data_5JCD # _entry.id 5JCD # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5JCD WWPDB D_1000220334 # _pdbx_database_related.db_name PDB _pdbx_database_related.details . _pdbx_database_related.db_id 5JCE _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5JCD _pdbx_database_status.recvd_initial_deposition_date 2016-04-15 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal _audit_author.identifier_ORCID 'Chai, J.J.' 1 ? 'Liu, S.M.' 2 ? 'Wang, J.Z.' 3 ? # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country UK _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev Structure _citation.journal_id_ASTM STRUE6 _citation.journal_id_CSD 2005 _citation.journal_id_ISSN 1878-4186 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 24 _citation.language ? _citation.page_first 1192 _citation.page_last 1200 _citation.title 'Molecular Mechanism for Fungal Cell Wall Recognition by Rice Chitin Receptor OsCEBiP' _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1016/j.str.2016.04.014 _citation.pdbx_database_id_PubMed 27238968 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Liu, S.M.' 1 primary 'Wang, J.Z.' 2 primary 'Han, Z.' 3 primary 'Gong, X.' 4 primary 'Zhang, H.' 5 primary 'Chai, J.J.' 6 # _cell.entry_id 5JCD _cell.length_a 47.772 _cell.length_b 77.274 _cell.length_c 111.391 _cell.angle_alpha 90.00 _cell.angle_beta 99.02 _cell.angle_gamma 90.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? # _symmetry.entry_id 5JCD _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # 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 man 'Chitin elicitor-binding protein' 20679.328 3 ? ? 'UNP residues 29-223' ? 2 non-polymer nat N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 water nat water 18.015 84 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name CEBiP # _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 ;ANFTCAVASGTTCKSAILYTSPNATTYGNLVARFNTTTLPDLLGANGLPDGTLSSAPVAANSTVKIPFRCRCNGDVGQSD RLPIYVVQPQDGLDAIARNVFNAFVTYQEIAAANNIPDPNKINVSQTLWIPLPCSCDKEEGSNVMHLAYSVGKGENTSAI AAKYGVTESTLLTRNKIDDPTKLQMGQILDVPLPV ; _entity_poly.pdbx_seq_one_letter_code_can ;ANFTCAVASGTTCKSAILYTSPNATTYGNLVARFNTTTLPDLLGANGLPDGTLSSAPVAANSTVKIPFRCRCNGDVGQSD RLPIYVVQPQDGLDAIARNVFNAFVTYQEIAAANNIPDPNKINVSQTLWIPLPCSCDKEEGSNVMHLAYSVGKGENTSAI AAKYGVTESTLLTRNKIDDPTKLQMGQILDVPLPV ; _entity_poly.pdbx_strand_id A,B,C _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 ALA n 1 2 ASN n 1 3 PHE n 1 4 THR n 1 5 CYS n 1 6 ALA n 1 7 VAL n 1 8 ALA n 1 9 SER n 1 10 GLY n 1 11 THR n 1 12 THR n 1 13 CYS n 1 14 LYS n 1 15 SER n 1 16 ALA n 1 17 ILE n 1 18 LEU n 1 19 TYR n 1 20 THR n 1 21 SER n 1 22 PRO n 1 23 ASN n 1 24 ALA n 1 25 THR n 1 26 THR n 1 27 TYR n 1 28 GLY n 1 29 ASN n 1 30 LEU n 1 31 VAL n 1 32 ALA n 1 33 ARG n 1 34 PHE n 1 35 ASN n 1 36 THR n 1 37 THR n 1 38 THR n 1 39 LEU n 1 40 PRO n 1 41 ASP n 1 42 LEU n 1 43 LEU n 1 44 GLY n 1 45 ALA n 1 46 ASN n 1 47 GLY n 1 48 LEU n 1 49 PRO n 1 50 ASP n 1 51 GLY n 1 52 THR n 1 53 LEU n 1 54 SER n 1 55 SER n 1 56 ALA n 1 57 PRO n 1 58 VAL n 1 59 ALA n 1 60 ALA n 1 61 ASN n 1 62 SER n 1 63 THR n 1 64 VAL n 1 65 LYS n 1 66 ILE n 1 67 PRO n 1 68 PHE n 1 69 ARG n 1 70 CYS n 1 71 ARG n 1 72 CYS n 1 73 ASN n 1 74 GLY n 1 75 ASP n 1 76 VAL n 1 77 GLY n 1 78 GLN n 1 79 SER n 1 80 ASP n 1 81 ARG n 1 82 LEU n 1 83 PRO n 1 84 ILE n 1 85 TYR n 1 86 VAL n 1 87 VAL n 1 88 GLN n 1 89 PRO n 1 90 GLN n 1 91 ASP n 1 92 GLY n 1 93 LEU n 1 94 ASP n 1 95 ALA n 1 96 ILE n 1 97 ALA n 1 98 ARG n 1 99 ASN n 1 100 VAL n 1 101 PHE n 1 102 ASN n 1 103 ALA n 1 104 PHE n 1 105 VAL n 1 106 THR n 1 107 TYR n 1 108 GLN n 1 109 GLU n 1 110 ILE n 1 111 ALA n 1 112 ALA n 1 113 ALA n 1 114 ASN n 1 115 ASN n 1 116 ILE n 1 117 PRO n 1 118 ASP n 1 119 PRO n 1 120 ASN n 1 121 LYS n 1 122 ILE n 1 123 ASN n 1 124 VAL n 1 125 SER n 1 126 GLN n 1 127 THR n 1 128 LEU n 1 129 TRP n 1 130 ILE n 1 131 PRO n 1 132 LEU n 1 133 PRO n 1 134 CYS n 1 135 SER n 1 136 CYS n 1 137 ASP n 1 138 LYS n 1 139 GLU n 1 140 GLU n 1 141 GLY n 1 142 SER n 1 143 ASN n 1 144 VAL n 1 145 MET n 1 146 HIS n 1 147 LEU n 1 148 ALA n 1 149 TYR n 1 150 SER n 1 151 VAL n 1 152 GLY n 1 153 LYS n 1 154 GLY n 1 155 GLU n 1 156 ASN n 1 157 THR n 1 158 SER n 1 159 ALA n 1 160 ILE n 1 161 ALA n 1 162 ALA n 1 163 LYS n 1 164 TYR n 1 165 GLY n 1 166 VAL n 1 167 THR n 1 168 GLU n 1 169 SER n 1 170 THR n 1 171 LEU n 1 172 LEU n 1 173 THR n 1 174 ARG n 1 175 ASN n 1 176 LYS n 1 177 ILE n 1 178 ASP n 1 179 ASP n 1 180 PRO n 1 181 THR n 1 182 LYS n 1 183 LEU n 1 184 GLN n 1 185 MET n 1 186 GLY n 1 187 GLN n 1 188 ILE n 1 189 LEU n 1 190 ASP n 1 191 VAL n 1 192 PRO n 1 193 LEU n 1 194 PRO n 1 195 VAL n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type 'Biological sequence' _entity_src_gen.pdbx_beg_seq_num 1 _entity_src_gen.pdbx_end_seq_num 195 _entity_src_gen.gene_src_common_name Rice _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'CEBIP, Os03g0133400, LOC_Os03g04110, OJ1006F06.19, OsJ_30068' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Oryza sativa subsp. japonica' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 39947 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Insect cell expression vector pTIE1' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 266783 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code CEBIP_ORYSJ _struct_ref.pdbx_db_accession Q8H8C7 _struct_ref.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;ANFTCAVASGTTCKSAILYTSPNATTYGNLVARFNTTTLPDLLGANGLPDGTLSSAPVAANSTVKIPFRCRCNGDVGQSD RLPIYVVQPQDGLDAIARNVFNAFVTYQEIAAANNIPDPNKINVSQTLWIPLPCSCDKEEGSNVMHLAYSVGKGENTSAI AAKYGVTESTLLTRNKIDDPTKLQMGQILDVPLPV ; _struct_ref.pdbx_align_begin 29 # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 5JCD A 1 ? 195 ? Q8H8C7 29 ? 223 ? 29 223 2 1 5JCD B 1 ? 195 ? Q8H8C7 29 ? 223 ? 29 223 3 1 5JCD C 1 ? 195 ? Q8H8C7 29 ? 223 ? 29 223 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5JCD _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 3.28 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 62.48 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 4.6 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 292 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate, 30%(w/v) PEG4000' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector CCD _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'AGILENT EOS CCD' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2015-09-06 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'SSRF BEAMLINE BL17U' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BL17U _diffrn_source.pdbx_synchrotron_site SSRF # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5JCD _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 2.39 _reflns.d_resolution_low 29.6 _reflns.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.number_all ? _reflns.number_obs 31051 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 98.3 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 4.0 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 22 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 2.40 _reflns_shell.d_res_low 2.48 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all ? _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 5JCD _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 31030 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.60 _refine.ls_d_res_high 2.40 _refine.ls_percent_reflns_obs 98.2 _refine.ls_R_factor_obs 0.223 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.220 _refine.ls_R_factor_R_free 0.276 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.070 _refine.ls_number_reflns_R_free 1572 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method 'FREE R-VALUE' _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct SAD _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.360 _refine.pdbx_overall_phase_error 31.390 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4319 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 54 _refine_hist.number_atoms_solvent 84 _refine_hist.number_atoms_total 4457 _refine_hist.d_res_high 2.40 _refine_hist.d_res_low 29.60 # 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 f_bond_d 0.009 ? ? 4494 'X-RAY DIFFRACTION' ? f_angle_d 1.403 ? ? 6138 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 14.663 ? ? 1637 'X-RAY DIFFRACTION' ? f_chiral_restr 0.077 ? ? 748 'X-RAY DIFFRACTION' ? f_plane_restr 0.007 ? ? 797 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 2.3969 2.4742 2580 0.2645 95.00 0.3387 . . 137 . . . . 'X-RAY DIFFRACTION' . 2.4742 2.5626 2603 0.2487 96.00 0.3391 . . 127 . . . . 'X-RAY DIFFRACTION' . 2.5626 2.6652 2610 0.2476 96.00 0.3076 . . 148 . . . . 'X-RAY DIFFRACTION' . 2.6652 2.7864 2662 0.2550 98.00 0.3250 . . 129 . . . . 'X-RAY DIFFRACTION' . 2.7864 2.9331 2679 0.2405 99.00 0.3217 . . 151 . . . . 'X-RAY DIFFRACTION' . 2.9331 3.1167 2678 0.2395 99.00 0.3298 . . 143 . . . . 'X-RAY DIFFRACTION' . 3.1167 3.3571 2724 0.2324 100.00 0.2881 . . 147 . . . . 'X-RAY DIFFRACTION' . 3.3571 3.6943 2715 0.2149 100.00 0.2585 . . 155 . . . . 'X-RAY DIFFRACTION' . 3.6943 4.2276 2716 0.2012 100.00 0.2346 . . 145 . . . . 'X-RAY DIFFRACTION' . 4.2276 5.3213 2771 0.1864 100.00 0.2496 . . 139 . . . . 'X-RAY DIFFRACTION' . 5.3213 29.6026 2720 0.2256 98.00 0.2710 . . 151 . . . . # _struct.entry_id 5JCD _struct.title 'Crystal structure of OsCEBiP' _struct.pdbx_descriptor 'Chitin elicitor-binding protein' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag N # _struct_keywords.entry_id 5JCD _struct_keywords.text 'chitin receptor, SUGAR BINDING PROTEIN' _struct_keywords.pdbx_keywords 'SUGAR BINDING PROTEIN' # 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 1 ? C N N 1 ? D N N 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 3 ? I N N 3 ? J N N 3 ? # 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 AA1 TYR A 27 ? ASN A 35 ? TYR A 55 ASN A 63 1 ? 9 HELX_P HELX_P2 AA2 THR A 38 ? ASN A 46 ? THR A 66 ASN A 74 1 ? 9 HELX_P HELX_P3 AA3 GLY A 92 ? VAL A 100 ? GLY A 120 VAL A 128 1 ? 9 HELX_P HELX_P4 AA4 THR A 106 ? ASN A 114 ? THR A 134 ASN A 142 1 ? 9 HELX_P HELX_P5 AA5 ASN A 156 ? TYR A 164 ? ASN A 184 TYR A 192 1 ? 9 HELX_P HELX_P6 AA6 THR A 167 ? ASN A 175 ? THR A 195 ASN A 203 1 ? 9 HELX_P HELX_P7 AA7 ASP A 179 ? LEU A 183 ? ASP A 207 LEU A 211 5 ? 5 HELX_P HELX_P8 AA8 TYR B 27 ? ASN B 35 ? TYR B 55 ASN B 63 1 ? 9 HELX_P HELX_P9 AA9 THR B 38 ? ASN B 46 ? THR B 66 ASN B 74 1 ? 9 HELX_P HELX_P10 AB1 GLY B 92 ? VAL B 100 ? GLY B 120 VAL B 128 1 ? 9 HELX_P HELX_P11 AB2 THR B 106 ? ASN B 114 ? THR B 134 ASN B 142 1 ? 9 HELX_P HELX_P12 AB3 ASN B 156 ? TYR B 164 ? ASN B 184 TYR B 192 1 ? 9 HELX_P HELX_P13 AB4 THR B 167 ? ASN B 175 ? THR B 195 ASN B 203 1 ? 9 HELX_P HELX_P14 AB5 ASP B 179 ? LEU B 183 ? ASP B 207 LEU B 211 5 ? 5 HELX_P HELX_P15 AB6 TYR C 27 ? ASN C 35 ? TYR C 55 ASN C 63 1 ? 9 HELX_P HELX_P16 AB7 THR C 38 ? ASN C 46 ? THR C 66 ASN C 74 1 ? 9 HELX_P HELX_P17 AB8 GLY C 92 ? VAL C 100 ? GLY C 120 VAL C 128 1 ? 9 HELX_P HELX_P18 AB9 GLN C 108 ? ALA C 113 ? GLN C 136 ALA C 141 1 ? 6 HELX_P HELX_P19 AC1 THR C 157 ? TYR C 164 ? THR C 185 TYR C 192 1 ? 8 HELX_P HELX_P20 AC2 THR C 167 ? ASN C 175 ? THR C 195 ASN C 203 1 ? 9 HELX_P HELX_P21 AC3 ASP C 179 ? LEU C 183 ? ASP C 207 LEU C 211 5 ? 5 # _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 72 SG ? ? A CYS 33 A CYS 100 1_555 ? ? ? ? ? ? ? 2.064 ? disulf2 disulf ? ? A CYS 13 SG ? ? ? 1_555 A CYS 136 SG ? ? A CYS 41 A CYS 164 1_555 ? ? ? ? ? ? ? 2.020 ? disulf3 disulf ? ? A CYS 70 SG ? ? ? 1_555 A CYS 134 SG ? ? A CYS 98 A CYS 162 1_555 ? ? ? ? ? ? ? 2.067 ? disulf4 disulf ? ? B CYS 5 SG ? ? ? 1_555 B CYS 72 SG ? ? B CYS 33 B CYS 100 1_555 ? ? ? ? ? ? ? 2.059 ? disulf5 disulf ? ? B CYS 13 SG ? ? ? 1_555 B CYS 136 SG ? ? B CYS 41 B CYS 164 1_555 ? ? ? ? ? ? ? 2.042 ? disulf6 disulf ? ? B CYS 70 SG ? ? ? 1_555 B CYS 134 SG ? ? B CYS 98 B CYS 162 1_555 ? ? ? ? ? ? ? 2.039 ? disulf7 disulf ? ? C CYS 5 SG ? ? ? 1_555 C CYS 72 SG ? ? C CYS 33 C CYS 100 1_555 ? ? ? ? ? ? ? 2.060 ? disulf8 disulf ? ? C CYS 13 SG ? ? ? 1_555 C CYS 136 SG ? ? C CYS 41 C CYS 164 1_555 ? ? ? ? ? ? ? 2.049 ? disulf9 disulf ? ? C CYS 70 SG ? ? ? 1_555 C CYS 134 SG ? ? C CYS 98 C CYS 162 1_555 ? ? ? ? ? ? ? 2.041 ? covale1 covale one ? A ASN 61 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 89 A NAG 302 1_555 ? ? ? ? ? ? ? 1.443 ? covale2 covale one ? A ASN 156 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 184 A NAG 301 1_555 ? ? ? ? ? ? ? 1.456 ? covale3 covale one ? B ASN 35 ND2 ? ? ? 1_555 F NAG . C1 ? ? B ASN 63 B NAG 301 1_555 ? ? ? ? ? ? ? 1.451 ? covale4 covale one ? B ASN 156 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 184 B NAG 302 1_555 ? ? ? ? ? ? ? 1.468 ? # 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 LEU 82 A . ? LEU 110 A PRO 83 A ? PRO 111 A 1 -3.41 2 LEU 82 B . ? LEU 110 B PRO 83 B ? PRO 111 B 1 -5.04 3 LEU 82 C . ? LEU 110 C PRO 83 C ? PRO 111 C 1 -2.24 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 6 ? AA2 ? 2 ? AA3 ? 2 ? AA4 ? 6 ? AA5 ? 2 ? AA6 ? 2 ? AA7 ? 6 ? AA8 ? 2 ? AA9 ? 2 ? # 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 AA1 1 2 ? anti-parallel AA1 2 3 ? anti-parallel AA1 3 4 ? anti-parallel AA1 4 5 ? parallel AA1 5 6 ? anti-parallel AA2 1 2 ? anti-parallel AA3 1 2 ? anti-parallel AA4 1 2 ? anti-parallel AA4 2 3 ? anti-parallel AA4 3 4 ? anti-parallel AA4 4 5 ? parallel AA4 5 6 ? anti-parallel AA5 1 2 ? anti-parallel AA6 1 2 ? anti-parallel AA7 1 2 ? anti-parallel AA7 2 3 ? anti-parallel AA7 3 4 ? anti-parallel AA7 4 5 ? parallel AA7 5 6 ? anti-parallel AA8 1 2 ? anti-parallel AA9 1 2 ? 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 AA1 1 PHE A 3 ? THR A 4 ? PHE A 31 THR A 32 AA1 2 VAL A 76 ? SER A 79 ? VAL A 104 SER A 107 AA1 3 THR A 63 ? CYS A 72 ? THR A 91 CYS A 100 AA1 4 THR A 12 ? THR A 20 ? THR A 40 THR A 48 AA1 5 MET A 145 ? SER A 150 ? MET A 173 SER A 178 AA1 6 ILE A 188 ? LEU A 193 ? ILE A 216 LEU A 221 AA2 1 THR A 25 ? THR A 26 ? THR A 53 THR A 54 AA2 2 PRO A 57 ? VAL A 58 ? PRO A 85 VAL A 86 AA3 1 ILE A 84 ? VAL A 86 ? ILE A 112 VAL A 114 AA3 2 THR A 127 ? TRP A 129 ? THR A 155 TRP A 157 AA4 1 PHE B 3 ? THR B 4 ? PHE B 31 THR B 32 AA4 2 VAL B 76 ? SER B 79 ? VAL B 104 SER B 107 AA4 3 THR B 63 ? CYS B 72 ? THR B 91 CYS B 100 AA4 4 THR B 12 ? THR B 20 ? THR B 40 THR B 48 AA4 5 MET B 145 ? SER B 150 ? MET B 173 SER B 178 AA4 6 ILE B 188 ? LEU B 193 ? ILE B 216 LEU B 221 AA5 1 THR B 25 ? THR B 26 ? THR B 53 THR B 54 AA5 2 PRO B 57 ? VAL B 58 ? PRO B 85 VAL B 86 AA6 1 ILE B 84 ? VAL B 86 ? ILE B 112 VAL B 114 AA6 2 THR B 127 ? TRP B 129 ? THR B 155 TRP B 157 AA7 1 PHE C 3 ? THR C 4 ? PHE C 31 THR C 32 AA7 2 VAL C 76 ? SER C 79 ? VAL C 104 SER C 107 AA7 3 THR C 63 ? CYS C 72 ? THR C 91 CYS C 100 AA7 4 THR C 12 ? THR C 20 ? THR C 40 THR C 48 AA7 5 VAL C 144 ? SER C 150 ? VAL C 172 SER C 178 AA7 6 ILE C 188 ? PRO C 194 ? ILE C 216 PRO C 222 AA8 1 THR C 25 ? THR C 26 ? THR C 53 THR C 54 AA8 2 PRO C 57 ? VAL C 58 ? PRO C 85 VAL C 86 AA9 1 ILE C 84 ? VAL C 86 ? ILE C 112 VAL C 114 AA9 2 THR C 127 ? TRP C 129 ? THR C 155 TRP C 157 # 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 AA1 1 2 N PHE A 3 ? N PHE A 31 O GLY A 77 ? O GLY A 105 AA1 2 3 O GLN A 78 ? O GLN A 106 N ARG A 71 ? N ARG A 99 AA1 3 4 O VAL A 64 ? O VAL A 92 N TYR A 19 ? N TYR A 47 AA1 4 5 N LEU A 18 ? N LEU A 46 O ALA A 148 ? O ALA A 176 AA1 5 6 N TYR A 149 ? N TYR A 177 O LEU A 189 ? O LEU A 217 AA2 1 2 N THR A 25 ? N THR A 53 O VAL A 58 ? O VAL A 86 AA3 1 2 N TYR A 85 ? N TYR A 113 O LEU A 128 ? O LEU A 156 AA4 1 2 N PHE B 3 ? N PHE B 31 O GLY B 77 ? O GLY B 105 AA4 2 3 O GLN B 78 ? O GLN B 106 N ARG B 71 ? N ARG B 99 AA4 3 4 O CYS B 70 ? O CYS B 98 N CYS B 13 ? N CYS B 41 AA4 4 5 N LEU B 18 ? N LEU B 46 O ALA B 148 ? O ALA B 176 AA4 5 6 N TYR B 149 ? N TYR B 177 O LEU B 189 ? O LEU B 217 AA5 1 2 N THR B 25 ? N THR B 53 O VAL B 58 ? O VAL B 86 AA6 1 2 N TYR B 85 ? N TYR B 113 O LEU B 128 ? O LEU B 156 AA7 1 2 N PHE C 3 ? N PHE C 31 O GLY C 77 ? O GLY C 105 AA7 2 3 O GLN C 78 ? O GLN C 106 N ARG C 71 ? N ARG C 99 AA7 3 4 O CYS C 70 ? O CYS C 98 N CYS C 13 ? N CYS C 41 AA7 4 5 N ALA C 16 ? N ALA C 44 O ALA C 148 ? O ALA C 176 AA7 5 6 N TYR C 149 ? N TYR C 177 O LEU C 189 ? O LEU C 217 AA8 1 2 N THR C 25 ? N THR C 53 O VAL C 58 ? O VAL C 86 AA9 1 2 N TYR C 85 ? N TYR C 113 O LEU C 128 ? O LEU C 156 # 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 A NAG 302 ? 