053 -0.0206 141 CYS A SG 1036 N N . ILE A 119 ? 0.3558 0.3120 0.2422 -0.0299 -0.0010 -0.0061 142 ILE A N 1037 C CA . ILE A 119 ? 0.3623 0.3057 0.2398 -0.0326 0.0017 -0.0036 142 ILE A CA 1038 C C . ILE A 119 ? 0.3726 0.3207 0.2487 -0.0348 0.0010 -0.0045 142 ILE A C 1039 O O . ILE A 119 ? 0.3702 0.3206 0.2511 -0.0307 -0.0014 -0.0033 142 ILE A O 1040 C CB . ILE A 119 ? 0.3497 0.2823 0.2278 -0.0276 0.0021 0.0000 142 ILE A CB 1041 C CG1 . ILE A 119 ? 0.4006 0.3299 0.2800 -0.0257 0.0026 0.0008 142 ILE A CG1 1042 C CG2 . ILE A 119 ? 0.3871 0.3079 0.2562 -0.0298 0.0048 0.0015 142 ILE A CG2 1043 C CD1 . ILE A 119 ? 0.4066 0.3281 0.2881 -0.0203 0.0027 0.0040 142 ILE A CD1 1044 N N . ASN A 120 ? 0.3963 0.3463 0.2654 -0.0418 0.0027 -0.0066 143 ASN A N 1045 C CA . ASN A 120 ? 0.3999 0.3574 0.2683 -0.0444 0.0018 -0.0081 143 ASN A CA 1046 C C . ASN A 120 ? 0.3865 0.3360 0.2520 -0.0429 0.0021 -0.0057 143 ASN A C 1047 O O . ASN A 120 ? 0.4189 0.3756 0.2873 -0.0419 -0.0001 -0.0058 143 ASN A O 1048 C CB . ASN A 120 ? 0.4006 0.3625 0.2616 -0.0534 0.0037 -0.0111 143 ASN A CB 1049 C CG . ASN A 120 ? 0.4282 0.3740 0.2772 -0.0586 0.0071 -0.0097 143 ASN A CG 1050 O OD1 . ASN A 120 ? 0.3934 0.3279 0.2385 -0.0583 0.0085 -0.0081 143 ASN A OD1 1051 N ND2 . ASN A 120 ? 0.4051 0.3496 0.2480 -0.0630 0.0080 -0.0105 143 ASN A ND2 1052 N N . THR A 121 ? 0.3715 0.3070 0.2317 -0.0423 0.0046 -0.0035 144 THR A N 1053 C CA . THR A 121 ? 0.3661 0.2951 0.2229 -0.0415 0.0054 -0.0019 144 THR A CA 1054 C C . THR A 121 ? 0.3670 0.2972 0.2309 -0.0349 0.0032 0.0010 144 THR A C 1055 O O . THR A 121 ? 0.4105 0.3370 0.2718 -0.0346 0.0039 0.0022 144 THR A O 1056 C CB . THR A 121 ? 0.3809 0.2949 0.2290 -0.0428 0.0088 -0.0015 144 THR A CB 1057 O OG1 . THR A 121 ? 0.3880 0.2964 0.2390 -0.0382 0.0089 0.0003 144 THR A OG1 1058 C CG2 . THR A 121 ? 0.3327 0.2421 0.1705 -0.0509 0.0109 -0.0040 144 THR A CG2 1059 N N A ILE A 122 ? 0.3716 0.3075 0.2438 -0.0307 0.0004 0.0016 145 ILE A N 1060 N N B ILE A 122 ? 0.3837 0.3183 0.2556 -0.0304 0.0007 0.0018 145 ILE A N 1061 C CA A ILE A 122 ? 0.3581 0.2941 0.2368 -0.0250 -0.0023 0.0044 145 ILE A CA 1062 C CA B ILE A 122 ? 0.3740 0.3100 0.2518 -0.0255 -0.0022 0.0045 145 ILE A CA 1063 C C A ILE A 122 ? 0.3231 0.2685 0.2068 -0.0236 -0.0067 0.0045 145 ILE A C 1064 C C B ILE A 122 ? 0.3796 0.3271 0.2637 -0.0244 -0.0063 0.0029 145 ILE A C 1065 O O A ILE A 122 ? 0.2875 0.2327 0.1757 -0.0198 -0.0097 0.0070 145 ILE A O 1066 O O B ILE A 122 ? 0.4096 0.3622 0.2992 -0.0221 -0.0079 0.0013 145 ILE A O 1067 C CB A ILE A 122 ? 0.3300 0.2648 0.2140 -0.0212 -0.0028 0.0047 145 ILE A CB 1068 C CB B ILE A 122 ? 0.3438 0.2733 0.2245 -0.0212 -0.0016 0.0066 145 ILE A CB 1069 C CG1 A ILE A 122 ? 0.3854 0.3100 0.2644 -0.0214 0.0008 0.0056 145 ILE A CG1 1070 C CG1 B ILE A 122 ? 0.3043 0.2383 0.1914 -0.0187 -0.0035 0.0055 145 ILE A CG1 1071 C CG2 A ILE A 122 ? 0.3670 0.3026 0.2580 -0.0160 -0.0062 0.0072 145 ILE A CG2 1072 C CG2 B ILE A 122 ? 0.3084 0.2284 0.1823 -0.0227 0.0024 0.0066 145 ILE A CG2 1073 C CD1 A ILE A 122 ? 0.2997 0.2227 0.1833 -0.0177 0.0004 0.0065 145 ILE A CD1 1074 C CD1 B ILE A 122 ? 0.2400 0.1690 0.1310 -0.0143 -0.0037 0.0079 145 ILE A CD1 1075 N N A GLU A 123 ? 0.3216 0.2758 0.2049 -0.0266 -0.0075 0.0016 146 GLU A N 1076 N N B GLU A 123 ? 0.3768 0.3292 0.2591 -0.0265 -0.0076 0.0027 146 GLU A N 1077 C CA A GLU A 123 ? 0.3309 0.2949 0.2197 -0.0241 -0.0123 0.0012 146 GLU A CA 1078 C CA B GLU A 123 ? 0.3675 0.3309 0.2550 -0.0249 -0.0119 0.0014 146 GLU A CA 1079 C C A GLU A 123 ? 0.3326 0.2941 0.2193 -0.0238 -0.0141 0.0046 146 GLU A C 1080 C C B GLU A 123 ? 0.3568 0.3178 0.2432 -0.0239 -0.0142 0.0049 146 GLU A C 1081 O O A GLU A 123 ? 0.3124 0.2677 0.1926 -0.0272 -0.0109 0.0058 146 GLU A O 1082 O O B GLU A 123 ? 0.3447 0.2994 0.2249 -0.0269 -0.0112 0.0065 146 GLU A O 1083 C CB A GLU A 123 ? 0.3466 0.3224 0.2350 -0.0278 -0.0125 -0.0031 146 GLU A CB 1084 C CB B GLU A 123 ? 0.3794 0.3516 0.2634 -0.0304 -0.0108 -0.0023 146 GLU A CB 1085 C CG A GLU A 123 ? 0.3471 0.3261 0.2371 -0.0289 -0.0107 -0.0063 146 GLU A CG 1086 C CG B GLU A 123 ? 0.3721 0.3494 0.2574 -0.0321 -0.0093 -0.0059 146 GLU A CG 1087 C CD A GLU A 123 ? 0.3916 0.3819 0.2792 -0.0347 -0.0096 -0.0105 146 GLU A CD 1088 C CD B GLU A 123 ? 0.4077 0.3953 0.3026 -0.0267 -0.0135 -0.0080 146 GLU A CD 1089 O OE1 A GLU A 123 ? 0.3758 0.3735 0.2624 -0.0366 -0.0111 -0.0114 146 GLU A OE1 1090 O OE1 B GLU A 123 ? 0.4267 0.4140 0.3270 -0.0207 -0.0177 -0.0060 146 GLU A OE1 1091 O OE2 A GLU A 123 ? 0.3640 0.3557 0.2502 -0.0377 -0.0073 -0.0128 146 GLU A OE2 1092 O OE2 B GLU A 123 ? 0.4973 0.4936 0.3938 -0.0286 -0.0127 -0.0118 146 GLU A OE2 1093 N N . PRO A 124 ? 0.3481 0.3138 0.2401 -0.0197 -0.0196 0.0061 147 PRO A N 1094 C CA . PRO A 124 ? 0.3662 0.3297 0.2557 -0.0199 -0.0221 0.0099 147 PRO A CA 1095 C C . PRO A 124 ? 0.3624 0.3291 0.2452 -0.0255 -0.0201 0.0095 147 PRO A C 1096 O O . PRO A 124 ? 0.3347 0.2968 0.2128 -0.0275 -0.0193 0.0125 147 PRO A O 1097 C CB . PRO A 124 ? 0.3786 0.3474 0.2746 -0.0146 -0.0291 0.0105 147 PRO A CB 1098 C CG . PRO A 124 ? 0.3825 0.3515 0.2850 -0.0102 -0.0298 0.0081 147 PRO A CG 1099 C CD . PRO A 124 ? 0.3522 0.3232 0.2523 -0.0143 -0.0239 0.0045 147 PRO A CD 1100 N N A SER A 125 ? 0.3628 0.3379 0.2448 -0.0284 -0.0191 0.0054 148 SER A N 1101 N N B SER A 125 ? 0.3609 0.3359 0.2426 -0.0287 -0.0190 0.0055 148 SER A N 1102 C CA A SER A 125 ? 0.3610 0.3396 0.2364 -0.0344 -0.0171 0.0042 148 SER A CA 1103 C CA B SER A 125 ? 0.3548 0.3327 0.2294 -0.0348 -0.0168 0.0045 148 SER A CA 1104 C C A SER A 125 ? 0.3579 0.3268 0.2250 -0.0391 -0.0111 0.0041 148 SER A C 1105 C C B SER A 125 ? 0.3546 0.3224 0.2214 -0.0389 -0.0111 0.0047 148 SER A C 1106 O O A SER A 125 ? 0.3585 0.3289 0.2195 -0.0441 -0.0094 0.0030 148 SER A O 1107 O O B SER A 125 ? 0.3500 0.3178 0.2106 -0.0433 -0.0095 0.0046 148 SER A O 1108 C CB A SER A 125 ? 0.3770 0.3678 0.2537 -0.0369 -0.0174 -0.0004 148 SER A CB 1109 C CB B SER A 125 ? 0.3725 0.3611 0.2469 -0.0383 -0.0163 -0.0001 148 SER A CB 1110 O OG A SER A 125 ? 0.3768 0.3675 0.2556 -0.0368 -0.0152 -0.0033 148 SER A OG 1111 O OG B SER A 125 ? 0.3547 0.3552 0.2361 -0.0343 -0.0219 -0.0010 148 SER A OG 1112 N N . CYS A 126 ? 0.3471 0.3064 0.2142 -0.0373 -0.0083 0.0047 149 CYS A N 1113 C CA . CYS A 126 ? 0.3330 0.2822 0.1932 -0.0398 -0.0032 0.0044 149 CYS A CA 1114 C C . CYS A 126 ? 0.3509 0.2950 0.2105 -0.0377 -0.0031 0.0079 149 CYS A C 1115 O O . CYS A 126 ? 0.3663 0.3024 0.2215 -0.0380 0.0008 0.0076 149 CYS A O 1116 C CB . CYS A 126 ? 0.3482 0.2910 0.2086 -0.0388 -0.0006 0.0029 149 CYS A CB 1117 S SG . CYS A 126 ? 0.3527 0.3018 0.2124 -0.0429 -0.0002 -0.0011 149 CYS A SG 1118 N N . TYR A 127 ? 0.3306 0.2793 0.1943 -0.0354 -0.0076 0.0111 150 TYR A N 1119 C CA . TYR A 127 ? 0.3497 0.2951 0.2125 -0.0345 -0.0080 0.0149 150 TYR A CA 1120 C C . TYR A 127 ? 0.3740 0.3241 0.2321 -0.0384 -0.0092 0.0162 150 TYR A C 1121 O O . TYR A 127 ? 0.3788 0.3357 0.2378 -0.0393 -0.0127 0.0162 150 TYR A O 1122 C CB . TYR A 127 ? 0.3458 0.2909 0.2153 -0.0299 -0.0125 0.0184 150 TYR A CB 1123 C CG . TYR A 127 ? 0.3349 0.2744 0.2080 -0.0265 -0.0106 0.0178 150 TYR A CG 1124 C CD1 . TYR A 127 ? 0.3232 0.2635 0.1997 -0.0248 -0.0102 0.0148 150 TYR A CD1 1125 C CD2 . TYR A 127 ? 0.3106 0.2452 0.1831 -0.0257 -0.0087 0.0199 150 TYR A CD2 1126 C CE1 . TYR A 127 ? 0.3256 0.2611 0.2045 -0.0223 -0.0083 0.0144 150 TYR A CE1 1127 C CE2 . TYR A 127 ? 0.3446 0.2749 0.2201 -0.0226 -0.0069 0.0193 150 TYR A CE2 1128 C CZ . TYR A 127 ? 0.2838 0.2141 0.1623 -0.0209 -0.0067 0.0167 150 TYR A CZ 1129 O OH . TYR A 127 ? 0.3170 0.2432 0.1983 -0.0180 -0.0052 0.0165 150 TYR A OH 1130 N N . THR A 128 ? 0.3621 0.3095 0.2159 -0.0403 -0.0068 0.0175 151 THR A N 1131 C CA . THR A 128 ? 0.3693 0.3210 0.2200 -0.0431 -0.0091 0.0206 151 THR A CA 1132 C C . THR A 128 ? 0.3560 0.3066 0.2099 -0.0409 -0.0134 0.0260 151 THR A C 1133 O O . THR A 128 ? 0.3632 0.3093 0.2196 -0.0386 -0.0121 0.0270 151 THR A O 1134 C CB . THR A 128 ? 0.3911 0.3419 0.2347 -0.0470 -0.0041 0.0187 151 THR A CB 1135 O OG1 . THR A 128 ? 0.4243 0.3743 0.2638 -0.0495 -0.0006 0.0137 151 THR A OG1 1136 C CG2 . THR A 128 ? 0.3738 0.3309 0.2131 -0.0514 -0.0065 0.0219 151 THR A CG2 1137 N N . ASP A 129 ? 0.3569 0.3114 0.2104 -0.0420 -0.0188 0.0295 152 ASP A N 1138 C CA . ASP A 129 ? 0.3580 0.3099 0.2133 -0.0406 -0.0239 0.0351 152 ASP A CA 1139 C C . ASP A 129 ? 0.3584 0.3049 0.2208 -0.0350 -0.0257 0.0352 152 ASP A C 1140 O O . ASP A 129 ? 0.3420 0.2841 0.2053 -0.0344 -0.0258 0.0379 152 ASP A O 1141 C CB . ASP A 129 ? 0.3727 0.3240 0.2228 -0.0448 -0.0215 0.0379 152 ASP A CB 1142 C CG . ASP A 129 ? 0.3623 0.3195 0.2053 -0.0505 -0.0212 0.0386 152 ASP A CG 1143 O OD1 . ASP A 129 ? 0.3862 0.3476 0.2284 -0.0512 -0.0232 0.0372 152 ASP A OD1 1144 O OD2 . ASP A 129 ? 0.4003 0.3591 0.2389 -0.0544 -0.0184 0.0396 152 ASP A OD2 1145 N N . TYR A 130 ? 0.3675 0.3159 0.2346 -0.0315 -0.0267 0.0318 153 TYR A N 1146 C CA . TYR A 130 ? 0.3563 0.3011 0.2302 -0.0262 -0.0283 0.0310 153 TYR A CA 1147 C C . TYR A 130 ? 0.3548 0.2953 0.2306 -0.0240 -0.0349 0.0360 153 TYR A C 1148 O O . TYR A 130 ? 0.3453 0.2871 0.2195 -0.0241 -0.0406 0.0388 153 TYR A O 1149 C CB . TYR A 130 ? 0.3588 0.3092 0.2369 -0.0236 -0.0295 0.0267 153 TYR A CB 1150 C CG . TYR A 130 ? 0.3353 0.2835 0.2206 -0.0181 -0.0316 0.0253 153 TYR A CG 1151 C CD1 . TYR A 130 ? 0.3350 0.2800 0.2220 -0.0174 -0.0269 0.0230 153 TYR A CD1 1152 C CD2 . TYR A 130 ? 0.3704 0.3201 0.2607 -0.0134 -0.0383 0.0259 153 TYR A CD2 1153 C CE1 . TYR A 130 ? 0.3028 0.2472 0.1961 -0.0129 -0.0287 0.0214 153 TYR A CE1 1154 C CE2 . TYR A 130 ? 0.3280 0.2768 0.2250 -0.0083 -0.0400 0.0236 153 TYR A CE2 1155 C CZ . TYR A 130 ? 0.3407 0.2872 0.2389 -0.0085 -0.0350 0.0214 153 TYR A CZ 1156 O OH . TYR A 130 ? 0.3172 0.2626 0.2217 -0.0039 -0.0367 0.0194 153 TYR A OH 1157 N N . TYR A 131 ? 0.3345 0.2692 0.2136 -0.0215 -0.0350 0.0369 154 TYR A N 1158 C CA . TYR A 131 ? 0.3554 0.2844 0.2370 -0.0186 -0.0419 0.0406 154 TYR A CA 1159 C C . TYR A 131 ? 0.3615 0.2890 0.2506 -0.0126 -0.0431 0.0371 154 TYR A C 1160 O O . TYR A 131 ? 0.3177 0.2472 0.2090 -0.0121 -0.0377 0.0333 154 TYR A O 1161 C CB . TYR A 131 ? 0.3782 0.3013 0.2559 -0.0222 -0.0418 0.0456 154 TYR A CB 1162 C CG . TYR A 131 ? 0.3658 0.2874 0.2455 -0.0222 -0.0362 0.0439 154 TYR A CG 1163 C CD1 . TYR A 131 ? 0.3908 0.3079 0.2757 -0.0183 -0.0378 0.0433 154 TYR A CD1 1164 C CD2 . TYR A 131 ? 0.3193 0.2440 0.1953 -0.0261 -0.0300 0.0433 154 TYR A CD2 1165 C CE1 . TYR A 131 ? 0.3812 0.2977 0.2679 -0.0183 -0.0332 0.0420 154 TYR A CE1 1166 C CE2 . TYR A 131 ? 0.3482 0.2722 0.2263 -0.0252 -0.0255 0.0417 154 TYR A CE2 1167 C CZ . TYR A 131 ? 0.3545 0.2745 0.2378 -0.0215 -0.0271 0.0413 154 TYR A CZ 1168 O OH . TYR A 131 ? 0.3673 0.2873 0.2525 -0.0208 -0.0229 0.0399 154 TYR A OH 1169 N N . ALA A 132 ? 0.3514 0.2756 0.2438 -0.0082 -0.0502 0.0382 155 ALA A N 1170 C CA . ALA A 132 ? 0.3410 0.2659 0.2409 -0.0021 -0.0517 0.0337 155 ALA A CA 1171 C C . ALA A 132 ? 0.3133 0.2353 0.2155 -0.0022 -0.0467 0.0323 155 ALA A C 1172 O O . ALA A 132 ? 0.3150 0.2301 0.2151 -0.0044 -0.0465 0.0360 155 ALA A O 1173 C CB . ALA A 132 ? 0.3560 0.2749 0.2588 0.0034 -0.0607 0.0352 155 ALA A CB 1174 N N . GLN A 133 ? 0.3127 0.2405 0.2189 -0.0004 -0.0430 0.0270 156 GLN A N 1175 C CA . GLN A 133 ? 0.3091 0.2357 0.2178 -0.0001 -0.0384 0.0249 156 GLN A CA 1176 C C . GLN A 133 ? 0.3023 0.2268 0.2063 -0.0045 -0.0323 0.0267 156 GLN A C 1177 O O . GLN A 133 ? 0.3135 0.2361 0.2191 -0.0041 -0.0291 0.0260 156 GLN A O 1178 C CB . GLN A 133 ? 0.2804 0.2008 0.1933 0.0036 -0.0425 0.0256 156 GLN A CB 1179 C CG . GLN A 133 ? 0.3190 0.2422 0.2378 0.0095 -0.0477 0.0217 156 GLN A CG 1180 C CD . GLN A 133 ? 0.3538 0.2743 0.2718 0.0119 -0.0552 0.0240 156 GLN A CD 1181 O OE1 . GLN A 133 ? 0.3995 0.3109 0.3134 0.0102 -0.0588 0.0294 156 GLN A OE1 1182 N NE2 . GLN A 133 ? 0.3497 0.2783 0.2709 0.0154 -0.0577 0.0201 156 GLN A NE2 1183 N N . GLU A 134 ? 0.3037 0.2299 0.2022 -0.0084 -0.0303 0.0282 157 GLU A N 1184 C CA . GLU A 134 ? 0.2807 0.2059 0.1750 -0.0118 -0.0244 0.0289 157 GLU A CA 1185 C C . GLU A 134 ? 0.2634 0.1895 0.1588 -0.0109 -0.0194 0.0250 157 GLU A C 1186 O O . GLU A 134 ? 0.2892 0.2128 0.1841 -0.0110 -0.0160 0.0253 157 GLU A O 1187 C CB . GLU A 134 ? 0.2987 0.2266 0.1869 -0.0161 -0.0227 0.0299 157 GLU A CB 1188 C CG . GLU A 134 ? 0.2948 0.2221 0.1787 -0.0188 -0.0170 0.0297 157 GLU A CG 1189 C CD . GLU A 134 ? 0.3093 0.2395 0.1867 -0.0232 -0.0153 0.0302 157 GLU A CD 1190 O OE1 . GLU A 134 ? 