10 'binding site for Mono-Saccharide NAG A 302 bound to ASN A 89' AC2 Software A NAG 301 ? 1 'binding site for Mono-Saccharide NAG A 301 bound to ASN A 184' AC3 Software B NAG 301 ? 2 'binding site for Mono-Saccharide NAG B 301 bound to ASN B 63' AC4 Software B NAG 302 ? 1 'binding site for Mono-Saccharide NAG B 302 bound to ASN B 184' # 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 10 PRO A 22 ? PRO A 50 . ? 1_555 ? 2 AC1 10 ASN A 23 ? ASN A 51 . ? 1_555 ? 3 AC1 10 ASN A 61 ? ASN A 89 . ? 1_555 ? 4 AC1 10 GLY B 152 ? GLY B 180 . ? 1_555 ? 5 AC1 10 LYS B 153 ? LYS B 181 . ? 1_555 ? 6 AC1 10 GLY B 154 ? GLY B 182 . ? 1_555 ? 7 AC1 10 GLU B 155 ? GLU B 183 . ? 1_555 ? 8 AC1 10 LEU B 183 ? LEU B 211 . ? 1_555 ? 9 AC1 10 GLN B 184 ? GLN B 212 . ? 1_555 ? 10 AC1 10 MET B 185 ? MET B 213 . ? 1_555 ? 11 AC2 1 ASN A 156 ? ASN A 184 . ? 1_555 ? 12 AC3 2 ALA B 32 ? ALA B 60 . ? 1_555 ? 13 AC3 2 ASN B 35 ? ASN B 63 . ? 1_555 ? 14 AC4 1 ASN B 156 ? ASN B 184 . ? 1_555 ? # _atom_sites.entry_id 5JCD _atom_sites.fract_transf_matrix[1][1] 0.020933 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.003323 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.012941 _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] 0.009090 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 1 ? 29.796 34.881 118.985 1.00 53.75 ? 29 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 28.376 34.613 119.251 1.00 65.08 ? 29 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 27.438 35.745 118.788 1.00 61.58 ? 29 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 27.643 36.904 119.146 1.00 42.08 ? 29 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 28.163 34.323 120.742 1.00 73.36 ? 29 ALA A CB 1 ATOM 6 N N . ASN A 1 2 ? 26.451 35.405 117.949 1.00 65.44 ? 30 ASN A N 1 ATOM 7 C CA . ASN A 1 2 ? 25.363 36.316 117.618 1.00 49.53 ? 30 ASN A CA 1 ATOM 8 C C . ASN A 1 2 ? 25.848 37.724 117.159 1.00 40.82 ? 30 ASN A C 1 ATOM 9 O O . ASN A 1 2 ? 26.820 37.817 116.401 1.00 38.24 ? 30 ASN A O 1 ATOM 10 C CB . ASN A 1 2 ? 24.513 36.350 118.900 1.00 66.45 ? 30 ASN A CB 1 ATOM 11 C CG . ASN A 1 2 ? 23.081 36.832 118.706 1.00 66.28 ? 30 ASN A CG 1 ATOM 12 O OD1 . ASN A 1 2 ? 22.840 38.037 118.816 1.00 58.00 ? 30 ASN A OD1 1 ATOM 13 N ND2 . ASN A 1 2 ? 22.111 35.893 118.526 1.00 45.81 ? 30 ASN A ND2 1 ATOM 14 N N . PHE A 1 3 ? 25.209 38.809 117.606 1.00 40.44 ? 31 PHE A N 1 ATOM 15 C CA . PHE A 1 3 ? 25.812 40.148 117.475 1.00 32.02 ? 31 PHE A CA 1 ATOM 16 C C . PHE A 1 3 ? 26.283 40.587 118.832 1.00 38.85 ? 31 PHE A C 1 ATOM 17 O O . PHE A 1 3 ? 25.640 40.351 119.841 1.00 38.79 ? 31 PHE A O 1 ATOM 18 C CB . PHE A 1 3 ? 24.858 41.225 116.939 1.00 32.09 ? 31 PHE A CB 1 ATOM 19 C CG . PHE A 1 3 ? 24.476 41.051 115.501 1.00 35.71 ? 31 PHE A CG 1 ATOM 20 C CD1 . PHE A 1 3 ? 25.117 40.101 114.699 1.00 33.36 ? 31 PHE A CD1 1 ATOM 21 C CD2 . PHE A 1 3 ? 23.471 41.838 114.945 1.00 25.97 ? 31 PHE A CD2 1 ATOM 22 C CE1 . PHE A 1 3 ? 24.752 39.928 113.386 1.00 33.70 ? 31 PHE A CE1 1 ATOM 23 C CE2 . PHE A 1 3 ? 23.096 41.675 113.618 1.00 26.54 ? 31 PHE A CE2 1 ATOM 24 C CZ . PHE A 1 3 ? 23.734 40.716 112.837 1.00 41.05 ? 31 PHE A CZ 1 ATOM 25 N N . THR A 1 4 ? 27.441 41.210 118.842 1.00 35.49 ? 32 THR A N 1 ATOM 26 C CA . THR A 1 4 ? 28.034 41.708 120.057 1.00 36.82 ? 32 THR A CA 1 ATOM 27 C C . THR A 1 4 ? 27.351 43.004 120.584 1.00 47.34 ? 32 THR A C 1 ATOM 28 O O . THR A 1 4 ? 26.869 43.827 119.813 1.00 34.74 ? 32 THR A O 1 ATOM 29 C CB . THR A 1 4 ? 29.554 41.883 119.777 1.00 33.36 ? 32 THR A CB 1 ATOM 30 O OG1 . THR A 1 4 ? 30.251 40.710 120.225 1.00 46.75 ? 32 THR A OG1 1 ATOM 31 C CG2 . THR A 1 4 ? 30.136 43.140 120.383 1.00 38.51 ? 32 THR A CG2 1 ATOM 32 N N . CYS A 1 5 ? 27.320 43.174 121.903 1.00 44.07 ? 33 CYS A N 1 ATOM 33 C CA . CYS A 1 5 ? 26.796 44.385 122.521 1.00 38.49 ? 33 CYS A CA 1 ATOM 34 C C . CYS A 1 5 ? 27.534 44.622 123.829 1.00 41.32 ? 33 CYS A C 1 ATOM 35 O O . CYS A 1 5 ? 27.602 43.725 124.670 1.00 45.44 ? 33 CYS A O 1 ATOM 36 C CB . CYS A 1 5 ? 25.296 44.264 122.799 1.00 34.83 ? 33 CYS A CB 1 ATOM 37 S SG . CYS A 1 5 ? 24.548 45.769 123.451 1.00 50.22 ? 33 CYS A SG 1 ATOM 38 N N . ALA A 1 6 ? 28.054 45.835 124.010 1.00 38.67 ? 34 ALA A N 1 ATOM 39 C CA . ALA A 1 6 ? 28.960 46.129 125.117 1.00 41.28 ? 34 ALA A CA 1 ATOM 40 C C . ALA A 1 6 ? 28.417 47.111 126.171 1.00 46.45 ? 34 ALA A C 1 ATOM 41 O O . ALA A 1 6 ? 29.139 47.474 127.100 1.00 40.79 ? 34 ALA A O 1 ATOM 42 C CB . ALA A 1 6 ? 30.267 46.663 124.561 1.00 31.87 ? 34 ALA A CB 1 ATOM 43 N N . VAL A 1 7 ? 27.158 47.519 126.033 1.00 34.11 ? 35 VAL A N 1 ATOM 44 C CA . VAL A 1 7 ? 26.540 48.451 126.963 1.00 39.07 ? 35 VAL A CA 1 ATOM 45 C C . VAL A 1 7 ? 26.011 47.734 128.188 1.00 46.30 ? 35 VAL A C 1 ATOM 46 O O . VAL A 1 7 ? 26.084 46.507 128.269 1.00 41.93 ? 35 VAL A O 1 ATOM 47 C CB . VAL A 1 7 ? 25.408 49.214 126.289 1.00 52.00 ? 35 VAL A CB 1 ATOM 48 C CG1 . VAL A 1 7 ? 25.937 49.948 125.029 1.00 26.74 ? 35 VAL A CG1 1 ATOM 49 C CG2 . VAL A 1 7 ? 24.302 48.260 125.925 1.00 48.05 ? 35 VAL A CG2 1 ATOM 50 N N . ALA A 1 8 ? 25.457 48.489 129.134 1.00 44.63 ? 36 ALA A N 1 ATOM 51 C CA . ALA A 1 8 ? 25.007 47.895 130.387 1.00 40.82 ? 36 ALA A CA 1 ATOM 52 C C . ALA A 1 8 ? 23.956 46.825 130.158 1.00 44.44 ? 36 ALA A C 1 ATOM 53 O O . ALA A 1 8 ? 22.987 47.018 129.408 1.00 42.78 ? 36 ALA A O 1 ATOM 54 C CB . ALA A 1 8 ? 24.459 48.953 131.327 1.00 33.35 ? 36 ALA A CB 1 ATOM 55 N N . SER A 1 9 ? 24.160 45.701 130.829 1.00 34.17 ? 37 SER A N 1 ATOM 56 C CA . SER A 1 9 ? 23.233 44.590 130.776 1.00 39.17 ? 37 SER A CA 1 ATOM 57 C C . SER A 1 9 ? 21.839 45.056 131.150 1.00 37.34 ? 37 SER A C 1 ATOM 58 O O . SER A 1 9 ? 21.670 45.827 132.088 1.00 32.98 ? 37 SER A O 1 ATOM 59 C CB . SER A 1 9 ? 23.689 43.492 131.718 1.00 38.52 ? 37 SER A CB 1 ATOM 60 O OG . SER A 1 9 ? 22.740 42.448 131.727 1.00 56.38 ? 37 SER A OG 1 ATOM 61 N N . GLY A 1 10 ? 20.845 44.590 130.403 1.00 39.43 ? 38 GLY A N 1 ATOM 62 C CA . GLY A 1 10 ? 19.470 45.008 130.614 1.00 37.57 ? 38 GLY A CA 1 ATOM 63 C C . GLY A 1 10 ? 19.080 46.154 129.704 1.00 41.27 ? 38 GLY A C 1 ATOM 64 O O . GLY A 1 10 ? 17.916 46.529 129.648 1.00 49.58 ? 38 GLY A O 1 ATOM 65 N N . THR A 1 11 ? 20.047 46.708 128.972 1.00 42.75 ? 39 THR A N 1 ATOM 66 C CA . THR A 1 11 ? 19.751 47.784 128.024 1.00 41.83 ? 39 THR A CA 1 ATOM 67 C C . THR A 1 11 ? 18.779 47.283 126.966 1.00 44.30 ? 39 THR A C 1 ATOM 68 O O . THR A 1 11 ? 18.934 46.202 126.407 1.00 40.30 ? 39 THR A O 1 ATOM 69 C CB . THR A 1 11 ? 21.022 48.303 127.313 1.00 37.51 ? 39 THR A CB 1 ATOM 70 O OG1 . THR A 1 11 ? 21.896 48.903 128.274 1.00 37.01 ? 39 THR A OG1 1 ATOM 71 C CG2 . THR A 1 11 ? 20.673 49.334 126.217 1.00 28.87 ? 39 THR A CG2 1 ATOM 72 N N . THR A 1 12 ? 17.782 48.100 126.690 1.00 42.31 ? 40 THR A N 1 ATOM 73 C CA . THR A 1 12 ? 16.815 47.787 125.683 1.00 42.31 ? 40 THR A CA 1 ATOM 74 C C . THR A 1 12 ? 16.829 48.870 124.605 1.00 41.24 ? 40 THR A C 1 ATOM 75 O O . THR A 1 12 ? 16.880 50.059 124.936 1.00 41.38 ? 40 THR A O 1 ATOM 76 C CB . THR A 1 12 ? 15.422 47.618 126.376 1.00 48.06 ? 40 THR A CB 1 ATOM 77 O OG1 . THR A 1 12 ? 15.099 46.220 126.455 1.00 48.78 ? 40 THR A OG1 1 ATOM 78 C CG2 . THR A 1 12 ? 14.324 48.395 125.674 1.00 46.42 ? 40 THR A CG2 1 ATOM 79 N N . CYS A 1 13 ? 16.770 48.447 123.335 1.00 29.83 ? 41 CYS A N 1 ATOM 80 C CA . CYS A 1 13 ? 16.664 49.351 122.178 1.00 32.48 ? 41 CYS A CA 1 ATOM 81 C C . CYS A 1 13 ? 15.866 48.684 121.045 1.00 37.35 ? 41 CYS A C 1 ATOM 82 O O . CYS A 1 13 ? 15.444 47.538 121.163 1.00 38.82 ? 41 CYS A O 1 ATOM 83 C CB . CYS A 1 13 ? 18.055 49.791 121.660 1.00 28.79 ? 41 CYS A CB 1 ATOM 84 S SG . CYS A 1 13 ? 19.161 48.442 121.009 1.00 32.77 ? 41 CYS A SG 1 ATOM 85 N N . LYS A 1 14 ? 15.636 49.426 119.968 1.00 33.35 ? 42 LYS A N 1 ATOM 86 C CA . LYS A 1 14 ? 14.980 48.898 118.781 1.00 34.98 ? 42 LYS A CA 1 ATOM 87 C C . LYS A 1 14 ? 15.986 48.381 117.711 1.00 35.38 ? 42 LYS A C 1 ATOM 88 O O . LYS A 1 14 ? 16.902 49.097 117.322 1.00 27.04 ? 42 LYS A O 1 ATOM 89 C CB . LYS A 1 14 ? 14.049 49.975 118.193 1.00 32.87 ? 42 LYS A CB 1 ATOM 90 C CG . LYS A 1 14 ? 12.973 49.403 117.274 1.00 54.32 ? 42 LYS A CG 1 ATOM 91 C CD . LYS A 1 14 ? 11.896 50.434 116.916 1.00 67.32 ? 42 LYS A CD 1 ATOM 92 C CE . LYS A 1 14 ? 12.169 51.176 115.610 1.00 68.15 ? 42 LYS A CE 1 ATOM 93 N NZ . LYS A 1 14 ? 12.898 52.474 115.774 1.00 66.25 ? 42 LYS A NZ 1 ATOM 94 N N . SER A 1 15 ? 15.799 47.147 117.235 1.00 34.35 ? 43 SER A N 1 ATOM 95 C CA . SER A 1 15 ? 16.632 46.566 116.172 1.00 23.43 ? 43 SER A CA 1 ATOM 96 C C . SER A 1 15 ? 15.738 45.964 115.106 1.00 32.28 ? 43 SER A C 1 ATOM 97 O O . SER A 1 15 ? 14.508 46.053 115.194 1.00 33.54 ? 43 SER A O 1 ATOM 98 C CB . SER A 1 15 ? 17.516 45.448 116.716 1.00 34.05 ? 43 SER A CB 1 ATOM 99 O OG . SER A 1 15 ? 18.489 45.910 117.620 1.00 37.49 ? 43 SER A OG 1 ATOM 100 N N . ALA A 1 16 ? 16.354 45.336 114.107 1.00 32.23 ? 44 ALA A N 1 ATOM 101 C CA . ALA A 1 16 ? 15.602 44.652 113.053 1.00 34.38 ? 44 ALA A CA 1 ATOM 102 C C . ALA A 1 16 ? 16.378 43.512 112.393 1.00 30.28 ? 44 ALA A C 1 ATOM 103 O O . ALA A 1 16 ? 17.605 43.490 112.438 1.00 34.36 ? 44 ALA A O 1 ATOM 104 C CB . ALA A 1 16 ? 15.154 45.667 111.964 1.00 19.47 ? 44 ALA A CB 1 ATOM 105 N N . ILE A 1 17 ? 15.655 42.585 111.768 1.00 27.54 ? 45 ILE A N 1 ATOM 106 C CA . ILE A 1 17 ? 16.251 41.700 110.768 1.00 25.99 ? 45 ILE A CA 1 ATOM 107 C C . ILE A 1 17 ? 15.629 42.023 109.425 1.00 24.74 ? 45 ILE A C 1 ATOM 108 O O . ILE A 1 17 ? 14.455 42.370 109.348 1.00 35.88 ? 45 ILE A O 1 ATOM 109 C CB . ILE A 1 17 ? 16.022 40.176 111.063 1.00 27.97 ? 45 ILE A CB 1 ATOM 110 C CG1 . ILE A 1 17 ? 14.512 39.859 111.138 1.00 31.76 ? 45 ILE A CG1 1 ATOM 111 C CG2 . ILE A 1 17 ? 16.762 39.741 112.330 1.00 27.22 ? 45 ILE A CG2 1 ATOM 112 C CD1 . ILE A 1 17 ? 14.139 38.338 111.345 1.00 21.55 ? 45 ILE A CD1 1 ATOM 113 N N . LEU A 1 18 ? 16.403 41.895 108.356 1.00 24.35 ? 46 LEU A N 1 ATOM 114 C CA . LEU A 1 18 ? 15.800 41.950 107.032 1.00 31.13 ? 46 LEU A CA 1 ATOM 115 C C . LEU A 1 18 ? 15.391 40.508 106.715 1.00 35.21 ? 46 LEU A C 1 ATOM 116 O O . LEU A 1 18 ? 16.232 39.649 106.427 1.00 34.59 ? 46 LEU A O 1 ATOM 117 C CB . LEU A 1 18 ? 16.774 42.510 105.994 1.00 25.21 ? 46 LEU A CB 1 ATOM 118 C CG . LEU A 1 18 ? 16.189 42.645 104.592 1.00 36.89 ? 46 LEU A CG 1 ATOM 119 C CD1 . LEU A 1 18 ? 15.050 43.691 104.570 1.00 28.62 ? 46 LEU A CD1 1 ATOM 120 C CD2 . LEU A 1 18 ? 17.249 42.954 103.534 1.00 31.50 ? 46 LEU A CD2 1 ATOM 121 N N . TYR A 1 19 ? 14.100 40.225 106.819 1.00 36.84 ? 47 TYR A N 1 ATOM 122 C CA . TYR A 1 19 ? 13.626 38.841 106.730 1.00 28.81 ? 47 TYR A CA 1 ATOM 123 C C . TYR A 1 19 ? 13.317 38.437 105.306 1.00 30.78 ? 47 TYR A C 1 ATOM 124 O O . TYR A 1 19 ? 12.610 39.149 104.597 1.00 33.59 ? 47 TYR A O 1 ATOM 125 C CB . TYR A 1 19 ? 12.378 38.654 107.606 1.00 24.53 ? 47 TYR A CB 1 ATOM 126 C CG . TYR A 1 19 ? 11.845 37.241 107.664 1.00 35.81 ? 47 TYR A CG 1 ATOM 127 C CD1 . TYR A 1 19 ? 12.615 36.214 108.204 1.00 35.42 ? 47 TYR A CD1 1 ATOM 128 C CD2 . TYR A 1 19 ? 10.553 36.939 107.237 1.00 29.91 ? 47 TYR A CD2 1 ATOM 129 C CE1 . TYR A 1 19 ? 12.137 34.925 108.298 1.00 34.60 ? 47 TYR A CE1 1 ATOM 130 C CE2 . TYR A 1 19 ? 10.064 35.642 107.325 1.00 27.04 ? 47 TYR A CE2 1 ATOM 131 C CZ . TYR A 1 19 ? 10.869 34.643 107.857 1.00 36.39 ? 47 TYR A CZ 1 ATOM 132 O OH . TYR A 1 19 ? 10.428 33.354 107.953 1.00 42.88 ? 47 TYR A OH 1 ATOM 133 N N . THR A 1 20 ? 13.849 37.283 104.894 1.00 32.61 ? 48 THR A N 1 ATOM 134 C CA . THR A 1 20 ? 13.522 36.714 103.592 1.00 26.14 ? 48 THR A CA 1 ATOM 135 C C . THR A 1 20 ? 12.433 35.702 103.820 1.00 31.76 ? 48 THR A C 1 ATOM 136 O O . THR A 1 20 ? 12.647 34.696 104.504 1.00 35.01 ? 48 THR A O 1 ATOM 137 C CB . THR A 1 20 ? 14.723 36.020 102.922 1.00 33.78 ? 48 THR A CB 1 ATOM 138 O OG1 . THR A 1 20 ? 15.773 36.973 102.700 1.00 30.97 ? 48 THR A OG1 1 ATOM 139 C CG2 . THR A 1 20 ? 14.297 35.403 101.582 1.00 25.49 ? 48 THR A CG2 1 ATOM 140 N N . SER A 1 21 ? 11.252 35.982 103.285 1.00 20.37 ? 49 SER A N 1 ATOM 141 C CA . SER A 1 21 ? 10.092 35.116 103.537 1.00 23.96 ? 49 SER A CA 1 ATOM 142 C C . SER A 1 21 ? 10.182 33.803 102.738 1.00 33.16 ? 49 SER A C 1 ATOM 143 O O . SER A 1 21 ? 10.170 33.829 101.510 1.00 32.71 ? 49 SER A O 1 ATOM 144 C CB . SER A 1 21 ? 8.806 35.863 103.187 1.00 28.14 ? 49 SER A CB 1 ATOM 145 O OG . SER A 1 21 ? 7.664 35.082 103.469 1.00 31.14 ? 49 SER A OG 1 ATOM 146 N N . PRO A 1 22 ? 10.256 32.653 103.434 1.00 32.35 ? 50 PRO A N 1 ATOM 147 C CA . PRO A 1 22 ? 10.384 31.380 102.723 1.00 29.68 ? 50 PRO A CA 1 ATOM 148 C C . PRO A 1 22 ? 9.189 31.144 101.799 1.00 40.50 ? 50 PRO A C 1 ATOM 149 O O . PRO A 1 22 ? 9.359 30.591 100.711 1.00 51.09 ? 50 PRO A O 1 ATOM 150 C CB . PRO A 1 22 ? 10.417 30.344 103.849 1.00 30.37 ? 50 PRO A CB 1 ATOM 151 C CG . PRO A 1 22 ? 10.865 31.115 105.086 1.00 27.59 ? 50 PRO A CG 1 ATOM 152 C CD . PRO A 1 22 ? 10.228 32.473 104.899 1.00 30.92 ? 50 PRO A CD 1 ATOM 153 N N . ASN A 1 23 ? 8.011 31.613 102.193 1.00 35.90 ? 51 ASN A N 1 ATOM 154 C CA . ASN A 1 23 ? 6.817 31.413 101.376 1.00 41.27 ? 51 ASN A CA 1 ATOM 155 C C . ASN A 1 23 ? 6.056 32.694 101.162 1.00 42.04 ? 51 ASN A C 1 ATOM 156 O O . ASN A 1 23 ? 6.397 33.723 101.738 1.00 48.06 ? 51 ASN A O 1 ATOM 157 C CB . ASN A 1 23 ? 5.880 30.405 102.028 1.00 43.71 ? 51 ASN A CB 1 ATOM 158 C CG . ASN A 1 23 ? 6.518 29.057 102.186 1.00 60.17 ? 51 ASN A CG 1 ATOM 159 O OD1 . ASN A 1 23 ? 7.391 28.688 101.398 1.00 60.81 ? 51 ASN A OD1 1 ATOM 160 N ND2 . ASN A 1 23 ? 6.093 28.304 103.205 1.00 69.89 ? 51 ASN A ND2 1 ATOM 161 N N . ALA A 1 24 ? 5.022 32.614 100.327 1.00 39.70 ? 52 ALA A N 1 ATOM 162 C CA . ALA A 1 24 ? 4.076 33.702 100.155 1.00 33.77 ? 52 ALA A CA 1 ATOM 163 C C . ALA A 1 24 ? 3.320 33.790 101.451 1.00 41.12 ? 52 ALA A C 1 ATOM 164 O O . ALA A 1 24 ? 2.916 32.771 102.017 1.00 45.73 ? 52 ALA A O 1 ATOM 165 C CB . ALA A 1 24 ? 3.108 33.412 98.984 1.00 25.36 ? 52 ALA A CB 1 ATOM 166 N N . THR A 1 25 ? 3.164 35.001 101.952 1.00 33.10 ? 53 THR A N 1 ATOM 167 C CA . THR A 1 25 ? 2.471 35.184 103.217 1.00 34.61 ? 53 THR A CA 1 ATOM 168 C C . THR A 1 25 ? 1.922 36.605 103.229 1.00 37.29 ? 53 THR A C 1 ATOM 169 O O . THR A 1 25 ? 1.834 37.263 102.185 1.00 40.26 ? 53 THR A O 1 ATOM 170 C CB . THR A 1 25 ? 3.407 34.924 104.437 1.00 42.21 ? 53 THR A CB 1 ATOM 171 O OG1 . THR A 1 25 ? 2.700 35.157 105.659 1.00 47.25 ? 53 THR A OG1 1 ATOM 172 C CG2 . THR A 1 25 ? 4.606 35.823 104.407 1.00 49.01 ? 53 THR A CG2 1 ATOM 173 N N . THR A 1 26 ? 1.568 37.095 104.403 1.00 31.39 ? 54 THR A N 1 ATOM 174 C CA . THR A 1 26 ? 1.064 38.455 104.501 1.00 28.23 ? 54 THR A CA 1 ATOM 175 C C . THR A 1 26 ? 1.700 39.147 105.694 1.00 29.16 ? 54 THR A C 1 ATOM 176 O O . THR A 1 26 ? 2.226 38.482 106.591 1.00 38.85 ? 54 THR A O 1 ATOM 177 C CB . THR A 1 26 ? -0.461 38.432 104.722 1.00 38.60 ? 54 THR A CB 1 ATOM 178 O OG1 . THR A 1 26 ? -0.734 37.844 106.003 1.00 41.80 ? 54 THR A OG1 1 ATOM 179 C CG2 . THR A 1 26 ? -1.163 37.605 103.635 1.00 28.47 ? 54 THR A CG2 1 ATOM 180 N N . TYR A 1 27 ? 1.594 40.473 105.743 1.00 42.15 ? 55 TYR A N 1 ATOM 181 C CA . TYR A 1 27 ? 2.094 41.221 106.897 1.00 40.95 ? 55 TYR A CA 1 ATOM 182 C C . TYR A 1 27 ? 1.450 40.741 108.191 1.00 42.78 ? 55 TYR A C 1 ATOM 183 O O . TYR A 1 27 ? 2.144 40.595 109.196 1.00 45.66 ? 55 TYR A O 1 ATOM 184 C CB . TYR A 1 27 ? 1.963 42.747 106.690 1.00 43.36 ? 55 TYR A CB 1 ATOM 185 C CG . TYR A 1 27 ? 3.099 43.334 105.836 1.00 43.97 ? 55 TYR A CG 1 ATOM 186 C CD1 . TYR A 1 27 ? 3.077 43.275 104.452 1.00 35.61 ? 55 TYR A CD1 1 ATOM 187 C CD2 . TYR A 1 27 ? 4.206 43.924 106.439 1.00 43.30 ? 55 TYR A CD2 1 ATOM 188 C CE1 . TYR A 1 27 ? 4.131 43.795 103.687 1.00 28.73 ? 55 TYR A CE1 1 ATOM 189 C CE2 . TYR A 1 27 ? 5.250 44.436 105.695 1.00 35.58 ? 55 TYR A CE2 1 ATOM 190 C CZ . TYR A 1 27 ? 5.211 44.359 104.318 1.00 37.43 ? 55 TYR A CZ 1 ATOM 191 O OH . TYR A 1 27 ? 