0.3228 0.2559 0.1989 -0.0245 -0.0188 0.0310 157 GLU A OE1 1191 O OE2 . GLU A 134 ? 0.3229 0.2532 0.1970 -0.0249 -0.0106 0.0294 157 GLU A OE2 1192 N N . GLU A 135 ? 0.2738 0.2040 0.1705 -0.0103 -0.0192 0.0213 158 GLU A N 1193 C CA . GLU A 135 ? 0.2603 0.1908 0.1567 -0.0105 -0.0147 0.0179 158 GLU A CA 1194 C C . GLU A 135 ? 0.2847 0.2132 0.1858 -0.0073 -0.0148 0.0173 158 GLU A C 1195 O O . GLU A 135 ? 0.2986 0.2249 0.1982 -0.0076 -0.0109 0.0161 158 GLU A O 1196 C CB . GLU A 135 ? 0.2838 0.2201 0.1795 -0.0120 -0.0146 0.0143 158 GLU A CB 1197 C CG . GLU A 135 ? 0.2850 0.2276 0.1869 -0.0091 -0.0180 0.0113 158 GLU A CG 1198 C CD . GLU A 135 ? 0.3097 0.2555 0.2158 -0.0059 -0.0241 0.0122 158 GLU A CD 1199 O OE1 . GLU A 135 ? 0.3223 0.2639 0.2267 -0.0059 -0.0266 0.0162 158 GLU A OE1 1200 O OE2 . GLU A 135 ? 0.3177 0.2705 0.2289 -0.0030 -0.0271 0.0088 158 GLU A OE2 1201 N N . VAL A 136 ? 0.3009 0.2297 0.2073 -0.0042 -0.0195 0.0180 159 VAL A N 1202 C CA . VAL A 136 ? 0.2904 0.2175 0.2012 -0.0015 -0.0198 0.0175 159 VAL A CA 1203 C C . VAL A 136 ? 0.3081 0.2305 0.2169 -0.0024 -0.0170 0.0203 159 VAL A C 1204 O O . VAL A 136 ? 0.3225 0.2443 0.2315 -0.0019 -0.0138 0.0192 159 VAL A O 1205 C CB . VAL A 136 ? 0.3128 0.2395 0.2287 0.0019 -0.0258 0.0177 159 VAL A CB 1206 C CG1 . VAL A 136 ? 0.2984 0.2232 0.2186 0.0043 -0.0260 0.0168 159 VAL A CG1 1207 C CG2 . VAL A 136 ? 0.3080 0.2413 0.2264 0.0037 -0.0285 0.0141 159 VAL A CG2 1208 N N . GLY A 137 ? 0.3065 0.2265 0.2130 -0.0041 -0.0182 0.0240 160 GLY A N 1209 C CA . GLY A 137 ? 0.3037 0.2219 0.2083 -0.0053 -0.0153 0.0262 160 GLY A CA 1210 C C . GLY A 137 ? 0.3200 0.2387 0.2207 -0.0062 -0.0098 0.0246 160 GLY A C 1211 O O . GLY A 137 ? 0.2893 0.2074 0.1903 -0.0049 -0.0068 0.0243 160 GLY A O 1212 N N . ASP A 138 ? 0.3002 0.2198 0.1969 -0.0080 -0.0085 0.0233 161 ASP A N 1213 C CA . ASP A 138 ? 0.2865 0.2048 0.1787 -0.0088 -0.0038 0.0212 161 ASP A CA 1214 C C . ASP A 138 ? 0.2885 0.2046 0.1815 -0.0069 -0.0019 0.0188 161 ASP A C 1215 O O . ASP A 138 ? 0.2927 0.2056 0.1830 -0.0060 0.0013 0.0181 161 ASP A O 1216 C CB . ASP A 138 ? 0.3189 0.2382 0.2064 -0.0117 -0.0033 0.0199 161 ASP A CB 1217 C CG . ASP A 138 ? 0.3499 0.2709 0.2342 -0.0142 -0.0034 0.0220 161 ASP A CG 1218 O OD1 . ASP A 138 ? 0.3571 0.2786 0.2424 -0.0141 -0.0038 0.0245 161 ASP A OD1 1219 O OD2 . ASP A 138 ? 0.3719 0.2943 0.2521 -0.0169 -0.0030 0.0211 161 ASP A OD2 1220 N N . PHE A 139 ? 0.3000 0.2181 0.1966 -0.0062 -0.0042 0.0175 162 PHE A N 1221 C CA . PHE A 139 ? 0.3058 0.2229 0.2027 -0.0055 -0.0027 0.0154 162 PHE A CA 1222 C C . PHE A 139 ? 0.2905 0.2060 0.1903 -0.0027 -0.0022 0.0167 162 PHE A C 1223 O O . PHE A 139 ? 0.2780 0.1900 0.1749 -0.0020 0.0005 0.0163 162 PHE A O 1224 C CB . PHE A 139 ? 0.3180 0.2402 0.2189 -0.0054 -0.0055 0.0132 162 PHE A CB 1225 C CG . PHE A 139 ? 0.3072 0.2303 0.2102 -0.0045 -0.0048 0.0114 162 PHE A CG 1226 C CD1 . PHE A 139 ? 0.3239 0.2458 0.2223 -0.0070 -0.0023 0.0097 162 PHE A CD1 1227 C CD2 . PHE A 139 ? 0.2983 0.2228 0.2070 -0.0016 -0.0069 0.0118 162 PHE A CD2 1228 C CE1 . PHE A 139 ? 0.3113 0.2344 0.2108 -0.0070 -0.0019 0.0084 162 PHE A CE1 1229 C CE2 . PHE A 139 ? 0.3116 0.2380 0.2220 -0.0012 -0.0063 0.0100 162 PHE A CE2 1230 C CZ . PHE A 139 ? 0.3099 0.2360 0.2157 -0.0039 -0.0038 0.0085 162 PHE A CZ 1231 N N . PHE A 140 ? 0.2702 0.1874 0.1746 -0.0013 -0.0048 0.0184 163 PHE A N 1232 C CA . PHE A 140 ? 0.2746 0.1914 0.1818 0.0007 -0.0044 0.0196 163 PHE A CA 1233 C C . PHE A 140 ? 0.2945 0.2100 0.1986 0.0012 -0.0013 0.0207 163 PHE A C 1234 O O . PHE A 140 ? 0.2821 0.1964 0.1858 0.0032 0.0006 0.0202 163 PHE A O 1235 C CB . PHE A 140 ? 0.2691 0.1873 0.1811 0.0012 -0.0082 0.0212 163 PHE A CB 1236 C CG . PHE A 140 ? 0.2399 0.1598 0.1563 0.0026 -0.0111 0.0190 163 PHE A CG 1237 C CD1 . PHE A 140 ? 0.2779 0.1989 0.1969 0.0041 -0.0105 0.0175 163 PHE A CD1 1238 C CD2 . PHE A 140 ? 0.2328 0.1540 0.1506 0.0026 -0.0145 0.0179 163 PHE A CD2 1239 C CE1 . PHE A 140 ? 0.2759 0.1999 0.1988 0.0052 -0.0127 0.0147 163 PHE A CE1 1240 C CE2 . PHE A 140 ? 0.2705 0.1947 0.1926 0.0046 -0.0169 0.0148 163 PHE A CE2 1241 C CZ . PHE A 140 ? 0.2972 0.2230 0.2219 0.0057 -0.0158 0.0130 163 PHE A CZ 1242 N N . GLN A 141 ? 0.2926 0.2084 0.1937 -0.0005 -0.0006 0.0216 164 GLN A N 1243 C CA . GLN A 141 ? 0.2924 0.2081 0.1902 0.0003 0.0027 0.0216 164 GLN A CA 1244 C C . GLN A 141 ? 0.3074 0.2181 0.2006 0.0018 0.0056 0.0192 164 GLN A C 1245 O O . GLN A 141 ? 0.2980 0.2077 0.1907 0.0047 0.0074 0.0188 164 GLN A O 1246 C CB . GLN A 141 ? 0.3135 0.2315 0.2084 -0.0024 0.0031 0.0225 164 GLN A CB 1247 C CG . GLN A 141 ? 0.3187 0.2389 0.2111 -0.0013 0.0064 0.0218 164 GLN A CG 1248 C CD . GLN A 141 ? 0.3377 0.2627 0.2342 0.0003 0.0064 0.0231 164 GLN A CD 1249 O OE1 . GLN A 141 ? 0.3637 0.2890 0.2606 0.0040 0.0084 0.0217 164 GLN A OE1 1250 N NE2 . GLN A 141 ? 0.3081 0.2367 0.2069 -0.0025 0.0040 0.0258 164 GLN A NE2 1251 N N . GLN A 142 ? 0.3022 0.2097 0.1921 -0.0002 0.0056 0.0176 165 GLN A N 1252 C CA . GLN A 142 ? 0.3300 0.2308 0.2140 0.0000 0.0079 0.0156 165 GLN A CA 1253 C C . GLN A 142 ? 0.3152 0.2135 0.2004 0.0024 0.0078 0.0158 165 GLN A C 1254 O O . GLN A 142 ? 0.3310 0.2238 0.2123 0.0046 0.0093 0.0153 165 GLN A O 1255 C CB . GLN A 142 ? 0.3586 0.2581 0.2390 -0.0039 0.0076 0.0141 165 GLN A CB 1256 C CG . GLN A 142 ? 0.3424 0.2340 0.2154 -0.0054 0.0095 0.0122 165 GLN A CG 1257 C CD . GLN A 142 ? 0.4285 0.3140 0.2954 -0.0043 0.0120 0.0110 165 GLN A CD 1258 O OE1 . GLN A 142 ? 0.4271 0.3160 0.2940 -0.0048 0.0126 0.0108 165 GLN A OE1 1259 N NE2 . GLN A 142 ? 0.4743 0.3510 0.3361 -0.0025 0.0132 0.0102 165 GLN A NE2 1260 N N . VAL A 143 ? 0.3101 0.2125 0.2004 0.0020 0.0056 0.0163 166 VAL A N 1261 C CA . VAL A 143 ? 0.3219 0.2232 0.2134 0.0037 0.0053 0.0165 166 VAL A CA 1262 C C . VAL A 143 ? 0.3116 0.2129 0.2044 0.0077 0.0062 0.0178 166 VAL A C 1263 O O . VAL A 143 ? 0.3171 0.2137 0.2067 0.0099 0.0071 0.0178 166 VAL A O 1264 C CB . VAL A 143 ? 0.2825 0.1896 0.1801 0.0031 0.0029 0.0164 166 VAL A CB 1265 C CG1 . VAL A 143 ? 0.2796 0.1857 0.1771 0.0042 0.0030 0.0164 166 VAL A CG1 1266 C CG2 . VAL A 143 ? 0.2704 0.1794 0.1671 -0.0002 0.0020 0.0146 166 VAL A CG2 1267 N N . VAL A 144 ? 0.3163 0.2231 0.2134 0.0084 0.0057 0.0189 167 VAL A N 1268 C CA . VAL A 144 ? 0.3112 0.2211 0.2105 0.0117 0.0064 0.0198 167 VAL A CA 1269 C C . VAL A 144 ? 0.3343 0.2400 0.2284 0.0144 0.0088 0.0185 167 VAL A C 1270 O O . VAL A 144 ? 0.3288 0.2337 0.2225 0.0185 0.0094 0.0183 167 VAL A O 1271 C CB . VAL A 144 ? 0.3169 0.2337 0.2206 0.0102 0.0053 0.0212 167 VAL A CB 1272 C CG1 . VAL A 144 ? 0.2914 0.2137 0.1962 0.0128 0.0070 0.0215 167 VAL A CG1 1273 C CG2 . VAL A 144 ? 0.2838 0.2034 0.1930 0.0091 0.0024 0.0222 167 VAL A CG2 1274 N N . ASP A 145 ? 0.3265 0.2297 0.2165 0.0125 0.0100 0.0173 168 ASP A N 1275 C CA . ASP A 145 ? 0.3318 0.2305 0.2164 0.0154 0.0122 0.0153 168 ASP A CA 1276 C C . ASP A 145 ? 0.3402 0.2288 0.2195 0.0176 0.0123 0.0145 168 ASP A C 1277 O O . ASP A 145 ? 0.3304 0.2161 0.2077 0.0224 0.0131 0.0135 168 ASP A O 1278 C CB . ASP A 145 ? 0.3321 0.2292 0.2123 0.0121 0.0134 0.0138 168 ASP A CB 1279 C CG . ASP A 145 ? 0.3218 0.2282 0.2056 0.0099 0.0134 0.0148 168 ASP A CG 1280 O OD1 . ASP A 145 ? 0.3746 0.2885 0.2633 0.0110 0.0130 0.0162 168 ASP A OD1 1281 O OD2 . ASP A 145 ? 0.3840 0.2900 0.2646 0.0066 0.0139 0.0140 168 ASP A OD2 1282 N N A LEU A 146 ? 0.3276 0.2114 0.2045 0.0141 0.0113 0.0150 169 LEU A N 1283 N N B LEU A 146 ? 0.3396 0.2233 0.2164 0.0140 0.0113 0.0150 169 LEU A N 1284 C CA A LEU A 146 ? 0.3376 0.2110 0.2081 0.0148 0.0111 0.0148 169 LEU A CA 1285 C CA B LEU A 146 ? 0.3572 0.2305 0.2276 0.0147 0.0110 0.0149 169 LEU A CA 1286 C C A LEU A 146 ? 0.3406 0.2154 0.2142 0.0187 0.0098 0.0165 169 LEU A C 1287 C C B LEU A 146 ? 0.3519 0.2265 0.2253 0.0185 0.0098 0.0165 169 LEU A C 1288 O O A LEU A 146 ? 0.3582 0.2256 0.2274 0.0229 0.0097 0.0165 169 LEU A O 1289 O O B LEU A 146 ? 0.3672 0.2339 0.2359 0.0225 0.0096 0.0166 169 LEU A O 1290 C CB A LEU A 146 ? 0.3207 0.1911 0.1879 0.0089 0.0105 0.0148 169 LEU A CB 1291 C CB B LEU A 146 ? 0.3549 0.2253 0.2222 0.0088 0.0104 0.0149 169 LEU A CB 1292 C CG A LEU A 146 ? 0.3215 0.1798 0.1796 0.0073 0.0103 0.0147 169 LEU A CG 1293 C CG B LEU A 146 ? 0.3890 0.2545 0.2500 0.0044 0.0114 0.0131 169 LEU A CG 1294 C CD1 A LEU A 146 ? 0.2810 0.1285 0.1313 0.0093 0.0115 0.0130 169 LEU A CD1 1295 C CD1 B LEU A 146 ? 0.4205 0.2882 0.2809 -0.0015 0.0105 0.0131 169 LEU A CD1 1296 C CD2 A LEU A 146 ? 0.2621 0.1223 0.1188 0.0005 0.0099 0.0143 169 LEU A CD2 1297 C CD2 B LEU A 146 ? 0.4012 0.2532 0.2525 0.0058 0.0125 0.0117 169 LEU A CD2 1298 N N . PHE A 147 ? 0.3254 0.2092 0.2062 0.0174 0.0087 0.0178 170 PHE A N 1299 C CA . PHE A 147 ? 0.3146 0.2020 0.1992 0.0205 0.0075 0.0193 170 PHE A CA 1300 C C . PHE A 147 ? 0.3272 0.2158 0.2124 0.0266 0.0081 0.0191 170 PHE A C 1301 O O . PHE A 147 ? 0.3791 0.2644 0.2626 0.0304 0.0072 0.0199 170 PHE A O 1302 C CB . PHE A 147 ? 0.2961 0.1939 0.1889 0.0187 0.0064 0.0201 170 PHE A CB 1303 C CG . PHE A 147 ? 0.2722 0.1753 0.1694 0.0213 0.0053 0.0213 170 PHE A CG 1304 C CD1 . PHE A 147 ? 0.3298 0.2300 0.2250 0.0209 0.0042 0.0221 170 PHE A CD1 1305 C CD2 . PHE A 147 ? 0.3087 0.2201 0.2116 0.0232 0.0053 0.0218 170 PHE A CD2 1306 C CE1 . PHE A 147 ? 0.3258 0.2317 0.2252 0.0230 0.0031 0.0232 170 PHE A CE1 1307 C CE2 . PHE A 147 ? 0.3440 0.2613 0.2512 0.0250 0.0042 0.0228 170 PHE A CE2 1308 C CZ . PHE A 147 ? 0.3086 0.2232 0.2142 0.0250 0.0031 0.0235 170 PHE A CZ 1309 N N . LYS A 148 ? 0.3231 0.2175 0.2109 0.0276 0.0094 0.0180 171 LYS A N 1310 C CA . LYS A 148 ? 0.3456 0.2443 0.2349 0.0336 0.0102 0.0169 171 LYS A CA 1311 C C . LYS A 148 ? 0.3697 0.2573 0.2518 0.0388 0.0103 0.0155 171 LYS A C 1312 O O . LYS A 148 ? 0.3875 0.2777 0.2709 0.0451 0.0099 0.0148 171 LYS A O 1313 C CB . LYS A 148 ? 0.3505 0.2575 0.2425 0.0330 0.0119 0.0155 171 LYS A CB 1314 C CG . LYS A 148 ? 0.3317 0.2499 0.2306 0.0289 0.0113 0.0174 171 LYS A CG 1315 C CD . LYS A 148 ? 0.3766 0.3018 0.2763 0.0271 0.0128 0.0164 171 LYS A CD 1316 C CE . LYS A 148 ? 0.3921 0.3262 0.2970 0.0227 0.0117 0.0186 171 LYS A CE 1317 N NZ . LYS A 148 ? 0.3741 0.3157 0.2788 0.0200 0.0132 0.0181 171 LYS A NZ 1318 N N . THR A 149 ? 0.3889 0.2644 0.2635 0.0362 0.0104 0.0149 172 THR A N 1319 C CA . THR A 149 ? 0.4175 0.2798 0.2840 0.0405 0.0099 0.0136 172 THR A CA 1320 C C . THR A 149 ? 0.4225 0.2760 0.2848 0.0414 0.0074 0.0162 172 THR A C 1321 O O . THR A 149 ? 0.4092 0.2488 0.2632 0.0447 0.0062 0.0158 172 THR A O 1322 C CB . THR A 149 ? 0.4374 0.2885 0.2956 0.0369 0.0111 0.0116 172 THR A CB 1323 O OG1 . THR A 149 ? 0.4253 0.2719 0.2805 0.0297 0.0104 0.0135 172 THR A OG1 1324 C CG2 . THR A 149 ? 0.4402 0.2990 0.3008 0.0355 0.0136 0.0088 172 THR A CG2 1325 N N . LEU A 150 ? 0.3817 0.2420 0.2487 0.0378 0.0065 0.0187 173 LEU A N 1326 C CA . LEU A 150 ? 0.3912 0.2440 0.2535 0.0363 0.0043 0.0213 173 LEU A CA 1327 C C . LEU A 150 ? 0.3829 0.2464 0.2525 0.0393 0.0030 0.0231 173 LEU A C 1328 O O . LEU A 150 ? 0.3620 0.2320 0.2355 0.0349 0.0025 0.0245 173 LEU A O 1329 C CB . LEU A 150 ? 0.3738 0.2257 0.2343 0.0277 0.0046 0.0219 173 LEU A CB 1330 C CG . LEU A 150 ? 0.4301 0.2709 0.2820 0.0236 0.0055 0.0204 173 LEU A CG 1331 C CD1 . LEU A 150 ? 0.3793 0.2249 0.2323 0.0157 0.0061 0.0203 173 LEU A CD1 1332 C CD2 . LEU A 150 ? 0.4059 0.2293 0.2461 0.0244 0.0040 0.0213 173 LEU A CD2 1333 N N . ASP A 151 ? 0.3963 0.2630 0.2683 0.0469 0.0025 0.0224 174 ASP A N 1334 C CA . ASP A 151 ? 0.3931 0.2716 0.2723 0.0502 0.0014 0.0238 174 ASP A CA 1335 C C . ASP A 151 ? 0.4105 0.2804 0.2839 0.0515 -0.0015 0.0266 174 ASP A C 1336 O O . ASP A 151 ? 0.3884 0.2522 0.2580 0.0583 -0.0034 0.0270 174 ASP A O 1337 C CB . ASP A 151 ? 0.4101 0.2968 0.2937 0.0577 0.0020 0.0216 174 ASP A CB 1338 C CG . ASP A 151 ? 0.4215 0.3223 0.3128 0.0602 0.0010 0.0227 174 ASP A CG 1339 O OD1 . ASP A 151 ? 0.3887 0.2906 0.2808 0.0571 -0.0004 0.0252 174 ASP A OD1 1340 O OD2 . ASP A 151 ? 0.4313 0.3425 0.3274 0.0656 0.0016 0.0208 174 ASP A OD2 1341 N N . SER A 152 ? 0.3925 0.2629 0.2655 0.0448 -0.0020 0.0285 175 SER A N 1342 C CA . SER A 152 ? 0.3842 0.2482 0.2515 0.0435 -0.0045 0.0314 175 SER A CA 1343 C C . SER A 152 ? 0.4013 0.2729 0.2728 0.0496 -0.0066 0.0329 175 SER A C 1344 O O . SER A 152 ? 0.4004 0.2631 0.2653 0.0530 -0.0094 0.0351 175 SER A O 1345 C CB . SER A 152 ? 0.3779 0.2471 0.2471 0.0348 -0.0039 0.0318 175 SER A CB 1346 O OG . SER A 152 ? 0.3640 0.2276 0.2296 0.0298 -0.0023 0.0303 175 SER A OG 1347 N N . TYR A 153 ? 0.3887 0.2762 0.2704 0.0505 -0.0056 0.0318 176 TYR A N 1348 C CA . TYR A 153 ? 