6.249 44.884 103.578 1.00 42.35 ? 55 TYR A OH 1 ATOM 192 N N . GLY A 1 28 ? 0.150 40.443 108.155 1.00 45.73 ? 56 GLY A N 1 ATOM 193 C CA . GLY A 1 28 ? -0.570 39.946 109.325 1.00 33.32 ? 56 GLY A CA 1 ATOM 194 C C . GLY A 1 28 ? 0.021 38.672 109.896 1.00 40.26 ? 56 GLY A C 1 ATOM 195 O O . GLY A 1 28 ? 0.152 38.529 111.113 1.00 46.80 ? 56 GLY A O 1 ATOM 196 N N . ASN A 1 29 ? 0.374 37.731 109.020 1.00 42.81 ? 57 ASN A N 1 ATOM 197 C CA . ASN A 1 29 ? 1.014 36.493 109.462 1.00 39.78 ? 57 ASN A CA 1 ATOM 198 C C . ASN A 1 29 ? 2.399 36.682 110.073 1.00 41.74 ? 57 ASN A C 1 ATOM 199 O O . ASN A 1 29 ? 2.782 35.991 111.026 1.00 45.61 ? 57 ASN A O 1 ATOM 200 C CB . ASN A 1 29 ? 1.123 35.506 108.316 1.00 47.62 ? 57 ASN A CB 1 ATOM 201 C CG . ASN A 1 29 ? -0.154 34.789 108.064 1.00 55.81 ? 57 ASN A CG 1 ATOM 202 O OD1 . ASN A 1 29 ? -0.643 34.742 106.940 1.00 60.46 ? 57 ASN A OD1 1 ATOM 203 N ND2 . ASN A 1 29 ? -0.720 34.222 109.115 1.00 64.44 ? 57 ASN A ND2 1 ATOM 204 N N . LEU A 1 30 ? 3.158 37.598 109.489 1.00 35.59 ? 58 LEU A N 1 ATOM 205 C CA . LEU A 1 30 ? 4.487 37.916 109.980 1.00 40.60 ? 58 LEU A CA 1 ATOM 206 C C . LEU A 1 30 ? 4.355 38.504 111.378 1.00 38.20 ? 58 LEU A C 1 ATOM 207 O O . LEU A 1 30 ? 5.072 38.111 112.297 1.00 46.71 ? 58 LEU A O 1 ATOM 208 C CB . LEU A 1 30 ? 5.183 38.891 109.012 1.00 41.29 ? 58 LEU A CB 1 ATOM 209 C CG . LEU A 1 30 ? 5.651 38.250 107.704 1.00 34.73 ? 58 LEU A CG 1 ATOM 210 C CD1 . LEU A 1 30 ? 6.218 39.264 106.706 1.00 27.60 ? 58 LEU A CD1 1 ATOM 211 C CD2 . LEU A 1 30 ? 6.702 37.231 108.051 1.00 40.30 ? 58 LEU A CD2 1 ATOM 212 N N . VAL A 1 31 ? 3.406 39.421 111.537 1.00 36.75 ? 59 VAL A N 1 ATOM 213 C CA . VAL A 1 31 ? 3.114 40.006 112.844 1.00 42.40 ? 59 VAL A CA 1 ATOM 214 C C . VAL A 1 31 ? 2.842 38.906 113.852 1.00 52.41 ? 59 VAL A C 1 ATOM 215 O O . VAL A 1 31 ? 3.292 38.979 114.994 1.00 52.48 ? 59 VAL A O 1 ATOM 216 C CB . VAL A 1 31 ? 1.910 40.957 112.798 1.00 32.71 ? 59 VAL A CB 1 ATOM 217 C CG1 . VAL A 1 31 ? 1.509 41.382 114.210 1.00 34.02 ? 59 VAL A CG1 1 ATOM 218 C CG2 . VAL A 1 31 ? 2.219 42.159 111.930 1.00 32.87 ? 59 VAL A CG2 1 ATOM 219 N N . ALA A 1 32 ? 2.099 37.894 113.409 1.00 53.17 ? 60 ALA A N 1 ATOM 220 C CA . ALA A 1 32 ? 1.773 36.743 114.242 1.00 57.49 ? 60 ALA A CA 1 ATOM 221 C C . ALA A 1 32 ? 2.956 35.804 114.527 1.00 58.12 ? 60 ALA A C 1 ATOM 222 O O . ALA A 1 32 ? 3.204 35.456 115.681 1.00 67.70 ? 60 ALA A O 1 ATOM 223 C CB . ALA A 1 32 ? 0.614 35.959 113.624 1.00 59.03 ? 60 ALA A CB 1 ATOM 224 N N . ARG A 1 33 ? 3.690 35.401 113.494 1.00 46.22 ? 61 ARG A N 1 ATOM 225 C CA . ARG A 1 33 ? 4.814 34.484 113.691 1.00 55.44 ? 61 ARG A CA 1 ATOM 226 C C . ARG A 1 33 ? 5.871 35.136 114.581 1.00 53.86 ? 61 ARG A C 1 ATOM 227 O O . ARG A 1 33 ? 6.487 34.495 115.429 1.00 59.07 ? 61 ARG A O 1 ATOM 228 C CB . ARG A 1 33 ? 5.460 34.105 112.347 1.00 64.38 ? 61 ARG A CB 1 ATOM 229 C CG . ARG A 1 33 ? 6.810 33.335 112.447 1.00 87.98 ? 61 ARG A CG 1 ATOM 230 C CD . ARG A 1 33 ? 7.413 33.066 111.051 1.00 80.44 ? 61 ARG A CD 1 ATOM 231 N NE . ARG A 1 33 ? 6.350 32.826 110.082 1.00 78.71 ? 61 ARG A NE 1 ATOM 232 C CZ . ARG A 1 33 ? 6.493 32.880 108.764 1.00 82.15 ? 61 ARG A CZ 1 ATOM 233 N NH1 . ARG A 1 33 ? 7.669 33.171 108.218 1.00 75.63 ? 61 ARG A NH1 1 ATOM 234 N NH2 . ARG A 1 33 ? 5.441 32.657 107.988 1.00 89.73 ? 61 ARG A NH2 1 ATOM 235 N N . PHE A 1 34 ? 6.062 36.429 114.391 1.00 44.23 ? 62 PHE A N 1 ATOM 236 C CA . PHE A 1 34 ? 7.116 37.117 115.102 1.00 42.24 ? 62 PHE A CA 1 ATOM 237 C C . PHE A 1 34 ? 6.646 37.680 116.433 1.00 45.83 ? 62 PHE A C 1 ATOM 238 O O . PHE A 1 34 ? 7.268 37.411 117.465 1.00 44.48 ? 62 PHE A O 1 ATOM 239 C CB . PHE A 1 34 ? 7.796 38.153 114.188 1.00 30.08 ? 62 PHE A CB 1 ATOM 240 C CG . PHE A 1 34 ? 8.785 37.533 113.246 1.00 33.34 ? 62 PHE A CG 1 ATOM 241 C CD1 . PHE A 1 34 ? 10.113 37.362 113.625 1.00 33.60 ? 62 PHE A CD1 1 ATOM 242 C CD2 . PHE A 1 34 ? 8.380 37.058 112.007 1.00 27.60 ? 62 PHE A CD2 1 ATOM 243 C CE1 . PHE A 1 34 ? 11.034 36.758 112.767 1.00 30.52 ? 62 PHE A CE1 1 ATOM 244 C CE2 . PHE A 1 34 ? 9.293 36.434 111.148 1.00 34.20 ? 62 PHE A CE2 1 ATOM 245 C CZ . PHE A 1 34 ? 10.621 36.282 111.534 1.00 30.23 ? 62 PHE A CZ 1 ATOM 246 N N . ASN A 1 35 ? 5.518 38.391 116.407 1.00 42.15 ? 63 ASN A N 1 ATOM 247 C CA . ASN A 1 35 ? 4.920 38.976 117.608 1.00 51.55 ? 63 ASN A CA 1 ATOM 248 C C . ASN A 1 35 ? 5.911 39.876 118.355 1.00 47.27 ? 63 ASN A C 1 ATOM 249 O O . ASN A 1 35 ? 5.941 39.908 119.581 1.00 57.65 ? 63 ASN A O 1 ATOM 250 C CB . ASN A 1 35 ? 4.355 37.887 118.529 1.00 55.68 ? 63 ASN A CB 1 ATOM 251 C CG . ASN A 1 35 ? 3.281 38.419 119.464 1.00 61.52 ? 63 ASN A CG 1 ATOM 252 O OD1 . ASN A 1 35 ? 2.583 39.383 119.130 1.00 57.95 ? 63 ASN A OD1 1 ATOM 253 N ND2 . ASN A 1 35 ? 3.124 37.781 120.626 1.00 64.44 ? 63 ASN A ND2 1 ATOM 254 N N . THR A 1 36 ? 6.724 40.599 117.600 1.00 42.72 ? 64 THR A N 1 ATOM 255 C CA . THR A 1 36 ? 7.772 41.428 118.181 1.00 46.05 ? 64 THR A CA 1 ATOM 256 C C . THR A 1 36 ? 7.473 42.903 118.017 1.00 41.48 ? 64 THR A C 1 ATOM 257 O O . THR A 1 36 ? 8.149 43.763 118.576 1.00 47.88 ? 64 THR A O 1 ATOM 258 C CB . THR A 1 36 ? 9.104 41.166 117.481 1.00 40.84 ? 64 THR A CB 1 ATOM 259 O OG1 . THR A 1 36 ? 8.967 41.424 116.074 1.00 38.48 ? 64 THR A OG1 1 ATOM 260 C CG2 . THR A 1 36 ? 9.535 39.737 117.704 1.00 28.23 ? 64 THR A CG2 1 ATOM 261 N N . THR A 1 37 ? 6.431 43.178 117.256 1.00 34.83 ? 65 THR A N 1 ATOM 262 C CA . THR A 1 37 ? 6.083 44.526 116.868 1.00 42.60 ? 65 THR A CA 1 ATOM 263 C C . THR A 1 37 ? 4.605 44.489 116.508 1.00 40.69 ? 65 THR A C 1 ATOM 264 O O . THR A 1 37 ? 4.044 43.419 116.317 1.00 42.79 ? 65 THR A O 1 ATOM 265 C CB . THR A 1 37 ? 6.935 45.004 115.654 1.00 46.42 ? 65 THR A CB 1 ATOM 266 O OG1 . THR A 1 37 ? 6.535 46.318 115.266 1.00 59.81 ? 65 THR A OG1 1 ATOM 267 C CG2 . THR A 1 37 ? 6.758 44.091 114.455 1.00 40.81 ? 65 THR A CG2 1 ATOM 268 N N . THR A 1 38 ? 3.976 45.648 116.427 1.00 39.63 ? 66 THR A N 1 ATOM 269 C CA . THR A 1 38 ? 2.591 45.721 116.008 1.00 45.61 ? 66 THR A CA 1 ATOM 270 C C . THR A 1 38 ? 2.539 45.818 114.495 1.00 49.91 ? 66 THR A C 1 ATOM 271 O O . THR A 1 38 ? 3.541 46.136 113.845 1.00 49.94 ? 66 THR A O 1 ATOM 272 C CB . THR A 1 38 ? 1.864 46.971 116.599 1.00 53.24 ? 66 THR A CB 1 ATOM 273 O OG1 . THR A 1 38 ? 2.376 48.167 115.992 1.00 41.32 ? 66 THR A OG1 1 ATOM 274 C CG2 . THR A 1 38 ? 2.023 47.048 118.124 1.00 40.84 ? 66 THR A CG2 1 ATOM 275 N N . LEU A 1 39 ? 1.359 45.560 113.939 1.00 54.99 ? 67 LEU A N 1 ATOM 276 C CA . LEU A 1 39 ? 1.140 45.723 112.509 1.00 54.74 ? 67 LEU A CA 1 ATOM 277 C C . LEU A 1 39 ? 1.520 47.097 111.955 1.00 54.58 ? 67 LEU A C 1 ATOM 278 O O . LEU A 1 39 ? 2.251 47.160 110.975 1.00 62.59 ? 67 LEU A O 1 ATOM 279 C CB . LEU A 1 39 ? -0.298 45.373 112.124 1.00 61.16 ? 67 LEU A CB 1 ATOM 280 C CG . LEU A 1 39 ? -0.683 45.717 110.682 1.00 67.63 ? 67 LEU A CG 1 ATOM 281 C CD1 . LEU A 1 39 ? 0.104 44.890 109.673 1.00 67.08 ? 67 LEU A CD1 1 ATOM 282 C CD2 . LEU A 1 39 ? -2.182 45.541 110.471 1.00 69.30 ? 67 LEU A CD2 1 ATOM 283 N N . PRO A 1 40 ? 1.042 48.203 112.570 1.00 56.76 ? 68 PRO A N 1 ATOM 284 C CA . PRO A 1 40 ? 1.418 49.484 111.948 1.00 53.59 ? 68 PRO A CA 1 ATOM 285 C C . PRO A 1 40 ? 2.926 49.768 111.966 1.00 52.57 ? 68 PRO A C 1 ATOM 286 O O . PRO A 1 40 ? 3.446 50.405 111.053 1.00 48.51 ? 68 PRO A O 1 ATOM 287 C CB . PRO A 1 40 ? 0.670 50.540 112.779 1.00 54.58 ? 68 PRO A CB 1 ATOM 288 C CG . PRO A 1 40 ? -0.061 49.830 113.812 1.00 55.12 ? 68 PRO A CG 1 ATOM 289 C CD . PRO A 1 40 ? 0.057 48.366 113.655 1.00 47.98 ? 68 PRO A CD 1 ATOM 290 N N . ASP A 1 41 ? 3.630 49.296 112.985 1.00 53.69 ? 69 ASP A N 1 ATOM 291 C CA . ASP A 1 41 ? 5.072 49.472 112.997 1.00 49.12 ? 69 ASP A CA 1 ATOM 292 C C . ASP A 1 41 ? 5.739 48.613 111.913 1.00 41.13 ? 69 ASP A C 1 ATOM 293 O O . ASP A 1 41 ? 6.706 49.042 111.297 1.00 29.70 ? 69 ASP A O 1 ATOM 294 C CB . ASP A 1 41 ? 5.658 49.186 114.381 1.00 49.67 ? 69 ASP A CB 1 ATOM 295 C CG . ASP A 1 41 ? 5.295 50.262 115.407 1.00 61.63 ? 69 ASP A CG 1 ATOM 296 O OD1 . ASP A 1 41 ? 4.901 51.387 115.011 1.00 53.19 ? 69 ASP A OD1 1 ATOM 297 O OD2 . ASP A 1 41 ? 5.388 49.979 116.619 1.00 69.71 ? 69 ASP A OD2 1 ATOM 298 N N . LEU A 1 42 ? 5.214 47.413 111.674 1.00 36.51 ? 70 LEU A N 1 ATOM 299 C CA . LEU A 1 42 ? 5.770 46.564 110.617 1.00 42.47 ? 70 LEU A CA 1 ATOM 300 C C . LEU A 1 42 ? 5.612 47.252 109.262 1.00 45.69 ? 70 LEU A C 1 ATOM 301 O O . LEU A 1 42 ? 6.552 47.302 108.477 1.00 52.51 ? 70 LEU A O 1 ATOM 302 C CB . LEU A 1 42 ? 5.128 45.159 110.616 1.00 40.56 ? 70 LEU A CB 1 ATOM 303 C CG . LEU A 1 42 ? 5.729 44.125 109.647 1.00 46.86 ? 70 LEU A CG 1 ATOM 304 C CD1 . LEU A 1 42 ? 7.254 44.023 109.836 1.00 29.50 ? 70 LEU A CD1 1 ATOM 305 C CD2 . LEU A 1 42 ? 5.099 42.717 109.812 1.00 24.38 ? 70 LEU A CD2 1 ATOM 306 N N . LEU A 1 43 ? 4.427 47.806 109.013 1.00 49.44 ? 71 LEU A N 1 ATOM 307 C CA . LEU A 1 43 ? 4.127 48.519 107.770 1.00 44.40 ? 71 LEU A CA 1 ATOM 308 C C . LEU A 1 43 ? 5.023 49.731 107.551 1.00 42.75 ? 71 LEU A C 1 ATOM 309 O O . LEU A 1 43 ? 5.537 49.958 106.444 1.00 39.90 ? 71 LEU A O 1 ATOM 310 C CB . LEU A 1 43 ? 2.654 48.939 107.758 1.00 55.09 ? 71 LEU A CB 1 ATOM 311 C CG . LEU A 1 43 ? 1.656 47.771 107.853 1.00 60.84 ? 71 LEU A CG 1 ATOM 312 C CD1 . LEU A 1 43 ? 0.223 48.258 108.045 1.00 65.52 ? 71 LEU A CD1 1 ATOM 313 C CD2 . LEU A 1 43 ? 1.743 46.860 106.644 1.00 54.59 ? 71 LEU A CD2 1 ATOM 314 N N . GLY A 1 44 ? 5.211 50.513 108.608 1.00 41.11 ? 72 GLY A N 1 ATOM 315 C CA . GLY A 1 44 ? 6.074 51.678 108.546 1.00 34.61 ? 72 GLY A CA 1 ATOM 316 C C . GLY A 1 44 ? 7.536 51.326 108.300 1.00 40.87 ? 72 GLY A C 1 ATOM 317 O O . GLY A 1 44 ? 8.252 52.036 107.594 1.00 40.90 ? 72 GLY A O 1 ATOM 318 N N . ALA A 1 45 ? 8.001 50.260 108.943 1.00 42.38 ? 73 ALA A N 1 ATOM 319 C CA . ALA A 1 45 ? 9.360 49.771 108.722 1.00 42.47 ? 73 ALA A CA 1 ATOM 320 C C . ALA A 1 45 ? 9.591 49.361 107.265 1.00 35.42 ? 73 ALA A C 1 ATOM 321 O O . ALA A 1 45 ? 10.717 49.329 106.792 1.00 38.69 ? 73 ALA A O 1 ATOM 322 C CB . ALA A 1 45 ? 9.660 48.614 109.645 1.00 41.30 ? 73 ALA A CB 1 ATOM 323 N N . ASN A 1 46 ? 8.520 49.018 106.564 1.00 39.64 ? 74 ASN A N 1 ATOM 324 C CA . ASN A 1 46 ? 8.635 48.661 105.156 1.00 42.75 ? 74 ASN A CA 1 ATOM 325 C C . ASN A 1 46 ? 8.046 49.696 104.205 1.00 51.93 ? 74 ASN A C 1 ATOM 326 O O . ASN A 1 46 ? 7.769 49.406 103.044 1.00 44.79 ? 74 ASN A O 1 ATOM 327 C CB . ASN A 1 46 ? 8.057 47.269 104.927 1.00 38.44 ? 74 ASN A CB 1 ATOM 328 C CG . ASN A 1 46 ? 8.920 46.205 105.557 1.00 34.49 ? 74 ASN A CG 1 ATOM 329 O OD1 . ASN A 1 46 ? 9.797 45.655 104.911 1.00 35.47 ? 74 ASN A OD1 1 ATOM 330 N ND2 . ASN A 1 46 ? 8.733 45.970 106.839 1.00 28.03 ? 74 ASN A ND2 1 ATOM 331 N N . GLY A 1 47 ? 7.878 50.914 104.716 1.00 54.03 ? 75 GLY A N 1 ATOM 332 C CA . GLY A 1 47 ? 7.432 52.038 103.918 1.00 45.96 ? 75 GLY A CA 1 ATOM 333 C C . GLY A 1 47 ? 6.056 51.944 103.293 1.00 39.20 ? 75 GLY A C 1 ATOM 334 O O . GLY A 1 47 ? 5.871 52.391 102.170 1.00 45.02 ? 75 GLY A O 1 ATOM 335 N N . LEU A 1 48 ? 5.109 51.333 103.999 1.00 28.59 ? 76 LEU A N 1 ATOM 336 C CA . LEU A 1 48 ? 3.711 51.251 103.547 1.00 40.08 ? 76 LEU A CA 1 ATOM 337 C C . LEU A 1 48 ? 2.764 52.177 104.374 1.00 62.49 ? 76 LEU A C 1 ATOM 338 O O . LEU A 1 48 ? 2.942 52.340 105.579 1.00 52.84 ? 76 LEU A O 1 ATOM 339 C CB . LEU A 1 48 ? 3.214 49.796 103.625 1.00 48.26 ? 76 LEU A CB 1 ATOM 340 C CG . LEU A 1 48 ? 3.899 48.732 102.752 1.00 46.44 ? 76 LEU A CG 1 ATOM 341 C CD1 . LEU A 1 48 ? 3.552 47.313 103.236 1.00 35.04 ? 76 LEU A CD1 1 ATOM 342 C CD2 . LEU A 1 48 ? 3.502 48.903 101.308 1.00 44.00 ? 76 LEU A CD2 1 ATOM 343 N N . PRO A 1 49 ? 1.725 52.743 103.730 1.00 66.92 ? 77 PRO A N 1 ATOM 344 C CA . PRO A 1 49 ? 0.726 53.678 104.295 1.00 68.81 ? 77 PRO A CA 1 ATOM 345 C C . PRO A 1 49 ? -0.140 53.108 105.424 1.00 72.45 ? 77 PRO A C 1 ATOM 346 O O . PRO A 1 49 ? -0.217 51.889 105.577 1.00 73.56 ? 77 PRO A O 1 ATOM 347 C CB . PRO A 1 49 ? -0.183 54.016 103.111 1.00 65.85 ? 77 PRO A CB 1 ATOM 348 C CG . PRO A 1 49 ? 0.413 53.398 101.927 1.00 66.34 ? 77 PRO A CG 1 ATOM 349 C CD . PRO A 1 49 ? 1.499 52.470 102.301 1.00 65.30 ? 77 PRO A CD 1 ATOM 350 N N . ASP A 1 50 ? -0.758 53.991 106.210 1.00 72.19 ? 78 ASP A N 1 ATOM 351 C CA . ASP A 1 50 ? -1.659 53.601 107.305 1.00 71.75 ? 78 ASP A CA 1 ATOM 352 C C . ASP A 1 50 ? -2.813 52.689 106.900 1.00 77.48 ? 78 ASP A C 1 ATOM 353 O O . ASP A 1 50 ? -3.147 51.745 107.621 1.00 87.55 ? 78 ASP A O 1 ATOM 354 C CB . ASP A 1 50 ? -2.273 54.851 107.935 1.00 75.37 ? 78 ASP A CB 1 ATOM 355 C CG . ASP A 1 50 ? -1.237 55.771 108.532 1.00 90.95 ? 78 ASP A CG 1 ATOM 356 O OD1 . ASP A 1 50 ? -0.129 55.834 107.966 1.00 97.88 ? 78 ASP A OD1 1 ATOM 357 O OD2 . ASP A 1 50 ? -1.550 56.478 109.521 1.00 90.91 ? 78 ASP A OD2 1 ATOM 358 N N . GLY A 1 51 ? -3.402 52.935 105.737 1.00 70.84 ? 79 GLY A N 1 ATOM 359 C CA . GLY A 1 51 ? -4.603 52.214 105.354 1.00 68.11 ? 79 GLY A CA 1 ATOM 360 C C . GLY A 1 51 ? -4.365 50.825 104.801 1.00 72.46 ? 79 GLY A C 1 ATOM 361 O O . GLY A 1 51 ? -5.302 50.165 104.345 1.00 74.32 ? 79 GLY A O 1 ATOM 362 N N . THR A 1 52 ? -3.108 50.391 104.829 1.00 68.09 ? 80 THR A N 1 ATOM 363 C CA . THR A 1 52 ? -2.722 49.078 104.327 1.00 61.97 ? 80 THR A CA 1 ATOM 364 C C . THR A 1 52 ? -3.283 47.947 105.195 1.00 55.49 ? 80 THR A C 1 ATOM 365 O O . THR A 1 52 ? -3.123 47.946 106.419 1.00 50.61 ? 80 THR A O 1 ATOM 366 C CB . THR A 1 52 ? -1.191 48.958 104.248 1.00 62.48 ? 80 THR A CB 1 ATOM 367 O OG1 . THR A 1 52 ? -0.665 50.051 103.480 1.00 57.56 ? 80 THR A OG1 1 ATOM 368 C CG2 . THR A 1 52 ? -0.788 47.642 103.600 1.00 63.99 ? 80 THR A CG2 1 ATOM 369 N N . LEU A 1 53 ? -3.951 46.991 104.557 1.00 53.90 ? 81 LEU A N 1 ATOM 370 C CA . LEU A 1 53 ? -4.555 45.870 105.279 1.00 52.62 ? 81 LEU A CA 1 ATOM 371 C C . LEU A 1 53 ? -3.520 44.853 105.703 1.00 48.38 ? 81 LEU A C 1 ATOM 372 O O . LEU A 1 53 ? -2.451 44.762 105.109 1.00 51.79 ? 81 LEU A O 1 ATOM 373 C CB . LEU A 1 53 ? -5.630 45.184 104.444 1.00 55.62 ? 81 LEU A CB 1 ATOM 374 C CG . LEU A 1 53 ? -6.815 46.066 104.070 1.00 55.13 ? 81 LEU A CG 1 ATOM 375 C CD1 . LEU A 1 53 ? -7.733 45.277 103.192 1.00 54.76 ? 81 LEU A CD1 1 ATOM 376 C CD2 . LEU A 1 53 ? -7.548 46.564 105.318 1.00 45.68 ? 81 LEU A CD2 1 ATOM 377 N N . SER A 1 54 ? -3.846 44.096 106.744 1.00 42.57 ? 82 SER A N 1 ATOM 378 C CA . SER A 1 54 ? -2.936 43.112 107.290 1.00 41.49 ? 82 SER A CA 1 ATOM 379 C C . SER A 1 54 ? -2.706 41.987 106.296 1.00 47.49 ? 82 SER A C 1 ATOM 380 O O . SER A 1 54 ? -1.779 41.191 106.455 1.00 45.97 ? 82 SER A O 1 ATOM 381 C CB . SER A 1 54 ? -3.470 42.532 108.587 1.00 43.16 ? 82 SER A CB 1 ATOM 382 O OG . SER A 1 54 ? -4.256 41.399 108.294 1.00 54.32 ? 82 SER A OG 1 ATOM 383 N N . SER A 1 55 ? -3.562 41.920 105.281 1.00 47.54 ? 83 SER A N 1 ATOM 384 C CA . SER A 1 55 ? -3.492 40.860 104.277 1.00 48.20 ? 83 SER A CA 1 ATOM 385 C C . SER A 1 55 ? -2.545 41.261 103.161 1.00 42.49 ? 83 SER A C 1 ATOM 386 O O . SER A 1 55 ? -2.399 40.543 102.170 1.00 38.41 ? 83 SER A O 1 ATOM 387 C CB . SER A 1 55 ? -4.876 40.546 103.692 1.00 42.93 ? 83 SER A CB 1 ATOM 388 O OG . SER A 1 55 ? -5.400 41.637 102.950 1.00 50.26 ? 83 SER A OG 1 ATOM 389 N N . ALA A 1 56 ? -1.906 42.416 103.320 1.00 41.33 ? 84 ALA A N 1 ATOM 390 C CA . ALA A 1 56 ? -0.956 42.885 102.310 1.00 45.95 ? 84 ALA A CA 1 ATOM 391 C C . ALA A 1 56 ? 0.103 41.801 102.049 1.00 44.57 ? 84 ALA A C 1 ATOM 392 O O . ALA A 1 56 ? 0.735 41.292 102.979 1.00 44.25 ? 84 ALA A O 1 ATOM 393 C CB . ALA A 1 56 ? -0.308 44.158 102.767 1.00 33.39 ? 84 ALA A CB 1 ATOM 394 N N . PRO A 1 57 ? 0.301 41.465 100.773 1.00 35.56 ? 85 PRO A N 1 ATOM 395 C CA . PRO A 1 57 ? 1.041 40.245 100.432 1.00 48.05 ? 85 PRO A CA 1 ATOM 396 C C . PRO A 1 57 ? 2.558 40.410 100.520 1.00 49.70 ? 85 PRO A C 1 ATOM 397 O O . PRO A 1 57 ? 3.110 41.454 100.189 1.00 43.64 ? 85 PRO A O 1 ATOM 398 C CB . PRO A 1 57 ? 0.610 39.981 98.987 1.00 38.19 ? 85 PRO A CB 1 ATOM 399 C CG . PRO A 1 57 ? 0.425 41.364 98.429 1.00 41.35 ? 85 PRO A CG 1 ATOM 400 C CD . PRO A 1 57 ? -0.155 42.185 99.575 1.00 36.82 ? 85 PRO A CD 1 ATOM 401 N N . VAL A 1 58 ? 3.219 39.365 100.994 1.00 50.97 ? 86 VAL A N 1 ATOM 402 C CA . VAL A 1 58 ? 4.661 39.268 100.879 1.00 42.34 ? 86 VAL A CA 1 ATOM 403 C C . VAL A 1 58 ? 4.939 38.043 100.038 1.00 37.63 ? 86 VAL A C 1 ATOM 404 O O . VAL A 1 58 ? 4.575 36.923 100.406 1.00 39.79 ? 86 VAL A O 1 ATOM 405 C CB . VAL A 1 58 ? 5.340 39.116 102.248 1.00 43.60 ? 86 VAL A CB 1 ATOM 406 C CG1 . VAL A 1 58 ? 6.845 39.035 102.075 1.00 40.46 ? 86 VAL A CG1 1 ATOM 407 C CG2 . VAL A 1 58 ? 4.944 40.256 103.171 1.00 46.81 ? 86 VAL A CG2 1 ATOM 408 N N . ALA A 1 59 ? 5.592 38.253 98.907 1.00 36.88 ? 87 ALA A N 1 ATOM 409 C CA . ALA A 1 59 ? 5.862 37.165 97.982 1.00 35.57 ? 87 ALA A CA 1 ATOM 410 C C . ALA A 1 59 ? 6.932 36.257 98.556 1.00 42.32 ? 87 ALA A C 1 ATOM 411 O O . ALA A 1 59 ? 7.752 36.678 99.378 1.00 42.02 ? 87 ALA A O 1 ATOM 412 C CB . ALA A 1 59 ? 6.296 37.702 96.640 1.00 27.94 ? 87 ALA A CB 1 ATOM 413 N N . ALA A 1 60 ? 6.907 35.007 98.123 1.00 40.12 ? 88 ALA A N 1 ATOM 414 C CA . ALA A 1 60 ? 7.977 34.075 98.414 1.00 41.33 ? 88 ALA A CA 1 ATOM 415 C C . ALA A 1 60 ? 9.319 34.664 97.984 1.00 33.81 ? 88 ALA A C 1 ATOM 416 O O . ALA A 1 60 ? 9.412 35.263 96.915 1.00 24.10 ? 88 ALA A O 1 ATOM 417 C CB . ALA A 1 60 ? 7.724 32.777 97.681 1.00 36.39 ? 88 ALA A CB 1 ATOM 418 N N . ASN A 1 61 ? 10.326 34.489 98.844 1.00 27.83 ? 89 ASN A N 1 ATOM 419 C CA . ASN A 1 61 ? 11.714 34.896 98.636 1.00 31.09 ? 89 ASN A CA 1 ATOM 420 C C . ASN A 1 61 ? 11.978 36.395 98.756 1.00 42.65 ? 89 ASN A C 1 ATOM 421 O O . ASN A 1 61 ? 13.134 36.809 98.744 1.00 43.54 ? 89 ASN A O 1 ATOM 422 C CB . ASN A 1 61 ? 12.237 34.414 97.276 1.00 31.86 ? 89 ASN A CB 1 ATOM 423 C CG . ASN A 1 61 ? 12.015 32.947 97.059 1.00 32.17 ? 89 ASN A CG 1 ATOM 424 O OD1 . ASN A 1 61 ? 12.696 32.110 97.665 1.00 38.51 ? 89 ASN A OD1 1 ATOM 425 N ND2 . ASN A 1 61 ? 11.022 32.618 96.208 1.00 31.67 ? 89 ASN A ND2 1 ATOM 426 N N . SER A 1 62 ? 10.920 37.195 98.910 1.00 41.74 ? 90 SER A N 1 ATOM 427 C CA . SER A 1 62 ? 11.064 38.649 99.022 1.00 36.67 ? 90 SER A CA 1 ATOM 428 C C . SER A 1 62 ? 11.382 39.017 100.453 1.00 31.73 ? 90 SER A C 1 ATOM 429 O O . SER A 1 62 ? 11.166 38.214 101.361 1.00 34.66 ? 90 SER A O 1 ATOM 430 C CB . SER A 1 62 ? 9.794 39.367 98.583 1.00 37.18 ? 90 SER A CB 1 ATOM 431 O OG . SER A 1 62 ? 8.827 39.354 99.613 1.00 45.37 ? 90 SER A OG 1 ATOM 432 N N . THR A 1 63 ? 11.912 40.218 100.660 1.00 36.06 ? 91 THR A N 1 ATOM 433 C CA . THR A 1 63 ? 12.379 40.603 101.993 1.00 38.21 ? 91 THR A CA 1 ATOM 434 C C . THR A 1 63 ? 11.426 41.549 102.711 1.00 35.66 ? 91 THR A C 1 ATOM 435 O O . THR A 1 63 ? 10.719 42.318 102.086 1.00 30.55 ? 91 THR A O 1 ATOM 436 C CB . THR A 1 63 ? 13.762 41.273 101.935 1.00 32.34 ? 91 THR A CB 1 ATOM 437 O OG1 . THR A 1 63 ? 13.671 42.474 101.166 1.00 39.25 ? 91 THR A OG1 1 ATOM 438 C CG2 . THR A 1 63 ? 14.790 40.328 101.297 1.00 25.20 ? 91 THR A CG2 1 ATOM 439 N N . VAL A 1 64 ? 11.415 41.458 104.035 1.00 32.87 ? 92 VAL A N 1 ATOM 440 C CA . VAL A 1 64 ? 10.623 42.328 104.871 1.00 30.24 ? 92 VAL A CA 1 ATOM 441 C C . VAL A 1 64 ? 11.443 42.709 106.068 1.00 28.66 ? 92 VAL A C 1 ATOM 442 O O . VAL A 1 64 ? 12.008 41.856 106.745 1.00 30.31 ? 92 VAL A O 1 ATOM 443 C CB . VAL A 1 64 ? 9.353 41.625 105.419 1.00 41.02 ? 92 VAL A CB 1 ATOM 444 C CG1 . VAL A 1 64 ? 8.514 42.603 106.274 1.00 37.27 ? 92 VAL A CG1 1 ATOM 445 C CG2 . VAL A 1 64 ? 8.528 41.060 104.298 1.00 34.87 ? 92 VAL A CG2 1 ATOM 446 N N . LYS A 1 65 ? 11.465 43.998 106.361 1.00 24.65 ? 93 LYS A N 1 ATOM 447 C CA . LYS A 1 65 ? 12.145 44.486 107.531 1.00 26.91 ? 93 LYS A CA 1 ATOM 448 C C . LYS A 1 65 ? 11.298 44.204 108.757 1.00 28.94 ? 93 LYS A C 1 ATOM 449 O O . LYS A 1 65 ? 10.181 44.676 108.860 1.00 36.73 ? 93 LYS A O 1 ATOM 450 C CB . LYS A 1 65 ? 12.351 45.974 107.381 1.00 31.99 ? 93 LYS A CB 1 ATOM 451 C CG . LYS A 1 65 ? 13.504 46.550 108.188 1.00 43.50 ? 93 LYS A CG 1 ATOM 452 C CD . LYS A 1 65 ? 13.745 47.992 107.727 1.00 42.63 ? 93 LYS A CD 1 ATOM 453 C CE . LYS A 1 65 ? 15.008 48.603 108.283 1.00 46.92 ? 93 LYS A CE 1 ATOM 454 N NZ . LYS A 1 65 ? 14.993 48.705 109.753 1.00 45.09 ? 93 LYS A NZ 1 ATOM 455 N N . ILE A 1 66 ? 11.841 43.474 109.710 1.00 29.69 ? 94 ILE A N 1 ATOM 456 C CA . ILE A 1 66 ? 11.079 43.156 110.905 1.00 27.12 ? 94 ILE A CA 1 ATOM 457 C C . ILE A 1 66 ? 11.770 43.727 112.138 1.00 29.43 ? 94 ILE A C 1 ATOM 458 O O . ILE A 1 66 ? 12.856 43.303 112.477 1.00 38.47 ? 94 ILE A O 1 ATOM 459 C CB . ILE A 1 66 ? 10.831 41.634 111.036 1.00 37.01 ? 94 ILE A CB 1 ATOM 460 C CG1 . ILE A 1 66 ? 10.100 41.137 109.776 1.00 34.20 ? 94 ILE A CG1 1 ATOM 461 C CG2 . ILE A 1 66 ? 10.058 41.318 112.324 1.00 34.62 ? 94 ILE A CG2 1 ATOM 462 C CD1 . ILE A 1 66 ? 9.731 39.703 109.787 1.00 41.08 ? 94 ILE A CD1 1 ATOM 463 N N . PRO A 1 67 ? 11.151 44.745 112.764 1.00 28.63 ? 95 PRO A N 1 ATOM 464 C CA . PRO A 1 67 ? 11.634 45.418 113.981 1.00 39.40 ? 95 PRO A CA 1 ATOM 465 C C . PRO A 1 67 ? 11.319 44.634 115.235 1.00 40.75 ? 95 PRO A C 1 ATOM 466 O O . PRO A 1 67 ? 10.341 43.888 115.261 1.00 38.10 ? 95 PRO A O 1 ATOM 467 C CB . PRO A 1 67 ? 10.871 46.759 113.994 1.00 37.18 ? 95 PRO A CB 1 ATOM 468 C CG . PRO A 1 67 ? 9.789 46.645 112.999 1.00 47.29 ? 95 PRO A CG 1 ATOM 469 C CD . PRO A 1 67 ? 9.878 45.307 112.288 1.00 40.20 ? 95 PRO A CD 1 ATOM 470 N N . PHE A 1 68 ? 12.166 44.756 116.246 1.00 33.04 ? 96 PHE A N 1 ATOM 471 C CA . PHE A 1 68 ? 11.885 44.095 117.503 1.00 34.93 ? 96 PHE A CA 1 ATOM 472 C C . PHE A 1 68 ? 12.656 44.737 118.637 1.00 33.11 ? 96 PHE A C 1 ATOM 473 O O . PHE A 1 68 ? 13.552 45.534 118.411 1.00 31.36 ? 96 PHE A O 1 ATOM 474 C CB . PHE A 1 68 ? 12.209 42.590 117.417 1.00 33.60 ? 96 PHE A CB 1 ATOM 475 C CG . PHE A 1 68 ? 13.631 42.287 117.029 1.00 37.39 ? 96 PHE A CG 1 ATOM 476 C CD1 . PHE A 1 68 ? 14.620 42.173 117.996 1.00 37.44 ? 96 PHE A CD1 1 ATOM 477 C CD2 . PHE A 1 68 ? 13.978 42.114 115.691 1.00 20.07 ? 96 PHE A CD2 1 ATOM 478 C CE1 . PHE A 1 68 ? 15.923 41.901 117.631 1.00 41.12 ? 96 PHE A CE1 1 ATOM 479 C CE2 . PHE A 1 68 ? 15.268 41.848 115.328 1.00 29.97 ? 96 PHE A CE2 1 ATOM 480 C CZ . PHE A 1 68 ? 16.249 41.737 116.287 1.00 30.73 ? 96 PHE A CZ 1 ATOM 481 N N . ARG A 1 69 ? 12.312 44.362 119.861 1.00 34.25 ? 97 ARG A N 1 ATOM 482 C CA . ARG A 1 69 ? 13.031 44.836 121.015 1.00 37.16 ? 97 ARG A CA 1 ATOM 483 C C . ARG A 1 69 ? 14.267 44.010 121.258 1.00 37.91 ? 97 ARG A C 1 ATOM 484 O O . ARG A 1 69 ? 14.201 42.805 121.387 1.00 40.26 ? 97 ARG A O 1 ATOM 485 C CB . ARG A 1 69 ? 12.131 44.834 122.248 1.00 35.04 ? 97 ARG A CB 1 ATOM 486 C CG . ARG A 1 69 ? 12.453 45.966 123.225 1.00 52.23 ? 97 ARG A CG 1 ATOM 487 C CD . ARG A 1 69 ? 12.421 45.481 124.664 1.00 66.78 ? 97 ARG A CD 1 ATOM 488 N NE . ARG A 1 69 ? 11.153 44.819 124.958 1.00 71.60 ? 97 ARG A NE 1 ATOM 489 C CZ . ARG A 1 69 ? 10.886 44.183 126.091 1.00 76.57 ? 97 ARG A CZ 1 ATOM 490 N NH1 . ARG A 1 69 ? 11.806 44.125 127.041 1.00 83.43 ? 97 ARG A NH1 1 ATOM 491 N NH2 . ARG A 1 69 ? 9.703 43.611 126.278 1.00 73.84 ? 97 ARG A NH2 1 ATOM 492 N N . CYS A 1 70 ? 15.411 44.676 121.266 1.00 39.56 ? 98 CYS A N 1 ATOM 493 C CA . CYS A 1 70 ? 16.660 44.023 121.576 1.00 28.20 ? 98 CYS A CA 1 ATOM 494 C C . CYS A 1 70 ? 17.015 44.181 123.052 1.00 35.71 ? 98 CYS A C 1 ATOM 495 O O . CYS A 1 70 ? 16.836 45.240 123.642 1.00 35.24 ? 98 CYS A O 1 ATOM 496 C CB . CYS A 1 70 ? 17.773 44.630 120.724 1.00 26.06 ? 98 CYS A CB 1 ATOM 497 S SG . CYS A 1 70 ? 19.390 43.892 121.011 1.00 34.12 ? 98 CYS A SG 1 ATOM 498 N N . ARG A 1 71 ? 17.497 43.107 123.654 1.00 38.37 ? 99 ARG A N 1 ATOM 499 C CA . ARG A 1 71 ? 18.063 43.169 124.991 1.00 42.29 ? 99 ARG A CA 1 ATOM 500 C C . ARG A 1 71 ? 19.515 42.740 124.986 1.00 38.27 ? 99 ARG A C 1 ATOM 501 O O . ARG A 1 71 ? 19.869 41.730 124.367 1.00 42.61 ? 99 ARG A O 1 ATOM 502 C CB . ARG A 1 71 ? 17.276 42.306 125.977 1.00 46.65 ? 99 ARG A CB 1 ATOM 503 C CG . ARG A 1 71 ? 17.964 42.173 127.313 1.00 48.94 ? 99 ARG A CG 1 ATOM 504 C CD . ARG A 1 71 ? 17.104 41.514 128.387 1.00 53.76 ? 99 ARG A CD 1 ATOM 505 N NE . ARG A 1 71 ? 17.853 41.363 129.642 1.00 60.13 ? 99 ARG A NE 1 ATOM 506 C CZ . ARG A 1 71 ? 17.533 41.918 130.811 1.00 68.77 ? 99 ARG A CZ 1 ATOM 507 N NH1 . ARG A 1 71 ? 16.461 42.699 130.932 1.00 68.82 ? 99 ARG A NH1 1 ATOM 508 N NH2 . ARG A 1 71 ? 18.298 41.687 131.870 1.00 67.63 ? 99 ARG A NH2 1 ATOM 509 N N . CYS A 1 72 ? 20.354 43.520 125.664 1.00 36.89 ? 100 CYS A N 1 ATOM 510 C CA . CYS A 1 72 ? 21.770 43.210 125.779 1.00 44.34 ? 100 CYS A CA 1 ATOM 511 C C . CYS A 1 72 ? 22.008 42.475 127.091 1.00 45.81 ? 100 CYS A C 1 ATOM 512 O O . CYS A 1 72 ? 21.430 42.831 128.112 1.00 41.93 ? 100 CYS A O 1 ATOM 513 C CB . CYS A 1 72 ? 22.608 44.488 125.706 1.00 42.54 ? 100 CYS A CB 1 ATOM 514 S SG . CYS A 1 72 ? 22.647 45.245 124.061 1.00 50.45 ? 100 CYS A SG 1 ATOM 515 N N . ASN A 1 73 ? 22.790 41.404 127.059 1.00 47.74 ? 101 ASN A N 1 ATOM 516 C CA . ASN A 1 73 ? 23.126 40.726 128.307 1.00 47.40 ? 101 ASN A CA 1 ATOM 517 C C . ASN A 1 73 ? 24.532 40.938 128.851 1.00 48.20 ? 101 ASN A C 1 ATOM 518 O O . ASN A 1 73 ? 24.943 40.227 129.757 1.00 52.29 ? 101 ASN A O 1 ATOM 519 C CB . ASN A 1 73 ? 22.840 39.222 128.233 1.00 43.48 ? 101 ASN A CB 1 ATOM 520 C CG . ASN A 1 73 ? 23.733 38.488 127.263 1.00 45.36 ? 101 ASN A CG 1 ATOM 521 O OD1 . ASN A 1 73 ? 24.723 39.018 126.759 1.00 40.01 ? 101 ASN A OD1 1 ATOM 522 N ND2 . ASN A 1 73 ? 23.421 37.217 127.051 1.00 59.52 ? 101 ASN A ND2 1 ATOM 523 N N . GLY A 1 74 ? 25.278 41.875 128.286 1.00 50.94 ? 102 GLY A N 1 ATOM 524 C CA . GLY A 1 74 ? 26.638 42.128 128.735 1.00 48.07 ? 102 GLY A CA 1 ATOM 525 C C . GLY A 1 74 ? 27.665 41.648 127.730 1.00 50.65 ? 102 GLY A C 1 ATOM 526 O O . GLY A 1 74 ? 28.790 42.155 127.684 1.00 45.88 ? 102 GLY A O 1 ATOM 527 N N . ASP A 1 75 ? 27.257 40.680 126.910 1.00 39.86 ? 103 ASP A N 1 ATOM 528 C CA . ASP A 1 75 ? 28.124 40.068 125.903 1.00 48.48 ? 103 ASP A CA 1 ATOM 529 C C . ASP A 1 75 ? 27.490 40.228 124.537 1.00 42.90 ? 103 ASP A C 1 ATOM 530 O O . ASP A 1 75 ? 28.158 40.496 123.539 1.00 34.37 ? 103 ASP A O 1 ATOM 531 C CB . ASP A 1 75 ? 28.329 38.571 126.163 1.00 53.62 ? 103 ASP A CB 1 ATOM 532 C CG . ASP A 1 75 ? 29.211 38.296 127.352 1.00 65.04 ? 103 ASP A CG 1 ATOM 533 O OD1 . ASP A 1 75 ? 30.235 38.994 127.503 1.00 75.99 ? 103 ASP A OD1 1 ATOM 534 O OD2 . ASP A 1 75 ? 28.900 37.377 128.130 1.00 65.10 ? 103 ASP A OD2 1 ATOM 535 N N . VAL A 1 76 ? 26.177 40.085 124.513 1.00 34.13 ? 104 VAL A N 1 ATOM 536 C CA . VAL A 1 76 ? 25.483 39.911 123.279 1.00 30.75 ? 104 VAL A CA 1 ATOM 537 C C . VAL A 1 76 ? 24.136 40.631 123.333 1.00 41.71 ? 104 VAL A C 1 ATOM 538 O O . VAL A 1 76 ? 23.631 40.979 124.415 1.00 38.44 ? 104 VAL A O 1 ATOM 539 C CB . VAL A 1 76 ? 25.348 38.365 123.008 1.00 46.31 ? 104 VAL A CB 1 ATOM 540 C CG1 . VAL A 1 76 ? 24.278 37.726 123.881 1.00 41.84 ? 104 VAL A CG1 1 ATOM 541 C CG2 . VAL A 1 76 ? 25.042 38.112 121.620 1.00 52.65 ? 104 VAL A CG2 1 ATOM 542 N N . GLY A 1 77 ? 23.601 40.934 122.159 1.00 40.82 ? 105 GLY A N 1 ATOM 543 C CA . GLY A 1 77 ? 22.261 41.469 122.045 1.00 41.97 ? 105 GLY A CA 1 ATOM 544 C C . GLY A 1 77 ? 21.352 40.411 121.439 1.00 40.55 ? 105 GLY A C 1 ATOM 545 O O . GLY A 1 77 ? 21.694 39.817 120.433 1.00 37.12 ? 105 GLY A O 1 ATOM 546 N N . GLN A 1 78 ? 20.193 40.178 122.038 1.00 27.70 ? 106 GLN A N 1 ATOM 547 C CA . GLN A 1 78 ? 19.251 39.189 121.522 1.00 35.59 ? 106 GLN A CA 1 ATOM 548 C C . GLN A 1 78 ? 17.858 39.775 121.507 1.00 33.93 ? 106 GLN A C 1 ATOM 549 O O . GLN A 1 78 ? 17.539 40.614 122.340 1.00 34.31 ? 106 GLN A O 1 ATOM 550 C CB . GLN A 1 78 ? 19.265 37.928 122.402 1.00 35.56 ? 106 GLN A CB 1 ATOM 551 C CG . GLN A 1 78 ? 20.647 37.297 122.464 1.00 39.27 ? 106 GLN A CG 1 ATOM 552 C CD . GLN A 1 78 ? 20.798 36.344 123.607 1.00 48.86 ? 106 GLN A CD 1 ATOM 553 O OE1 . GLN A 1 78 ? 20.315 36.600 124.711 1.00 53.90 ? 106 GLN A OE1 1 ATOM 554 N NE2 . GLN A 1 78 ? 21.441 35.209 123.343 1.00 42.74 ? 106 GLN A NE2 1 ATOM 555 N N . SER A 1 79 ? 17.034 39.343 120.560 1.00 34.16 ? 107 SER A N 1 ATOM 556 C CA . SER A 1 79 ? 15.635 39.751 120.544 1.00 30.20 ? 107 SER A CA 1 ATOM 557 C C . SER A 1 79 ? 15.033 39.309 121.886 1.00 37.50 ? 107 SER A C 1 ATOM 558 O O . SER A 1 79 ? 15.275 38.200 122.359 1.00 33.54 ? 107 SER A O 1 ATOM 559 C CB . SER A 1 79 ? 14.910 39.117 119.352 1.00 37.88 ? 107 SER A CB 1 ATOM 560 O OG . SER A 1 79 ? 14.964 37.702 119.395 1.00 34.02 ? 107 SER A OG 1 ATOM 561 N N . ASP A 1 80 ? 14.294 40.200 122.524 1.00 45.58 ? 108 ASP A N 1 ATOM 562 C CA . ASP A 1 80 ? 13.999 40.072 123.950 1.00 42.33 ? 108 ASP A CA 1 ATOM 563 C C . ASP A 1 80 ? 12.887 39.064 124.288 1.00 43.31 ? 108 ASP A C 1 ATOM 564 O O . ASP A 1 80 ? 11.711 39.423 124.384 1.00 44.96 ? 108 ASP A O 1 ATOM 565 C CB . ASP A 1 80 ? 13.664 41.451 124.487 1.00 41.19 ? 108 ASP A CB 1 ATOM 566 C CG . ASP A 1 80 ? 13.595 41.495 125.994 1.00 47.16 ? 108 ASP A CG 1 ATOM 567 O OD1 . ASP A 1 80 ? 13.942 40.502 126.654 1.00 56.33 ? 108 ASP A OD1 1 ATOM 568 O OD2 . ASP A 1 80 ? 13.229 42.560 126.512 1.00 48.55 ? 108 ASP A OD2 1 ATOM 569 N N . ARG A 1 81 ? 13.282 37.811 124.489 1.00 49.98 ? 109 ARG A N 1 ATOM 570 C CA . ARG A 1 81 ? 12.363 36.696 124.773 1.00 50.24 ? 109 ARG A CA 1 ATOM 571 C C . ARG A 1 81 ? 11.291 36.494 123.705 1.00 45.60 ? 109 ARG A C 1 ATOM 572 O O . ARG A 1 81 ? 10.332 35.772 123.924 1.00 59.34 ? 109 ARG A O 1 ATOM 573 C CB . ARG A 1 81 ? 11.757 36.798 126.181 1.00 46.79 ? 109 ARG A CB 1 ATOM 574 C CG . ARG A 1 81 ? 12.812 36.884 127.281 1.00 57.48 ? 109 ARG A CG 1 ATOM 575 C CD . ARG A 1 81 ? 13.539 35.558 127.442 1.00 75.06 ? 109 ARG A CD 1 ATOM 576 N NE . ARG A 1 81 ? 14.841 35.693 128.099 1.00 86.66 ? 109 ARG A NE 1 ATOM 577 C CZ . ARG A 1 81 ? 15.494 34.690 128.686 1.00 89.16 ? 109 ARG A CZ 1 ATOM 578 N NH1 . ARG A 1 81 ? 14.960 33.471 128.718 1.00 89.19 ? 109 ARG A NH1 1 ATOM 579 N NH2 . ARG A 1 81 ? 16.677 34.905 129.249 1.00 83.07 ? 109 ARG A NH2 1 ATOM 580 N N . LEU A 1 82 ? 11.483 37.129 122.551 1.00 43.25 ? 110 LEU A N 1 ATOM 581 C CA . LEU A 1 82 ? 10.643 36.964 121.368 1.00 35.31 ? 110 LEU A CA 1 ATOM 582 C C . LEU A 1 82 ? 11.574 36.902 120.180 1.00 38.31 ? 110 LEU A C 1 ATOM 583 O O . LEU A 1 82 ? 12.708 37.387 120.266 1.00 37.54 ? 110 LEU A O 1 ATOM 584 C CB . LEU A 1 82 ? 9.714 38.160 121.212 1.00 36.79 ? 110 LEU A CB 1 ATOM 585 C CG . LEU A 1 82 ? 8.616 38.233 122.265 1.00 42.35 ? 110 LEU A CG 1 ATOM 586 C CD1 . LEU A 1 82 ? 7.949 39.603 122.280 1.00 31.73 ? 110 LEU A CD1 1 ATOM 587 C CD2 . LEU A 1 82 ? 7.600 37.129 121.980 1.00 46.36 ? 110 LEU A CD2 1 ATOM 588 N N . PRO A 1 83 ? 11.130 36.288 119.072 1.00 36.17 ? 111 PRO A N 1 ATOM 589 C CA . PRO A 1 83 ? 9.860 35.597 118.880 1.00 46.02 ? 111 PRO A CA 1 ATOM 590 C C . PRO A 1 83 ? 9.847 34.204 119.516 1.00 39.66 ? 111 PRO A C 1 ATOM 591 O O . PRO A 1 83 ? 10.896 33.671 119.871 1.00 39.58 ? 111 PRO A O 1 ATOM 592 C CB . PRO A 1 83 ? 9.769 35.476 117.364 1.00 44.84 ? 111 PRO A CB 1 ATOM 593 C CG . PRO A 1 83 ? 11.158 35.398 116.924 1.00 39.44 ? 111 PRO A CG 1 ATOM 594 C CD . PRO A 1 83 ? 11.951 36.252 117.849 1.00 35.24 ? 111 PRO A CD 1 ATOM 595 N N . ILE A 1 84 ? 8.654 33.636 119.655 1.00 44.58 ? 112 ILE A N 1 ATOM 596 C CA . ILE A 1 84 ? 8.481 32.292 120.210 1.00 53.05 ? 112 ILE A CA 1 ATOM 597 C C . ILE A 1 84 ? 8.167 31.300 119.102 1.00 53.56 ? 112 ILE A C 1 ATOM 598 O O . ILE A 1 84 ? 7.286 31.548 118.276 1.00 53.45 ? 112 ILE A O 1 ATOM 599 C CB . ILE A 1 84 ? 7.339 32.288 121.239 1.00 57.73 ? 112 ILE A CB 1 ATOM 600 C CG1 . ILE A 1 84 ? 7.862 32.828 122.563 1.00 49.89 ? 112 ILE A CG1 1 ATOM 601 C CG2 . ILE A 1 84 ? 6.768 30.888 121.438 1.00 58.85 ? 112 ILE A CG2 1 ATOM 602 C CD1 . ILE A 1 84 ? 9.094 32.119 122.993 1.00 51.64 ? 112 ILE A CD1 1 ATOM 603 N N . TYR A 1 85 ? 8.890 30.183 119.070 1.00 52.10 ? 113 TYR A N 1 ATOM 604 C CA . TYR A 1 85 ? 8.612 29.170 118.053 1.00 58.94 ? 113 TYR A CA 1 ATOM 605 C C . TYR A 1 85 ? 8.136 27.848 118.656 1.00 66.32 ? 113 TYR A C 1 ATOM 606 O O . TYR A 1 85 ? 8.789 27.269 119.536 1.00 67.24 ? 113 TYR A O 1 ATOM 607 C CB . TYR A 1 85 ? 9.833 28.927 117.160 1.00 47.16 ? 113 TYR A CB 1 ATOM 608 C CG . TYR A 1 85 ? 9.538 27.978 116.031 1.00 52.45 ? 113 TYR A CG 1 ATOM 609 C CD1 . TYR A 1 85 ? 9.019 28.439 114.828 1.00 43.67 ? 