0.3836 0.2799 0.2694 0.0554 -0.0075 0.0331 176 TYR A CA 1349 C C . TYR A 153 ? 0.4107 0.3019 0.2933 0.0651 -0.0090 0.0326 176 TYR A C 1350 O O . TYR A 153 ? 0.4008 0.2886 0.2800 0.0697 -0.0123 0.0350 176 TYR A O 1351 C CB . TYR A 153 ? 0.3700 0.2840 0.2667 0.0544 -0.0059 0.0316 176 TYR A CB 1352 C CG . TYR A 153 ? 0.3573 0.2817 0.2581 0.0586 -0.0079 0.0328 176 TYR A CG 1353 C CD1 . TYR A 153 ? 0.3906 0.3212 0.2938 0.0544 -0.0089 0.0343 176 TYR A CD1 1354 C CD2 . TYR A 153 ? 0.4162 0.3451 0.3186 0.0672 -0.0088 0.0320 176 TYR A CD2 1355 C CE1 . TYR A 153 ? 0.3711 0.3117 0.2779 0.0578 -0.0108 0.0354 176 TYR A CE1 1356 C CE2 . TYR A 153 ? 0.4237 0.3639 0.3302 0.0710 -0.0109 0.0331 176 TYR A CE2 1357 C CZ . TYR A 153 ? 0.4105 0.3558 0.3188 0.0658 -0.0118 0.0350 176 TYR A CZ 1358 O OH . TYR A 153 ? 0.4418 0.3984 0.3537 0.0681 -0.0138 0.0363 176 TYR A OH 1359 N N . THR A 154 ? 0.4078 0.2982 0.2912 0.0685 -0.0071 0.0296 177 THR A N 1360 C CA . THR A 154 ? 0.4276 0.3144 0.3088 0.0785 -0.0086 0.0280 177 THR A CA 1361 C C . THR A 154 ? 0.4651 0.3303 0.3339 0.0806 -0.0116 0.0299 177 THR A C 1362 O O . THR A 154 ? 0.4763 0.3359 0.3415 0.0886 -0.0150 0.0309 177 THR A O 1363 C CB . THR A 154 ? 0.4330 0.3257 0.3180 0.0809 -0.0057 0.0238 177 THR A CB 1364 O OG1 . THR A 154 ? 0.4359 0.3485 0.3313 0.0785 -0.0038 0.0231 177 THR A OG1 1365 C CG2 . THR A 154 ? 0.4733 0.3624 0.3559 0.0923 -0.0071 0.0209 177 THR A CG2 1366 N N . ALA A 155 ? 0.4687 0.3212 0.3305 0.0735 -0.0106 0.0305 178 ALA A N 1367 C CA . ALA A 155 ? 0.4910 0.3216 0.3397 0.0740 -0.0135 0.0325 178 ALA A CA 1368 C C . ALA A 155 ? 0.4882 0.3151 0.3326 0.0741 -0.0174 0.0371 178 ALA A C 1369 O O . ALA A 155 ? 0.5076 0.3196 0.3430 0.0793 -0.0213 0.0390 178 ALA A O 1370 C CB . ALA A 155 ? 0.4771 0.2974 0.3192 0.0647 -0.0117 0.0325 178 ALA A CB 1371 N N . LEU A 156 ? 0.4572 0.2966 0.3073 0.0681 -0.0167 0.0389 179 LEU A N 1372 C CA . LEU A 156 ? 0.4812 0.3203 0.3283 0.0673 -0.0200 0.0430 179 LEU A CA 1373 C C . LEU A 156 ? 0.4938 0.3403 0.3452 0.0775 -0.0228 0.0434 179 LEU A C 1374 O O . LEU A 156 ? 0.5104 0.3464 0.3541 0.0819 -0.0273 0.0467 179 LEU A O 1375 C CB . LEU A 156 ? 0.4667 0.3184 0.3192 0.0582 -0.0183 0.0438 179 LEU A CB 1376 C CG . LEU A 156 ? 0.4499 0.2943 0.2963 0.0476 -0.0168 0.0442 179 LEU A CG 1377 C CD1 . LEU A 156 ? 0.3721 0.2331 0.2278 0.0408 -0.0142 0.0427 179 LEU A CD1 1378 C CD2 . LEU A 156 ? 0.4433 0.2728 0.2767 0.0436 -0.0200 0.0484 179 LEU A CD2 1379 N N . SER A 157 ? 0.4810 0.3448 0.3438 0.0813 -0.0205 0.0402 180 SER A N 1380 C CA . SER A 157 ? 0.5032 0.3781 0.3717 0.0905 -0.0226 0.0398 180 SER A CA 1381 C C . SER A 157 ? 0.5420 0.4036 0.4037 0.1014 -0.0261 0.0391 180 SER A C 1382 O O . SER A 157 ? 0.5425 0.4051 0.4033 0.1091 -0.0302 0.0409 180 SER A O 1383 C CB . SER A 157 ? 0.5013 0.3962 0.3820 0.0918 -0.0190 0.0357 180 SER A CB 1384 O OG . SER A 157 ? 0.5227 0.4319 0.4097 0.0992 -0.0209 0.0354 180 SER A OG 1385 N N . ASP A 158 ? 0.5322 0.3819 0.3894 0.1024 -0.0246 0.0364 181 ASP A N 1386 C CA . ASP A 158 ? 0.5716 0.4073 0.4222 0.1129 -0.0276 0.0347 181 ASP A CA 1387 C C . ASP A 158 ? 0.6030 0.4166 0.4401 0.1140 -0.0331 0.0395 181 ASP A C 1388 O O . ASP A 158 ? 0.6049 0.4064 0.4362 0.1245 -0.0371 0.0388 181 ASP A O 1389 C CB . ASP A 158 ? 0.5775 0.4037 0.4248 0.1123 -0.0246 0.0305 181 ASP A CB 1390 C CG . ASP A 158 ? 0.5757 0.4217 0.4347 0.1144 -0.0202 0.0252 181 ASP A CG 1391 O OD1 . ASP A 158 ? 0.5661 0.4329 0.4355 0.1178 -0.0197 0.0242 181 ASP A OD1 1392 O OD2 . ASP A 158 ? 0.6121 0.4529 0.4692 0.1115 -0.0172 0.0222 181 ASP A OD2 1393 N N . ALA A 159 ? 0.5865 0.3940 0.4180 0.1031 -0.0331 0.0439 182 ALA A N 1394 C CA . ALA A 159 ? 0.5909 0.3787 0.4087 0.1010 -0.0381 0.0494 182 ALA A CA 1395 C C . ALA A 159 ? 0.5893 0.3876 0.4098 0.1008 -0.0410 0.0536 182 ALA A C 1396 O O . ALA A 159 ? 0.6068 0.3923 0.4166 0.0962 -0.0445 0.0587 182 ALA A O 1397 C CB . ALA A 159 ? 0.5835 0.3587 0.3924 0.0881 -0.0362 0.0512 182 ALA A CB 1398 N N . GLY A 160 ? 0.5555 0.3767 0.3892 0.1057 -0.0397 0.0515 183 GLY A N 1399 C CA . GLY A 160 ? 0.5647 0.3979 0.4016 0.1061 -0.0424 0.0550 183 GLY A CA 1400 C C . GLY A 160 ? 0.5618 0.4047 0.4012 0.0931 -0.0397 0.0571 183 GLY A C 1401 O O . GLY A 160 ? 0.5523 0.4013 0.3912 0.0910 -0.0422 0.0607 183 GLY A O 1402 N N . ILE A 161 ? 0.5287 0.3742 0.3712 0.0846 -0.0347 0.0544 184 ILE A N 1403 C CA . ILE A 161 ? 0.4842 0.3377 0.3285 0.0728 -0.0324 0.0557 184 ILE A CA 1404 C C . ILE A 161 ? 0.4798 0.3553 0.3388 0.0710 -0.0278 0.0514 184 ILE A C 1405 O O . ILE A 161 ? 0.4499 0.3271 0.3132 0.0701 -0.0242 0.0478 184 ILE A O 1406 C CB . ILE A 161 ? 0.4989 0.3372 0.3336 0.0634 -0.0309 0.0563 184 ILE A CB 1407 C CG1 . ILE A 161 ? 0.5298 0.3449 0.3484 0.0635 -0.0357 0.0609 184 ILE A CG1 1408 C CG2 . ILE A 161 ? 0.4374 0.2861 0.2752 0.0523 -0.0283 0.0563 184 ILE A CG2 1409 C CD1 . ILE A 161 ? 0.5413 0.3393 0.3495 0.0554 -0.0342 0.0608 184 ILE A CD1 1410 N N . THR A 162 ? 0.4859 0.3776 0.3519 0.0709 -0.0285 0.0521 185 THR A N 1411 C CA . THR A 162 ? 0.4672 0.3788 0.3461 0.0697 -0.0252 0.0487 185 THR A CA 1412 C C . THR A 162 ? 0.4593 0.3810 0.3411 0.0617 -0.0248 0.0496 185 THR A C 1413 O O . THR A 162 ? 0.4483 0.3660 0.3236 0.0593 -0.0277 0.0532 185 THR A O 1414 C CB . THR A 162 ? 0.4825 0.4065 0.3686 0.0791 -0.0262 0.0472 185 THR A CB 1415 O OG1 . THR A 162 ? 0.5051 0.4312 0.3886 0.0836 -0.0306 0.0506 185 THR A OG1 1416 C CG2 . THR A 162 ? 0.4930 0.4092 0.3775 0.0871 -0.0259 0.0449 185 THR A CG2 1417 N N . PRO A 163 ? 0.4233 0.3569 0.3138 0.0565 -0.0213 0.0464 186 PRO A N 1418 C CA . PRO A 163 ? 0.4045 0.3472 0.2976 0.0493 -0.0211 0.0465 186 PRO A CA 1419 C C . PRO A 163 ? 0.4233 0.3763 0.3182 0.0523 -0.0240 0.0486 186 PRO A C 1420 O O . PRO A 163 ? 0.4323 0.3931 0.3319 0.0594 -0.0249 0.0482 186 PRO A O 1421 C CB . PRO A 163 ? 0.3906 0.3453 0.2941 0.0460 -0.0177 0.0424 186 PRO A CB 1422 C CG . PRO A 163 ? 0.4090 0.3554 0.3117 0.0481 -0.0156 0.0408 186 PRO A CG 1423 C CD . PRO A 163 ? 0.4205 0.3590 0.3180 0.0567 -0.0179 0.0427 186 PRO A CD 1424 N N A SER A 164 ? 0.4342 0.3882 0.3253 0.0468 -0.0254 0.0505 187 SER A N 1425 N N B SER A 164 ? 0.4392 0.3945 0.3313 0.0465 -0.0252 0.0502 187 SER A N 1426 C CA A SER A 164 ? 0.4339 0.3971 0.3251 0.0485 -0.0287 0.0531 187 SER A CA 1427 C CA B SER A 164 ? 0.4511 0.4164 0.3441 0.0484 -0.0281 0.0524 187 SER A CA 1428 C C A SER A 164 ? 0.4297 0.4003 0.3210 0.0398 -0.0282 0.0526 187 SER A C 1429 C C B SER A 164 ? 0.4455 0.4164 0.3372 0.0399 -0.0282 0.0525 187 SER A C 1430 O O A SER A 164 ? 0.4002 0.3640 0.2866 0.0331 -0.0271 0.0524 187 SER A O 1431 O O B SER A 164 ? 0.4299 0.3931 0.3160 0.0335 -0.0273 0.0525 187 SER A O 1432 C CB A SER A 164 ? 0.4581 0.4087 0.3390 0.0543 -0.0332 0.0580 187 SER A CB 1433 C CB B SER A 164 ? 0.4680 0.4229 0.3525 0.0558 -0.0325 0.0568 187 SER A CB 1434 O OG A SER A 164 ? 0.4089 0.3672 0.2884 0.0558 -0.0369 0.0611 187 SER A OG 1435 O OG B SER A 164 ? 0.5042 0.4398 0.3778 0.0538 -0.0332 0.0590 187 SER A OG 1436 N N . GLU A 165 ? 0.4632 0.4490 0.3603 0.0398 -0.0292 0.0522 188 GLU A N 1437 C CA . GLU A 165 ? 0.4925 0.4869 0.3898 0.0322 -0.0292 0.0515 188 GLU A CA 1438 C C . GLU A 165 ? 0.5380 0.5245 0.4240 0.0303 -0.0325 0.0564 188 GLU A C 1439 O O . GLU A 165 ? 0.5679 0.5546 0.4500 0.0223 -0.0318 0.0558 188 GLU A O 1440 C CB . GLU A 165 ? 0.5164 0.5289 0.4220 0.0328 -0.0296 0.0500 188 GLU A CB 1441 C CG . GLU A 165 ? 0.5652 0.5867 0.4812 0.0344 -0.0270 0.0459 188 GLU A CG 1442 C CD . GLU A 165 ? 0.6422 0.6630 0.5622 0.0278 -0.0236 0.0415 188 GLU A CD 1443 O OE1 . GLU A 165 ? 0.6459 0.6615 0.5614 0.0223 -0.0232 0.0409 188 GLU A OE1 1444 O OE2 . GLU A 165 ? 0.6845 0.7100 0.6117 0.0282 -0.0217 0.0386 188 GLU A OE2 1445 N N . ASP A 166 ? 0.5497 0.5277 0.4294 0.0374 -0.0362 0.0610 189 ASP A N 1446 C CA . ASP A 166 ? 0.5982 0.5674 0.4657 0.0358 -0.0405 0.0667 189 ASP A CA 1447 C C . ASP A 166 ? 0.5847 0.5322 0.4400 0.0373 -0.0427 0.0706 189 ASP A C 1448 O O . ASP A 166 ? 0.6012 0.5404 0.4455 0.0316 -0.0450 0.0745 189 ASP A O 1449 C CB . ASP A 166 ? 0.6207 0.5972 0.4885 0.0428 -0.0450 0.0701 189 ASP A CB 1450 C CG . ASP A 166 ? 0.7151 0.7126 0.5941 0.0419 -0.0435 0.0667 189 ASP A CG 1451 O OD1 . ASP A 166 ? 0.8170 0.8236 0.6975 0.0333 -0.0419 0.0648 189 ASP A OD1 1452 O OD2 . ASP A 166 ? 0.8547 0.8603 0.7415 0.0494 -0.0436 0.0652 189 ASP A OD2 1453 N N . ALA A 167 ? 0.5659 0.5043 0.4222 0.0450 -0.0425 0.0700 190 ALA A N 1454 C CA . ALA A 167 ? 0.5672 0.4831 0.4115 0.0464 -0.0445 0.0731 190 ALA A CA 1455 C C . ALA A 167 ? 0.5638 0.4722 0.4031 0.0361 -0.0413 0.0718 190 ALA A C 1456 O O . ALA A 167 ? 0.5190 0.4379 0.3667 0.0310 -0.0367 0.0668 190 ALA A O 1457 C CB . ALA A 167 ? 0.5738 0.4829 0.4211 0.0572 -0.0446 0.0714 190 ALA A CB 1458 N N . THR A 168 ? 0.5491 0.4395 0.3742 0.0327 -0.0440 0.0762 191 THR A N 1459 C CA . THR A 168 ? 0.5629 0.4454 0.3825 0.0235 -0.0411 0.0748 191 THR A CA 1460 C C . THR A 168 ? 0.5600 0.4195 0.3685 0.0262 -0.0431 0.0773 191 THR A C 1461 O O . THR A 168 ? 0.5948 0.4427 0.3978 0.0349 -0.0476 0.0808 191 THR A O 1462 C CB . THR A 168 ? 0.5697 0.4559 0.3822 0.0116 -0.0413 0.0766 191 THR A CB 1463 O OG1 . THR A 168 ? 0.6225 0.4941 0.4203 0.0112 -0.0468 0.0837 191 THR A OG1 1464 C CG2 . THR A 168 ? 0.5742 0.4834 0.3973 0.0091 -0.0396 0.0737 191 THR A CG2 1465 N N . TYR A 169 ? 0.5442 0.3968 0.3494 0.0195 -0.0399 0.0752 192 TYR A N 1466 C CA . TYR A 169 ? 0.5411 0.3733 0.3384 0.0227 -0.0407 0.0758 192 TYR A CA 1467 C C . TYR A 169 ? 0.5468 0.3642 0.3301 0.0120 -0.0408 0.0779 192 TYR A C 1468 O O . TYR A 169 ? 0.5463 0.3724 0.3284 0.0010 -0.0386 0.0772 192 TYR A O 1469 C CB . TYR A 169 ? 0.5362 0.3746 0.3456 0.0276 -0.0361 0.0697 192 TYR A CB 1470 C CG . TYR A 169 ? 0.4957 0.3460 0.3169 0.0382 -0.0362 0.0678 192 TYR A CG 1471 C CD1 . TYR A 169 ? 0.5437 0.3843 0.3623 0.0494 -0.0398 0.0694 192 TYR A CD1 1472 C CD2 . TYR A 169 ? 0.4705 0.3418 0.3054 0.0372 -0.0330 0.0640 192 TYR A CD2 1473 C CE1 . TYR A 169 ? 0.5291 0.3832 0.3589 0.0588 -0.0397 0.0672 192 TYR A CE1 1474 C CE2 . TYR A 169 ? 0.4360 0.3194 0.2813 0.0456 -0.0330 0.0623 192 TYR A CE2 1475 C CZ . TYR A 169 ? 0.5101 0.3858 0.3531 0.0563 -0.0362 0.0637 192 TYR A CZ 1476 O OH . TYR A 169 ? 0.4478 0.3378 0.3015 0.0645 -0.0360 0.0615 192 TYR A OH 1477 N N . LYS A 170 ? 0.5665 0.3617 0.3389 0.0153 -0.0434 0.0803 193 LYS A N 1478 C CA . LYS A 170 ? 0.5926 0.3711 0.3502 0.0052 -0.0439 0.0826 193 LYS A CA 1479 C C . LYS A 170 ? 0.5686 0.3467 0.3301 0.0024 -0.0390 0.0773 193 LYS A C 1480 O O . LYS A 170 ? 0.5802 0.3554 0.3478 0.0111 -0.0379 0.0742 193 LYS A O 1481 C CB . LYS A 170 ? 0.6404 0.3917 0.3813 0.0092 -0.0503 0.0885 193 LYS A CB 1482 C CG . LYS A 170 ? 0.7013 0.4511 0.4339 0.0078 -0.0559 0.0952 193 LYS A CG 1483 C CD . LYS A 170 ? 0.8089 0.5412 0.5341 0.0198 -0.0629 0.0999 193 LYS A CD 1484 C CE . LYS A 170 ? 0.7755 0.5178 0.5018 0.0235 -0.0674 0.1044 193 LYS A CE 1485 N NZ . LYS A 170 ? 0.8232 0.5474 0.5429 0.0377 -0.0749 0.1084 193 LYS A NZ 1486 N N . LEU A 171 ? 0.5606 0.3405 0.3171 -0.0101 -0.0366 0.0765 194 LEU A N 1487 C CA . LEU A 171 ? 0.5560 0.3355 0.3149 -0.0135 -0.0325 0.0720 194 LEU A CA 1488 C C . LEU A 171 ? 0.5775 0.3357 0.3292 -0.0079 -0.0339 0.0722 194 LEU A C 1489 O O . LEU A 171 ? 0.5274 0.2886 0.2872 -0.0037 -0.0305 0.0674 194 LEU A O 1490 C CB . LEU A 171 ? 0.5653 0.3495 0.3179 -0.0281 -0.0304 0.0715 194 LEU A CB 1491 C CG . LEU A 171 ? 0.5329 0.3200 0.2884 -0.0330 -0.0260 0.0665 194 LEU A CG 1492 C CD1 . LEU A 171 ? 0.4661 0.2728 0.2412 -0.0262 -0.0219 0.0603 194 LEU A CD1 1493 C CD2 . LEU A 171 ? 0.5819 0.3743 0.3297 -0.0481 -0.0245 0.0662 194 LEU A CD2 1494 N N . SER A 172 ? 0.5743 0.3097 0.3095 -0.0085 -0.0389 0.0777 195 SER A N 1495 C CA . SER A 172 ? 0.5955 0.3080 0.3215 -0.0047 -0.0404 0.0775 195 SER A CA 1496 C C . SER A 172 ? 0.5665 0.2795 0.3023 0.0108 -0.0409 0.0748 195 SER A C 1497 O O . SER A 172 ? 0.5901 0.2932 0.3253 0.0153 -0.0398 0.0716 195 SER A O 1498 C CB . SER A 172 ? 0.6307 0.3154 0.3349 -0.0091 -0.0466 0.0843 195 SER A CB 1499 O OG . SER A 172 ? 0.6738 0.3523 0.3766 0.0014 -0.0519 0.0882 195 SER A OG 1500 N N . ASP A 173 ? 0.5644 0.2898 0.3094 0.0190 -0.0425 0.0757 196 ASP A N 1501 C CA . ASP A 173 ? 0.5567 0.2863 0.3122 0.0335 -0.0426 0.0726 196 ASP A CA 1502 C C . ASP A 173 ? 0.5494 0.2981 0.3206 0.0340 -0.0362 0.0660 196 ASP A C 1503 O O . ASP A 173 ? 0.5495 0.2962 0.3255 0.0421 -0.0350 0.0623 196 ASP A O 1504 C CB . ASP A 173 ? 0.5588 0.2993 0.3204 0.0413 -0.0457 0.0749 196 ASP A CB 1505 C CG . ASP A 173 ? 