113 TYR A CD1 1 ATOM 610 C CD2 . TYR A 1 85 ? 9.742 26.607 116.179 1.00 51.00 ? 113 TYR A CD2 1 ATOM 611 C CE1 . TYR A 1 85 ? 8.731 27.559 113.794 1.00 45.13 ? 113 TYR A CE1 1 ATOM 612 C CE2 . TYR A 1 85 ? 9.464 25.726 115.160 1.00 51.87 ? 113 TYR A CE2 1 ATOM 613 C CZ . TYR A 1 85 ? 8.960 26.195 113.968 1.00 52.63 ? 113 TYR A CZ 1 ATOM 614 O OH . TYR A 1 85 ? 8.690 25.292 112.957 1.00 44.92 ? 113 TYR A OH 1 ATOM 615 N N . VAL A 1 86 ? 6.997 27.371 118.164 1.00 65.72 ? 114 VAL A N 1 ATOM 616 C CA . VAL A 1 86 ? 6.458 26.072 118.579 1.00 60.70 ? 114 VAL A CA 1 ATOM 617 C C . VAL A 1 86 ? 6.927 24.919 117.678 1.00 52.60 ? 114 VAL A C 1 ATOM 618 O O . VAL A 1 86 ? 6.627 24.871 116.486 1.00 54.64 ? 114 VAL A O 1 ATOM 619 C CB . VAL A 1 86 ? 4.917 26.125 118.671 1.00 65.68 ? 114 VAL A CB 1 ATOM 620 C CG1 . VAL A 1 86 ? 4.501 27.029 119.808 1.00 56.91 ? 114 VAL A CG1 1 ATOM 621 C CG2 . VAL A 1 86 ? 4.315 26.652 117.372 1.00 74.29 ? 114 VAL A CG2 1 ATOM 622 N N . VAL A 1 87 ? 7.675 23.996 118.267 1.00 52.07 ? 115 VAL A N 1 ATOM 623 C CA . VAL A 1 87 ? 8.239 22.857 117.554 1.00 58.73 ? 115 VAL A CA 1 ATOM 624 C C . VAL A 1 87 ? 7.171 22.003 116.873 1.00 70.57 ? 115 VAL A C 1 ATOM 625 O O . VAL A 1 87 ? 6.127 21.714 117.456 1.00 69.72 ? 115 VAL A O 1 ATOM 626 C CB . VAL A 1 87 ? 9.027 21.950 118.498 1.00 56.34 ? 115 VAL A CB 1 ATOM 627 C CG1 . VAL A 1 87 ? 9.616 20.772 117.734 1.00 56.26 ? 115 VAL A CG1 1 ATOM 628 C CG2 . VAL A 1 87 ? 10.098 22.734 119.191 1.00 51.60 ? 115 VAL A CG2 1 ATOM 629 N N . GLN A 1 88 ? 7.421 21.651 115.619 1.00 72.99 ? 116 GLN A N 1 ATOM 630 C CA . GLN A 1 88 ? 6.486 20.850 114.849 1.00 77.85 ? 116 GLN A CA 1 ATOM 631 C C . GLN A 1 88 ? 6.859 19.368 114.765 1.00 82.52 ? 116 GLN A C 1 ATOM 632 O O . GLN A 1 88 ? 7.998 19.001 115.072 1.00 79.76 ? 116 GLN A O 1 ATOM 633 C CB . GLN A 1 88 ? 6.304 21.485 113.475 1.00 77.57 ? 116 GLN A CB 1 ATOM 634 C CG . GLN A 1 88 ? 5.909 22.931 113.595 1.00 82.12 ? 116 GLN A CG 1 ATOM 635 C CD . GLN A 1 88 ? 4.515 23.107 114.187 1.00 85.91 ? 116 GLN A CD 1 ATOM 636 O OE1 . GLN A 1 88 ? 4.234 22.662 115.306 1.00 78.16 ? 116 GLN A OE1 1 ATOM 637 N NE2 . GLN A 1 88 ? 3.637 23.771 113.441 1.00 90.12 ? 116 GLN A NE2 1 ATOM 638 N N . PRO A 1 89 ? 5.886 18.516 114.361 1.00 82.02 ? 117 PRO A N 1 ATOM 639 C CA . PRO A 1 89 ? 6.074 17.069 114.230 1.00 80.29 ? 117 PRO A CA 1 ATOM 640 C C . PRO A 1 89 ? 7.449 16.636 113.746 1.00 75.91 ? 117 PRO A C 1 ATOM 641 O O . PRO A 1 89 ? 8.091 15.846 114.444 1.00 83.81 ? 117 PRO A O 1 ATOM 642 C CB . PRO A 1 89 ? 5.016 16.688 113.193 1.00 78.12 ? 117 PRO A CB 1 ATOM 643 C CG . PRO A 1 89 ? 3.912 17.680 113.399 1.00 74.58 ? 117 PRO A CG 1 ATOM 644 C CD . PRO A 1 89 ? 4.481 18.888 114.097 1.00 77.42 ? 117 PRO A CD 1 ATOM 645 N N . GLN A 1 90 ? 7.897 17.152 112.608 1.00 61.64 ? 118 GLN A N 1 ATOM 646 C CA . GLN A 1 90 ? 9.196 16.776 112.055 1.00 62.80 ? 118 GLN A CA 1 ATOM 647 C C . GLN A 1 90 ? 10.168 17.953 111.936 1.00 70.31 ? 118 GLN A C 1 ATOM 648 O O . GLN A 1 90 ? 10.795 18.144 110.901 1.00 67.05 ? 118 GLN A O 1 ATOM 649 C CB . GLN A 1 90 ? 9.056 16.047 110.714 1.00 68.25 ? 118 GLN A CB 1 ATOM 650 C CG . GLN A 1 90 ? 7.697 16.193 110.038 1.00 77.53 ? 118 GLN A CG 1 ATOM 651 C CD . GLN A 1 90 ? 7.578 15.348 108.772 1.00 83.50 ? 118 GLN A CD 1 ATOM 652 O OE1 . GLN A 1 90 ? 8.582 14.970 108.169 1.00 85.40 ? 118 GLN A OE1 1 ATOM 653 N NE2 . GLN A 1 90 ? 6.346 15.034 108.377 1.00 86.29 ? 118 GLN A NE2 1 ATOM 654 N N . ASP A 1 91 ? 10.270 18.746 112.998 1.00 70.17 ? 119 ASP A N 1 ATOM 655 C CA . ASP A 1 91 ? 11.184 19.876 113.035 1.00 57.01 ? 119 ASP A CA 1 ATOM 656 C C . ASP A 1 91 ? 12.490 19.456 113.664 1.00 65.44 ? 119 ASP A C 1 ATOM 657 O O . ASP A 1 91 ? 12.522 18.550 114.496 1.00 73.01 ? 119 ASP A O 1 ATOM 658 C CB . ASP A 1 91 ? 10.615 21.030 113.857 1.00 51.94 ? 119 ASP A CB 1 ATOM 659 C CG . ASP A 1 91 ? 9.838 22.012 113.020 1.00 46.42 ? 119 ASP A CG 1 ATOM 660 O OD1 . ASP A 1 91 ? 9.874 21.902 111.779 1.00 44.43 ? 119 ASP A OD1 1 ATOM 661 O OD2 . ASP A 1 91 ? 9.200 22.909 113.601 1.00 43.45 ? 119 ASP A OD2 1 ATOM 662 N N . GLY A 1 92 ? 13.570 20.101 113.233 1.00 68.06 ? 120 GLY A N 1 ATOM 663 C CA . GLY A 1 92 ? 14.873 19.998 113.865 1.00 62.47 ? 120 GLY A CA 1 ATOM 664 C C . GLY A 1 92 ? 15.388 21.409 114.067 1.00 66.44 ? 120 GLY A C 1 ATOM 665 O O . GLY A 1 92 ? 15.100 22.292 113.256 1.00 63.93 ? 120 GLY A O 1 ATOM 666 N N . LEU A 1 93 ? 16.168 21.610 115.124 1.00 60.89 ? 121 LEU A N 1 ATOM 667 C CA . LEU A 1 93 ? 16.668 22.924 115.493 1.00 51.61 ? 121 LEU A CA 1 ATOM 668 C C . LEU A 1 93 ? 17.358 23.571 114.301 1.00 57.78 ? 121 LEU A C 1 ATOM 669 O O . LEU A 1 93 ? 17.151 24.744 114.014 1.00 57.94 ? 121 LEU A O 1 ATOM 670 C CB . LEU A 1 93 ? 17.662 22.794 116.636 1.00 44.04 ? 121 LEU A CB 1 ATOM 671 C CG . LEU A 1 93 ? 17.021 22.633 118.011 1.00 48.85 ? 121 LEU A CG 1 ATOM 672 C CD1 . LEU A 1 93 ? 18.087 22.664 119.084 1.00 57.12 ? 121 LEU A CD1 1 ATOM 673 C CD2 . LEU A 1 93 ? 15.908 23.661 118.282 1.00 49.31 ? 121 LEU A CD2 1 ATOM 674 N N . ASP A 1 94 ? 18.160 22.781 113.601 1.00 54.82 ? 122 ASP A N 1 ATOM 675 C CA . ASP A 1 94 ? 18.924 23.253 112.451 1.00 52.10 ? 122 ASP A CA 1 ATOM 676 C C . ASP A 1 94 ? 18.020 23.634 111.287 1.00 52.99 ? 122 ASP A C 1 ATOM 677 O O . ASP A 1 94 ? 18.305 24.582 110.568 1.00 55.34 ? 122 ASP A O 1 ATOM 678 C CB . ASP A 1 94 ? 19.905 22.179 112.004 1.00 45.13 ? 122 ASP A CB 1 ATOM 679 C CG . ASP A 1 94 ? 20.899 22.680 110.980 1.00 48.93 ? 122 ASP A CG 1 ATOM 680 O OD1 . ASP A 1 94 ? 21.844 23.386 111.390 1.00 45.66 ? 122 ASP A OD1 1 ATOM 681 O OD2 . ASP A 1 94 ? 20.757 22.344 109.777 1.00 48.36 ? 122 ASP A OD2 1 ATOM 682 N N . ALA A 1 95 ? 16.957 22.869 111.070 1.00 48.67 ? 123 ALA A N 1 ATOM 683 C CA . ALA A 1 95 ? 16.004 23.207 110.021 1.00 48.65 ? 123 ALA A CA 1 ATOM 684 C C . ALA A 1 95 ? 15.181 24.452 110.396 1.00 51.67 ? 123 ALA A C 1 ATOM 685 O O . ALA A 1 95 ? 14.832 25.256 109.542 1.00 52.88 ? 123 ALA A O 1 ATOM 686 C CB . ALA A 1 95 ? 15.086 22.036 109.734 1.00 44.72 ? 123 ALA A CB 1 ATOM 687 N N . ILE A 1 96 ? 14.867 24.606 111.674 1.00 45.08 ? 124 ILE A N 1 ATOM 688 C CA . ILE A 1 96 ? 14.158 25.785 112.142 1.00 42.46 ? 124 ILE A CA 1 ATOM 689 C C . ILE A 1 96 ? 15.033 27.028 111.968 1.00 43.76 ? 124 ILE A C 1 ATOM 690 O O . ILE A 1 96 ? 14.613 28.016 111.382 1.00 44.17 ? 124 ILE A O 1 ATOM 691 C CB . ILE A 1 96 ? 13.804 25.648 113.618 1.00 44.87 ? 124 ILE A CB 1 ATOM 692 C CG1 . ILE A 1 96 ? 12.773 24.522 113.810 1.00 46.30 ? 124 ILE A CG1 1 ATOM 693 C CG2 . ILE A 1 96 ? 13.287 27.002 114.161 1.00 43.99 ? 124 ILE A CG2 1 ATOM 694 C CD1 . ILE A 1 96 ? 12.674 23.989 115.231 1.00 33.66 ? 124 ILE A CD1 1 ATOM 695 N N . ALA A 1 97 ? 16.262 26.935 112.454 1.00 36.33 ? 125 ALA A N 1 ATOM 696 C CA . ALA A 1 97 ? 17.248 27.970 112.319 1.00 30.95 ? 125 ALA A CA 1 ATOM 697 C C . ALA A 1 97 ? 17.432 28.401 110.857 1.00 50.12 ? 125 ALA A C 1 ATOM 698 O O . ALA A 1 97 ? 17.367 29.596 110.534 1.00 52.28 ? 125 ALA A O 1 ATOM 699 C CB . ALA A 1 97 ? 18.576 27.486 112.910 1.00 31.50 ? 125 ALA A CB 1 ATOM 700 N N . ARG A 1 98 ? 17.626 27.428 109.971 1.00 48.64 ? 126 ARG A N 1 ATOM 701 C CA . ARG A 1 98 ? 17.960 27.720 108.578 1.00 40.80 ? 126 ARG A CA 1 ATOM 702 C C . ARG A 1 98 ? 16.778 27.980 107.652 1.00 41.49 ? 126 ARG A C 1 ATOM 703 O O . ARG A 1 98 ? 16.854 28.829 106.773 1.00 46.87 ? 126 ARG A O 1 ATOM 704 C CB . ARG A 1 98 ? 18.810 26.599 107.995 1.00 39.54 ? 126 ARG A CB 1 ATOM 705 C CG . ARG A 1 98 ? 20.116 26.407 108.707 1.00 46.63 ? 126 ARG A CG 1 ATOM 706 C CD . ARG A 1 98 ? 21.010 25.435 107.971 1.00 38.51 ? 126 ARG A CD 1 ATOM 707 N NE . ARG A 1 98 ? 22.384 25.914 108.008 1.00 44.01 ? 126 ARG A NE 1 ATOM 708 C CZ . ARG A 1 98 ? 23.211 25.662 109.007 1.00 46.02 ? 126 ARG A CZ 1 ATOM 709 N NH1 . ARG A 1 98 ? 22.786 24.929 110.025 1.00 55.79 ? 126 ARG A NH1 1 ATOM 710 N NH2 . ARG A 1 98 ? 24.452 26.137 108.993 1.00 38.31 ? 126 ARG A NH2 1 ATOM 711 N N . ASN A 1 99 ? 15.715 27.204 107.817 1.00 43.96 ? 127 ASN A N 1 ATOM 712 C CA . ASN A 1 99 ? 14.566 27.242 106.922 1.00 36.27 ? 127 ASN A CA 1 ATOM 713 C C . ASN A 1 99 ? 13.443 28.148 107.397 1.00 33.83 ? 127 ASN A C 1 ATOM 714 O O . ASN A 1 99 ? 12.557 28.498 106.616 1.00 45.33 ? 127 ASN A O 1 ATOM 715 C CB . ASN A 1 99 ? 14.036 25.829 106.659 1.00 42.87 ? 127 ASN A CB 1 ATOM 716 C CG . ASN A 1 99 ? 15.129 24.886 106.188 1.00 49.88 ? 127 ASN A CG 1 ATOM 717 O OD1 . ASN A 1 99 ? 16.030 25.289 105.469 1.00 43.14 ? 127 ASN A OD1 1 ATOM 718 N ND2 . ASN A 1 99 ? 15.081 23.637 106.644 1.00 59.04 ? 127 ASN A ND2 1 ATOM 719 N N . VAL A 1 100 ? 13.431 28.473 108.687 1.00 29.54 ? 128 VAL A N 1 ATOM 720 C CA . VAL A 1 100 ? 12.446 29.435 109.189 1.00 43.41 ? 128 VAL A CA 1 ATOM 721 C C . VAL A 1 100 ? 13.042 30.834 109.471 1.00 42.35 ? 128 VAL A C 1 ATOM 722 O O . VAL A 1 100 ? 12.446 31.856 109.133 1.00 39.60 ? 128 VAL A O 1 ATOM 723 C CB . VAL A 1 100 ? 11.727 28.904 110.432 1.00 43.88 ? 128 VAL A CB 1 ATOM 724 C CG1 . VAL A 1 100 ? 10.555 29.815 110.797 1.00 33.32 ? 128 VAL A CG1 1 ATOM 725 C CG2 . VAL A 1 100 ? 11.231 27.498 110.162 1.00 38.91 ? 128 VAL A CG2 1 ATOM 726 N N . PHE A 1 101 ? 14.230 30.868 110.064 1.00 37.83 ? 129 PHE A N 1 ATOM 727 C CA . PHE A 1 101 ? 14.827 32.123 110.489 1.00 27.39 ? 129 PHE A CA 1 ATOM 728 C C . PHE A 1 101 ? 16.106 32.507 109.737 1.00 38.64 ? 129 PHE A C 1 ATOM 729 O O . PHE A 1 101 ? 17.015 33.157 110.299 1.00 33.70 ? 129 PHE A O 1 ATOM 730 C CB . PHE A 1 101 ? 15.027 32.102 111.998 1.00 31.60 ? 129 PHE A CB 1 ATOM 731 C CG . PHE A 1 101 ? 13.746 31.937 112.745 1.00 38.03 ? 129 PHE A CG 1 ATOM 732 C CD1 . PHE A 1 101 ? 12.863 32.997 112.867 1.00 33.09 ? 129 PHE A CD1 1 ATOM 733 C CD2 . PHE A 1 101 ? 13.390 30.702 113.280 1.00 40.39 ? 129 PHE A CD2 1 ATOM 734 C CE1 . PHE A 1 101 ? 11.664 32.853 113.528 1.00 32.42 ? 129 PHE A CE1 1 ATOM 735 C CE2 . PHE A 1 101 ? 12.186 30.537 113.950 1.00 32.29 ? 129 PHE A CE2 1 ATOM 736 C CZ . PHE A 1 101 ? 11.320 31.614 114.080 1.00 39.17 ? 129 PHE A CZ 1 ATOM 737 N N . ASN A 1 102 ? 16.177 32.084 108.472 1.00 33.53 ? 130 ASN A N 1 ATOM 738 C CA . ASN A 1 102 ? 17.179 32.598 107.558 1.00 34.59 ? 130 ASN A CA 1 ATOM 739 C C . ASN A 1 102 ? 18.601 32.305 108.028 1.00 29.60 ? 130 ASN A C 1 ATOM 740 O O . ASN A 1 102 ? 19.544 32.947 107.582 1.00 30.18 ? 130 ASN A O 1 ATOM 741 C CB . ASN A 1 102 ? 17.032 34.139 107.430 1.00 34.18 ? 130 ASN A CB 1 ATOM 742 C CG . ASN A 1 102 ? 15.757 34.583 106.725 1.00 36.10 ? 130 ASN A CG 1 ATOM 743 O OD1 . ASN A 1 102 ? 15.517 35.783 106.584 1.00 46.06 ? 130 ASN A OD1 1 ATOM 744 N ND2 . ASN A 1 102 ? 14.955 33.639 106.257 1.00 29.29 ? 130 ASN A ND2 1 ATOM 745 N N . ALA A 1 103 ? 18.754 31.339 108.924 1.00 37.52 ? 131 ALA A N 1 ATOM 746 C CA . ALA A 1 103 ? 20.035 31.115 109.602 1.00 40.77 ? 131 ALA A CA 1 ATOM 747 C C . ALA A 1 103 ? 20.578 32.376 110.299 1.00 43.09 ? 131 ALA A C 1 ATOM 748 O O . ALA A 1 103 ? 21.792 32.515 110.465 1.00 41.34 ? 131 ALA A O 1 ATOM 749 C CB . ALA A 1 103 ? 21.085 30.536 108.635 1.00 20.70 ? 131 ALA A CB 1 ATOM 750 N N . PHE A 1 104 ? 19.689 33.273 110.733 1.00 32.58 ? 132 PHE A N 1 ATOM 751 C CA . PHE A 1 104 ? 20.126 34.399 111.564 1.00 28.67 ? 132 PHE A CA 1 ATOM 752 C C . PHE A 1 104 ? 20.646 33.904 112.899 1.00 34.27 ? 132 PHE A C 1 ATOM 753 O O . PHE A 1 104 ? 21.392 34.603 113.575 1.00 36.12 ? 132 PHE A O 1 ATOM 754 C CB . PHE A 1 104 ? 19.015 35.442 111.791 1.00 24.81 ? 132 PHE A CB 1 ATOM 755 C CG . PHE A 1 104 ? 18.837 36.386 110.649 1.00 22.89 ? 132 PHE A CG 1 ATOM 756 C CD1 . PHE A 1 104 ? 19.901 37.166 110.210 1.00 26.31 ? 132 PHE A CD1 1 ATOM 757 C CD2 . PHE A 1 104 ? 17.607 36.517 110.024 1.00 23.52 ? 132 PHE A CD2 1 ATOM 758 C CE1 . PHE A 1 104 ? 19.753 38.052 109.142 1.00 23.54 ? 132 PHE A CE1 1 ATOM 759 C CE2 . PHE A 1 104 ? 17.451 37.393 108.954 1.00 25.21 ? 132 PHE A CE2 1 ATOM 760 C CZ . PHE A 1 104 ? 18.525 38.166 108.517 1.00 27.06 ? 132 PHE A CZ 1 ATOM 761 N N . VAL A 1 105 ? 20.215 32.710 113.296 1.00 36.21 ? 133 VAL A N 1 ATOM 762 C CA . VAL A 1 105 ? 20.790 32.037 114.455 1.00 34.80 ? 133 VAL A CA 1 ATOM 763 C C . VAL A 1 105 ? 21.260 30.637 114.068 1.00 48.63 ? 133 VAL A C 1 ATOM 764 O O . VAL A 1 105 ? 20.759 30.058 113.100 1.00 54.28 ? 133 VAL A O 1 ATOM 765 C CB . VAL A 1 105 ? 19.770 31.895 115.585 1.00 36.06 ? 133 VAL A CB 1 ATOM 766 C CG1 . VAL A 1 105 ? 19.238 33.267 115.984 1.00 35.43 ? 133 VAL A CG1 1 ATOM 767 C CG2 . VAL A 1 105 ? 18.621 30.979 115.158 1.00 25.36 ? 133 VAL A CG2 1 ATOM 768 N N . THR A 1 106 ? 22.194 30.074 114.831 1.00 51.29 ? 134 THR A N 1 ATOM 769 C CA . THR A 1 106 ? 22.540 28.655 114.661 1.00 48.73 ? 134 THR A CA 1 ATOM 770 C C . THR A 1 106 ? 21.750 27.808 115.631 1.00 42.61 ? 134 THR A C 1 ATOM 771 O O . THR A 1 106 ? 21.181 28.325 116.599 1.00 42.94 ? 134 THR A O 1 ATOM 772 C CB . THR A 1 106 ? 24.005 28.392 114.952 1.00 41.11 ? 134 THR A CB 1 ATOM 773 O OG1 . THR A 1 106 ? 24.242 28.640 116.342 1.00 51.58 ? 134 THR A OG1 1 ATOM 774 C CG2 . THR A 1 106 ? 24.879 29.298 114.130 1.00 28.78 ? 134 THR A CG2 1 ATOM 775 N N . TYR A 1 107 ? 21.723 26.501 115.391 1.00 43.29 ? 135 TYR A N 1 ATOM 776 C CA . TYR A 1 107 ? 20.968 25.602 116.276 1.00 38.85 ? 135 TYR A CA 1 ATOM 777 C C . TYR A 1 107 ? 21.596 25.573 117.659 1.00 33.96 ? 135 TYR A C 1 ATOM 778 O O . TYR A 1 107 ? 20.900 25.391 118.666 1.00 48.34 ? 135 TYR A O 1 ATOM 779 C CB . TYR A 1 107 ? 20.829 24.190 115.666 1.00 55.19 ? 135 TYR A CB 1 ATOM 780 C CG . TYR A 1 107 ? 22.123 23.405 115.645 1.00 57.87 ? 135 TYR A CG 1 ATOM 781 C CD1 . TYR A 1 107 ? 22.586 22.751 116.780 1.00 63.70 ? 135 TYR A CD1 1 ATOM 782 C CD2 . TYR A 1 107 ? 22.882 23.324 114.487 1.00 51.79 ? 135 TYR A CD2 1 ATOM 783 C CE1 . TYR A 1 107 ? 23.772 22.047 116.763 1.00 70.73 ? 135 TYR A CE1 1 ATOM 784 C CE2 . TYR A 1 107 ? 24.071 22.625 114.456 1.00 56.13 ? 135 TYR A CE2 1 ATOM 785 C CZ . TYR A 1 107 ? 24.511 21.986 115.599 1.00 69.55 ? 135 TYR A CZ 1 ATOM 786 O OH . TYR A 1 107 ? 25.690 21.280 115.586 1.00 76.97 ? 135 TYR A OH 1 ATOM 787 N N . GLN A 1 108 ? 22.910 25.792 117.703 1.00 36.93 ? 136 GLN A N 1 ATOM 788 C CA . GLN A 1 108 ? 23.636 25.937 118.962 1.00 44.39 ? 136 GLN A CA 1 ATOM 789 C C . GLN A 1 108 ? 23.102 27.118 119.772 1.00 61.50 ? 136 GLN A C 1 ATOM 790 O O . GLN A 1 108 ? 22.861 26.995 120.975 1.00 76.72 ? 136 GLN A O 1 ATOM 791 C CB . GLN A 1 108 ? 25.124 26.186 118.705 1.00 53.03 ? 136 GLN A CB 1 ATOM 792 C CG . GLN A 1 108 ? 25.911 25.077 118.022 1.00 59.29 ? 136 GLN A CG 1 ATOM 793 C CD . GLN A 1 108 ? 25.868 25.159 116.506 1.00 62.70 ? 136 GLN A CD 1 ATOM 794 O OE1 . GLN A 1 108 ? 24.864 25.551 115.925 1.00 71.97 ? 136 GLN A OE1 1 ATOM 795 N NE2 . GLN A 1 108 ? 26.986 24.846 115.865 1.00 57.37 ? 136 GLN A NE2 1 ATOM 796 N N . GLU A 1 109 ? 22.907 28.261 119.112 1.00 54.95 ? 137 GLU A N 1 ATOM 797 C CA . GLU A 1 109 ? 22.361 29.436 119.789 1.00 51.45 ? 137 GLU A CA 1 ATOM 798 C C . GLU A 1 109 ? 20.947 29.187 120.239 1.00 38.52 ? 137 GLU A C 1 ATOM 799 O O . GLU A 1 109 ? 20.553 29.630 121.306 1.00 49.99 ? 137 GLU A O 1 ATOM 800 C CB . GLU A 1 109 ? 22.428 30.694 118.909 1.00 53.11 ? 137 GLU A CB 1 ATOM 801 C CG . GLU A 1 109 ? 23.834 31.218 118.750 1.00 51.24 ? 137 GLU A CG 1 ATOM 802 C CD . GLU A 1 109 ? 23.972 32.181 117.595 1.00 50.92 ? 137 GLU A CD 1 ATOM 803 O OE1 . GLU A 1 109 ? 23.101 32.174 116.698 1.00 51.11 ? 137 GLU A OE1 1 ATOM 804 O OE2 . GLU A 1 109 ? 24.991 32.896 117.548 1.00 44.43 ? 137 GLU A OE2 1 ATOM 805 N N . ILE A 1 110 ? 20.161 28.508 119.412 1.00 33.73 ? 138 ILE A N 1 ATOM 806 C CA . ILE A 1 110 ? 18.823 28.151 119.862 1.00 46.11 ? 138 ILE A CA 1 ATOM 807 C C . ILE A 1 110 ? 18.925 27.184 121.039 1.00 54.93 ? 138 ILE A C 1 ATOM 808 O O . ILE A 1 110 ? 18.086 27.189 121.935 1.00 53.83 ? 138 ILE A O 1 ATOM 809 C CB . ILE A 1 110 ? 17.977 27.534 118.748 1.00 47.77 ? 138 ILE A CB 1 ATOM 810 C CG1 . ILE A 1 110 ? 17.977 28.458 117.532 1.00 38.50 ? 138 ILE A CG1 1 ATOM 811 C CG2 . ILE A 1 110 ? 16.558 27.262 119.253 1.00 43.69 ? 138 ILE A CG2 1 ATOM 812 C CD1 . ILE A 1 110 ? 17.122 27.970 116.407 1.00 41.53 ? 138 ILE A CD1 1 ATOM 813 N N . ALA A 1 111 ? 19.975 26.369 121.039 1.00 59.23 ? 139 ALA A N 1 ATOM 814 C CA . ALA A 1 111 ? 20.182 25.422 122.121 1.00 61.06 ? 139 ALA A CA 1 ATOM 815 C C . ALA A 1 111 ? 20.511 26.137 123.436 1.00 54.93 ? 139 ALA A C 1 ATOM 816 O O . ALA A 1 111 ? 19.825 25.945 124.449 1.00 44.96 ? 139 ALA A O 1 ATOM 817 C CB . ALA A 1 111 ? 21.269 24.412 121.754 1.00 58.66 ? 139 ALA A CB 1 ATOM 818 N N . ALA A 1 112 ? 21.538 26.983 123.409 1.00 48.41 ? 140 ALA A N 1 ATOM 819 C CA . ALA A 1 112 ? 21.957 27.693 124.617 1.00 55.31 ? 140 ALA A CA 1 ATOM 820 C C . ALA A 1 112 ? 20.848 28.569 125.197 1.00 60.62 ? 140 ALA A C 1 ATOM 821 O O . ALA A 1 112 ? 20.644 28.591 126.410 1.00 65.79 ? 140 ALA A O 1 ATOM 822 C CB . ALA A 1 112 ? 23.194 28.532 124.335 1.00 52.93 ? 140 ALA A CB 1 ATOM 823 N N . ALA A 1 113 ? 20.101 29.238 124.322 1.00 55.90 ? 141 ALA A N 1 ATOM 824 C CA . ALA A 1 113 ? 19.045 30.158 124.732 1.00 52.14 ? 141 ALA A CA 1 ATOM 825 C C . ALA A 1 113 ? 17.860 29.498 125.443 1.00 57.27 ? 141 ALA A C 1 ATOM 826 O O . ALA A 1 113 ? 17.193 30.130 126.262 1.00 55.17 ? 141 ALA A O 1 ATOM 827 C CB . ALA A 1 113 ? 18.553 30.952 123.523 1.00 45.76 ? 141 ALA A CB 1 ATOM 828 N N . ASN A 1 114 ? 17.577 28.241 125.134 1.00 66.44 ? 142 ASN A N 1 ATOM 829 C CA . ASN A 1 114 ? 16.419 27.601 125.747 1.00 58.87 ? 142 ASN A CA 1 ATOM 830 C C . ASN A 1 114 ? 16.802 26.627 126.850 1.00 63.16 ? 142 ASN A C 1 ATOM 831 O O . ASN A 1 114 ? 15.972 25.854 127.327 1.00 61.41 ? 142 ASN A O 1 ATOM 832 C CB . ASN A 1 114 ? 15.548 26.936 124.687 1.00 55.69 ? 142 ASN A CB 1 ATOM 833 C CG . ASN A 1 114 ? 14.917 27.940 123.744 1.00 55.68 ? 142 ASN A CG 1 ATOM 834 O OD1 . ASN A 1 114 ? 13.830 28.455 124.003 1.00 51.98 ? 142 ASN A OD1 1 ATOM 835 N ND2 . ASN A 1 114 ? 15.599 28.222 122.636 1.00 54.72 ? 142 ASN A ND2 1 ATOM 836 N N . ASN A 1 115 ? 18.073 26.687 127.242 1.00 74.08 ? 143 ASN A N 1 ATOM 837 C CA . ASN A 1 115 ? 18.641 25.962 128.390 1.00 84.21 ? 143 ASN A CA 1 ATOM 838 C C . ASN A 1 115 ? 18.455 24.456 128.444 1.00 87.59 ? 143 ASN A C 1 ATOM 839 O O . ASN A 1 115 ? 19.366 23.734 128.839 1.00 88.56 ? 143 ASN A O 1 ATOM 840 C CB . ASN A 1 115 ? 18.089 26.545 129.698 1.00 87.60 ? 143 ASN A CB 1 ATOM 841 C CG . ASN A 1 115 ? 18.866 27.753 130.170 1.00 87.12 ? 143 ASN A CG 1 ATOM 842 O OD1 . ASN A 1 115 ? 20.045 27.915 129.843 1.00 85.16 ? 143 ASN A OD1 1 ATOM 843 N ND2 . ASN A 1 115 ? 18.207 28.617 130.939 1.00 87.09 ? 143 ASN A ND2 1 ATOM 844 N N . ILE A 1 116 ? 17.284 23.987 128.037 1.00 95.07 ? 144 ILE A N 1 ATOM 845 C CA . ILE A 1 116 ? 16.977 22.564 128.051 1.00 105.98 ? 144 ILE A CA 1 ATOM 846 C C . ILE A 1 116 ? 17.829 21.761 127.050 1.00 107.75 ? 144 ILE A C 1 ATOM 847 O O . ILE A 1 116 ? 18.208 20.617 127.337 1.00 105.11 ? 144 ILE A O 1 ATOM 848 C CB . ILE A 1 116 ? 15.464 22.317 127.801 1.00 100.18 ? 144 ILE A CB 1 ATOM 849 C CG1 . ILE A 1 116 ? 14.623 23.130 128.797 1.00 98.46 ? 144 ILE A CG1 1 ATOM 850 C CG2 . ILE A 1 116 ? 15.139 20.833 127.896 1.00 99.94 ? 144 ILE A CG2 1 ATOM 851 C CD1 . ILE A 1 116 ? 13.123 22.952 128.642 1.00 95.76 ? 144 ILE A CD1 1 ATOM 852 N N . PRO A 1 117 ? 18.132 22.338 125.869 1.00 102.98 ? 145 PRO A N 1 ATOM 853 C CA . PRO A 1 117 ? 18.997 21.496 125.037 1.00 100.53 ? 145 PRO A CA 1 ATOM 854 C C . PRO A 1 117 ? 20.480 21.564 125.402 1.00 103.12 ? 145 PRO A C 1 ATOM 855 O O . PRO A 1 117 ? 21.077 22.638 125.460 1.00 107.50 ? 145 PRO A O 1 ATOM 856 C CB . PRO A 1 117 ? 18.752 22.006 123.612 1.00 96.77 ? 145 PRO A CB 1 ATOM 857 C CG . PRO A 1 117 ? 17.874 23.189 123.719 1.00 95.33 ? 145 PRO A CG 1 ATOM 858 C CD . PRO A 1 117 ? 17.603 23.504 125.140 1.00 97.19 ? 145 PRO A CD 1 ATOM 859 N N . ASP A 1 118 ? 21.049 20.393 125.665 1.00 102.12 ? 146 ASP A N 1 ATOM 860 C CA . ASP A 1 118 ? 22.487 20.216 125.777 1.00 97.78 ? 146 ASP A CA 1 ATOM 861 C C . ASP A 1 118 ? 22.872 19.334 124.599 1.00 100.60 ? 146 ASP A C 1 ATOM 862 O O . ASP A 1 118 ? 23.960 19.478 124.046 1.00 102.73 ? 146 ASP A O 1 ATOM 863 C CB . ASP A 1 118 ? 22.874 19.603 127.119 1.00 96.59 ? 146 ASP A CB 1 ATOM 864 C CG . ASP A 1 118 ? 21.688 19.454 128.045 1.00 97.29 ? 146 ASP A CG 1 ATOM 865 O OD1 . ASP A 1 118 ? 21.855 19.649 129.269 1.00 102.26 ? 146 ASP A OD1 1 ATOM 866 O OD2 . ASP A 1 118 ? 20.588 19.142 127.544 1.00 91.59 ? 146 ASP A OD2 1 ATOM 867 N N . PRO A 1 119 ? 21.993 18.378 124.239 1.00 104.66 ? 147 PRO A N 1 ATOM 868 C CA . PRO A 1 119 ? 22.082 17.860 122.875 1.00 103.04 ? 147 PRO A CA 1 ATOM 869 C C . PRO A 1 119 ? 20.781 18.216 122.160 1.00 99.16 ? 147 PRO A C 1 ATOM 870 O O . PRO A 1 119 ? 19.884 18.779 122.784 1.00 93.77 ? 147 PRO A O 1 ATOM 871 C CB . PRO A 1 119 ? 22.199 16.341 123.069 1.00 100.36 ? 147 PRO A CB 1 ATOM 872 C CG . PRO A 1 119 ? 21.830 16.082 124.532 1.00 103.65 ? 147 PRO A CG 1 ATOM 873 C CD . PRO A 1 119 ? 21.364 17.381 125.121 1.00 107.23 ? 147 PRO A CD 1 ATOM 874 N N . ASN A 1 120 ? 20.664 17.894 120.880 1.00 99.06 ? 148 ASN A N 1 ATOM 875 C CA . ASN A 1 120 ? 19.436 18.210 120.166 1.00 94.86 ? 148 ASN A CA 1 ATOM 876 C C . ASN A 1 120 ? 18.376 17.104 120.223 1.00 90.39 ? 148 ASN A C 1 ATOM 877 O O . ASN A 1 120 ? 18.276 16.215 119.362 1.00 69.64 ? 148 ASN A O 1 ATOM 878 C CB . ASN A 1 120 ? 19.760 18.649 118.749 1.00 95.69 ? 148 ASN A CB 1 ATOM 879 C CG . ASN A 1 120 ? 20.972 19.542 118.708 1.00 99.83 ? 148 ASN A CG 1 ATOM 880 O OD1 . ASN A 1 120 ? 21.358 20.129 119.727 1.00 87.04 ? 148 ASN A OD1 1 ATOM 881 N ND2 . ASN A 1 120 ? 21.575 19.669 117.532 1.00 108.65 ? 148 ASN A ND2 1 ATOM 882 N N . LYS A 1 121 ? 17.638 17.157 121.324 1.00 93.47 ? 149 LYS A N 1 ATOM 883 C CA . LYS A 1 121 ? 16.539 16.261 121.593 1.00 97.55 ? 149 LYS A CA 1 ATOM 884 C C . LYS A 1 121 ? 15.383 17.186 121.969 1.00 83.77 ? 149 LYS A C 1 ATOM 885 O O . LYS A 1 121 ? 15.456 17.881 122.982 1.00 84.71 ? 149 LYS A O 1 ATOM 886 C CB . LYS A 1 121 ? 16.938 15.302 122.721 1.00 115.31 ? 149 LYS A CB 1 ATOM 887 C CG . LYS A 1 121 ? 18.448 14.992 122.713 1.00 127.02 ? 149 LYS A CG 1 ATOM 888 C CD . LYS A 1 121 ? 18.787 14.058 121.548 1.00 134.37 ? 149 LYS A CD 1 ATOM 889 C CE . LYS A 1 121 ? 20.283 13.995 121.242 1.00 135.73 ? 149 LYS A CE 1 ATOM 890 N NZ . LYS A 1 121 ? 21.085 13.323 122.295 1.00 135.16 ? 149 LYS A NZ 1 ATOM 891 N N . ILE A 1 122 ? 14.303 17.178 121.190 1.00 69.53 ? 150 ILE A N 1 ATOM 892 C CA . ILE A 1 122 ? 13.224 18.143 121.413 1.00 66.68 ? 150 ILE A CA 1 ATOM 893 C C . ILE A 1 122 ? 11.839 17.563 121.180 1.00 80.41 ? 150 ILE A C 1 ATOM 894 O O . ILE A 1 122 ? 11.687 16.549 120.501 1.00 83.47 ? 150 ILE A O 1 ATOM 895 C CB . ILE A 1 122 ? 13.352 19.380 120.470 1.00 88.07 ? 150 ILE A CB 1 ATOM 896 C CG1 . ILE A 1 122 ? 13.113 18.973 119.010 1.00 84.95 ? 150 ILE A CG1 1 ATOM 897 C CG2 . ILE A 1 122 ? 14.701 20.078 120.631 1.00 85.19 ? 150 ILE A CG2 1 ATOM 898 C CD1 . ILE A 1 122 ? 13.273 20.097 118.011 1.00 82.16 ? 150 ILE A CD1 1 ATOM 899 N N . ASN A 1 123 ? 10.828 18.195 121.765 1.00 81.79 ? 151 ASN A N 1 ATOM 900 C CA . ASN A 1 123 ? 9.467 17.688 121.651 1.00 81.06 ? 151 ASN A CA 1 ATOM 901 C C . ASN A 1 123 ? 8.508 18.615 120.921 1.00 73.09 ? 151 ASN A C 1 ATOM 902 O O . ASN A 1 123 ? 8.563 19.824 121.072 1.00 83.79 ? 151 ASN A O 1 ATOM 903 C CB . ASN A 1 123 ? 8.946 17.336 123.036 1.00 87.77 ? 151 ASN A CB 1 ATOM 904 C CG . ASN A 1 123 ? 9.532 16.039 123.541 1.00 93.81 ? 151 ASN A CG 1 ATOM 905 O OD1 . ASN A 1 123 ? 8.921 14.978 123.412 1.00 100.42 ? 151 ASN A OD1 1 ATOM 906 N ND2 . ASN A 1 123 ? 10.758 16.106 124.058 1.00 90.69 ? 151 ASN A ND2 1 ATOM 907 N N . VAL A 1 124 ? 7.629 18.028 120.127 1.00 68.88 ? 152 VAL A N 1 ATOM 908 C CA . VAL A 1 124 ? 6.611 18.765 119.386 1.00 70.38 ? 152 VAL A CA 1 ATOM 909 C C . VAL A 1 124 ? 5.721 19.635 120.284 1.00 76.19 ? 152 VAL A C 1 ATOM 910 O O . VAL A 1 124 ? 5.396 19.245 121.410 1.00 75.04 ? 152 VAL A O 1 ATOM 911 C CB . VAL A 1 124 ? 5.736 17.779 118.601 1.00 64.24 ? 152 VAL A CB 1 ATOM 912 C CG1 . VAL A 1 124 ? 4.643 18.506 117.823 1.00 68.15 ? 152 VAL A CG1 1 ATOM 913 C CG2 . VAL A 1 124 ? 6.608 16.952 117.671 1.00 64.70 ? 152 VAL A CG2 1 ATOM 914 N N . SER A 1 125 ? 5.384 20.828 119.788 1.00 73.46 ? 153 SER A N 1 ATOM 915 C CA . SER A 1 125 ? 4.488 21.785 120.459 1.00 69.40 ? 153 SER A CA 1 ATOM 916 C C . SER A 1 125 ? 5.137 22.506 121.640 1.00 62.52 ? 153 SER A C 1 ATOM 917 O O . SER A 1 125 ? 4.525 23.375 122.281 1.00 67.21 ? 153 SER A O 1 ATOM 918 C CB . SER A 1 125 ? 3.151 21.143 120.855 1.00 76.37 ? 153 SER A CB 1 ATOM 919 O OG . SER A 1 125 ? 2.119 22.109 120.847 1.00 77.55 ? 153 SER A OG 1 ATOM 920 N N . GLN A 1 126 ? 6.385 22.142 121.907 1.00 52.30 ? 154 GLN A N 1 ATOM 921 C CA . GLN A 1 126 ? 7.237 22.871 122.832 1.00 57.29 ? 154 GLN A CA 1 ATOM 922 C C . GLN A 1 126 ? 7.501 24.292 122.290 1.00 64.67 ? 154 GLN A C 1 ATOM 923 O O . GLN A 1 126 ? 7.593 24.492 121.075 1.00 58.05 ? 154 GLN A O 1 ATOM 924 C CB . GLN A 1 126 ? 8.560 22.125 122.981 1.00 56.93 ? 154 GLN A CB 1 ATOM 925 C CG . GLN A 1 126 ? 9.642 22.849 123.763 1.00 59.33 ? 154 GLN A CG 1 ATOM 926 C CD . GLN A 1 126 ? 10.947 22.085 123.749 1.00 61.56 ? 154 GLN A CD 1 ATOM 927 O OE1 . GLN A 1 126 ? 11.075 21.071 123.065 1.00 72.79 ? 154 GLN A OE1 1 ATOM 928 N NE2 . GLN A 1 126 ? 11.915 22.555 124.514 1.00 66.20 ? 154 GLN A NE2 1 ATOM 929 N N . THR A 1 127 ? 7.587 25.277 123.183 1.00 63.33 ? 155 THR A N 1 ATOM 930 C CA . THR A 1 127 ? 7.893 26.639 122.764 1.00 66.88 ? 155 THR A CA 1 ATOM 931 C C . THR A 1 127 ? 9.383 26.939 122.900 1.00 64.85 ? 155 THR A C 1 ATOM 932 O O . THR A 1 127 ? 9.999 26.671 123.936 1.00 61.15 ? 155 THR A O 1 ATOM 933 C CB . THR A 1 127 ? 7.132 27.684 123.581 1.00 65.15 ? 155 THR A CB 1 ATOM 934 O OG1 . THR A 1 127 ? 7.386 27.451 124.966 1.00 73.40 ? 155 THR A OG1 1 ATOM 935 C CG2 . THR A 1 127 ? 5.625 27.624 123.308 1.00 59.03 ? 155 THR A CG2 1 ATOM 936 N N . LEU A 1 128 ? 9.952 27.502 121.840 1.00 57.78 ? 156 LEU A N 1 ATOM 937 C CA . LEU A 1 128 ? 11.364 27.865 121.817 1.00 57.41 ? 156 LEU A CA 1 ATOM 938 C C . LEU A 1 128 ? 11.505 29.384 121.673 1.00 54.06 ? 156 LEU A C 1 ATOM 939 O O . LEU A 1 128 ? 10.805 30.012 120.867 1.00 50.03 ? 156 LEU A O 1 ATOM 940 C CB . LEU A 1 128 ? 12.077 27.176 120.649 1.00 60.04 ? 156 LEU A CB 1 ATOM 941 C CG . LEU A 1 128 ? 12.113 25.654 120.520 1.00 62.79 ? 156 LEU A CG 1 ATOM 942 C CD1 . LEU A 1 128 ? 12.661 25.253 119.157 1.00 58.70 ? 156 LEU A CD1 1 ATOM 943 C CD2 . LEU A 1 128 ? 12.968 25.061 121.625 1.00 59.49 ? 156 LEU A CD2 1 ATOM 944 N N . TRP A 1 129 ? 12.386 29.977 122.472 1.00 57.29 ? 157 TRP A N 1 ATOM 945 C CA . TRP A 1 129 ? 12.756 31.379 122.287 1.00 52.23 ? 157 TRP A CA 1 ATOM 946 C C . TRP A 1 129 ? 13.819 31.454 121.205 1.00 49.21 ? 157 TRP A C 1 ATOM 947 O O . TRP A 1 129 ? 14.890 30.875 121.355 1.00 48.20 ? 157 TRP A O 1 ATOM 948 C CB . TRP A 1 129 ? 13.320 31.969 123.583 1.00 51.18 ? 157 TRP A CB 1 ATOM 949 C CG . TRP A 1 129 ? 13.963 33.329 123.403 1.00 54.12 ? 157 TRP A CG 1 ATOM 950 C CD1 . TRP A 1 129 ? 13.557 34.327 122.549 1.00 50.87 ? 157 TRP A CD1 1 ATOM 951 C CD2 . TRP A 1 129 ? 15.145 33.823 124.059 1.00 56.00 ? 157 TRP A CD2 1 ATOM 952 N NE1 . TRP A 1 129 ? 14.393 35.410 122.654 1.00 55.95 ? 157 TRP A NE1 1 ATOM 953 C CE2 . TRP A 1 129 ? 15.378 35.136 123.569 1.00 53.88 ? 157 TRP A CE2 1 ATOM 954 C CE3 . TRP A 1 129 ? 16.020 33.294 125.023 1.00 47.98 ? 157 TRP A CE3 1 ATOM 955 C CZ2 . TRP A 1 129 ? 16.454 35.929 124.005 1.00 35.37 ? 157 TRP A CZ2 1 ATOM 956 C CZ3 . TRP A 1 129 ? 17.094 34.085 125.460 1.00 51.72 ? 157 TRP A CZ3 1 ATOM 957 C CH2 . TRP A 1 129 ? 17.302 35.392 124.943 1.00 39.77 ? 157 TRP A CH2 1 ATOM 958 N N . ILE A 1 130 ? 13.545 32.192 120.136 1.00 45.45 ? 158 ILE A N 1 ATOM 959 C CA . ILE A 1 130 ? 14.530 32.382 119.079 1.00 43.12 ? 158 ILE A CA 1 ATOM 960 C C . ILE A 1 130 ? 15.289 33.706 119.310 1.00 45.70 ? 158 ILE A C 1 ATOM 961 O O . ILE A 1 130 ? 14.722 34.785 119.171 1.00 38.75 ? 158 ILE A O 1 ATOM 962 C CB . ILE A 1 130 ? 13.839 32.408 117.696 1.00 39.44 ? 158 ILE A CB 1 ATOM 963 C CG1 . ILE A 1 130 ? 12.935 31.181 117.510 1.00 39.12 ? 158 ILE A CG1 1 ATOM 964 C CG2 . ILE A 1 130 ? 14.856 32.533 116.575 1.00 36.34 ? 158 ILE A CG2 1 ATOM 965 C CD1 . ILE A 1 130 ? 13.660 29.834 117.592 1.00 38.11 ? 158 ILE A CD1 1 ATOM 966 N N . PRO A 1 131 ? 16.580 33.627 119.657 1.00 39.98 ? 159 PRO A N 1 ATOM 967 C CA . PRO A 1 131 ? 17.355 34.841 119.936 1.00 37.84 ? 159 PRO A CA 1 ATOM 968 C C . PRO A 1 131 ? 17.909 35.521 118.678 1.00 32.83 ? 159 PRO A C 1 ATOM 969 O O . PRO A 1 131 ? 19.101 35.418 118.416 1.00 32.79 ? 159 PRO A O 1 ATOM 970 C CB . PRO A 1 131 ? 18.526 34.307 120.755 1.00 43.62 ? 159 PRO A CB 1 ATOM 971 C CG . PRO A 1 131 ? 18.759 32.927 120.171 1.00 41.00 ? 159 PRO A CG 1 ATOM 972 C CD . PRO A 1 131 ? 17.387 32.406 119.807 1.00 37.85 ? 159 PRO A CD 1 ATOM 973 N N . LEU A 1 132 ? 17.070 36.220 117.924 1.00 35.16 ? 160 LEU A N 1 ATOM 974 C CA . LEU A 1 132 ? 17.556 37.004 116.778 1.00 34.73 ? 160 LEU A CA 1 ATOM 975 C C . LEU A 1 132 ? 18.688 37.952 117.181 1.00 36.30 ? 160 LEU A C 1 ATOM 976 O O . LEU A 1 132 ? 18.643 38.603 118.243 1.00 38.67 ? 160 LEU A O 1 ATOM 977 C CB . LEU A 1 132 ? 16.407 37.798 116.161 1.00 30.18 ? 160 LEU A CB 1 ATOM 978 C CG . LEU A 1 132 ? 15.197 36.937 115.791 1.00 28.57 ? 160 LEU A CG 1 ATOM 979 C CD1 . LEU A 1 132 ? 14.038 37.798 115.383 1.00 31.29 ? 160 LEU A CD1 1 ATOM 980 C CD2 . LEU A 1 132 ? 15.578 35.996 114.643 1.00 35.31 ? 160 LEU A CD2 1 ATOM 981 N N . PRO A 1 133 ? 19.721 38.023 116.342 1.00 32.49 ? 161 PRO A N 1 ATOM 982 C CA . PRO A 1 133 ? 20.898 38.818 116.690 1.00 28.69 ? 161 PRO A CA 1 ATOM 983 C C . PRO A 1 133 ? 20.660 40.334 116.591 1.00 37.88 ? 161 PRO A C 1 ATOM 984 O O . PRO A 1 133 ? 20.030 40.843 115.656 1.00 30.38 ? 161 PRO A O 1 ATOM 985 C CB . PRO A 1 133 ? 21.932 38.356 115.663 1.00 25.25 ? 161 PRO A CB 1 ATOM 986 C CG . PRO A 1 133 ? 21.113 38.003 114.468 1.00 23.62 ? 161 PRO A CG 1 ATOM 987 C CD . PRO A 1 133 ? 19.793 37.493 114.970 1.00 33.54 ? 161 PRO A CD 1 ATOM 988 N N . CYS A 1 134 ? 21.188 41.051 117.570 1.00 33.23 ? 162 CYS A N 1 ATOM 989 C CA . CYS A 1 134 ? 21.004 42.484 117.632 1.00 28.89 ? 162 CYS A CA 1 ATOM 990 C C . CYS A 1 134 ? 22.048 43.085 118.542 1.00 33.06 ? 162 CYS A C 1 ATOM 991 O O . CYS A 1 134 ? 22.868 42.378 119.116 1.00 29.48 ? 162 CYS A O 1 ATOM 992 C CB . CYS A 1 134 ? 19.593 42.840 118.146 1.00 23.36 ? 162 CYS A CB 1 ATOM 993 S SG . CYS A 1 134 ? 19.170 42.222 119.813 1.00 32.09 ? 162 CYS A SG 1 ATOM 994 N N . SER A 1 135 ? 22.008 44.406 118.653 1.00 29.75 ? 163 SER A N 1 ATOM 995 C CA . SER A 1 135 ? 22.881 45.128 119.556 1.00 37.23 ? 163 SER A CA 1 ATOM 996 C C . SER A 1 135 ? 22.277 46.484 119.815 1.00 37.56 ? 163 SER A C 1 ATOM 997 O O . SER A 1 135 ? 21.433 46.963 119.039 1.00 33.50 ? 163 SER A O 1 ATOM 998 C CB . SER A 1 135 ? 24.271 45.306 118.952 1.00 36.95 ? 163 SER A CB 1 ATOM 999 O OG . SER A 1 135 ? 25.126 46.013 119.839 1.00 34.17 ? 163 SER A OG 1 ATOM 1000 N N . CYS A 1 136 ? 22.728 47.119 120.885 1.00 34.35 ? 164 CYS A N 1 ATOM 1001 C CA . CYS A 1 136 ? 22.352 48.500 121.111 1.00 42.02 ? 164 CYS A CA 1 ATOM 1002 C C . CYS A 1 136 ? 23.613 49.383 121.131 1.00 40.38 ? 164 CYS A C 1 ATOM 1003 O O . CYS A 1 136 ? 23.547 50.532 121.560 1.00 37.33 ? 164 CYS A O 1 ATOM 1004 C CB . CYS A 1 136 ? 21.559 48.639 122.410 1.00 36.12 ? 164 CYS A CB 1 ATOM 1005 S SG . CYS A 1 136 ? 20.080 47.552 122.572 1.00 41.09 ? 164 CYS A SG 1 ATOM 1006 N N . ASP A 1 137 ? 24.759 48.844 120.697 1.00 32.34 ? 165 ASP A N 1 ATOM 1007 C CA . ASP A 1 137 ? 26.013 49.612 120.669 1.00 29.56 ? 165 ASP A CA 1 ATOM 1008 C C . ASP A 1 137 ? 25.807 50.790 119.754 1.00 36.58 ? 165 ASP A C 1 ATOM 1009 O O . ASP A 1 137 ? 25.107 50.676 118.753 1.00 37.08 ? 165 ASP A O 1 ATOM 1010 C CB . ASP A 1 137 ? 27.187 48.814 120.088 1.00 30.68 ? 165 ASP A CB 1 ATOM 1011 C CG . ASP A 1 137 ? 27.708 47.732 121.020 1.00 40.13 ? 165 ASP A CG 1 ATOM 1012 O OD1 . ASP A 1 137 ? 27.569 47.867 122.254 1.00 45.43 ? 165 ASP A OD1 1 ATOM 1013 O OD2 . ASP A 1 137 ? 28.251 46.732 120.500 1.00 43.99 ? 165 ASP A OD2 1 ATOM 1014 N N . LYS A 1 138 ? 26.414 51.918 120.108 1.00 40.75 ? 166 LYS A N 1 ATOM 1015 C CA . LYS A 1 138 ? 26.512 53.060 119.212 1.00 45.74 ? 166 LYS A CA 1 ATOM 1016 C C . LYS A 1 138 ? 27.589 52.801 118.146 1.00 44.03 ? 