0.6278 0.3472 0.3741 0.0448 -0.0532 0.0814 196 ASP A CG 1506 O OD1 . ASP A 173 ? 0.6200 0.3153 0.3530 0.0451 -0.0559 0.0828 196 ASP A OD1 1507 O OD2 . ASP A 173 ? 0.6124 0.3399 0.3602 0.0467 -0.0562 0.0849 196 ASP A OD2 1508 N N . ILE A 174 ? 0.5418 0.3081 0.3200 0.0253 -0.0328 0.0649 197 ILE A N 1509 C CA . ILE A 174 ? 0.5226 0.3075 0.3155 0.0245 -0.0272 0.0592 197 ILE A CA 1510 C C . ILE A 174 ? 0.5260 0.3001 0.3141 0.0211 -0.0249 0.0565 197 ILE A C 1511 O O . ILE A 174 ? 0.5265 0.3036 0.3217 0.0268 -0.0225 0.0526 197 ILE A O 1512 C CB . ILE A 174 ? 0.5069 0.3102 0.3065 0.0158 -0.0247 0.0583 197 ILE A CB 1513 C CG1 . ILE A 174 ? 0.5001 0.3172 0.3070 0.0197 -0.0263 0.0598 197 ILE A CG1 1514 C CG2 . ILE A 174 ? 0.4421 0.2588 0.2534 0.0139 -0.0196 0.0526 197 ILE A CG2 1515 C CD1 . ILE A 174 ? 0.4474 0.2794 0.2574 0.0105 -0.0249 0.0595 197 ILE A CD1 1516 N N . GLU A 175 ? 0.5463 0.3074 0.3212 0.0115 -0.0258 0.0588 198 GLU A N 1517 C CA . GLU A 175 ? 0.5584 0.3078 0.3265 0.0069 -0.0240 0.0567 198 GLU A CA 1518 C C . GLU A 175 ? 0.5791 0.3106 0.3423 0.0165 -0.0257 0.0557 198 GLU A C 1519 O O . GLU A 175 ? 0.5744 0.3054 0.3407 0.0177 -0.0228 0.0515 198 GLU A O 1520 C CB . GLU A 175 ? 0.5873 0.3257 0.3405 -0.0059 -0.0254 0.0600 198 GLU A CB 1521 C CG . GLU A 175 ? 0.5522 0.3097 0.3106 -0.0163 -0.0225 0.0589 198 GLU A CG 1522 C CD . GLU A 175 ? 0.6209 0.3699 0.3643 -0.0295 -0.0239 0.0622 198 GLU A CD 1523 O OE1 . GLU A 175 ? 0.6380 0.3666 0.3668 -0.0301 -0.0283 0.0672 198 GLU A OE1 1524 O OE2 . GLU A 175 ? 0.5953 0.3588 0.3418 -0.0391 -0.0207 0.0597 198 GLU A OE2 1525 N N . ASP A 176 ? 0.5879 0.3050 0.3436 0.0237 -0.0306 0.0591 199 ASP A N 1526 C CA . ASP A 176 ? 0.6006 0.2993 0.3502 0.0327 -0.0328 0.0577 199 ASP A CA 1527 C C . ASP A 176 ? 0.5694 0.2840 0.3346 0.0434 -0.0300 0.0526 199 ASP A C 1528 O O . ASP A 176 ? 0.5531 0.2620 0.3184 0.0471 -0.0283 0.0486 199 ASP A O 1529 C CB . ASP A 176 ? 0.6191 0.2991 0.3575 0.0393 -0.0395 0.0625 199 ASP A CB 1530 C CG . ASP A 176 ? 0.6795 0.3382 0.3987 0.0287 -0.0433 0.0682 199 ASP A CG 1531 O OD1 . ASP A 176 ? 0.6886 0.3424 0.4006 0.0168 -0.0411 0.0679 199 ASP A OD1 1532 O OD2 . ASP A 176 ? 0.7194 0.3652 0.4297 0.0328 -0.0491 0.0731 199 ASP A OD2 1533 N N . ALA A 177 ? 0.5648 0.2997 0.3426 0.0473 -0.0294 0.0528 200 ALA A N 1534 C CA . ALA A 177 ? 0.5358 0.2879 0.3285 0.0567 -0.0270 0.0486 200 ALA A CA 1535 C C . ALA A 177 ? 0.5361 0.2978 0.3361 0.0524 -0.0216 0.0439 200 ALA A C 1536 O O . ALA A 177 ? 0.5450 0.3108 0.3511 0.0596 -0.0198 0.0397 200 ALA A O 1537 C CB . ALA A 177 ? 0.5107 0.2833 0.3145 0.0583 -0.0270 0.0499 200 ALA A CB 1538 N N . LEU A 178 ? 0.5161 0.2817 0.3152 0.0410 -0.0193 0.0444 201 LEU A N 1539 C CA . LEU A 178 ? 0.5097 0.2869 0.3166 0.0364 -0.0146 0.0404 201 LEU A CA 1540 C C . LEU A 178 ? 0.5244 0.2856 0.3215 0.0331 -0.0138 0.0387 201 LEU A C 1541 O O . LEU A 178 ? 0.5213 0.2869 0.3232 0.0342 -0.0108 0.0348 201 LEU A O 1542 C CB . LEU A 178 ? 0.4749 0.2654 0.2863 0.0269 -0.0128 0.0412 201 LEU A CB 1543 C CG . LEU A 178 ? 0.4679 0.2766 0.2907 0.0297 -0.0130 0.0419 201 LEU A CG 1544 C CD1 . LEU A 178 ? 0.4571 0.2775 0.2830 0.0204 -0.0118 0.0422 201 LEU A CD1 1545 C CD2 . LEU A 178 ? 0.4313 0.2531 0.2667 0.0378 -0.0112 0.0388 201 LEU A CD2 1546 N N . ALA A 179 ? 0.5456 0.2870 0.3280 0.0291 -0.0167 0.0416 202 ALA A N 1547 C CA . ALA A 179 ? 0.5537 0.2770 0.3250 0.0263 -0.0166 0.0401 202 ALA A CA 1548 C C . ALA A 179 ? 0.5736 0.2907 0.3464 0.0373 -0.0167 0.0363 202 ALA A C 1549 O O . ALA A 179 ? 0.5677 0.2777 0.3366 0.0354 -0.0147 0.0330 202 ALA A O 1550 C CB . ALA A 179 ? 0.5887 0.2893 0.3421 0.0204 -0.0208 0.0447 202 ALA A CB 1551 N N . ALA A 180 ? 0.5761 0.2963 0.3539 0.0486 -0.0189 0.0365 203 ALA A N 1552 C CA . ALA A 180 ? 0.5871 0.3038 0.3671 0.0605 -0.0193 0.0325 203 ALA A CA 1553 C C . ALA A 180 ? 0.5677 0.3020 0.3596 0.0612 -0.0143 0.0274 203 ALA A C 1554 O O . ALA A 180 ? 0.5849 0.3153 0.3766 0.0677 -0.0135 0.0230 203 ALA A O 1555 C CB . ALA A 180 ? 0.5784 0.3011 0.3640 0.0722 -0.0227 0.0338 203 ALA A CB 1556 N N . ILE A 181 ? 0.5344 0.2876 0.3362 0.0547 -0.0112 0.0278 204 ILE A N 1557 C CA . ILE A 181 ? 0.5006 0.2692 0.3124 0.0540 -0.0068 0.0237 204 ILE A CA 1558 C C . ILE A 181 ? 0.5063 0.2721 0.3141 0.0436 -0.0042 0.0227 204 ILE A C 1559 O O . ILE A 181 ? 0.4840 0.2631 0.2997 0.0411 -0.0008 0.0201 204 ILE A O 1560 C CB . ILE A 181 ? 0.4799 0.2718 0.3062 0.0556 -0.0052 0.0238 204 ILE A CB 1561 C CG1 . ILE A 181 ? 0.4743 0.2738 0.3032 0.0474 -0.0052 0.0272 204 ILE A CG1 1562 C CG2 . ILE A 181 ? 0.4895 0.2861 0.3202 0.0664 -0.0072 0.0235 204 ILE A CG2 1563 C CD1 . ILE A 181 ? 0.4643 0.2862 0.3074 0.0472 -0.0032 0.0266 204 ILE A CD1 1564 N N . HIS A 182 ? 0.5144 0.2631 0.3095 0.0371 -0.0059 0.0248 205 HIS A N 1565 C CA . HIS A 182 ? 0.5160 0.2637 0.3070 0.0260 -0.0039 0.0244 205 HIS A CA 1566 C C . HIS A 182 ? 0.5587 0.2827 0.3337 0.0224 -0.0056 0.0246 205 HIS A C 1567 O O . HIS A 182 ? 0.5523 0.2702 0.3191 0.0120 -0.0059 0.0265 205 HIS A O 1568 C CB . HIS A 182 ? 0.4959 0.2546 0.2905 0.0182 -0.0038 0.0275 205 HIS A CB 1569 C CG . HIS A 182 ? 0.5019 0.2672 0.2967 0.0078 -0.0013 0.0263 205 HIS A CG 1570 N ND1 . HIS A 182 ? 0.5145 0.2928 0.3181 0.0072 0.0017 0.0230 205 HIS A ND1 1571 C CD2 . HIS A 182 ? 0.4816 0.2437 0.2690 -0.0024 -0.0016 0.0278 205 HIS A CD2 1572 C CE1 . HIS A 182 ? 0.4544 0.2362 0.2559 -0.0021 0.0029 0.0224 205 HIS A CE1 1573 N NE2 . HIS A 182 ? 0.5145 0.2877 0.3066 -0.0082 0.0012 0.0250 205 HIS A NE2 1574 N N A ASP A 183 ? 0.5853 0.2959 0.3552 0.0308 -0.0070 0.0223 206 ASP A N 1575 N N B ASP A 183 ? 0.5858 0.2966 0.3559 0.0308 -0.0070 0.0222 206 ASP A N 1576 C CA A ASP A 183 ? 0.6286 0.3146 0.3828 0.0286 -0.0089 0.0215 206 ASP A CA 1577 C CA B ASP A 183 ? 0.6299 0.3159 0.3842 0.0287 -0.0089 0.0215 206 ASP A CA 1578 C C A ASP A 183 ? 0.6536 0.3206 0.3937 0.0232 -0.0130 0.0265 206 ASP A C 1579 C C B ASP A 183 ? 0.6530 0.3212 0.3935 0.0225 -0.0128 0.0266 206 ASP A C 1580 O O A ASP A 183 ? 0.6838 0.3319 0.4098 0.0163 -0.0141 0.0267 206 ASP A O 1581 O O B ASP A 183 ? 0.6803 0.3321 0.4076 0.0141 -0.0134 0.0269 206 ASP A O 1582 C CB A ASP A 183 ? 0.6322 0.3194 0.3840 0.0196 -0.0054 0.0184 206 ASP A CB 1583 C CB B ASP A 183 ? 0.6349 0.3218 0.3869 0.0206 -0.0054 0.0181 206 ASP A CB 1584 C CG A ASP A 183 ? 0.6858 0.3514 0.4252 0.0212 -0.0063 0.0150 206 ASP A CG 1585 C CG B ASP A 183 ? 0.6615 0.3577 0.4217 0.0275 -0.0025 0.0126 206 ASP A CG 1586 O OD1 A ASP A 183 ? 0.7389 0.3973 0.4783 0.0326 -0.0079 0.0126 206 ASP A OD1 1587 O OD1 B ASP A 183 ? 0.7005 0.4018 0.4675 0.0386 -0.0031 0.0111 206 ASP A OD1 1588 O OD2 A ASP A 183 ? 0.7257 0.3822 0.4557 0.0113 -0.0054 0.0144 206 ASP A OD2 1589 O OD2 B ASP A 183 ? 0.7397 0.4393 0.4996 0.0215 0.0004 0.0097 206 ASP A OD2 1590 N N . GLY A 184 ? 0.6510 0.3223 0.3937 0.0256 -0.0155 0.0307 207 GLY A N 1591 C CA . GLY A 184 ? 0.6704 0.3244 0.3990 0.0196 -0.0197 0.0361 207 GLY A CA 1592 C C . GLY A 184 ? 0.6587 0.3220 0.3861 0.0055 -0.0181 0.0389 207 GLY A C 1593 O O . GLY A 184 ? 0.6452 0.2977 0.3618 -0.0007 -0.0213 0.0437 207 GLY A O 1594 N N . TYR A 185 ? 0.6387 0.3230 0.3775 0.0008 -0.0134 0.0359 208 TYR A N 1595 C CA . TYR A 185 ? 0.6099 0.3080 0.3508 -0.0106 -0.0118 0.0375 208 TYR A CA 1596 C C . TYR A 185 ? 0.5949 0.3146 0.3501 -0.0069 -0.0112 0.0386 208 TYR A C 1597 O O . TYR A 185 ? 0.5611 0.2975 0.3307 -0.0007 -0.0087 0.0357 208 TYR A O 1598 C CB . TYR A 185 ? 0.6170 0.3251 0.3616 -0.0174 -0.0077 0.0336 208 TYR A CB 1599 C CG . TYR A 185 ? 0.6574 0.3473 0.3881 -0.0238 -0.0079 0.0323 208 TYR A CG 1600 C CD1 . TYR A 185 ? 0.7242 0.4028 0.4406 -0.0359 -0.0094 0.0351 208 TYR A CD1 1601 C CD2 . TYR A 185 ? 0.6800 0.3639 0.4109 -0.0188 -0.0064 0.0282 208 TYR A CD2 1602 C CE1 . TYR A 185 ? 0.7820 0.4426 0.4841 -0.0431 -0.0095 0.0339 208 TYR A CE1 1603 C CE2 . TYR A 185 ? 0.7470 0.4133 0.4642 -0.0253 -0.0065 0.0266 208 TYR A CE2 1604 C CZ . TYR A 185 ? 0.7851 0.4392 0.4877 -0.0375 -0.0082 0.0296 208 TYR A CZ 1605 O OH . TYR A 185 ? 0.8104 0.4467 0.4989 -0.0447 -0.0085 0.0282 208 TYR A OH 1606 N N . PRO A 186 ? 0.5856 0.3053 0.3368 -0.0110 -0.0135 0.0428 209 PRO A N 1607 C CA . PRO A 186 ? 0.5629 0.3027 0.3266 -0.0088 -0.0129 0.0434 209 PRO A CA 1608 C C . PRO A 186 ? 0.5220 0.2833 0.2966 -0.0148 -0.0090 0.0401 209 PRO A C 1609 O O . PRO A 186 ? 0.5113 0.2724 0.2814 -0.0237 -0.0073 0.0387 209 PRO A O 1610 C CB . PRO A 186 ? 0.5819 0.3156 0.3358 -0.0150 -0.0161 0.0485 209 PRO A CB 1611 C CG . PRO A 186 ? 0.6191 0.3311 0.3558 -0.0218 -0.0181 0.0504 209 PRO A CG 1612 C CD . PRO A 186 ? 0.6129 0.3131 0.3465 -0.0186 -0.0170 0.0472 209 PRO A CD 1613 N N . PRO A 187 ? 0.4989 0.2787 0.2882 -0.0097 -0.0077 0.0388 210 PRO A N 1614 C CA . PRO A 187 ? 0.4629 0.2623 0.2619 -0.0153 -0.0049 0.0360 210 PRO A CA 1615 C C . PRO A 187 ? 0.4692 0.2744 0.2643 -0.0241 -0.0057 0.0377 210 PRO A C 1616 O O . PRO A 187 ? 0.4670 0.2632 0.2538 -0.0251 -0.0084 0.0416 210 PRO A O 1617 C CB . PRO A 187 ? 0.4493 0.2633 0.2631 -0.0068 -0.0042 0.0346 210 PRO A CB 1618 C CG . PRO A 187 ? 0.4485 0.2554 0.2598 0.0000 -0.0071 0.0380 210 PRO A CG 1619 C CD . PRO A 187 ? 0.4872 0.2710 0.2837 0.0004 -0.0092 0.0400 210 PRO A CD 1620 N N . TYR A 188 ? 0.4613 0.2822 0.2624 -0.0304 -0.0035 0.0347 211 TYR A N 1621 C CA . TYR A 188 ? 0.4686 0.3032 0.2729 -0.0353 -0.0038 0.0348 211 TYR A CA 1622 C C . TYR A 188 ? 0.4523 0.2943 0.2659 -0.0272 -0.0049 0.0359 211 TYR A C 1623 O O . TYR A 188 ? 0.4401 0.2876 0.2639 -0.0198 -0.0040 0.0341 211 TYR A O 1624 C CB . TYR A 188 ? 0.4408 0.2934 0.2526 -0.0409 -0.0014 0.0302 211 TYR A CB 1625 C CG . TYR A 188 ? 0.4432 0.3118 0.2604 -0.0440 -0.0015 0.0291 211 TYR A CG 1626 C CD1 . TYR A 188 ? 0.4809 0.3508 0.2888 -0.0536 -0.0021 0.0305 211 TYR A CD1 1627 C CD2 . TYR A 188 ? 0.3742 0.2572 0.2056 -0.0379 -0.0011 0.0264 211 TYR A CD2 1628 C CE1 . TYR A 188 ? 0.4839 0.3707 0.2976 -0.0563 -0.0020 0.0286 211 TYR A CE1 1629 C CE2 . TYR A 188 ? 0.3926 0.2901 0.2291 -0.0402 -0.0012 0.0248 211 TYR A CE2 1630 C CZ . TYR A 188 ? 0.4463 0.3463 0.2743 -0.0492 -0.0015 0.0256 211 TYR A CZ 1631 O OH . TYR A 188 ? 0.4430 0.3595 0.2773 -0.0510 -0.0015 0.0230 211 TYR A OH 1632 N N . VAL A 189 ? 0.4373 0.2790 0.2463 -0.0294 -0.0069 0.0390 212 VAL A N 1633 C CA . VAL A 189 ? 0.4280 0.2776 0.2443 -0.0235 -0.0082 0.0401 212 VAL A CA 1634 C C . VAL A 189 ? 0.4367 0.3036 0.2577 -0.0298 -0.0075 0.0382 212 VAL A C 1635 O O . VAL A 189 ? 0.4443 0.3104 0.2561 -0.0383 -0.0082 0.0398 212 VAL A O 1636 C CB . VAL A 189 ? 0.4564 0.2919 0.2635 -0.0201 -0.0116 0.0454 212 VAL A CB 1637 C CG1 . VAL A 189 ? 0.4192 0.2667 0.2358 -0.0142 -0.0127 0.0460 212 VAL A CG1 1638 C CG2 . VAL A 189 ? 0.4357 0.2539 0.2383 -0.0127 -0.0126 0.0465 212 VAL A CG2 1639 N N . GLY A 190 ? 0.4009 0.2832 0.2356 -0.0259 -0.0061 0.0344 213 GLY A N 1640 C CA . GLY A 190 ? 0.3927 0.2929 0.2341 -0.0301 -0.0053 0.0311 213 GLY A CA 1641 C C . GLY A 190 ? 0.4005 0.3076 0.2479 -0.0255 -0.0067 0.0321 213 GLY A C 1642 O O . GLY A 190 ? 0.3802 0.2858 0.2337 -0.0176 -0.0071 0.0328 213 GLY A O 1643 N N . CYS A 191 ? 0.4162 0.3310 0.2606 -0.0312 -0.0074 0.0324 214 CYS A N 1644 C CA . CYS A 191 ? 0.3942 0.3175 0.2436 -0.0285 -0.0086 0.0329 214 CYS A CA 1645 C C . CYS A 191 ? 0.3993 0.3413 0.2577 -0.0317 -0.0071 0.0270 214 CYS A C 1646 O O . CYS A 191 ? 0.3938 0.3425 0.2510 -0.0381 -0.0057 0.0235 214 CYS A O 1647 C CB . CYS A 191 ? 0.4156 0.3325 0.2527 -0.0331 -0.0111 0.0383 214 CYS A CB 1648 S SG . CYS A 191 ? 0.4579 0.3532 0.2862 -0.0261 -0.0141 0.0451 214 CYS A SG 1649 N N . GLU A 192 ? 0.4063 0.3571 0.2730 -0.0275 -0.0077 0.0258 215 GLU A N 1650 C CA . GLU A 192 ? 0.4167 0.3846 0.2916 -0.0298 -0.0069 0.0199 215 GLU A CA 1651 C C . GLU A 192 ? 0.4208 0.3939 0.2952 -0.0297 -0.0085 0.0220 215 GLU A C 1652 O O . GLU A 192 ? 0.4145 0.3834 0.2912 -0.0239 -0.0098 0.0249 215 GLU A O 1653 C CB . GLU A 192 ? 0.4048 0.3781 0.2923 -0.0240 -0.0061 0.0151 215 GLU A CB 1654 C CG . GLU A 192 ? 0.4664 0.4553 0.3618 -0.0260 -0.0055 0.0081 215 GLU A CG 1655 C CD . GLU A 192 ? 0.4864 0.4809 0.3802 -0.0312 -0.0041 0.0040 215 GLU A CD 1656 O OE1 . GLU A 192 ? 0.6288 0.6145 0.5192 -0.0311 -0.0035 0.0057 215 GLU A OE1 1657 O OE2 . GLU A 192 ? 0.5289 0.5373 0.4249 -0.0353 -0.0036 -0.0012 215 GLU A OE2 1658 N N . ASP A 193 ? 0.4361 0.4193 0.3074 -0.0366 -0.0084 0.0202 216 ASP A N 1659 C CA . ASP A 193 ? 0.4660 0.4569 0.3371 -0.0377 -0.0097 0.0212 216 ASP A CA 1660 C C . ASP A 193 ? 0.4698 0.4467 0.3318 -0.0352 -0.0123 0.0296 216 ASP A C 1661 O O . ASP A 193 ? 0.4514 0.4300 0.3169 -0.0303 -0.0139 0.0314 216 ASP A O 1662 C CB . ASP A 193 ? 0.4536 0.4542 0.3375 -0.0321 -0.0096 0.0167 216 ASP A CB 1663 C CG . ASP A 193 ? 0.5143 0.5284 0.4071 -0.0337 -0.0078 0.0078 216 ASP A CG 1664 O OD1 . ASP A 193 ? 0.6210 0.6455 0.5109 -0.0403 -0.0071 0.0048 216 ASP A OD1 1665 O OD2 . ASP A 193 ? 0.5113 0.5254 0.4131 -0.0286 -0.0074 0.0040 216 ASP A OD2 1666 N N . GLY A 194 ? 0.4740 0.4369 0.3250 -0.0377 -0.0130 0.0341 217 GLY A N 1667 C CA . GLY A 194 ? 0.4806 0.4282 0.3229 -0.0341 -0.0160 0.0415 217 GLY A CA 1668 C C . GLY A 194 ? 0.4497 0.3897 0.2979 -0.0235 -0.0166 0.0430 217 GLY A C 1669 O O . GLY A 194 ? 0.4414 0.3713 0.2839 -0.0192 -0.0194 0.0483 217 GLY A O 1670 N N . ALA A 195 ? 0.3968 0.3417 0.2559 -0.0196 -0.0143 0.0382 218 ALA A N 1671 C CA . ALA A 195 ? 0.3932 0.3334 0.2585 -0.0108 -0.0144 0.0387 218 ALA A CA 1672 C C . ALA A 195 ? 0.3754 0.3055 0.2397 -0.0095 -0.0127 0.0377 218 ALA A C 1673 O O . ALA A 195 ? 0.3630 0.2960 0.2285 -0.0140 -0.0107 0.0341 218 ALA A O 1674 C CB . ALA A 195 ? 0.3633 0.3169 0.2416 -0.0076 -0.0133 0.0344 218 ALA A CB 1675 N N . LEU A 196 ? 0.3915 0.3105 0.2537 -0.0030 -0.0137 0.0407 219 LEU A N 1676 C CA . LEU A 196 ? 0.3990 0.3086 0.2601 -0.0012 -0.0123 0.0399 219 LEU A CA 1677 C C . LEU A 196 ? 0.3716 0.2917 0.2449 0.0002 -0.0099 0.0348 219 LEU A C 1678 O O . LEU A 196 ? 0.3808 0.3098 0.2630 0.0040 -0.0099 0.0335 219 LEU A O 1679 C CB . LEU A 196 ? 0.4442 0.3416 0.3010 0.0064 -0.0142 0.0437 219 LEU A CB 1680 C CG . LEU A 196 ? 0.4886 0.3724 0.3410 0.0095 -0.0136 0.0439 219 LEU A CG 1681 C CD1 . LEU A 196 ? 0.4389 0.3098 0.2791 0.0027 -0.0138 0.0454 219 LEU A CD1 1682 C CD2 . LEU A 196 ? 0.4094 0.2874 0.2615 0.0190 -0.0158 0.0465 219 LEU A CD2 1683 N N . SER A 197 ? 0.3663 0.2849 0.2392 -0.0033 -0.0081 0.0322 220 SER A N 1684 C CA . SER A 197 ? 0.3590 0.2872 0.2416 -0.0037 -0.0064 0.0273 220 SER A CA 1685 C C . SER A 197 ? 0.3508 0.2736 0.2339 -0.0032 -0.0049 0.0257 220 SER A C 1686 O O . SER A 197 ? 0.3450 0.2722 0.2362 -0.0002 -0.0043 0.0234 220 SER A O 1687 C CB . SER A 197 ? 0.3763 0.3147 0.2598 -0.0101 -0.0061 0.0240 220 SER A CB 1688 O OG . SER A 197 ? 0.4313 0.3782 0.3239 -0.0097 -0.0051 0.0190 220 SER A OG 1689 N N . GLN A 198 ? 0.3592 0.2728 0.2333 -0.0068 -0.0045 0.0268 221 GLN A N 1690 C CA . GLN A 198 ? 0.3503 0.2603 0.2245 -0.0076 -0.0030 0.0248 221 GLN A CA 1691 C C . GLN A 198 ? 0.3622 0.2566 0.2255 -0.0077 -0.0032 0.0280 221 GLN A C 1692 O O . GLN A 198 ? 0.3767 0.2639 0.2307 -0.0106 -0.0045 0.0310 221 GLN A O 1693 C CB . GLN A 198 ? 0.3547 0.2730 0.2295 -0.0141 -0.0021 0.0211 221 GLN A CB 1694 C CG . GLN A 198 ? 0.3593 0.2920 0.2451 -0.0132 -0.0022 0.0169 221 GLN A CG 1695 C CD . GLN A 198 ? 0.3936 0.3352 0.2824 -0.0171 -0.0015 0.0121 221 GLN A CD 1696 O OE1 . GLN A 198 ? 0.3597 0.2982 0.2479 -0.0174 -0.0007 0.0112 221 GLN A OE1 1697 N NE2 . GLN A 198 ? 0.3812 0.3354 0.2739 -0.0198 -0.0018 0.0085 221 GLN A NE2 1698 N N . LEU A 199 ? 0.3407 0.2298 0.2045 -0.0054 -0.0020 0.0271 222 LEU A N 1699 C CA . LEU A 199 ? 0.3535 0.2276 0.2073 -0.0059 -0.0019 0.0288 222 LEU A CA 1700 C C . LEU A 199 ? 0.3681 0.2428 0.2223 -0.0091 -0.0002 0.0259 222 LEU A C 1701 O O . LEU A 199 ? 0.3372 0.2209 0.2008 -0.0069 0.0008 0.0233 222 LEU A O 1702 C CB . LEU A 199 ? 0.3462 0.2120 0.1996 0.0022 -0.0026 0.0307 222 LEU A CB 1703 C CG . LEU A 199 ? 0.3627 0.2281 0.2161 0.0070 -0.0047 0.0336 222 LEU A CG 1704 C CD1 . LEU A 199 ? 0.3697 0.2315 0.2258 0.0158 -0.0049 0.0339 222 LEU A CD1 1705 C CD2 . LEU A 199 ? 0.3659 0.2190 0.2063 0.0032 -0.0069 0.0372 222 LEU A CD2 1706 N N . TYR A 200 ? 0.3879 0.2536 0.2317 -0.0150 0.0001 0.0264 223 TYR A N 1707 C CA . TYR A 200 ? 0.3847 0.2490 0.2273 -0.0179 0.0017 0.0239 223 TYR A CA 1708 C C . TYR A 200 ? 0.4097 0.2564 0.2418 -0.0170 0.0016 0.0256 223 TYR A C 1709 O O . TYR A 200 ? 0.4356 0.2698 0.2558 -0.0210 0.0004 0.0280 223 TYR A O 1710 C CB . TYR A 200 ? 0.3752 0.2461 0.2149 -0.0268 0.0025 0.0217 223 TYR A CB 1711 C CG . TYR A 200 ? 0.3529 0.2397 0.1992 -0.0298 0.0023 0.0195 223 TYR A CG 1712 C CD1 . TYR A 200 ? 0.3500 0.2476 0.2076 -0.0245 0.0018 0.0183 223 TYR A CD1 1713 C CD2 . TYR A 200 ? 0.3742 0.2663 0.2149 -0.0390 0.0028 0.0180 223 TYR A CD2 1714 C CE1 . TYR A 200 ? 0.3484 0.2602 0.2118 -0.0271 0.0016 0.0155 223 TYR A CE1 1715 C CE2 . TYR A 200 ? 0.4052 0.3136 0.2521 -0.0418 0.0028 0.0150 223 TYR A CE2 1716 C CZ . TYR A 200 ? 0.3814 0.2991 0.2396 -0.0355 0.0022 0.0136 223 TYR A CZ 1717 O OH . TYR A 200 ? 0.3881 0.3217 0.2525 -0.0377 0.0021 0.0099 223 TYR A OH 1718 N N . TYR A 201 ? 0.3994 0.2443 0.2353 -0.0115 0.0026 0.0244 224 TYR A N 1719 C CA . TYR A 201 ? 0.3984 0.2276 0.2251 -0.0105 0.0027 0.0247 224 TYR A CA 1720 C C . TYR A 201 ? 0.4042 0.2329 0.2274 -0.0166 0.0043 0.0223 224 TYR A C 1721 O O . TYR A 201 ? 0.3930 0.2314 0.2240 -0.0156 0.0057 0.0199 224 TYR A O 1722 C CB . TYR A 201 ? 0.3942 0.2215 0.2255 -0.0013 0.0030 0.0244 224 TYR A CB 1723 C CG . TYR A 201 ? 0.4066 0.2338 0.2408 0.0059 0.0013 0.0266 224 TYR A CG 1724 C CD1 . TYR A 201 ? 0.3852 0.1977 0.2108 0.0100 -0.0006 0.0285 224 TYR A CD1 1725 C CD2 . TYR A 201 ? 0.3777 0.2196 0.2231 0.0087 0.0013 0.0265 224 TYR A CD2 1726 C CE1 . TYR A 201 ? 0.4256 0.2395 0.2544 0.0172 -0.0023 0.0302 224 TYR A CE1 1727 C CE2 . TYR A 201 ? 0.4034 0.2465 0.2514 0.0148 -0.0002 0.0283 224 TYR A CE2 1728 C CZ . TYR A 201 ? 0.3846 0.2146 0.2247 0.0191 -0.0020 0.0302 224 TYR A CZ 1729 O OH . TYR A 201 ? 0.4384 0.2709 0.2814 0.0256 -0.0037 0.0318 224 TYR A OH 1730 N N . TYR A 202 ? 0.4313 0.2469 0.2416 -0.0229 0.0040 0.0230 225 TYR A N 1731 C CA . TYR A 202 ? 0.4327 0.2488 0.2387 -0.0304 0.0055 0.0206 225 TYR A CA 1732 C C . TYR A 202 ? 0.4524 0.2567 0.2535 -0.0277 0.0063 0.0193 225 TYR A C 1733 O O . TYR A 202 ? 0.4725 0.2605 0.2662 -0.0231 0.0051 0.0205 225 TYR A O 1734 C CB . TYR A 202 ? 0.4603 0.2708 0.2547 -0.0409 0.0048 0.0217 225 TYR A CB 1735 C CG . TYR A 202 ? 0.4513 0.2759 0.2496 -0.0457 0.0045 0.0220 225 TYR A CG 1736 C CD1 . TYR A 202 ? 0.4689 0.3068 0.2686 -0.0538 0.0056 0.0193 225 TYR A CD1 1737 C CD2 . TYR A 202 ? 0.5076 0.3329 0.3081 -0.0420 0.0029 0.0247 225 TYR A CD2 1738 C CE1 . TYR A 202 ? 0.4520 0.3045 0.2559 -0.0577 0.0054 0.0187 225 TYR A CE1 1739 C CE2 . TYR A 202 ? 0.4521 0.2907 0.2560 -0.0465 0.0026 0.0245 225 TYR A CE2 1740 C CZ . TYR A 202 ? 0.4660 0.3178 0.2713 -0.0543 0.0039 0.0214 225 TYR A CZ 1741 O OH . TYR A 202 ? 0.4426 0.3092 0.2517 -0.0584 0.0038 0.0203 225 TYR A OH 1742 N N . PHE A 203 ? 0.4431 0.2550 0.2473 -0.0305 0.0080 0.0164 226 PHE A N 1743 C CA . PHE A 203 ? 0.4431 0.2461 0.2426 -0.0294 0.0091 0.0144 226 PHE A CA 1744 C C . PHE A 203 ? 0.4339 0.2401 0.2291 -0.0384 0.0104 0.0121 226 PHE A C 1745 O O . PHE A 203 ? 0.4262 0.2471 0.2265 -0.0436 0.0107 0.0112 226 PHE A O 1746 C CB . PHE A 203 ? 0.4375 0.2506 0.2484 -0.0219 0.0102 0.0130 226 PHE A CB 1747 C CG . PHE A 203 ? 0.4302 0.2426 0.2464 -0.0128 0.0094 0.0145 226 PHE A CG 1748 C CD1 . PHE A 203 ? 0.4179 0.2178 0.2291 -0.0068 0.0093 0.0140 226 PHE A CD1 1749 C CD2 . PHE A 203 ? 0.4019 0.2260 0.2275 -0.0102 0.0086 0.0160 226 PHE A CD2 1750 C CE1 . PHE A 203 ? 0.4103 0.2120 0.2269 0.0017 0.0086 0.0149 226 PHE A CE1 1751 C CE2 . PHE A 203 ? 0.4214 0.2463 0.2520 -0.0024 0.0079 0.0172 226 PHE A CE2 1752 C CZ . PHE A 203 ? 0.4353 0.2494 0.2614 0.0036 0.0079 0.0167 226 PHE A CZ 1753 N N . ASN A 204 ? 0.4555 0.2485 0.2413 -0.0401 0.0110 0.0108 227 ASN A N 1754 C CA . ASN A 204 ? 0.4514 0.2488 0.2349 -0.0467 0.0125 0.0079 227 ASN A CA 1755 C C . ASN A 204 ? 0.4441 0.2432 0.2328 -0.0401 0.0137 0.0059 227 ASN A C 1756 O O . ASN A 204 ? 0.4650 0.2586 0.2561 -0.0314 0.0135 0.0064 227 ASN A O 1757 C CB . ASN A 204 ? 0.4958 0.2773 0.2637 -0.0553 0.0123 0.0077 227 ASN A CB 1758 C CG . ASN A 204 ? 0.5225 0.3038 0.2844 -0.0636 0.0111 0.0100 227 ASN A CG 1759 O OD1 . ASN A 204 ? 0.5351 0.3337 0.3048 -0.0662 0.0112 0.0100 227 ASN A OD1 1760 N ND2 . ASN A 204 ? 0.4921 0.2535 0.2398 -0.0674 0.0098 0.0117 227 ASN A ND2 1761 N N . VAL A 205 ? 0.4441 0.2522 0.2346 -0.0442 0.0150 0.0035 228 VAL A N 1762 C CA . VAL A 205 ? 0.4288 0.2449 0.2267 -0.0392 0.0161 0.0018 228 VAL A CA 1763 C C . VAL A 205 ? 0.4440 0.2548 0.2335 -0.0446 0.0175 -0.0012 228 VAL A C 1764 O O . VAL A 205 ? 0.4452 0.2584 0.2300 -0.0531 0.0176 -0.0022 228 VAL A O 1765 C CB . VAL A 205 ? 0.3921 0.2281 0.2031 -0.0378 0.0156 0.0023 228 VAL A CB 1766 C CG1 . VAL A 205 ? 0.3853 0.2272 0.2018 -0.0335 0.0164 0.0013 228 VAL A CG1 1767 C CG2 . VAL A 205 ? 0.3834 0.2243 0.2028 -0.0322 0.0142 0.0049 228 VAL A CG2 1768 N N . LYS A 206 ? 0.4722 0.2763 0.2602 -0.0394 0.0185 -0.0028 229 LYS A N 1769 C CA . LYS A 206 ? 0.4912 0.2930 0.2737 -0.0427 0.0200 -0.0061 229 LYS A CA 1770 C C . LYS A 206 ? 0.4549 0.2743 0.2482 -0.0402 0.0205 -0.0063 229 LYS A C 1771 O O . LYS A 206 ? 0.4541 0.2771 0.2540 -0.0329 0.0208 -0.0057 229 LYS A O 1772 C CB . LYS A 206 ? 0.5103 0.2953 0.2852 -0.0376 0.0207 -0.0082 229 LYS A CB 1773 C CG . LYS A 206 ? 0.5899 0.3534 0.3520 -0.0396 0.0193 -0.0077 229 LYS A CG 1774 C CD . LYS A 206 ? 0.6784 0.4236 0.4332 -0.0323 0.0191 -0.0101 229 LYS A CD 1775 C CE . LYS A 206 ? 0.7546 0.4892 0.4991 -0.0362 0.0204 -0.0147 229 LYS A CE 1776 N NZ . LYS A 206 ? 0.8125 0.5344 0.5434 -0.0474 0.0199 -0.0150 229 LYS A NZ 1777 N N . GLY A 207 ? 0.4480 0.2780 0.2424 -0.0466 0.0205 -0.0071 230 GLY A N 1778 C CA . GLY A 207 ? 0.4345 0.2800 0.2377 -0.0452 0.0203 -0.0068 230 GLY A CA 1779 C C . GLY A 207 ? 0.4311 0.2905 0.2457 -0.0431 0.0182 -0.0040 230 GLY A C 1780 O O . GLY A 207 ? 0.4305 0.2930 0.2457 -0.0464 0.0172 -0.0034 230 GLY A O 1781 N N . SER A 208 ? 0.4059 0.2744 0.2289 -0.0383 0.0175 -0.0026 231 SER A N 1782 C CA . SER A 208 ? 0.3975 0.2782 0.2307 -0.0363 0.0151 -0.0003 231 SER A CA 1783 C C . SER A 208 ? 0.3762 0.2539 0.2139 -0.0311 0.0146 0.0016 231 SER A C 1784 O O . SER A 208 ? 0.3904 0.2591 0.2255 -0.0271 0.0159 0.0018 231 SER A O 1785 C CB . SER A 208 ? 0.4027 0.2929 0.2424 -0.0336 0.0140 0.0011 231 SER A CB 1786 O OG . SER A 208 ? 0.3916 0.2914 0.2405 -0.0314 0.0110 0.0031 231 SER A OG 1787 N N . ALA A 209 ? 0.3802 0.2656 0.2242 -0.0310 0.0126 0.0027 232 ALA A N 1788 C CA . ALA A 209 ? 0.3779 0.2625 0.2273 -0.0260 0.0118 0.0046 232 ALA A CA 1789 C C . ALA A 209 ? 0.3791 0.2660 0.2343 -0.0204 0.0115 0.0064 232 ALA A C 1790 O O . ALA A 209 ? 0.4018 0.2859 0.2595 -0.0160 0.0116 0.0077 232 ALA A O 1791 C CB . ALA A 209 ? 0.3686 0.2623 0.2243 -0.0267 0.0097 0.0048 232 ALA A CB 1792 N N . ILE A 210 ? 0.3803 0.2734 0.2378 -0.0207 0.0109 0.0067 233 ILE A N 1793 C CA . ILE A 210 ? 0.3989 0.2937 0.2599 -0.0167 0.0110 0.0084 233 ILE A CA 1794 C C . ILE A 210 ? 0.4073 0.2966 0.2617 -0.0169 0.0138 0.0066 233 ILE A C 1795 O O . ILE A 210 ? 0.3968 0.2875 0.2472 -0.0205 0.0143 0.0053 233 ILE A O 1796 C CB . ILE A 210 ? 0.4134 0.3175 0.2802 -0.0171 0.0083 0.0104 233 ILE A CB 1797 C CG1 . ILE A 210 ? 0.4874 0.3970 0.3601 -0.0170 0.0052 0.0109 233 ILE A CG1 1798 C CG2 . ILE A 210 ? 0.4282 0.3342 0.2974 -0.0144 0.0086 0.0123 233 ILE A CG2 1799 C CD1 . ILE A 210 ? 0.4017 0.3118 0.2804 -0.0132 0.0039 0.0123 233 ILE A CD1 1800 N N . GLY A 211 ? 0.4080 0.2918 0.2612 -0.0128 0.0153 0.0063 234 GLY A N 1801 C CA . GLY A 211 ? 0.4322 0.3114 0.2797 -0.0118 0.0178 0.0038 234 GLY A CA 1802 C C . GLY A 211 ? 0.4533 0.3204 0.2915 -0.0133 0.0194 0.0009 234 GLY A C 1803 O O . GLY A 211 ? 0.4693 0.3314 0.3027 -0.0114 0.0214 -0.0018 234 GLY A O 1804 N N . GLY A 212 ? 0.4368 0.2991 0.2718 -0.0170 0.0185 0.0010 235 GLY A N 1805 C CA . GLY A 212 ? 0.4445 0.2932 0.2692 -0.0191 0.0197 -0.0014 235 GLY A CA 1806 C C . GLY A 212 ? 0.4527 0.2902 0.2745 -0.0139 0.0197 -0.0013 235 GLY A C 1807 O O . GLY A 212 ? 0.4655 0.3068 0.2937 -0.0083 0.0192 0.0004 235 GLY A O 1808 N N . THR A 213 ? 0.4698 0.2924 0.2811 -0.0156 0.0202 -0.0031 236 THR A N 1809 C CA . THR A 213 ? 0.4957 0.3053 0.3028 -0.0102 0.0195 -0.0030 236 THR A CA 1810 C C . THR A 213 ? 0.4886 0.2943 0.2942 -0.0132 0.0177 -0.0001 236 THR A C 1811 O O . THR A 213 ? 0.4960 0.2976 0.2950 -0.0210 0.0174 0.0000 236 THR A O 1812 C CB . THR A 213 ? 0.5352 0.3276 0.3302 -0.0101 0.0203 -0.0066 236 THR A CB 1813 O OG1 . THR A 213 ? 0.5136 0.3118 0.3103 -0.0080 0.0223 -0.0099 236 THR A OG1 1814 C CG2 . THR A 213 ? 0.5652 0.3428 0.3554 -0.0033 0.0189 -0.0064 236 THR A CG2 1815 N N . TYR A 214 ? 0.4825 0.2913 0.2942 -0.0075 0.0166 0.0023 237 TYR A N 1816 C CA . TYR A 214 ? 0.4709 0.2778 0.2822 -0.0096 0.0148 0.0052 237 TYR A CA 1817 C C . TYR A 214 ? 0.4995 0.2877 0.3005 -0.0072 0.0136 0.0056 237 TYR A C 1818 O O . TYR A 214 ? 