166 LYS A C 1 ATOM 1017 O O . LYS A 1 138 ? 28.427 51.900 118.284 1.00 34.63 ? 166 LYS A O 1 ATOM 1018 C CB . LYS A 1 138 ? 26.856 54.313 120.015 1.00 50.32 ? 166 LYS A CB 1 ATOM 1019 C CG . LYS A 1 138 ? 25.680 54.831 120.858 1.00 47.53 ? 166 LYS A CG 1 ATOM 1020 C CD . LYS A 1 138 ? 26.084 55.930 121.831 1.00 42.83 ? 166 LYS A CD 1 ATOM 1021 C CE . LYS A 1 138 ? 24.912 56.286 122.768 1.00 53.67 ? 166 LYS A CE 1 ATOM 1022 N NZ . LYS A 1 138 ? 24.259 57.604 122.493 1.00 66.23 ? 166 LYS A NZ 1 ATOM 1023 N N . GLU A 1 139 ? 27.538 53.561 117.063 1.00 41.11 ? 167 GLU A N 1 ATOM 1024 C CA . GLU A 1 139 ? 28.573 53.478 116.043 1.00 46.16 ? 167 GLU A CA 1 ATOM 1025 C C . GLU A 1 139 ? 29.413 54.762 116.055 1.00 54.13 ? 167 GLU A C 1 ATOM 1026 O O . GLU A 1 139 ? 28.969 55.821 115.583 1.00 48.16 ? 167 GLU A O 1 ATOM 1027 C CB . GLU A 1 139 ? 27.965 53.224 114.660 1.00 40.45 ? 167 GLU A CB 1 ATOM 1028 C CG . GLU A 1 139 ? 28.999 52.929 113.576 1.00 39.65 ? 167 GLU A CG 1 ATOM 1029 C CD . GLU A 1 139 ? 29.951 51.817 113.981 1.00 48.59 ? 167 GLU A CD 1 ATOM 1030 O OE1 . GLU A 1 139 ? 31.120 51.840 113.543 1.00 54.60 ? 167 GLU A OE1 1 ATOM 1031 O OE2 . GLU A 1 139 ? 29.531 50.909 114.729 1.00 41.36 ? 167 GLU A OE2 1 ATOM 1032 N N . GLU A 1 140 ? 30.619 54.651 116.608 1.00 53.80 ? 168 GLU A N 1 ATOM 1033 C CA . GLU A 1 140 ? 31.507 55.793 116.794 1.00 56.13 ? 168 GLU A CA 1 ATOM 1034 C C . GLU A 1 140 ? 30.788 56.963 117.481 1.00 59.43 ? 168 GLU A C 1 ATOM 1035 O O . GLU A 1 140 ? 30.826 58.104 117.000 1.00 58.80 ? 168 GLU A O 1 ATOM 1036 C CB . GLU A 1 140 ? 32.115 56.233 115.458 1.00 67.12 ? 168 GLU A CB 1 ATOM 1037 C CG . GLU A 1 140 ? 33.639 56.034 115.372 1.00 81.36 ? 168 GLU A CG 1 ATOM 1038 C CD . GLU A 1 140 ? 34.060 54.865 114.484 1.00 89.01 ? 168 GLU A CD 1 ATOM 1039 O OE1 . GLU A 1 140 ? 34.093 55.023 113.242 1.00 86.07 ? 168 GLU A OE1 1 ATOM 1040 O OE2 . GLU A 1 140 ? 34.374 53.784 115.035 1.00 91.96 ? 168 GLU A OE2 1 ATOM 1041 N N . GLY A 1 141 ? 30.115 56.666 118.594 1.00 49.81 ? 169 GLY A N 1 ATOM 1042 C CA . GLY A 1 141 ? 29.456 57.688 119.392 1.00 37.19 ? 169 GLY A CA 1 ATOM 1043 C C . GLY A 1 141 ? 28.057 58.096 118.944 1.00 54.98 ? 169 GLY A C 1 ATOM 1044 O O . GLY A 1 141 ? 27.365 58.848 119.647 1.00 49.35 ? 169 GLY A O 1 ATOM 1045 N N . SER A 1 142 ? 27.619 57.599 117.789 1.00 54.39 ? 170 SER A N 1 ATOM 1046 C CA . SER A 1 142 ? 26.298 57.962 117.277 1.00 50.49 ? 170 SER A CA 1 ATOM 1047 C C . SER A 1 142 ? 25.278 56.850 117.508 1.00 53.68 ? 170 SER A C 1 ATOM 1048 O O . SER A 1 142 ? 25.628 55.671 117.589 1.00 39.03 ? 170 SER A O 1 ATOM 1049 C CB . SER A 1 142 ? 26.351 58.260 115.786 1.00 55.59 ? 170 SER A CB 1 ATOM 1050 O OG . SER A 1 142 ? 26.901 59.526 115.534 1.00 59.51 ? 170 SER A OG 1 ATOM 1051 N N . ASN A 1 143 ? 24.011 57.237 117.612 1.00 53.55 ? 171 ASN A N 1 ATOM 1052 C CA . ASN A 1 143 ? 22.945 56.265 117.761 1.00 48.57 ? 171 ASN A CA 1 ATOM 1053 C C . ASN A 1 143 ? 22.559 55.626 116.436 1.00 45.48 ? 171 ASN A C 1 ATOM 1054 O O . ASN A 1 143 ? 22.406 56.302 115.417 1.00 42.86 ? 171 ASN A O 1 ATOM 1055 C CB . ASN A 1 143 ? 21.734 56.884 118.454 1.00 43.00 ? 171 ASN A CB 1 ATOM 1056 C CG . ASN A 1 143 ? 21.930 56.978 119.955 1.00 61.94 ? 171 ASN A CG 1 ATOM 1057 O OD1 . ASN A 1 143 ? 22.267 58.031 120.497 1.00 69.32 ? 171 ASN A OD1 1 ATOM 1058 N ND2 . ASN A 1 143 ? 21.744 55.847 120.638 1.00 63.60 ? 171 ASN A ND2 1 ATOM 1059 N N . VAL A 1 144 ? 22.440 54.303 116.458 1.00 35.52 ? 172 VAL A N 1 ATOM 1060 C CA . VAL A 1 144 ? 22.111 53.553 115.250 1.00 35.93 ? 172 VAL A CA 1 ATOM 1061 C C . VAL A 1 144 ? 21.031 52.517 115.534 1.00 35.13 ? 172 VAL A C 1 ATOM 1062 O O . VAL A 1 144 ? 20.833 52.094 116.667 1.00 36.08 ? 172 VAL A O 1 ATOM 1063 C CB . VAL A 1 144 ? 23.345 52.812 114.684 1.00 30.29 ? 172 VAL A CB 1 ATOM 1064 C CG1 . VAL A 1 144 ? 24.251 53.764 113.904 1.00 27.87 ? 172 VAL A CG1 1 ATOM 1065 C CG2 . VAL A 1 144 ? 24.098 52.111 115.802 1.00 24.52 ? 172 VAL A CG2 1 ATOM 1066 N N . MET A 1 145 ? 20.348 52.100 114.481 1.00 34.72 ? 173 MET A N 1 ATOM 1067 C CA . MET A 1 145 ? 19.511 50.929 114.542 1.00 26.30 ? 173 MET A CA 1 ATOM 1068 C C . MET A 1 145 ? 20.254 49.759 113.904 1.00 31.57 ? 173 MET A C 1 ATOM 1069 O O . MET A 1 145 ? 20.613 49.820 112.728 1.00 28.42 ? 173 MET A O 1 ATOM 1070 C CB . MET A 1 145 ? 18.197 51.163 113.791 1.00 30.75 ? 173 MET A CB 1 ATOM 1071 C CG . MET A 1 145 ? 17.150 50.081 114.117 1.00 36.64 ? 173 MET A CG 1 ATOM 1072 S SD . MET A 1 145 ? 15.944 49.821 112.832 1.00 56.01 ? 173 MET A SD 1 ATOM 1073 C CE . MET A 1 145 ? 15.373 51.483 112.520 1.00 40.87 ? 173 MET A CE 1 ATOM 1074 N N . HIS A 1 146 ? 20.518 48.718 114.682 1.00 27.23 ? 174 HIS A N 1 ATOM 1075 C CA . HIS A 1 146 ? 21.186 47.538 114.130 1.00 31.01 ? 174 HIS A CA 1 ATOM 1076 C C . HIS A 1 146 ? 20.270 46.624 113.314 1.00 32.96 ? 174 HIS A C 1 ATOM 1077 O O . HIS A 1 146 ? 19.236 46.163 113.782 1.00 38.84 ? 174 HIS A O 1 ATOM 1078 C CB . HIS A 1 146 ? 21.881 46.755 115.230 1.00 28.78 ? 174 HIS A CB 1 ATOM 1079 C CG . HIS A 1 146 ? 23.043 47.487 115.825 1.00 34.02 ? 174 HIS A CG 1 ATOM 1080 N ND1 . HIS A 1 146 ? 24.329 47.336 115.371 1.00 26.33 ? 174 HIS A ND1 1 ATOM 1081 C CD2 . HIS A 1 146 ? 23.099 48.377 116.843 1.00 35.91 ? 174 HIS A CD2 1 ATOM 1082 C CE1 . HIS A 1 146 ? 25.142 48.091 116.094 1.00 28.78 ? 174 HIS A CE1 1 ATOM 1083 N NE2 . HIS A 1 146 ? 24.419 48.733 116.988 1.00 35.40 ? 174 HIS A NE2 1 ATOM 1084 N N . LEU A 1 147 ? 20.692 46.357 112.089 1.00 36.39 ? 175 LEU A N 1 ATOM 1085 C CA . LEU A 1 147 ? 19.950 45.533 111.152 1.00 29.04 ? 175 LEU A CA 1 ATOM 1086 C C . LEU A 1 147 ? 20.752 44.292 110.814 1.00 31.37 ? 175 LEU A C 1 ATOM 1087 O O . LEU A 1 147 ? 21.913 44.386 110.402 1.00 27.21 ? 175 LEU A O 1 ATOM 1088 C CB . LEU A 1 147 ? 19.691 46.309 109.871 1.00 23.11 ? 175 LEU A CB 1 ATOM 1089 C CG . LEU A 1 147 ? 19.032 45.581 108.700 1.00 30.36 ? 175 LEU A CG 1 ATOM 1090 C CD1 . LEU A 1 147 ? 17.594 45.215 109.036 1.00 27.93 ? 175 LEU A CD1 1 ATOM 1091 C CD2 . LEU A 1 147 ? 19.080 46.412 107.411 1.00 25.86 ? 175 LEU A CD2 1 ATOM 1092 N N . ALA A 1 148 ? 20.133 43.135 111.025 1.00 27.43 ? 176 ALA A N 1 ATOM 1093 C CA . ALA A 1 148 ? 20.716 41.855 110.651 1.00 21.12 ? 176 ALA A CA 1 ATOM 1094 C C . ALA A 1 148 ? 20.440 41.632 109.193 1.00 22.66 ? 176 ALA A C 1 ATOM 1095 O O . ALA A 1 148 ? 19.276 41.655 108.772 1.00 30.27 ? 176 ALA A O 1 ATOM 1096 C CB . ALA A 1 148 ? 20.119 40.724 111.477 1.00 19.89 ? 176 ALA A CB 1 ATOM 1097 N N . TYR A 1 149 ? 21.511 41.426 108.426 1.00 22.37 ? 177 TYR A N 1 ATOM 1098 C CA . TYR A 1 149 ? 21.433 41.353 106.970 1.00 22.04 ? 177 TYR A CA 1 ATOM 1099 C C . TYR A 1 149 ? 22.102 40.086 106.432 1.00 32.64 ? 177 TYR A C 1 ATOM 1100 O O . TYR A 1 149 ? 23.270 39.812 106.754 1.00 28.39 ? 177 TYR A O 1 ATOM 1101 C CB . TYR A 1 149 ? 22.114 42.572 106.376 1.00 25.58 ? 177 TYR A CB 1 ATOM 1102 C CG . TYR A 1 149 ? 22.065 42.620 104.890 1.00 24.92 ? 177 TYR A CG 1 ATOM 1103 C CD1 . TYR A 1 149 ? 20.942 43.114 104.236 1.00 26.63 ? 177 TYR A CD1 1 ATOM 1104 C CD2 . TYR A 1 149 ? 23.151 42.201 104.124 1.00 31.21 ? 177 TYR A CD2 1 ATOM 1105 C CE1 . TYR A 1 149 ? 20.879 43.160 102.852 1.00 28.66 ? 177 TYR A CE1 1 ATOM 1106 C CE2 . TYR A 1 149 ? 23.106 42.256 102.730 1.00 24.01 ? 177 TYR A CE2 1 ATOM 1107 C CZ . TYR A 1 149 ? 21.959 42.727 102.111 1.00 28.47 ? 177 TYR A CZ 1 ATOM 1108 O OH . TYR A 1 149 ? 21.882 42.796 100.761 1.00 32.21 ? 177 TYR A OH 1 ATOM 1109 N N . SER A 1 150 ? 21.359 39.304 105.642 1.00 21.95 ? 178 SER A N 1 ATOM 1110 C CA . SER A 1 150 ? 21.907 38.116 105.011 1.00 23.51 ? 178 SER A CA 1 ATOM 1111 C C . SER A 1 150 ? 22.427 38.436 103.609 1.00 30.61 ? 178 SER A C 1 ATOM 1112 O O . SER A 1 150 ? 21.650 38.772 102.729 1.00 28.04 ? 178 SER A O 1 ATOM 1113 C CB . SER A 1 150 ? 20.849 37.006 104.941 1.00 31.81 ? 178 SER A CB 1 ATOM 1114 O OG . SER A 1 150 ? 21.367 35.845 104.304 1.00 36.12 ? 178 SER A OG 1 ATOM 1115 N N . VAL A 1 151 ? 23.734 38.294 103.407 1.00 27.80 ? 179 VAL A N 1 ATOM 1116 C CA . VAL A 1 151 ? 24.362 38.643 102.142 1.00 26.23 ? 179 VAL A CA 1 ATOM 1117 C C . VAL A 1 151 ? 23.798 37.822 100.970 1.00 30.98 ? 179 VAL A C 1 ATOM 1118 O O . VAL A 1 151 ? 23.703 36.579 101.013 1.00 32.46 ? 179 VAL A O 1 ATOM 1119 C CB . VAL A 1 151 ? 25.896 38.420 102.196 1.00 24.76 ? 179 VAL A CB 1 ATOM 1120 C CG1 . VAL A 1 151 ? 26.487 38.573 100.822 1.00 23.97 ? 179 VAL A CG1 1 ATOM 1121 C CG2 . VAL A 1 151 ? 26.572 39.373 103.198 1.00 27.15 ? 179 VAL A CG2 1 ATOM 1122 N N . GLY A 1 152 ? 23.405 38.537 99.931 1.00 27.14 ? 180 GLY A N 1 ATOM 1123 C CA . GLY A 1 152 ? 22.909 37.941 98.712 1.00 29.27 ? 180 GLY A CA 1 ATOM 1124 C C . GLY A 1 152 ? 24.026 37.496 97.789 1.00 38.42 ? 180 GLY A C 1 ATOM 1125 O O . GLY A 1 152 ? 25.162 37.939 97.924 1.00 42.91 ? 180 GLY A O 1 ATOM 1126 N N . LYS A 1 153 ? 23.709 36.598 96.866 1.00 44.66 ? 181 LYS A N 1 ATOM 1127 C CA . LYS A 1 153 ? 24.693 36.110 95.909 1.00 43.56 ? 181 LYS A CA 1 ATOM 1128 C C . LYS A 1 153 ? 25.154 37.207 94.957 1.00 41.03 ? 181 LYS A C 1 ATOM 1129 O O . LYS A 1 153 ? 24.343 37.901 94.349 1.00 37.22 ? 181 LYS A O 1 ATOM 1130 C CB . LYS A 1 153 ? 24.116 34.927 95.124 1.00 49.29 ? 181 LYS A CB 1 ATOM 1131 C CG . LYS A 1 153 ? 24.540 34.835 93.665 1.00 57.05 ? 181 LYS A CG 1 ATOM 1132 C CD . LYS A 1 153 ? 24.441 33.396 93.160 1.00 60.18 ? 181 LYS A CD 1 ATOM 1133 C CE . LYS A 1 153 ? 25.557 32.518 93.754 1.00 67.16 ? 181 LYS A CE 1 ATOM 1134 N NZ . LYS A 1 153 ? 26.764 32.397 92.858 1.00 59.06 ? 181 LYS A NZ 1 ATOM 1135 N N . GLY A 1 154 ? 26.472 37.328 94.819 1.00 35.13 ? 182 GLY A N 1 ATOM 1136 C CA . GLY A 1 154 ? 27.069 38.306 93.936 1.00 32.52 ? 182 GLY A CA 1 ATOM 1137 C C . GLY A 1 154 ? 27.218 39.660 94.604 1.00 38.78 ? 182 GLY A C 1 ATOM 1138 O O . GLY A 1 154 ? 27.753 40.565 94.009 1.00 40.89 ? 182 GLY A O 1 ATOM 1139 N N . GLU A 1 155 ? 26.784 39.792 95.854 1.00 34.41 ? 183 GLU A N 1 ATOM 1140 C CA . GLU A 1 155 ? 26.912 41.060 96.557 1.00 35.58 ? 183 GLU A CA 1 ATOM 1141 C C . GLU A 1 155 ? 28.326 41.354 97.089 1.00 41.55 ? 183 GLU A C 1 ATOM 1142 O O . GLU A 1 155 ? 29.126 40.450 97.342 1.00 48.36 ? 183 GLU A O 1 ATOM 1143 C CB . GLU A 1 155 ? 25.870 41.161 97.681 1.00 31.45 ? 183 GLU A CB 1 ATOM 1144 C CG . GLU A 1 155 ? 24.440 41.330 97.145 1.00 38.67 ? 183 GLU A CG 1 ATOM 1145 C CD . GLU A 1 155 ? 23.333 41.362 98.212 1.00 50.98 ? 183 GLU A CD 1 ATOM 1146 O OE1 . GLU A 1 155 ? 23.596 41.144 99.419 1.00 44.30 ? 183 GLU A OE1 1 ATOM 1147 O OE2 . GLU A 1 155 ? 22.168 41.595 97.821 1.00 64.83 ? 183 GLU A OE2 1 ATOM 1148 N N . ASN A 1 156 ? 28.623 42.638 97.240 1.00 35.22 ? 184 ASN A N 1 ATOM 1149 C CA . ASN A 1 156 ? 29.884 43.079 97.810 1.00 34.77 ? 184 ASN A CA 1 ATOM 1150 C C . ASN A 1 156 ? 29.651 44.068 98.967 1.00 33.49 ? 184 ASN A C 1 ATOM 1151 O O . ASN A 1 156 ? 28.577 44.650 99.093 1.00 36.65 ? 184 ASN A O 1 ATOM 1152 C CB . ASN A 1 156 ? 30.797 43.675 96.730 1.00 41.60 ? 184 ASN A CB 1 ATOM 1153 C CG . ASN A 1 156 ? 30.145 44.817 95.964 1.00 43.78 ? 184 ASN A CG 1 ATOM 1154 O OD1 . ASN A 1 156 ? 30.004 45.925 96.491 1.00 54.42 ? 184 ASN A OD1 1 ATOM 1155 N ND2 . ASN A 1 156 ? 29.784 44.558 94.698 1.00 44.14 ? 184 ASN A ND2 1 ATOM 1156 N N . THR A 1 157 ? 30.655 44.255 99.807 1.00 30.61 ? 185 THR A N 1 ATOM 1157 C CA . THR A 1 157 ? 30.496 45.073 101.001 1.00 38.20 ? 185 THR A CA 1 ATOM 1158 C C . THR A 1 157 ? 30.332 46.546 100.653 1.00 42.07 ? 185 THR A C 1 ATOM 1159 O O . THR A 1 157 ? 29.721 47.308 101.403 1.00 47.21 ? 185 THR A O 1 ATOM 1160 C CB . THR A 1 157 ? 31.702 44.892 101.954 1.00 46.12 ? 185 THR A CB 1 ATOM 1161 O OG1 . THR A 1 157 ? 32.916 45.040 101.210 1.00 47.50 ? 185 THR A OG1 1 ATOM 1162 C CG2 . THR A 1 157 ? 31.701 43.498 102.548 1.00 47.34 ? 185 THR A CG2 1 ATOM 1163 N N . SER A 1 158 ? 30.871 46.938 99.504 1.00 43.43 ? 186 SER A N 1 ATOM 1164 C CA . SER A 1 158 ? 30.761 48.305 99.040 1.00 33.61 ? 186 SER A CA 1 ATOM 1165 C C . SER A 1 158 ? 29.317 48.655 98.758 1.00 35.33 ? 186 SER A C 1 ATOM 1166 O O . SER A 1 158 ? 28.787 49.626 99.296 1.00 47.45 ? 186 SER A O 1 ATOM 1167 C CB . SER A 1 158 ? 31.610 48.534 97.788 1.00 40.57 ? 186 SER A CB 1 ATOM 1168 O OG . SER A 1 158 ? 31.585 49.904 97.419 1.00 52.46 ? 186 SER A OG 1 ATOM 1169 N N . ALA A 1 159 ? 28.674 47.860 97.915 1.00 39.90 ? 187 ALA A N 1 ATOM 1170 C CA . ALA A 1 159 ? 27.294 48.147 97.544 1.00 35.00 ? 187 ALA A CA 1 ATOM 1171 C C . ALA A 1 159 ? 26.341 47.970 98.724 1.00 39.30 ? 187 ALA A C 1 ATOM 1172 O O . ALA A 1 159 ? 25.350 48.682 98.833 1.00 47.47 ? 187 ALA A O 1 ATOM 1173 C CB . ALA A 1 159 ? 26.868 47.299 96.393 1.00 30.94 ? 187 ALA A CB 1 ATOM 1174 N N . ILE A 1 160 ? 26.640 47.017 99.604 1.00 33.57 ? 188 ILE A N 1 ATOM 1175 C CA . ILE A 1 160 ? 25.798 46.803 100.768 1.00 33.40 ? 188 ILE A CA 1 ATOM 1176 C C . ILE A 1 160 ? 25.884 48.013 101.701 1.00 31.83 ? 188 ILE A C 1 ATOM 1177 O O . ILE A 1 160 ? 24.874 48.530 102.141 1.00 35.98 ? 188 ILE A O 1 ATOM 1178 C CB . ILE A 1 160 ? 26.187 45.504 101.512 1.00 30.81 ? 188 ILE A CB 1 ATOM 1179 C CG1 . ILE A 1 160 ? 25.795 44.262 100.688 1.00 25.70 ? 188 ILE A CG1 1 ATOM 1180 C CG2 . ILE A 1 160 ? 25.535 45.451 102.879 1.00 24.25 ? 188 ILE A CG2 1 ATOM 1181 C CD1 . ILE A 1 160 ? 26.438 42.976 101.198 1.00 20.38 ? 188 ILE A CD1 1 ATOM 1182 N N . ALA A 1 161 ? 27.098 48.455 101.997 1.00 36.20 ? 189 ALA A N 1 ATOM 1183 C CA . ALA A 1 161 ? 27.293 49.620 102.841 1.00 40.23 ? 189 ALA A CA 1 ATOM 1184 C C . ALA A 1 161 ? 26.586 50.832 102.261 1.00 47.02 ? 189 ALA A C 1 ATOM 1185 O O . ALA A 1 161 ? 25.872 51.529 102.975 1.00 50.80 ? 189 ALA A O 1 ATOM 1186 C CB . ALA A 1 161 ? 28.773 49.909 103.016 1.00 43.32 ? 189 ALA A CB 1 ATOM 1187 N N . ALA A 1 162 ? 26.755 51.053 100.960 1.00 44.71 ? 190 ALA A N 1 ATOM 1188 C CA . ALA A 1 162 ? 26.185 52.239 100.324 1.00 43.98 ? 190 ALA A CA 1 ATOM 1189 C C . ALA A 1 162 ? 24.680 52.203 100.374 1.00 43.57 ? 190 ALA A C 1 ATOM 1190 O O . ALA A 1 162 ? 24.052 53.206 100.694 1.00 52.53 ? 190 ALA A O 1 ATOM 1191 C CB . ALA A 1 162 ? 26.664 52.387 98.878 1.00 34.66 ? 190 ALA A CB 1 ATOM 1192 N N . LYS A 1 163 ? 24.098 51.052 100.064 1.00 35.33 ? 191 LYS A N 1 ATOM 1193 C CA . LYS A 1 163 ? 22.647 50.931 100.121 1.00 32.52 ? 191 LYS A CA 1 ATOM 1194 C C . LYS A 1 163 ? 22.101 51.305 101.524 1.00 34.95 ? 191 LYS A C 1 ATOM 1195 O O . LYS A 1 163 ? 20.980 51.780 101.650 1.00 39.80 ? 191 LYS A O 1 ATOM 1196 C CB . LYS A 1 163 ? 22.149 49.532 99.692 1.00 38.09 ? 191 LYS A CB 1 ATOM 1197 C CG . LYS A 1 163 ? 20.665 49.401 100.029 1.00 56.76 ? 191 LYS A CG 1 ATOM 1198 C CD . LYS A 1 163 ? 19.847 48.363 99.311 1.00 64.17 ? 191 LYS A CD 1 ATOM 1199 C CE . LYS A 1 163 ? 18.365 48.740 99.533 1.00 69.69 ? 191 LYS A CE 1 ATOM 1200 N NZ . LYS A 1 163 ? 17.373 47.917 98.795 1.00 74.96 ? 191 LYS A NZ 1 ATOM 1201 N N . TYR A 1 164 ? 22.884 51.094 102.576 1.00 38.81 ? 192 TYR A N 1 ATOM 1202 C CA . TYR A 1 164 ? 22.389 51.402 103.914 1.00 45.92 ? 192 TYR A CA 1 ATOM 1203 C C . TYR A 1 164 ? 22.961 52.690 104.483 1.00 42.45 ? 192 TYR A C 1 ATOM 1204 O O . TYR A 1 164 ? 22.894 52.922 105.695 1.00 38.56 ? 192 TYR A O 1 ATOM 1205 C CB . TYR A 1 164 ? 22.556 50.207 104.873 1.00 39.90 ? 192 TYR A CB 1 ATOM 1206 C CG . TYR A 1 164 ? 21.602 49.102 104.477 1.00 41.78 ? 192 TYR A CG 1 ATOM 1207 C CD1 . TYR A 1 164 ? 20.224 49.290 104.586 1.00 34.13 ? 192 TYR A CD1 1 ATOM 1208 C CD2 . TYR A 1 164 ? 22.066 47.890 103.955 1.00 29.70 ? 192 TYR A CD2 1 ATOM 1209 C CE1 . TYR A 1 164 ? 19.336 48.302 104.188 1.00 34.93 ? 192 TYR A CE1 1 ATOM 1210 C CE2 . TYR A 1 164 ? 21.178 46.885 103.566 1.00 28.83 ? 192 TYR A CE2 1 ATOM 1211 C CZ . TYR A 1 164 ? 19.825 47.100 103.685 1.00 35.65 ? 192 TYR A CZ 1 ATOM 1212 O OH . TYR A 1 164 ? 18.951 46.127 103.287 1.00 40.94 ? 192 TYR A OH 1 ATOM 1213 N N . GLY A 1 165 ? 23.536 53.508 103.602 1.00 42.29 ? 193 GLY A N 1 ATOM 1214 C CA . GLY A 1 165 ? 24.003 54.842 103.971 1.00 44.11 ? 193 GLY A CA 1 ATOM 1215 C C . GLY A 1 165 ? 25.054 54.730 105.047 1.00 48.43 ? 193 GLY A C 1 ATOM 1216 O O . GLY A 1 165 ? 25.081 55.467 106.030 1.00 56.66 ? 193 GLY A O 1 ATOM 1217 N N . VAL A 1 166 ? 25.919 53.758 104.851 1.00 39.90 ? 