0.5345 0.3191 0.3371 0.0011 0.0132 0.0053 237 TYR A O 1819 C CB . TYR A 214 ? 0.4591 0.2789 0.2819 -0.0054 0.0140 0.0076 237 TYR A CB 1820 C CG . TYR A 214 ? 0.4349 0.2703 0.2660 -0.0093 0.0140 0.0080 237 TYR A CG 1821 C CD1 . TYR A 214 ? 0.4181 0.2623 0.2538 -0.0094 0.0150 0.0067 237 TYR A CD1 1822 C CD2 . TYR A 214 ? 0.4048 0.2461 0.2390 -0.0126 0.0127 0.0095 237 TYR A CD2 1823 C CE1 . TYR A 214 ? 0.4031 0.2596 0.2458 -0.0120 0.0142 0.0072 237 TYR A CE1 1824 C CE2 . TYR A 214 ? 0.4145 0.2696 0.2565 -0.0151 0.0122 0.0093 237 TYR A CE2 1825 C CZ . TYR A 214 ? 0.3998 0.2615 0.2457 -0.0144 0.0127 0.0083 237 TYR A CZ 1826 O OH . TYR A 214 ? 0.3674 0.2413 0.2206 -0.0161 0.0115 0.0083 237 TYR A OH 1827 N N . VAL A 215 ? 0.4998 0.2771 0.2905 -0.0144 0.0128 0.0063 238 VAL A N 1828 C CA . VAL A 215 ? 0.5071 0.2631 0.2851 -0.0139 0.0109 0.0071 238 VAL A CA 1829 C C . VAL A 215 ? 0.5152 0.2705 0.2924 -0.0160 0.0088 0.0111 238 VAL A C 1830 O O . VAL A 215 ? 0.4924 0.2549 0.2695 -0.0244 0.0090 0.0121 238 VAL A O 1831 C CB . VAL A 215 ? 0.5281 0.2703 0.2929 -0.0218 0.0114 0.0049 238 VAL A CB 1832 C CG1 . VAL A 215 ? 0.5425 0.2589 0.2915 -0.0226 0.0087 0.0061 238 VAL A CG1 1833 C CG2 . VAL A 215 ? 0.5213 0.2652 0.2875 -0.0186 0.0135 0.0006 238 VAL A CG2 1834 N N . ALA A 216 ? 0.5279 0.2756 0.3045 -0.0085 0.0067 0.0130 239 ALA A N 1835 C CA . ALA A 216 ? 0.5338 0.2809 0.3096 -0.0097 0.0045 0.0170 239 ALA A CA 1836 C C . ALA A 216 ? 0.5547 0.2906 0.3177 -0.0204 0.0035 0.0186 239 ALA A C 1837 O O . ALA A 216 ? 0.5756 0.2939 0.3262 -0.0234 0.0029 0.0176 239 ALA A O 1838 C CB . ALA A 216 ? 0.5395 0.2775 0.3146 0.0005 0.0020 0.0186 239 ALA A CB 1839 N N . SER A 217 ? 0.5341 0.2814 0.2999 -0.0274 0.0035 0.0204 240 SER A N 1840 C CA . SER A 217 ? 0.5541 0.2929 0.3072 -0.0391 0.0027 0.0219 240 SER A CA 1841 C C . SER A 217 ? 0.5585 0.2993 0.3096 -0.0427 0.0007 0.0258 240 SER A C 1842 O O . SER A 217 ? 0.5145 0.2649 0.2750 -0.0364 0.0001 0.0273 240 SER A O 1843 C CB . SER A 217 ? 0.5712 0.3239 0.3270 -0.0481 0.0053 0.0191 240 SER A CB 1844 O OG . SER A 217 ? 0.5096 0.2850 0.2797 -0.0470 0.0064 0.0184 240 SER A OG 1845 N N . GLU A 218 ? 0.5750 0.3067 0.3131 -0.0536 -0.0002 0.0275 241 GLU A N 1846 C CA . GLU A 218 ? 0.6100 0.3418 0.3436 -0.0584 -0.0023 0.0315 241 GLU A CA 1847 C C . GLU A 218 ? 0.5651 0.3234 0.3117 -0.0611 -0.0006 0.0304 241 GLU A C 1848 O O . GLU A 218 ? 0.5655 0.3397 0.3181 -0.0662 0.0019 0.0270 241 GLU A O 1849 C CB . GLU A 218 ? 0.6267 0.3422 0.3416 -0.0711 -0.0038 0.0336 241 GLU A CB 1850 C CG . GLU A 218 ? 0.7150 0.4222 0.4213 -0.0740 -0.0071 0.0389 241 GLU A CG 1851 C CD . GLU A 218 ? 0.8582 0.5445 0.5438 -0.0860 -0.0094 0.0418 241 GLU A CD 1852 O OE1 . GLU A 218 ? 0.9582 0.6229 0.6332 -0.0851 -0.0105 0.0413 241 GLU A OE1 1853 O OE2 . GLU A 218 ? 0.9400 0.6310 0.6194 -0.0964 -0.0102 0.0446 241 GLU A OE2 1854 N N . ARG A 219 ? 0.5600 0.3232 0.3110 -0.0573 -0.0021 0.0331 242 ARG A N 1855 C CA . ARG A 219 ? 0.5202 0.3065 0.2820 -0.0600 -0.0008 0.0318 242 ARG A CA 1856 C C . ARG A 219 ? 0.5429 0.3370 0.2982 -0.0736 0.0000 0.0310 242 ARG A C 1857 O O . ARG A 219 ? 0.5489 0.3288 0.2883 -0.0827 -0.0016 0.0340 242 ARG A O 1858 C CB . ARG A 219 ? 0.5216 0.3106 0.2878 -0.0542 -0.0028 0.0348 242 ARG A CB 1859 C CG . ARG A 219 ? 0.5221 0.2954 0.2727 -0.0600 -0.0061 0.0400 242 ARG A CG 1860 C CD . ARG A 219 ? 0.5931 0.3676 0.3488 -0.0514 -0.0083 0.0429 242 ARG A CD 1861 N NE . ARG A 219 ? 0.6351 0.3932 0.3757 -0.0559 -0.0119 0.0484 242 ARG A NE 1862 C CZ . ARG A 219 ? 0.7260 0.4820 0.4667 -0.0507 -0.0147 0.0521 242 ARG A CZ 1863 N NH1 . ARG A 219 ? 0.6920 0.4633 0.4480 -0.0414 -0.0139 0.0505 242 ARG A NH1 1864 N NH2 . ARG A 219 ? 0.7105 0.4496 0.4354 -0.0558 -0.0186 0.0575 242 ARG A NH2 1865 N N . LEU A 220 ? 0.5366 0.3533 0.3034 -0.0757 0.0022 0.0269 243 LEU A N 1866 C CA . LEU A 220 ? 0.5695 0.3985 0.3322 -0.0882 0.0033 0.0250 243 LEU A CA 1867 C C . LEU A 220 ? 0.6096 0.4533 0.3760 -0.0910 0.0028 0.0256 243 LEU A C 1868 O O . LEU A 220 ? 0.6135 0.4704 0.3772 -0.1015 0.0037 0.0236 243 LEU A O 1869 C CB . LEU A 220 ? 0.5670 0.4133 0.3394 -0.0890 0.0057 0.0195 243 LEU A CB 1870 C CG . LEU A 220 ? 0.5789 0.4147 0.3493 -0.0864 0.0066 0.0182 243 LEU A CG 1871 C CD1 . LEU A 220 ? 0.5643 0.4205 0.3460 -0.0867 0.0086 0.0129 243 LEU A CD1 1872 C CD2 . LEU A 220 ? 0.6024 0.4183 0.3548 -0.0953 0.0060 0.0204 243 LEU A CD2 1873 N N . GLU A 221 ? 0.5951 0.4379 0.3678 -0.0821 0.0014 0.0277 244 GLU A N 1874 C CA . GLU A 221 ? 0.6134 0.4678 0.3890 -0.0838 0.0006 0.0285 244 GLU A CA 1875 C C . GLU A 221 ? 0.6066 0.4442 0.3780 -0.0765 -0.0021 0.0339 244 GLU A C 1876 O O . GLU A 221 ? 0.6055 0.4344 0.3811 -0.0668 -0.0024 0.0343 244 GLU A O 1877 C CB . GLU A 221 ? 0.5947 0.4732 0.3882 -0.0787 0.0023 0.0231 244 GLU A CB 1878 C CG . GLU A 221 ? 0.6968 0.5931 0.4933 -0.0840 0.0025 0.0213 244 GLU A CG 1879 C CD . GLU A 221 ? 0.7396 0.6554 0.5536 -0.0763 0.0032 0.0167 244 GLU A CD 1880 O OE1 . GLU A 221 ? 0.7447 0.6651 0.5691 -0.0695 0.0039 0.0135 244 GLU A OE1 1881 O OE2 . GLU A 221 ? 0.7680 0.6939 0.5844 -0.0775 0.0026 0.0164 244 GLU A OE2 1882 N N A ASP A 222 ? 0.6413 0.4741 0.4037 -0.0812 -0.0043 0.0381 245 ASP A N 1883 N N B ASP A 222 ? 0.6300 0.4642 0.3932 -0.0812 -0.0042 0.0378 245 ASP A N 1884 C CA A ASP A 222 ? 0.6484 0.4625 0.4048 -0.0740 -0.0076 0.0436 245 ASP A CA 1885 C CA B ASP A 222 ? 0.6355 0.4508 0.3916 -0.0751 -0.0075 0.0435 245 ASP A CA 1886 C C A ASP A 222 ? 0.6266 0.4517 0.3956 -0.0645 -0.0083 0.0437 245 ASP A C 1887 C C B ASP A 222 ? 0.6166 0.4410 0.3847 -0.0650 -0.0083 0.0438 245 ASP A C 1888 O O A ASP A 222 ? 0.6310 0.4514 0.4072 -0.0529 -0.0088 0.0439 245 ASP A O 1889 O O B ASP A 222 ? 0.6250 0.4432 0.3992 -0.0536 -0.0090 0.0443 245 ASP A O 1890 C CB A ASP A 222 ? 0.6920 0.4899 0.4294 -0.0834 -0.0108 0.0494 245 ASP A CB 1891 C CB B ASP A 222 ? 0.6707 0.4743 0.4090 -0.0862 -0.0101 0.0485 245 ASP A CB 1892 C CG A ASP A 222 ? 0.7309 0.5088 0.4526 -0.0908 -0.0114 0.0508 245 ASP A CG 1893 C CG B ASP A 222 ? 0.6618 0.4850 0.3998 -0.0985 -0.0082 0.0460 245 ASP A CG 1894 O OD1 A ASP A 222 ? 0.7491 0.5233 0.4743 -0.0871 -0.0096 0.0477 245 ASP A OD1 1895 O OD1 B ASP A 222 ? 0.6473 0.4873 0.3935 -0.0975 -0.0079 0.0450 245 ASP A OD1 1896 O OD2 A ASP A 222 ? 0.7535 0.5186 0.4587 -0.1006 -0.0138 0.0554 245 ASP A OD2 1897 O OD2 B ASP A 222 ? 0.6984 0.5214 0.4285 -0.1089 -0.0069 0.0446 245 ASP A OD2 1898 N N . SER A 223 ? 0.5821 0.4222 0.3535 -0.0695 -0.0082 0.0433 246 SER A N 1899 C CA . SER A 223 ? 0.5281 0.3782 0.3098 -0.0621 -0.0089 0.0434 246 SER A CA 1900 C C . SER A 223 ? 0.5282 0.3960 0.3112 -0.0700 -0.0082 0.0418 246 SER A C 1901 O O . SER A 223 ? 0.5172 0.3824 0.2875 -0.0814 -0.0089 0.0440 246 SER A O 1902 C CB . SER A 223 ? 0.5363 0.3693 0.3108 -0.0559 -0.0126 0.0495 246 SER A CB 1903 O OG . SER A 223 ? 0.4735 0.3185 0.2588 -0.0491 -0.0131 0.0492 246 SER A OG 1904 N N . ASN A 224 ? 0.4977 0.3821 0.2941 -0.0648 -0.0075 0.0388 247 ASN A N 1905 C CA . ASN A 224 ? 0.5083 0.4090 0.3055 -0.0713 -0.0073 0.0374 247 ASN A CA 1906 C C . ASN A 224 ? 0.5058 0.4047 0.3033 -0.0664 -0.0099 0.0413 247 ASN A C 1907 O O . ASN A 224 ? 0.4931 0.4081 0.2954 -0.0689 -0.0096 0.0393 247 ASN A O 1908 C CB . ASN A 224 ? 0.4901 0.4140 0.3027 -0.0702 -0.0045 0.0295 247 ASN A CB 1909 C CG . ASN A 224 ? 0.4985 0.4265 0.3257 -0.0581 -0.0045 0.0276 247 ASN A CG 1910 O OD1 . ASN A 224 ? 0.4468 0.3619 0.2731 -0.0510 -0.0060 0.0315 247 ASN A OD1 1911 N ND2 . ASN A 224 ? 0.4204 0.3657 0.2600 -0.0562 -0.0030 0.0213 247 ASN A ND2 1912 N N . CYS A 225 ? 0.4952 0.3766 0.2887 -0.0590 -0.0124 0.0464 248 CYS A N 1913 C CA . CYS A 225 ? 0.4995 0.3793 0.2927 -0.0542 -0.0152 0.0503 248 CYS A CA 1914 C C . CYS A 225 ? 0.5334 0.4022 0.3093 -0.0625 -0.0185 0.0568 248 CYS A C 1915 O O . CYS A 225 ? 0.5568 0.4123 0.3195 -0.0700 -0.0191 0.0592 248 CYS A O 1916 C CB . CYS A 225 ? 0.4943 0.3609 0.2899 -0.0424 -0.0169 0.0529 248 CYS A CB 1917 S SG . CYS A 225 ? 0.4697 0.3461 0.2834 -0.0327 -0.0137 0.0468 248 CYS A SG 1918 N N . LYS A 226 ? 0.5658 0.4393 0.3418 -0.0610 -0.0208 0.0596 249 LYS A N 1919 C CA . LYS A 226 ? 0.6205 0.4801 0.3798 -0.0661 -0.0252 0.0672 249 LYS A CA 1920 C C . LYS A 226 ? 0.6333 0.4691 0.3860 -0.0572 -0.0288 0.0722 249 LYS A C 1921 O O . LYS A 226 ? 0.5927 0.4268 0.3554 -0.0462 -0.0278 0.0698 249 LYS A O 1922 C CB . LYS A 226 ? 0.6423 0.5137 0.4039 -0.0658 -0.0271 0.0691 249 LYS A CB 1923 C CG . LYS A 226 ? 0.7098 0.6075 0.4803 -0.0725 -0.0238 0.0632 249 LYS A CG 1924 C CD . LYS A 226 ? 0.8241 0.7283 0.5889 -0.0852 -0.0211 0.0600 249 LYS A CD 1925 C CE . LYS A 226 ? 0.8886 0.8189 0.6596 -0.0923 -0.0188 0.0548 249 LYS A CE 1926 N NZ . LYS A 226 ? 0.9309 0.8633 0.6868 -0.1072 -0.0194 0.0574 249 LYS A NZ 1927 N N . ASP A 227 ? 0.6355 0.4527 0.3706 -0.0617 -0.0333 0.0793 250 ASP A N 1928 C CA . ASP A 227 ? 0.6403 0.4323 0.3665 -0.0544 -0.0371 0.0837 250 ASP A CA 1929 C C . ASP A 227 ? 0.5979 0.3895 0.3313 -0.0409 -0.0399 0.0854 250 ASP A C 1930 O O . ASP A 227 ? 0.6380 0.4134 0.3699 -0.0309 -0.0421 0.0865 250 ASP A O 1931 C CB . ASP A 227 ? 0.7084 0.4788 0.4121 -0.0642 -0.0417 0.0910 250 ASP A CB 1932 C CG . ASP A 227 ? 0.7646 0.5318 0.4601 -0.0766 -0.0391 0.0893 250 ASP A CG 1933 O OD1 . ASP A 227 ? 0.8596 0.6281 0.5626 -0.0736 -0.0355 0.0840 250 ASP A OD1 1934 O OD2 . ASP A 227 ? 0.9194 0.6836 0.6007 -0.0899 -0.0406 0.0930 250 ASP A OD2 1935 N N . SER A 228 ? 0.5710 0.3805 0.3120 -0.0404 -0.0400 0.0852 251 SER A N 1936 C CA . SER A 228 ? 0.5641 0.3756 0.3115 -0.0287 -0.0428 0.0870 251 SER A CA 1937 C C . SER A 228 ? 0.5438 0.3822 0.3054 -0.0296 -0.0400 0.0829 251 SER A C 1938 O O . SER A 228 ? 0.5751 0.4275 0.3394 -0.0390 -0.0365 0.0793 251 SER A O 1939 C CB . SER A 228 ? 0.6216 0.4149 0.3524 -0.0288 -0.0498 0.0955 251 SER A CB 1940 O OG . SER A 228 ? 0.6453 0.4479 0.3695 -0.0405 -0.0505 0.0981 251 SER A OG 1941 N N . GLY A 229 ? 0.5223 0.3681 0.2930 -0.0196 -0.0414 0.0831 252 GLY A N 1942 C CA . GLY A 229 ? 0.5182 0.3876 0.3017 -0.0198 -0.0393 0.0795 252 GLY A CA 1943 C C . GLY A 229 ? 0.4837 0.3665 0.2837 -0.0159 -0.0341 0.0719 252 GLY A C 1944 O O . GLY A 229 ? 0.4844 0.3858 0.2952 -0.0167 -0.0320 0.0679 252 GLY A O 1945 N N . ILE A 230 ? 0.4806 0.3528 0.2818 -0.0115 -0.0327 0.0703 253 ILE A N 1946 C CA . ILE A 230 ? 0.4720 0.3552 0.2873 -0.0091 -0.0279 0.0634 253 ILE A CA 1947 C C . ILE A 230 ? 0.4542 0.3480 0.2823 0.0005 -0.0278 0.0616 253 ILE A C 1948 O O . ILE A 230 ? 0.4736 0.3605 0.3008 0.0091 -0.0305 0.0644 253 ILE A O 1949 C CB . ILE A 230 ? 0.4724 0.3413 0.2841 -0.0080 -0.0265 0.0624 253 ILE A CB 1950 C CG1 . ILE A 230 ? 0.4448 0.3062 0.2449 -0.0190 -0.0260 0.0633 253 ILE A CG1 1951 C CG2 . ILE A 230 ? 0.4644 0.3442 0.2902 -0.0050 -0.0222 0.0561 253 ILE A CG2 1952 C CD1 . ILE A 230 ? 0.4321 0.2740 0.2239 -0.0186 -0.0258 0.0638 253 ILE A CD1 1953 N N . LYS A 231 ? 0.4472 0.3586 0.2872 -0.0011 -0.0248 0.0566 254 LYS A N 1954 C CA . LYS A 231 ? 0.4452 0.3676 0.2972 0.0061 -0.0244 0.0544 254 LYS A CA 1955 C C . LYS A 231 ? 0.4224 0.3436 0.2823 0.0108 -0.0216 0.0507 254 LYS A C 1956 O O . LYS A 231 ? 0.4104 0.3290 0.2700 0.0066 -0.0192 0.0481 254 LYS A O 1957 C CB . LYS A 231 ? 0.4455 0.3864 0.3060 0.0015 -0.0228 0.0505 254 LYS A CB 1958 C CG . LYS A 231 ? 0.5168 0.4628 0.3710 -0.0041 -0.0249 0.0531 254 LYS A CG 1959 C CD . LYS A 231 ? 0.6245 0.5893 0.4877 -0.0073 -0.0236 0.0488 254 LYS A CD 1960 C CE . LYS A 231 ? 0.6566 0.6292 0.5247 -0.0135 -0.0201 0.0423 254 LYS A CE 1961 N NZ . LYS A 231 ? 0.6785 0.6677 0.5588 -0.0130 -0.0188 0.0368 254 LYS A NZ 1962 N N . TYR A 232 ? 0.4196 0.3437 0.2860 0.0189 -0.0220 0.0506 255 TYR A N 1963 C CA . TYR A 232 ? 0.4179 0.3423 0.2916 0.0232 -0.0196 0.0475 255 TYR A CA 1964 C C . TYR A 232 ? 0.3975 0.3381 0.2827 0.0253 -0.0188 0.0450 255 TYR A C 1965 O O . TYR A 232 ? 0.3996 0.3444 0.2877 0.0316 -0.0204 0.0464 255 TYR A O 1966 C CB . TYR A 232 ? 0.4401 0.3522 0.3090 0.0309 -0.0212 0.0499 255 TYR A CB 1967 C CG . TYR A 232 ? 0.3723 0.2821 0.2460 0.0352 -0.0188 0.0470 255 TYR A CG 1968 C CD1 . TYR A 232 ? 0.4070 0.3239 0.2885 0.0316 -0.0154 0.0429 255 TYR A CD1 1969 C CD2 . TYR A 232 ? 0.4092 0.3087 0.2788 0.0424 -0.0201 0.0483 255 TYR A CD2 1970 C CE1 . TYR A 232 ? 0.3876 0.3015 0.2718 0.0350 -0.0135 0.0410 255 TYR A CE1 1971 C CE2 . TYR A 232 ? 0.4196 0.3171 0.2924 0.0461 -0.0180 0.0457 255 TYR A CE2 1972 C CZ . TYR A 232 ? 0.3995 0.3044 0.2795 0.0418 -0.0146 0.0422 255 TYR A CZ 1973 O OH . TYR A 232 ? 0.3554 0.2592 0.2384 0.0453 -0.0126 0.0398 255 TYR A OH 1974 N N . PRO A 233 ? 0.3565 0.3067 0.2477 0.0196 -0.0169 0.0413 256 PRO A N 1975 C CA . PRO A 233 ? 0.3677 0.3325 0.2680 0.0203 -0.0169 0.0394 256 PRO A CA 1976 C C . PRO A 233 ? 0.3703 0.3393 0.2785 0.0252 -0.0157 0.0378 256 PRO A C 1977 O O . PRO A 233 ? 0.3736 0.3372 0.2831 0.0256 -0.0138 0.0361 256 PRO A O 1978 C CB . PRO A 233 ? 0.3672 0.3391 0.2709 0.0133 -0.0154 0.0353 256 PRO A CB 1979 C CG . PRO A 233 ? 0.3647 0.3282 0.2600 0.0085 -0.0151 0.0359 256 PRO A CG 1980 C CD . PRO A 233 ? 0.3686 0.3181 0.2577 0.0122 -0.0153 0.0389 256 PRO A CD 1981 N N . PRO A 234 ? 0.3774 0.3564 0.2904 0.0287 -0.0168 0.0384 257 PRO A N 1982 C CA . PRO A 234 ? 0.3743 0.3587 0.2941 0.0322 -0.0156 0.0369 257 PRO A CA 1983 C C . PRO A 234 ? 0.3474 0.3364 0.2736 0.0271 -0.0136 0.0330 257 PRO A C 1984 O O . PRO A 234 ? 0.3437 0.3369 0.2714 0.0223 -0.0138 0.0311 257 PRO A O 1985 C CB . PRO A 234 ? 0.3966 0.3934 0.3201 0.0354 -0.0174 0.0380 257 PRO A CB 1986 C CG . PRO A 234 ? 0.3999 0.3927 0.3161 0.0370 -0.0202 0.0416 257 PRO A CG 1987 C CD . PRO A 234 ? 0.3763 0.3615 0.2874 0.0301 -0.0195 0.0411 257 PRO A CD 1988 N N . LYS A 235 ? 0.3369 0.3236 0.2660 0.0283 -0.0120 0.0318 258 LYS A N 1989 C CA . LYS A 235 ? 0.3024 0.2926 0.2371 0.0241 -0.0109 0.0287 258 LYS A CA 1990 C C . LYS A 235 ? 0.2989 0.3016 0.2397 0.0230 -0.0115 0.0279 258 LYS A C 1991 O O . LYS A 235 ? 0.3349 0.3440 0.2765 0.0268 -0.0120 0.0296 258 LYS A O 1992 C CB . LYS A 235 ? 0.2858 0.2698 0.2209 0.0250 -0.0093 0.0281 258 LYS A CB 1993 C CG . LYS A 235 ? 0.2740 0.2463 0.2036 0.0247 -0.0085 0.0282 258 LYS A CG 1994 C CD . LYS A 235 ? 0.2753 0.2433 0.2059 0.0251 -0.0070 0.0274 258 LYS A CD 1995 C CE . LYS A 235 ? 0.2973 0.2552 0.2236 0.0235 -0.0062 0.0268 258 LYS A CE 1996 N NZ . LYS A 235 ? 0.2526 0.2069 0.1796 0.0237 -0.0049 0.0261 258 LYS A NZ 1997 N N . TYR A 236 ? 0.3159 0.3214 0.2605 0.0180 -0.0115 0.0250 259 TYR A N 1998 C CA . TYR A 236 ? 0.3407 0.3564 0.2904 0.0154 -0.0121 0.0239 259 TYR A CA 1999 C C . TYR A 236 ? 0.3932 0.4189 0.3430 0.0166 -0.0133 0.0251 259 TYR A C 2000 O O . TYR A 236 ? 0.3475 0.3831 0.3003 0.0173 -0.0136 0.0257 259 TYR A O 2001 C CB . TYR A 236 ? 0.3268 0.3453 0.2788 0.0167 -0.0111 0.0247 259 TYR A CB 2002 C CG . TYR A 236 ? 0.2960 0.3045 0.2472 0.0157 -0.0100 0.0241 259 TYR A CG 2003 C CD1 . TYR A 236 ? 0.2785 0.2821 0.2310 0.0112 -0.0106 0.0217 259 TYR A CD1 2004 C CD2 . TYR A 236 ? 0.2913 0.2952 0.2400 0.0197 -0.0087 0.0256 259 TYR A CD2 2005 C CE1 . TYR A 236 ? 0.2644 0.2592 0.2158 0.0108 -0.0101 0.0214 259 TYR A CE1 2006 C CE2 . TYR A 236 ? 0.2544 0.2499 0.2019 0.0187 -0.0078 0.0251 259 TYR A CE2 2007 C CZ . TYR A 236 ? 0.2253 0.2166 0.1742 0.0142 -0.0086 0.0233 259 TYR A CZ 2008 O OH . TYR A 236 ? 0.2751 0.2584 0.2228 0.0133 -0.0081 0.0229 259 TYR A OH 2009 N N A SER A 237 ? 0.4273 0.4511 0.3735 0.0165 -0.0142 0.0256 260 SER A N 2010 N N B SER A 237 ? 0.4284 0.4520 0.3745 0.0165 -0.0142 0.0257 260 SER A N 2011 C CA A SER A 237 ? 0.4826 0.5135 0.4270 0.0191 -0.0158 0.0282 260 SER A CA 2012 C CA B SER A 237 ? 0.4852 0.5160 0.4295 0.0189 -0.0158 0.0281 260 SER A CA 2013 C C A SER A 237 ? 0.5377 0.5820 0.4861 0.0163 -0.0168 0.0270 260 SER A C 2014 C C B SER A 237 ? 0.5375 0.5817 0.4863 0.0162 -0.0167 0.0269 260 SER A C 2015 O O A SER A 237 ? 0.5682 0.6218 0.5178 0.0196 -0.0179 0.0290 260 SER A O 2016 O O B SER A 237 ? 0.5698 0.6235 0.5204 0.0193 -0.0175 0.0286 260 SER A O 2017 C CB A SER A 237 ? 0.4816 0.5067 0.4197 0.0187 -0.0166 0.0295 260 SER A CB 2018 C CB B SER A 237 ? 0.4816 0.5081 0.4208 0.0169 -0.0165 0.0284 260 SER A CB 2019 O OG A SER A 237 ? 0.4530 0.4871 0.3903 0.0185 -0.0185 0.0310 260 SER A OG 2020 O OG B SER A 237 ? 0.4644 0.4940 0.4066 0.0113 -0.0162 0.0243 260 SER A OG # 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 THR 1 24 24 THR THR A . n A 1 2 ILE 2 25 25 ILE ILE A . n A 1 3 ASP 3 26 26 ASP ASP A . n A 1 4 THR 4 27 27 THR THR A . n A 1 5 CYS 5 28 28 CYS CYS A . n A 1 6 SER 6 29 29 SER SER A . n A 1 7 SER 7 30 30 SER SER A . n A 1 8 ASP 8 31 31 ASP ASP A . n A 1 9 SER 9 32 32 SER SER A . n A 1 10 PRO 10 33 33 PRO PRO A . n A 1 11 LEU 11 34 34 LEU LEU A . n A 1 12 SER 12 35 35 SER SER A . n A 1 13 CYS 13 36 36 CYS CYS A . n A 1 14 GLN 14 37 37 GLN GLN A . n A 1 15 THR 15 38 38 THR THR A . n A 1 16 ASP 16 39 39 ASP ASP A . n A 1 17 ASN 17 40 40 ASN ASN A . n A 1 18 GLU 18 41 41 GLU GLU A . n A 1 19 ALA 19 42 42 ALA ALA A . n A 1 20 SER 20 43 43 SER SER A . n A 1 21 CYS 21 44 44 CYS CYS A . n A 1 22 CYS 22 45 45 CYS CYS A . n A 1 23 PHE 23 46 46 PHE PHE A . n A 1 24 ASN 24 47 47 ASN ASN A . n A 1 25 SER 25 48 48 SER SER A . n A 1 26 PRO 26 49 49 PRO PRO A . n A 1 27 GLY 27 50 50 GLY GLY A . n A 1 28 GLY 28 51 51 GLY GLY A . n A 1 29 SER 29 52 52 SER SER A . n A 1 30 LEU 30 53 53 LEU LEU A . n A 1 31 LEU 31 54 54 LEU LEU A . n A 1 32 GLN 32 55 55 GLN GLN A . n A 1 33 THR 33 56 56 THR THR A . n A 1 34 GLN 34 57 57 GLN GLN A . n A 1 35 PHE 35 58 58 PHE PHE A . n A 1 36 TRP 36 59 59 TRP TRP A . n A 1 37 ASP 37 60 60 ASP ASP A . n A 1 38 TYR 38 61 61 TYR TYR A . n A 1 39 ASP 39 62 62 ASP ASP A . n A 1 40 PRO 40 63 63 PRO PRO A . n A 1 41 SER 41 64 64 SER SER A . n A 1 42 ASP 42 65 65 ASP ASP A . n A 1 43 GLY 43 66 66 GLY GLY A . n A 1 44 PRO 44 67 67 PRO PRO A . n A 1 45 SER 45 68 68 SER SER A . n A 1 46 ASP 46 69 69 ASP ASP A . n A 1 47 SER 47 70 70 SER SER A . n A 1 48 TRP 48 71 71 TRP TRP A . n A 1 49 THR 49 72 72 THR THR A . n A 1 50 ILE 50 73 73 ILE ILE A . n A 1 51 HIS 51 74 74 HIS HIS A . n A 1 52 GLY 52 75 75 GLY GLY A . n A 1 53 LEU 53 76 76 LEU LEU A . n A 1 54 TRP 54 77 77 TRP TRP A . n A 1 55 PRO 55 78 78 PRO PRO A . n A 1 56 ASP 56 79 79 ASP ASP A . n A 1 57 ASN 57 80 80 ASN ASN A . n A 1 58 CYS 58 81 81 CYS CYS A . n A 1 59 ASP 59 82 82 ASP ASP A . n A 1 60 GLY 60 83 83 GLY GLY A . n A 1 61 THR 61 84 84 THR THR A . n A 1 62 TYR 62 85 85 TYR TYR A . n A 1 63 GLN 63 86 86 GLN GLN A . n A 1 64 GLU 64 87 87 GLU GLU A . n A 1 65 TYR 65 88 88 TYR TYR A . n A 1 66 CYS 66 89 89 CYS CYS A . n A 1 67 ASP 67 90 90 ASP ASP A . n A 1 68 GLU 68 91 91 GLU GLU A . n A 1 69 SER 69 92 92 SER SER A . n A 1 70 ARG 70 93 93 ARG ARG A . n A 1 71 GLU 71 94 94 GLU GLU A . n A 1 72 TYR 72 95 95 TYR TYR A . n A 1 73 SER 73 96 96 SER SER A . n A 1 74 ASN 74 97 97 ASN ASN A . n A 1 75 ILE 75 98 98 ILE ILE A . n A 1 76 THR 76 99 99 THR THR A . n A 1 77 SER 77 100 100 SER SER A . n A 1 78 ILE 78 101 101 ILE ILE A . n A 1 79 LEU 79 102 102 LEU LEU A . n A 1 80 GLU 80 103 103 GLU GLU A . n A 1 81 ALA 81 104 104 ALA ALA A . n A 1 82 GLN 82 105 105 GLN GLN A . n A 1 83 ASN 83 106 106 ASN ASN A . n A 1 84 ARG 84 107 107 ARG ARG A . n A 1 85 THR 85 108 108 THR THR A . n A 1 86 GLU 86 109 109 GLU GLU A . n A 1 87 LEU 87 110 110 LEU LEU A . n A 1 88 LEU 88 111 111 LEU LEU A . n A 1 89 SER 89 112 112 SER SER A . n A 1 90 TYR 90 113 113 TYR TYR A . n A 1 91 MET 91 114 114 MET MET A . n A 1 92 LYS 92 115 115 LYS LYS A . n A 1 93 GLU 93 116 116 GLU GLU A . n A 1 94 TYR 94 117 117 TYR TYR A . n A 1 95 TRP 95 118 118 TRP TRP A . n A 1 96 PRO 96 119 119 PRO PRO A . n A 1 97 ASP 97 120 120 ASP ASP A . n A 1 98 TYR 98 121 121 TYR TYR A . n A 1 99 GLU 99 122 122 GLU GLU A . n A 1 100 GLY 100 123 123 GLY GLY A . n A 1 101 ALA 101 124 124 ALA ALA A . n A 1 102 ASP 102 125 125 ASP ASP A . n A 1 103 GLU 103 126 126 GLU GLU A . n A 1 104 ASP 104 127 127 ASP ASP A . n A 1 105 GLU 105 128 128 GLU GLU A . n A 1 106 SER 106 129 129 SER SER A . n A 1 107 PHE 107 130 130 PHE PHE A . n A 1 108 TRP 108 131 131 TRP TRP A . n A 1 109 GLU 109 132 132 GLU GLU A . n A 1 110 HIS 110 133 133 HIS HIS A . n A 1 111 GLU 111 134 134 GLU GLU A . n A 1 112 TRP 112 135 135 TRP TRP A . n A 1 113 ASN 113 136 136 ASN ASN A . n A 1 114 LYS 114 137 137 LYS LYS A . n A 1 115 HIS 115 138 138 HIS HIS A . n A 1 116 GLY 116 139 139 GLY GLY A . n A 1 117 THR 117 140 140 THR THR A . n A 1 118 CYS 118 141 141 CYS CYS A . n A 1 119 ILE 119 142 142 ILE ILE A . n A 1 120 ASN 120 143 143 ASN ASN A . n A 1 121 THR 121 144 144 THR THR A . n A 1 122 ILE 122 145 145 ILE ILE A . n A 1 123 GLU 123 146 146 GLU GLU A . n A 1 124 PRO 124 147 147 PRO PRO A . n A 1 125 SER 125 148 148 SER SER A . n A 1 126 CYS 126 149 149 CYS CYS A . n A 1 127 TYR 127 150 150 TYR TYR A . n A 1 128 THR 128 151 151 THR THR A . n A 1 129 ASP 129 152 152 ASP ASP A . n A 1 130 TYR 130 153 153 TYR TYR A . n A 1 131 TYR 131 154 154 TYR TYR A . n A 1 132 ALA 132 155 155 ALA ALA A . n A 1 133 GLN 133 156 156 GLN GLN A . n A 1 134 GLU 134 157 157 GLU GLU A . n A 1 135 GLU 135 158 158 GLU GLU A . n A 1 136 VAL 136 159 159 VAL VAL A . n A 1 137 GLY 137 160 160 GLY GLY A . n A 1 138 ASP 138 161 161 ASP ASP A . n A 1 139 PHE 139 162 162 PHE PHE A . n A 1 140 PHE 140 163 163 PHE PHE A . n A 1 141 GLN 141 164 164 GLN GLN A . n A 1 142 GLN 142 165 165 GLN GLN A . n A 1 143 VAL 143 166 166 VAL VAL A . n A 1 144 VAL 144 167 167 VAL VAL A . n A 1 145 ASP 145 168 168 ASP ASP A . n A 1 146 LEU 146 169 169 LEU LEU A . n A 1 147 PHE 147 170 170 PHE PHE A . n A 1 148 LYS 148 171 171 LYS LYS A . n A 1 149 THR 149 172 172 THR THR A . n A 1 150 LEU 150 173 173 LEU LEU A . n A 1 151 ASP 151 174 174 ASP ASP A . n A 1 152 SER 152 175 175 SER SER A . n A 1 153 TYR 153 176 176 TYR TYR A . n A 1 154 THR 154 177 177 THR THR A . n A 1 155 ALA 155 178 178 ALA ALA A . n A 1 156 LEU 156 179 179 LEU LEU A . n A 1 157 SER 157 180 180 SER SER A . n A 1 158 ASP 158 181 181 ASP ASP A . n A 1 159 ALA 159 182 182 ALA ALA A . n A 1 160 GLY 160 183 183 GLY GLY A . n A 1 161 ILE 161 184 184 ILE ILE A . n A 1 162 THR 162 185 185 THR THR A . n A 1 163 PRO 163 186 186 PRO PRO A . n A 1 164 SER 164 187 187 SER SER A . n A 1 165 GLU 165 188 188 GLU GLU A . n A 1 166 ASP 166 189 189 ASP ASP A . n A 1 167 ALA 167 190 190 ALA ALA A . n A 1 168 THR 168 191 191 THR THR A . n A 1 169 TYR 169 192 192 TYR TYR A . n A 1 170 LYS 170 193 193 LYS LYS A . n A 1 171 LEU 171 194 194 LEU LEU A . n A 1 172 SER 172 195 195 SER SER A . n A 1 173 ASP 173 196 196 ASP ASP A . n A 1 174 ILE 174 197 197 ILE ILE A . n A 1 175 GLU 175 198 198 GLU GLU A . n A 1 176 ASP 176 199 199 ASP ASP A . n A 1 177 ALA 177 200 200 ALA ALA A . n A 1 178 LEU 178 201 201 LEU LEU A . n A 1 179 ALA 179 202 202 ALA ALA A . n A 1 180 ALA 180 203 203 ALA ALA A . n A 1 181 ILE 181 204 204 ILE ILE A . n A 1 182 HIS 182 205 205 HIS HIS A . n A 1 183 ASP 183 206 206 ASP ASP A . n A 1 184 GLY 184 207 207 GLY GLY A . n A 1 185 TYR 185 208 208 TYR TYR A . n A 1 186 PRO 186 209 209 PRO PRO A . n A 1 187 PRO 187 210 210 PRO PRO A . n A 1 188 TYR 188 211 211 TYR TYR A . n A 1 189 VAL 189 212 212 VAL VAL A . n A 1 190 GLY 190 213 213 GLY GLY A . n A 1 191 CYS 191 214 214 CYS CYS A . n A 1 192 GLU 192 215 215 GLU GLU A . n A 1 193 ASP 193 216 216 ASP ASP A . n A 1 194 GLY 194 217 217 GLY GLY A . n A 1 195 ALA 195 218 218 ALA ALA A . n A 1 196 LEU 196 219 219 LEU LEU A . n A 1 197 SER 197 220 220 SER SER A . n A 1 198 GLN 198 221 221 GLN GLN A . n A 1 199 LEU 199 222 222 LEU LEU A . n A 1 200 TYR 200 223 223 TYR TYR A . n A 1 201 TYR 201 224 224 TYR TYR A . n A 1 202 TYR 202 225 225 TYR TYR A . n A 1 203 PHE 203 226 226 PHE PHE A . n A 1 204 ASN 204 227 227 ASN ASN A . n A 1 205 VAL 205 228 228 VAL VAL A . n A 1 206 LYS 206 229 229 LYS LYS A . n A 1 207 GLY 207 230 230 GLY GLY A . n A 1 208 SER 208 231 231 SER SER A . n A 1 209 ALA 209 232 232 ALA ALA A . n A 1 210 ILE 210 233 233 ILE ILE A . n A 1 211 GLY 211 234 234 GLY GLY A . n A 1 212 GLY 212 235 235 GLY GLY A . n A 1 213 THR 213 236 236 THR THR A . n A 1 214 TYR 214 237 237 TYR TYR A . n A 1 215 VAL 215 238 238 VAL VAL A . n A 1 216 ALA 216 239 239 ALA ALA A . n A 1 217 SER 217 240 240 SER SER A . n A 1 218 GLU 218 241 241 GLU GLU A . n A 1 219 ARG 219 242 242 ARG ARG A . n A 1 220 LEU 220 243 243 LEU LEU A . n A 1 221 GLU 221 244 244 GLU GLU A . n A 1 222 ASP 222 245 245 ASP ASP A . n A 1 223 SER 223 246 246 SER SER A . n A 1 224 ASN 224 247 247 ASN ASN A . n A 1 225 CYS 225 248 248 CYS CYS A . n A 1 226 LYS 226 249 249 LYS LYS A . n A 1 227 ASP 227 250 250 ASP ASP A . n A 1 228 SER 228 251 251 SER SER A . n A 1 229 GLY 229 252 252 GLY GLY A . n A 1 230 ILE 230 253 253 ILE ILE A . n A 1 231 LYS 231 254 254 LYS LYS A . n A 1 232 TYR 232 255 255 TYR TYR A . n A 1 233 PRO 233 256 256 PRO PRO A . n A 1 234 PRO 234 257 257 PRO PRO A . n A 1 235 LYS 235 258 258 LYS LYS A . n A 1 236 TYR 236 259 259 TYR TYR A . n A 1 237 SER 237 260 260 SER SER A . n # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 83 A ASN 106 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 74 A ASN 97 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2012-08-22 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 29.6420 _pdbx_refine_tls.origin_y -16.5890 _pdbx_refine_tls.origin_z 37.0430 _pdbx_refine_tls.T[1][1] 0.1334 _pdbx_refine_tls.T[2][2] 0.0324 _pdbx_refine_tls.T[3][3] 0.0195 _pdbx_refine_tls.T[1][2] -0.0012 _pdbx_refine_tls.T[1][3] 0.0037 _pdbx_refine_tls.T[2][3] 0.0155 _pdbx_refine_tls.L[1][1] 0.6316 _pdbx_refine_tls.L[2][2] 0.2179 _pdbx_refine_tls.L[3][3] 1.1620 _pdbx_refine_tls.L[1][2] 0.2629 _pdbx_refine_tls.L[1][3] 0.2854 _pdbx_refine_tls.L[2][3] 0.2369 _pdbx_refine_tls.S[1][1] 0.0071 _pdbx_refine_tls.S[1][2] 0.0363 _pdbx_refine_tls.S[1][3] 0.0101 _pdbx_refine_tls.S[2][1] 0.0044 _pdbx_refine_tls.S[2][2] 0.0390 _pdbx_refine_tls.S[2][3] 0.0290 _pdbx_refine_tls.S[3][1] -0.1958 _pdbx_refine_tls.S[3][2] 0.0594 _pdbx_refine_tls.S[3][3] -0.0461 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 24 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 260 _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ? # _pdbx_phasing_MR.entry_id 3TBJ _pdbx_phasing_MR.method_rotation ? _pdbx_phasing_MR.method_translation ? _pdbx_phasing_MR.model_details ? _pdbx_phasing_MR.R_factor ? _pdbx_phasing_MR.R_rigid_body ? _pdbx_phasing_MR.correlation_coeff_Fo_to_Fc ? _pdbx_phasing_MR.correlation_coeff_Io_to_Ic ? _pdbx_phasing_MR.d_res_high_rotation 3.000 _pdbx_phasing_MR.d_res_low_rotation 32.290 _pdbx_phasing_MR.d_res_high_translation 3.000 _pdbx_phasing_MR.d_res_low_translation 32.290 _pdbx_phasing_MR.packing ? _pdbx_phasing_MR.reflns_percent_rotation ? _pdbx_phasing_MR.reflns_percent_translation ? _pdbx_phasing_MR.sigma_F_rotation ? _pdbx_phasing_MR.sigma_F_translation ? _pdbx_phasing_MR.sigma_I_rotation ? _pdbx_phasing_MR.sigma_I_translation ? # _phasing.method MR # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 SCALA 3.3.16 2010/01/06 other 'Phil R. Evans' pre@mrc-lmb.cam.ac.uk 'data scaling' http://www.ccp4.ac.uk/dist/html/scala.html Fortran_77 ? 2 MOLREP . ? program 'Alexei Vaguine' alexei@ysbl.york.ac.uk phasing http://www.ccp4.ac.uk/dist/html/molrep.html Fortran_77 ? 3 REFMAC . ? program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 4 PDB_EXTRACT 3.10 'June 10, 2010' package PDB deposit@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 5 Blu-Ice . ? ? ? ? 'data collection' ? ? ? # _pdbx_entry_details.entry_id 3TBJ _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'AUTHORS STATE THAT RESIDUE 69 IS ASP ACCORDING TO THE CRYSTAL STRUCTURE, AND THIS IS A WILD TYPE NATIVE PROTEIN.' _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 OE2 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 GLU _pdbx_validate_close_contact.auth_seq_id_1 94 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 HOH _pdbx_validate_close_contact.auth_seq_id_2 445 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.16 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 79 ? ? CG A ASP 79 ? ? OD2 A ASP 79 ? ? 111.71 118.30 -6.59 0.90 N 2 1 NE A ARG 93 ? ? CZ A ARG 93 ? ? NH1 A ARG 93 ? ? 124.28 120.30 3.98 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 CYS A 36 ? ? 63.71 -42.18 2 1 ASN A 97 ? ? -151.96 49.92 3 1 ASN A 97 ? ? -154.23 49.92 4 1 ARG A 107 ? ? -95.13 57.15 5 1 HIS A 205 ? ? -144.62 38.13 6 1 HIS A 205 ? ? -144.62 38.70 7 1 SER A 220 ? ? -140.48 -41.21 8 1 ASP A 245 ? A -90.79 -63.44 9 1 ASP A 245 ? B -91.82 -65.34 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 'PHOSPHATE ION' PO4 4 1,2-ETHANEDIOL EDO 5 water HOH # 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 1 NAG NAG A . C 2 NAG 2 302 2 NAG NAG A . D 2 NAG 1 303 3 NAG NAG A . E 3 PO4 1 304 2 PO4 PO4 A . F 3 PO4 1 305 1 PO4 PO4 A . G 4 EDO 1 306 1 EDO EDO A . H 4 EDO 1 307 2 EDO EDO A . I 4 EDO 1 308 3 EDO EDO A . J 5 HOH 1 401 4 HOH HOH A . J 5 HOH 2 402 7 HOH HOH A . J 5 HOH 3 403 8 HOH HOH A . J 5 HOH 4 404 12 HOH HOH A . J 5 HOH 5 405 14 HOH HOH A . J 5 HOH 6 406 16 HOH HOH A . J 5 HOH 7 407 18 HOH HOH A . J 5 HOH 8 408 19 HOH HOH A . J 5 HOH 9 409 22 HOH HOH A . J 5 HOH 10 410 266 HOH HOH A . J 5 HOH 11 411 269 HOH HOH A . J 5 HOH 12 412 271 HOH HOH A . J 5 HOH 13 413 272 HOH HOH A . J 5 HOH 14 414 273 HOH HOH A . J 5 HOH 15 415 278 HOH HOH A . J 5 HOH 16 416 284 HOH HOH A . J 5 HOH 17 417 286 HOH HOH A . J 5 HOH 18 418 288 HOH HOH A . J 5 HOH 19 419 289 HOH HOH A . J 5 HOH 20 420 290 HOH HOH A . J 5 HOH 21 421 292 HOH HOH A . J 5 HOH 22 422 294 HOH HOH A . J 5 HOH 23 423 295 HOH HOH A . J 5 HOH 24 424 296 HOH HOH A . J 5 HOH 25 425 297 HOH HOH A . J 5 HOH 26 426 299 HOH HOH A . J 5 HOH 27 427 301 HOH HOH A . J 5 HOH 28 428 305 HOH HOH A . J 5 HOH 29 429 306 HOH HOH A . J 5 HOH 30 430 307 HOH HOH A . J 5 HOH 31 431 311 HOH HOH A . J 5 HOH 32 432 316 HOH HOH A . J 5 HOH 33 433 321 HOH HOH A . J 5 HOH 34 434 323 HOH HOH A . J 5 HOH 35 435 327 HOH HOH A . J 5 HOH 36 436 329 HOH HOH A . J 5 HOH 37 437 330 HOH HOH A . J 5 HOH 38 438 331 HOH HOH A . J 5 HOH 39 439 334 HOH HOH A . J 5 HOH 40 440 335 HOH HOH A . J 5 HOH 41 441 337 HOH HOH A . J 5 HOH 42 442 338 HOH HOH A . J 5 HOH 43 443 339 HOH HOH A . J 5 HOH 44 444 340 HOH HOH A . J 5 HOH 45 445 341 HOH HOH A . J 5 HOH 46 446 348 HOH HOH A . J 5 HOH 47 447 356 HOH HOH A . J 5 HOH 48 448 359 HOH HOH A . J 5 HOH 49 449 370 HOH HOH A . J 5 HOH 50 450 372 HOH HOH A . J 5 HOH 51 451 375 HOH HOH A . J 5 HOH 52 452 378 HOH HOH A . J 5 HOH 53 453 382 HOH HOH A . J 5 HOH 54 454 384 HOH HOH A . J 5 HOH 55 455 386 HOH HOH A . J 5 HOH 56 456 391 HOH HOH A . J 5 HOH 57 457 392 HOH HOH A . J 5 HOH 58 458 393 HOH HOH A . J 5 HOH 59 459 395 HOH HOH A . J 5 HOH 60 460 397 HOH HOH A . J 5 HOH 61 461 398 HOH HOH A . J 5 HOH 62 462 399 HOH HOH A . J 5 HOH 63 463 400 HOH HOH A . J 5 HOH 64 464 402 HOH HOH A . J 5 HOH 65 465 404 HOH HOH A . J 5 HOH 66 466 406 HOH HOH A . J 5 HOH 67 467 412 HOH HOH A . J 5 HOH 68 468 413 HOH HOH A . J 5 HOH 69 469 414 HOH HOH A . J 5 HOH 70 470 415 HOH HOH A . J 5 HOH 71 471 416 HOH HOH A . J 5 HOH 72 472 417 HOH HOH A . J 5 HOH 73 473 418 HOH HOH A . J 5 HOH 74 474 419 HOH HOH A . J 5 HOH 75 475 423 HOH HOH A . J 5 HOH 76 476 427 HOH HOH A . J 5 HOH 77 477 431 HOH HOH A . J 5 HOH 78 478 432 HOH HOH A . J 5 HOH 79 479 434 HOH HOH A . J 5 HOH 80 480 439 HOH HOH A . J 5 HOH 81 481 441 HOH HOH A . J 5 HOH 82 482 442 HOH HOH A . J 5 HOH 83 483 443 HOH HOH A . J 5 HOH 84 484 445 HOH HOH A . J 5 HOH 85 485 447 HOH HOH A . J 5 HOH 86 486 453 HOH HOH A . J 5 HOH 87 487 454 HOH HOH A . J 5 HOH 88 488 455 HOH HOH A . J 5 HOH 89 489 459 HOH HOH A . J 5 HOH 90 490 462 HOH HOH A . J 5 HOH 91 491 465 HOH HOH A . J 5 HOH 92 492 468 HOH HOH A . J 5 HOH 93 493 473 HOH HOH A . J 5 HOH 94 494 476 HOH HOH A . J 5 HOH 95 495 477 HOH HOH A . J 5 HOH 96 496 478 HOH HOH A . J 5 HOH 97 497 479 HOH HOH A . J 5 HOH 98 498 480 HOH HOH A . J 5 HOH 99 499 481 HOH HOH A . J 5 HOH 100 500 482 HOH HOH A . J 5 HOH 101 501 484 HOH HOH A . J 5 HOH 102 502 485 HOH HOH A . J 5 HOH 103 503 487 HOH HOH A . J 5 HOH 104 504 488 HOH HOH A . J 5 HOH 105 505 489 HOH HOH A . J 5 HOH 106 506 490 HOH HOH A . J 5 HOH 107 507 491 HOH HOH A . J 5 HOH 108 508 493 HOH HOH A . J 5 HOH 109 509 494 HOH HOH A . J 5 HOH 110 510 495 HOH HOH A . J 5 HOH 111 511 497 HOH HOH A . J 5 HOH 112 512 499 HOH HOH A . J 5 HOH 113 513 500 HOH HOH A . J 5 HOH 114 514 502 HOH HOH A . J 5 HOH 115 515 503 HOH HOH A . J 5 HOH 116 516 504 HOH HOH A . J 5 HOH 117 517 505 HOH HOH A . J 5 HOH 118 518 506 HOH HOH A . J 5 HOH 119 519 510 HOH HOH A . J 5 HOH 120 520 512 HOH HOH A . J 5 HOH 121 521 513 HOH HOH A . J 5 HOH 122 522 514 HOH HOH A . J 5 HOH 123 523 515 HOH HOH A . J 5 HOH 124 524 517 HOH HOH A . J 5 HOH 125 525 519 HOH HOH A . J 5 HOH 126 526 1000 HOH HOH A . J 5 HOH 127 527 1001 HOH HOH A . J 5 HOH 128 528 1 HOH HOH A . J 5 HOH 129 529 2 HOH HOH A . J 5 HOH 130 530 24 HOH HOH A . J 5 HOH 131 531 26 HOH HOH A . J 5 HOH 132 532 27 HOH HOH A . J 5 HOH 133 533 28 HOH HOH A . J 5 HOH 134 534 33 HOH HOH A . J 5 HOH 135 535 34 HOH HOH A . J 5 HOH 136 536 35 HOH HOH A . J 5 HOH 137 537 36 HOH HOH A . J 5 HOH 138 538 37 HOH HOH A . J 5 HOH 139 539 38 HOH HOH A . J 5 HOH 140 540 40 HOH HOH A . J 5 HOH 141 541 42 HOH HOH A . J 5 HOH 142 542 43 HOH HOH A . J 5 HOH 143 543 44 HOH HOH A . J 5 HOH 144 544 45 HOH HOH A . J 5 HOH 145 545 47 HOH HOH A . J 5 HOH 146 546 49 HOH HOH A . J 5 HOH 147 547 50 HOH HOH A . J 5 HOH 148 548 51 HOH HOH A . J 5 HOH 149 549 53 HOH HOH A . J 5 HOH 150 550 55 HOH HOH A . J 5 HOH 151 551 56 HOH HOH A . J 5 HOH 152 552 57 HOH HOH A . J 5 HOH 153 553 59 HOH HOH A . J 5 HOH 154 554 61 HOH HOH A . J 5 HOH 155 555 63 HOH HOH A . J 5 HOH 156 556 65 HOH HOH A . J 5 HOH 157 557 67 HOH HOH A . J 5 HOH 158 558 69 HOH HOH A . J 5 HOH 159 559 70 HOH HOH A . J 5 HOH 160 560 71 HOH HOH A . J 5 HOH 161 561 72 HOH HOH A . J 5 HOH 162 562 73 HOH HOH A . J 5 HOH 163 563 74 HOH HOH A . J 5 HOH 164 564 75 HOH HOH A . J 5 HOH 165 565 77 HOH HOH A . J 5 HOH 166 566 78 HOH HOH A . J 5 HOH 167 567 79 HOH HOH A . J 5 HOH 168 568 80 HOH HOH A . J 5 HOH 169 569 81 HOH HOH A . J 5 HOH 170 570 82 HOH HOH A . J 5 HOH 171 571 83 HOH HOH A . J 5 HOH 172 572 84 HOH HOH A . J 5 HOH 173 573 85 HOH HOH A . J 5 HOH 174 574 86 HOH HOH A . J 5 HOH 175 575 87 HOH HOH A . J 5 HOH 176 576 88 HOH HOH A . J 5 HOH 177 577 89 HOH HOH A . J 5 HOH 178 578 91 HOH HOH A . J 5 HOH 179 579 92 HOH HOH A . J 5 HOH 180 580 93 HOH HOH A . J 5 HOH 181 581 94 HOH HOH A . J 5 HOH 182 582 95 HOH HOH A . J 5 HOH 183 583 98 HOH HOH A . J 5 HOH 184 584 102 HOH HOH A . J 5 HOH 185 585 103 HOH HOH A . J 5 HOH 186 586 104 HOH HOH A . J 5 HOH 187 587 105 HOH HOH A . J 5 HOH 188 588 106 HOH HOH A . J 5 HOH 189 589 107 HOH HOH A . J 5 HOH 190 590 108 HOH HOH A . J 5 HOH 191 591 110 HOH HOH A . J 5 HOH 192 592 111 HOH HOH A . J 5 HOH 193 593 112 HOH HOH A . J 5 HOH 194 594 113 HOH HOH A . J 5 HOH 195 595 116 HOH HOH A . J 5 HOH 196 596 118 HOH HOH A . J 5 HOH 197 597 121 HOH HOH A . J 5 HOH 198 598 122 HOH HOH A . J 5 HOH 199 599 123 HOH HOH A . J 5 HOH 200 600 124 HOH HOH A . J 5 HOH 201 601 125 HOH HOH A . J 5 HOH 202 602 126 HOH HOH A . J 5 HOH 203 603 128 HOH HOH A . J 5 HOH 204 604 129 HOH HOH A . J 5 HOH 205 605 130 HOH HOH A . J 5 HOH 206 606 132 HOH HOH A . J 5 HOH 207 607 135 HOH HOH A . J 5 HOH 208 608 137 HOH HOH A . J 5 HOH 209 609 138 HOH HOH A . J 5 HOH 210 610 139 HOH HOH A . J 5 HOH 211 611 140 HOH HOH A . J 5 HOH 212 612 141 HOH HOH A . J 5 HOH 213 613 142 HOH HOH A . J 5 HOH 214 614 144 HOH HOH A . J 5 HOH 215 615 145 HOH HOH A . J 5 HOH 216 616 149 HOH HOH A . J 5 HOH 217 617 158 HOH HOH A . J 5 HOH 218 618 161 HOH HOH A . J 5 HOH 219 619 162 HOH HOH A . J 5 HOH 220 620 164 HOH HOH A . J 5 HOH 221 621 167 HOH HOH A . J 5 HOH 222 622 168 HOH HOH A . J 5 HOH 223 623 171 HOH HOH A . J 5 HOH 224 624 172 HOH HOH A . J 5 HOH 225 625 173 HOH HOH A . J 5 HOH 226 626 175 HOH HOH A . J 5 HOH 227 627 177 HOH HOH A . J 5 HOH 228 628 178 HOH HOH A . J 5 HOH 229 629 180 HOH HOH A . J 5 HOH 230 630 181 HOH HOH A . J 5 HOH 231 631 182 HOH HOH A . J 5 HOH 232 632 183 HOH HOH A . J 5 HOH 233 633 184 HOH HOH A . J 5 HOH 234 634 185 HOH HOH A . J 5 HOH 235 635 186 HOH HOH A . J 5 HOH 236 636 187 HOH HOH A . J 5 HOH 237 637 188 HOH HOH A . J 5 HOH 238 638 189 HOH HOH A . J 5 HOH 239 639 191 HOH HOH A . J 5 HOH 240 640 192 HOH HOH A . J 5 HOH 241 641 193 HOH HOH A . J 5 HOH 242 642 194 HOH HOH A . J 5 HOH 243 643 195 HOH HOH A . J 5 HOH 244 644 196 HOH HOH A . J 5 HOH 245 645 197 HOH HOH A . J 5 HOH 246 646 198 HOH HOH A . J 5 HOH 247 647 199 HOH HOH A . J 5 HOH 248 648 200 HOH HOH A . J 5 HOH 249 649 201 HOH HOH A . J 5 HOH 250 650 202 HOH HOH A . J 5 HOH 251 651 203 HOH HOH A . J 5 HOH 252 652 204 HOH HOH A . J 5 HOH 253 653 205 HOH HOH A . J 5 HOH 254 654 206 HOH HOH A . J 5 HOH 255 655 210 HOH HOH A . J 5 HOH 256 656 212 HOH HOH A . J 5 HOH 257 657 213 HOH HOH A . J 5 HOH 258 658 214 HOH HOH A . J 5 HOH 259 659 215 HOH HOH A . J 5 HOH 260 660 218 HOH HOH A . J 5 HOH 261 661 219 HOH HOH A . J 5 HOH 262 662 220 HOH HOH A . J 5 HOH 263 663 221 HOH HOH A . J 5 HOH 264 664 226 HOH HOH A . J 5 HOH 265 665 228 HOH HOH A . J 5 HOH 266 666 229 HOH HOH A . J 5 HOH 267 667 232 HOH HOH A . J 5 HOH 268 668 233 HOH HOH A . J 5 HOH 269 669 234 HOH HOH A . J 5 HOH 270 670 238 HOH HOH A . J 5 HOH 271 671 241 HOH HOH A . J 5 HOH 272 672 244 HOH HOH A . J 5 HOH 273 673 246 HOH HOH A . J 5 HOH 274 674 247 HOH HOH A . J 5 HOH 275 675 248 HOH HOH A . J 5 HOH 276 676 249 HOH HOH A . J 5 HOH 277 677 257 HOH HOH A . J 5 HOH 278 678 263 HOH HOH A . #