194 VAL A N 1 ATOM 1218 C CA . VAL A 1 166 ? 26.964 53.483 105.788 1.00 43.94 ? 194 VAL A CA 1 ATOM 1219 C C . VAL A 1 166 ? 28.284 53.424 105.041 1.00 45.46 ? 194 VAL A C 1 ATOM 1220 O O . VAL A 1 166 ? 28.325 53.151 103.844 1.00 53.08 ? 194 VAL A O 1 ATOM 1221 C CB . VAL A 1 166 ? 26.626 52.183 106.563 1.00 51.09 ? 194 VAL A CB 1 ATOM 1222 C CG1 . VAL A 1 166 ? 27.824 51.283 106.749 1.00 42.58 ? 194 VAL A CG1 1 ATOM 1223 C CG2 . VAL A 1 166 ? 25.963 52.526 107.880 1.00 46.51 ? 194 VAL A CG2 1 ATOM 1224 N N . THR A 1 167 ? 29.352 53.775 105.733 1.00 48.51 ? 195 THR A N 1 ATOM 1225 C CA . THR A 1 167 ? 30.687 53.649 105.181 1.00 53.28 ? 195 THR A CA 1 ATOM 1226 C C . THR A 1 167 ? 31.111 52.179 105.096 1.00 47.13 ? 195 THR A C 1 ATOM 1227 O O . THR A 1 167 ? 30.830 51.386 106.002 1.00 45.45 ? 195 THR A O 1 ATOM 1228 C CB . THR A 1 167 ? 31.682 54.482 106.020 1.00 56.52 ? 195 THR A CB 1 ATOM 1229 O OG1 . THR A 1 167 ? 32.041 55.653 105.278 1.00 60.39 ? 195 THR A OG1 1 ATOM 1230 C CG2 . THR A 1 167 ? 32.932 53.720 106.305 1.00 46.36 ? 195 THR A CG2 1 ATOM 1231 N N . GLU A 1 168 ? 31.797 51.822 104.014 1.00 39.11 ? 196 GLU A N 1 ATOM 1232 C CA . GLU A 1 168 ? 32.259 50.454 103.848 1.00 39.68 ? 196 GLU A CA 1 ATOM 1233 C C . GLU A 1 168 ? 33.170 49.985 104.994 1.00 44.50 ? 196 GLU A C 1 ATOM 1234 O O . GLU A 1 168 ? 32.999 48.872 105.499 1.00 44.41 ? 196 GLU A O 1 ATOM 1235 C CB . GLU A 1 168 ? 32.951 50.257 102.486 1.00 34.37 ? 196 GLU A CB 1 ATOM 1236 C CG . GLU A 1 168 ? 33.394 48.815 102.276 1.00 42.61 ? 196 GLU A CG 1 ATOM 1237 C CD . GLU A 1 168 ? 34.001 48.530 100.920 1.00 53.19 ? 196 GLU A CD 1 ATOM 1238 O OE1 . GLU A 1 168 ? 33.974 49.415 100.038 1.00 56.72 ? 196 GLU A OE1 1 ATOM 1239 O OE2 . GLU A 1 168 ? 34.487 47.389 100.731 1.00 54.15 ? 196 GLU A OE2 1 ATOM 1240 N N . SER A 1 169 ? 34.089 50.834 105.453 1.00 41.95 ? 197 SER A N 1 ATOM 1241 C CA . SER A 1 169 ? 34.984 50.437 106.552 1.00 46.60 ? 197 SER A CA 1 ATOM 1242 C C . SER A 1 169 ? 34.228 50.249 107.859 1.00 41.86 ? 197 SER A C 1 ATOM 1243 O O . SER A 1 169 ? 34.585 49.386 108.678 1.00 40.64 ? 197 SER A O 1 ATOM 1244 C CB . SER A 1 169 ? 36.173 51.396 106.720 1.00 51.83 ? 197 SER A CB 1 ATOM 1245 O OG . SER A 1 169 ? 35.742 52.727 106.847 1.00 62.42 ? 197 SER A OG 1 ATOM 1246 N N . THR A 1 170 ? 33.226 51.094 108.082 1.00 35.13 ? 198 THR A N 1 ATOM 1247 C CA . THR A 1 170 ? 32.305 50.889 109.199 1.00 44.69 ? 198 THR A CA 1 ATOM 1248 C C . THR A 1 170 ? 31.677 49.486 109.114 1.00 45.45 ? 198 THR A C 1 ATOM 1249 O O . THR A 1 170 ? 31.636 48.737 110.092 1.00 40.16 ? 198 THR A O 1 ATOM 1250 C CB . THR A 1 170 ? 31.185 51.954 109.222 1.00 47.92 ? 198 THR A CB 1 ATOM 1251 O OG1 . THR A 1 170 ? 31.725 53.228 109.602 1.00 60.93 ? 198 THR A OG1 1 ATOM 1252 C CG2 . THR A 1 170 ? 30.122 51.573 110.206 1.00 34.79 ? 198 THR A CG2 1 ATOM 1253 N N . LEU A 1 171 ? 31.197 49.129 107.930 1.00 45.64 ? 199 LEU A N 1 ATOM 1254 C CA . LEU A 1 171 ? 30.588 47.821 107.756 1.00 40.84 ? 199 LEU A CA 1 ATOM 1255 C C . LEU A 1 171 ? 31.642 46.758 108.047 1.00 37.18 ? 199 LEU A C 1 ATOM 1256 O O . LEU A 1 171 ? 31.374 45.805 108.765 1.00 34.71 ? 199 LEU A O 1 ATOM 1257 C CB . LEU A 1 171 ? 30.010 47.659 106.347 1.00 35.04 ? 199 LEU A CB 1 ATOM 1258 C CG . LEU A 1 171 ? 29.133 46.418 106.107 1.00 40.36 ? 199 LEU A CG 1 ATOM 1259 C CD1 . LEU A 1 171 ? 27.916 46.498 107.015 1.00 31.37 ? 199 LEU A CD1 1 ATOM 1260 C CD2 . LEU A 1 171 ? 28.688 46.320 104.641 1.00 29.13 ? 199 LEU A CD2 1 ATOM 1261 N N . LEU A 1 172 ? 32.854 46.970 107.534 1.00 43.83 ? 200 LEU A N 1 ATOM 1262 C CA . LEU A 1 172 ? 33.963 46.018 107.676 1.00 37.86 ? 200 LEU A CA 1 ATOM 1263 C C . LEU A 1 172 ? 34.511 45.878 109.088 1.00 43.29 ? 200 LEU A C 1 ATOM 1264 O O . LEU A 1 172 ? 34.773 44.765 109.538 1.00 45.79 ? 200 LEU A O 1 ATOM 1265 C CB . LEU A 1 172 ? 35.103 46.386 106.723 1.00 43.35 ? 200 LEU A CB 1 ATOM 1266 C CG . LEU A 1 172 ? 34.690 46.216 105.259 1.00 45.35 ? 200 LEU A CG 1 ATOM 1267 C CD1 . LEU A 1 172 ? 35.707 46.786 104.255 1.00 40.84 ? 200 LEU A CD1 1 ATOM 1268 C CD2 . LEU A 1 172 ? 34.328 44.768 104.969 1.00 45.55 ? 200 LEU A CD2 1 ATOM 1269 N N . THR A 1 173 ? 34.658 46.985 109.811 1.00 43.44 ? 201 THR A N 1 ATOM 1270 C CA . THR A 1 173 ? 35.182 46.884 111.177 1.00 41.80 ? 201 THR A CA 1 ATOM 1271 C C . THR A 1 173 ? 34.127 46.328 112.124 1.00 35.01 ? 201 THR A C 1 ATOM 1272 O O . THR A 1 173 ? 34.423 45.548 113.020 1.00 37.95 ? 201 THR A O 1 ATOM 1273 C CB . THR A 1 173 ? 35.692 48.236 111.719 1.00 45.58 ? 201 THR A CB 1 ATOM 1274 O OG1 . THR A 1 173 ? 34.595 49.146 111.843 1.00 62.51 ? 201 THR A OG1 1 ATOM 1275 C CG2 . THR A 1 173 ? 36.744 48.822 110.787 1.00 36.59 ? 201 THR A CG2 1 ATOM 1276 N N . ARG A 1 174 ? 32.896 46.786 111.955 1.00 33.14 ? 202 ARG A N 1 ATOM 1277 C CA . ARG A 1 174 ? 31.799 46.305 112.773 1.00 37.56 ? 202 ARG A CA 1 ATOM 1278 C C . ARG A 1 174 ? 31.667 44.790 112.619 1.00 39.50 ? 202 ARG A C 1 ATOM 1279 O O . ARG A 1 174 ? 31.374 44.078 113.570 1.00 39.48 ? 202 ARG A O 1 ATOM 1280 C CB . ARG A 1 174 ? 30.491 47.007 112.377 1.00 40.77 ? 202 ARG A CB 1 ATOM 1281 C CG . ARG A 1 174 ? 29.290 46.613 113.212 1.00 37.48 ? 202 ARG A CG 1 ATOM 1282 C CD . ARG A 1 174 ? 29.459 47.074 114.637 1.00 35.03 ? 202 ARG A CD 1 ATOM 1283 N NE . ARG A 1 174 ? 28.580 46.365 115.552 1.00 32.27 ? 202 ARG A NE 1 ATOM 1284 C CZ . ARG A 1 174 ? 28.579 46.538 116.867 1.00 35.95 ? 202 ARG A CZ 1 ATOM 1285 N NH1 . ARG A 1 174 ? 29.409 47.409 117.425 1.00 41.90 ? 202 ARG A NH1 1 ATOM 1286 N NH2 . ARG A 1 174 ? 27.737 45.844 117.623 1.00 37.31 ? 202 ARG A NH2 1 ATOM 1287 N N . ASN A 1 175 ? 31.888 44.277 111.416 1.00 38.56 ? 203 ASN A N 1 ATOM 1288 C CA . ASN A 1 175 ? 31.719 42.848 111.256 1.00 34.54 ? 203 ASN A CA 1 ATOM 1289 C C . ASN A 1 175 ? 32.995 42.022 111.244 1.00 36.71 ? 203 ASN A C 1 ATOM 1290 O O . ASN A 1 175 ? 32.956 40.844 110.920 1.00 40.87 ? 203 ASN A O 1 ATOM 1291 C CB . ASN A 1 175 ? 30.858 42.578 110.032 1.00 38.06 ? 203 ASN A CB 1 ATOM 1292 C CG . ASN A 1 175 ? 29.425 43.032 110.245 1.00 37.38 ? 203 ASN A CG 1 ATOM 1293 O OD1 . ASN A 1 175 ? 28.650 42.325 110.879 1.00 32.55 ? 203 ASN A OD1 1 ATOM 1294 N ND2 . ASN A 1 175 ? 29.067 44.209 109.714 1.00 33.72 ? 203 ASN A ND2 1 ATOM 1295 N N . LYS A 1 176 ? 34.110 42.652 111.619 1.00 51.65 ? 204 LYS A N 1 ATOM 1296 C CA . LYS A 1 176 ? 35.432 42.027 111.641 1.00 45.34 ? 204 LYS A CA 1 ATOM 1297 C C . LYS A 1 176 ? 35.728 41.247 110.361 1.00 39.83 ? 204 LYS A C 1 ATOM 1298 O O . LYS A 1 176 ? 36.031 40.066 110.396 1.00 39.52 ? 204 LYS A O 1 ATOM 1299 C CB . LYS A 1 176 ? 35.617 41.138 112.871 1.00 49.77 ? 204 LYS A CB 1 ATOM 1300 C CG . LYS A 1 176 ? 35.156 41.769 114.158 1.00 58.91 ? 204 LYS A CG 1 ATOM 1301 C CD . LYS A 1 176 ? 35.218 40.748 115.269 1.00 71.40 ? 204 LYS A CD 1 ATOM 1302 C CE . LYS A 1 176 ? 34.744 41.308 116.598 1.00 82.88 ? 204 LYS A CE 1 ATOM 1303 N NZ . LYS A 1 176 ? 33.328 40.875 116.870 1.00 84.60 ? 204 LYS A NZ 1 ATOM 1304 N N . ILE A 1 177 ? 35.625 41.923 109.232 1.00 35.70 ? 205 ILE A N 1 ATOM 1305 C CA . ILE A 1 177 ? 35.878 41.309 107.944 1.00 48.03 ? 205 ILE A CA 1 ATOM 1306 C C . ILE A 1 177 ? 37.227 41.784 107.436 1.00 52.98 ? 205 ILE A C 1 ATOM 1307 O O . ILE A 1 177 ? 37.377 42.943 107.041 1.00 48.61 ? 205 ILE A O 1 ATOM 1308 C CB . ILE A 1 177 ? 34.773 41.684 106.930 1.00 44.62 ? 205 ILE A CB 1 ATOM 1309 C CG1 . ILE A 1 177 ? 33.461 40.983 107.285 1.00 31.62 ? 205 ILE A CG1 1 ATOM 1310 C CG2 . ILE A 1 177 ? 35.163 41.326 105.511 1.00 38.35 ? 205 ILE A CG2 1 ATOM 1311 C CD1 . ILE A 1 177 ? 32.264 41.566 106.527 1.00 30.58 ? 205 ILE A CD1 1 ATOM 1312 N N . ASP A 1 178 ? 38.198 40.872 107.451 1.00 54.61 ? 206 ASP A N 1 ATOM 1313 C CA . ASP A 1 178 ? 39.562 41.168 107.028 1.00 52.97 ? 206 ASP A CA 1 ATOM 1314 C C . ASP A 1 178 ? 39.606 41.328 105.523 1.00 57.90 ? 206 ASP A C 1 ATOM 1315 O O . ASP A 1 178 ? 40.265 42.230 105.005 1.00 64.98 ? 206 ASP A O 1 ATOM 1316 C CB . ASP A 1 178 ? 40.505 40.045 107.443 1.00 51.53 ? 206 ASP A CB 1 ATOM 1317 C CG . ASP A 1 178 ? 40.616 39.915 108.938 1.00 61.56 ? 206 ASP A CG 1 ATOM 1318 O OD1 . ASP A 1 178 ? 40.572 40.959 109.635 1.00 60.49 ? 206 ASP A OD1 1 ATOM 1319 O OD2 . ASP A 1 178 ? 40.735 38.766 109.415 1.00 65.82 ? 206 ASP A OD2 1 ATOM 1320 N N . ASP A 1 179 ? 38.927 40.427 104.820 1.00 50.98 ? 207 ASP A N 1 ATOM 1321 C CA . ASP A 1 179 ? 38.945 40.444 103.365 1.00 42.01 ? 207 ASP A CA 1 ATOM 1322 C C . ASP A 1 179 ? 37.533 40.439 102.765 1.00 41.14 ? 207 ASP A C 1 ATOM 1323 O O . ASP A 1 179 ? 36.851 39.408 102.764 1.00 40.25 ? 207 ASP A O 1 ATOM 1324 C CB . ASP A 1 179 ? 39.774 39.258 102.850 1.00 38.61 ? 207 ASP A CB 1 ATOM 1325 C CG . ASP A 1 179 ? 39.996 39.297 101.340 1.00 43.96 ? 207 ASP A CG 1 ATOM 1326 O OD1 . ASP A 1 179 ? 39.697 40.326 100.701 1.00 50.81 ? 207 ASP A OD1 1 ATOM 1327 O OD2 . ASP A 1 179 ? 40.506 38.296 100.795 1.00 58.04 ? 207 ASP A OD2 1 ATOM 1328 N N . PRO A 1 180 ? 37.102 41.593 102.245 1.00 47.87 ? 208 PRO A N 1 ATOM 1329 C CA . PRO A 1 180 ? 35.808 41.812 101.586 1.00 44.89 ? 208 PRO A CA 1 ATOM 1330 C C . PRO A 1 180 ? 35.551 40.784 100.499 1.00 44.93 ? 208 PRO A C 1 ATOM 1331 O O . PRO A 1 180 ? 34.406 40.354 100.347 1.00 49.56 ? 208 PRO A O 1 ATOM 1332 C CB . PRO A 1 180 ? 35.964 43.205 100.954 1.00 42.98 ? 208 PRO A CB 1 ATOM 1333 C CG . PRO A 1 180 ? 36.957 43.898 101.848 1.00 42.59 ? 208 PRO A CG 1 ATOM 1334 C CD . PRO A 1 180 ? 37.911 42.825 102.298 1.00 50.47 ? 208 PRO A CD 1 ATOM 1335 N N . THR A 1 181 ? 36.585 40.415 99.742 1.00 46.52 ? 209 THR A N 1 ATOM 1336 C CA . THR A 1 181 ? 36.405 39.511 98.599 1.00 46.27 ? 209 THR A CA 1 ATOM 1337 C C . THR A 1 181 ? 35.961 38.133 99.038 1.00 37.15 ? 209 THR A C 1 ATOM 1338 O O . THR A 1 181 ? 35.464 37.348 98.242 1.00 55.19 ? 209 THR A O 1 ATOM 1339 C CB . THR A 1 181 ? 37.683 39.389 97.731 1.00 48.13 ? 209 THR A CB 1 ATOM 1340 O OG1 . THR A 1 181 ? 38.721 38.752 98.486 1.00 53.13 ? 209 THR A OG1 1 ATOM 1341 C CG2 . THR A 1 181 ? 38.142 40.773 97.274 1.00 43.79 ? 209 THR A CG2 1 ATOM 1342 N N . LYS A 1 182 ? 36.141 37.843 100.315 1.00 40.79 ? 210 LYS A N 1 ATOM 1343 C CA . LYS A 1 182 ? 35.788 36.537 100.867 1.00 36.43 ? 210 LYS A CA 1 ATOM 1344 C C . LYS A 1 182 ? 34.340 36.489 101.333 1.00 38.83 ? 210 LYS A C 1 ATOM 1345 O O . LYS A 1 182 ? 33.926 35.514 101.950 1.00 41.37 ? 210 LYS A O 1 ATOM 1346 C CB . LYS A 1 182 ? 36.700 36.199 102.046 1.00 46.29 ? 210 LYS A CB 1 ATOM 1347 C CG . LYS A 1 182 ? 38.185 36.177 101.715 1.00 52.13 ? 210 LYS A CG 1 ATOM 1348 C CD . LYS A 1 182 ? 38.585 35.034 100.800 1.00 66.23 ? 210 LYS A CD 1 ATOM 1349 C CE . LYS A 1 182 ? 40.106 34.936 100.723 1.00 77.33 ? 210 LYS A CE 1 ATOM 1350 N NZ . LYS A 1 182 ? 40.785 35.887 101.673 1.00 79.29 ? 210 LYS A NZ 1 ATOM 1351 N N . LEU A 1 183 ? 33.581 37.554 101.069 1.00 43.22 ? 211 LEU A N 1 ATOM 1352 C CA . LEU A 1 183 ? 32.181 37.644 101.506 1.00 34.66 ? 211 LEU A CA 1 ATOM 1353 C C . LEU A 1 183 ? 31.395 36.434 100.995 1.00 28.80 ? 211 LEU A C 1 ATOM 1354 O O . LEU A 1 183 ? 31.382 36.159 99.811 1.00 33.50 ? 211 LEU A O 1 ATOM 1355 C CB . LEU A 1 183 ? 31.534 38.932 100.972 1.00 33.34 ? 211 LEU A CB 1 ATOM 1356 C CG . LEU A 1 183 ? 30.280 39.442 101.677 1.00 44.23 ? 211 LEU A CG 1 ATOM 1357 C CD1 . LEU A 1 183 ? 30.652 39.958 103.040 1.00 39.22 ? 211 LEU A CD1 1 ATOM 1358 C CD2 . LEU A 1 183 ? 29.547 40.517 100.888 1.00 48.54 ? 211 LEU A CD2 1 ATOM 1359 N N . GLN A 1 184 ? 30.746 35.701 101.886 1.00 33.59 ? 212 GLN A N 1 ATOM 1360 C CA . GLN A 1 184 ? 29.920 34.581 101.451 1.00 34.41 ? 212 GLN A CA 1 ATOM 1361 C C . GLN A 1 184 ? 28.432 34.869 101.382 1.00 35.83 ? 212 GLN A C 1 ATOM 1362 O O . GLN A 1 184 ? 27.886 35.645 102.172 1.00 48.38 ? 212 GLN A O 1 ATOM 1363 C CB . GLN A 1 184 ? 30.171 33.377 102.339 1.00 41.79 ? 212 GLN A CB 1 ATOM 1364 C CG . GLN A 1 184 ? 31.438 32.673 101.972 1.00 54.25 ? 212 GLN A CG 1 ATOM 1365 C CD . GLN A 1 184 ? 31.744 31.551 102.899 1.00 63.10 ? 212 GLN A CD 1 ATOM 1366 O OE1 . GLN A 1 184 ? 31.023 31.326 103.870 1.00 66.79 ? 212 GLN A OE1 1 ATOM 1367 N NE2 . GLN A 1 184 ? 32.789 30.791 102.582 1.00 69.14 ? 212 GLN A NE2 1 ATOM 1368 N N . MET A 1 185 ? 27.785 34.229 100.420 1.00 30.89 ? 213 MET A N 1 ATOM 1369 C CA . MET A 1 185 ? 26.341 34.235 100.352 1.00 35.36 ? 213 MET A CA 1 ATOM 1370 C C . MET A 1 185 ? 25.796 33.661 101.665 1.00 40.05 ? 213 MET A C 1 ATOM 1371 O O . MET A 1 185 ? 26.284 32.652 102.164 1.00 32.12 ? 213 MET A O 1 ATOM 1372 C CB . MET A 1 185 ? 25.887 33.398 99.175 1.00 40.38 ? 213 MET A CB 1 ATOM 1373 C CG . MET A 1 185 ? 24.384 33.364 98.969 1.00 58.32 ? 213 MET A CG 1 ATOM 1374 S SD . MET A 1 185 ? 23.912 32.102 97.769 1.00 84.93 ? 213 MET A SD 1 ATOM 1375 C CE . MET A 1 185 ? 22.209 32.540 97.404 1.00 78.28 ? 213 MET A CE 1 ATOM 1376 N N . GLY A 1 186 ? 24.820 34.347 102.257 1.00 31.37 ? 214 GLY A N 1 ATOM 1377 C CA . GLY A 1 186 ? 24.195 33.858 103.469 1.00 20.02 ? 214 GLY A CA 1 ATOM 1378 C C . GLY A 1 186 ? 24.954 34.219 104.733 1.00 32.73 ? 214 GLY A C 1 ATOM 1379 O O . GLY A 1 186 ? 24.467 33.980 105.828 1.00 40.33 ? 214 GLY A O 1 ATOM 1380 N N . GLN A 1 187 ? 26.118 34.836 104.585 1.00 21.92 ? 215 GLN A N 1 ATOM 1381 C CA . GLN A 1 187 ? 26.797 35.437 105.731 1.00 35.47 ? 215 GLN A CA 1 ATOM 1382 C C . GLN A 1 187 ? 25.906 36.530 106.351 1.00 32.16 ? 215 GLN A C 1 ATOM 1383 O O . GLN A 1 187 ? 25.353 37.374 105.654 1.00 32.85 ? 215 GLN A O 1 ATOM 1384 C CB . GLN A 1 187 ? 28.116 36.081 105.300 1.00 30.92 ? 215 GLN A CB 1 ATOM 1385 C CG . GLN A 1 187 ? 28.956 36.594 106.469 1.00 34.42 ? 215 GLN A CG 1 ATOM 1386 C CD . GLN A 1 187 ? 30.388 36.930 106.050 1.00 37.92 ? 215 GLN A CD 1 ATOM 1387 O OE1 . GLN A 1 187 ? 30.774 36.731 104.893 1.00 39.63 ? 215 GLN A OE1 1 ATOM 1388 N NE2 . GLN A 1 187 ? 31.183 37.421 106.993 1.00 33.38 ? 215 GLN A NE2 1 ATOM 1389 N N . ILE A 1 188 ? 25.791 36.499 107.664 1.00 36.16 ? 216 ILE A N 1 ATOM 1390 C CA . ILE A 1 188 ? 24.971 37.433 108.397 1.00 38.40 ? 216 ILE A CA 1 ATOM 1391 C C . ILE A 1 188 ? 25.774 38.647 108.848 1.00 38.21 ? 216 ILE A C 1 ATOM 1392 O O . ILE A 1 188 ? 26.694 38.523 109.643 1.00 37.78 ? 216 ILE A O 1 ATOM 1393 C CB . ILE A 1 188 ? 24.381 36.764 109.643 1.00 35.88 ? 216 ILE A CB 1 ATOM 1394 C CG1 . ILE A 1 188 ? 23.668 35.462 109.256 1.00 34.63 ? 216 ILE A CG1 1 ATOM 1395 C CG2 . ILE A 1 188 ? 23.469 37.724 110.372 1.00 26.12 ? 216 ILE A CG2 1 ATOM 1396 C CD1 . ILE A 1 188 ? 22.529 35.634 108.277 1.00 22.71 ? 216 ILE A CD1 1 ATOM 1397 N N . LEU A 1 189 ? 25.394 39.820 108.363 1.00 33.49 ? 217 LEU A N 1 ATOM 1398 C CA . LEU A 1 189 ? 26.070 41.053 108.724 1.00 29.61 ? 217 LEU A CA 1 ATOM 1399 C C . LEU A 1 189 ? 25.240 41.904 109.713 1.00 29.15 ? 217 LEU A C 1 ATOM 1400 O O . LEU A 1 189 ? 24.021 42.008 109.599 1.00 31.83 ? 217 LEU A O 1 ATOM 1401 C CB . LEU A 1 189 ? 26.345 41.868 107.450 1.00 33.80 ? 217 LEU A CB 1 ATOM 1402 C CG . LEU A 1 189 ? 27.278 41.289 106.371 1.00 40.25 ? 217 LEU A CG 1 ATOM 1403 C CD1 . LEU A 1 189 ? 27.504 42.283 105.232 1.00 42.26 ? 217 LEU A CD1 1 ATOM 1404 C CD2 . LEU A 1 189 ? 28.614 40.930 106.962 1.00 35.90 ? 217 LEU A CD2 1 ATOM 1405 N N . ASP A 1 190 ? 25.939 42.533 110.649 1.00 31.59 ? 218 ASP A N 1 ATOM 1406 C CA . ASP A 1 190 ? 25.389 43.521 111.570 1.00 30.52 ? 218 ASP A CA 1 ATOM 1407 C C . ASP A 1 190 ? 25.589 44.887 110.924 1.00 33.78 ? 218 ASP A C 1 ATOM 1408 O O . ASP A 1 190 ? 26.698 45.395 110.887 1.00 30.71 ? 218 ASP A O 1 ATOM 1409 C CB . ASP A 1 190 ? 26.125 43.468 112.914 1.00 22.15 ? 218 ASP A CB 1 ATOM 1410 C CG . ASP A 1 190 ? 25.696 44.589 113.898 1.00 40.76 ? 218 ASP A CG 1 ATOM 1411 O OD1 . ASP A 1 190 ? 24.847 45.437 113.549 1.00 32.85 ? 218 ASP A OD1 1 ATOM 1412 O OD2 . ASP A 1 190 ? 26.235 44.628 115.027 1.00 39.76 ? 218 ASP A OD2 1 ATOM 1413 N N . VAL A 1 191 ? 24.510 45.456 110.396 1.00 32.93 ? 219 VAL A N 1 ATOM 1414 C CA . VAL A 1 191 ? 24.562 46.746 109.714 1.00 32.38 ? 219 VAL A CA 1 ATOM 1415 C C . VAL A 1 191 ? 24.081 47.900 110.604 1.00 33.95 ? 219 VAL A C 1 ATOM 1416 O O . VAL A 1 191 ? 22.901 47.969 110.957 1.00 32.31 ? 219 VAL A O 1 ATOM 1417 C CB . VAL A 1 191 ? 23.696 46.700 108.458 1.00 31.50 ? 219 VAL A CB 1 ATOM 1418 C CG1 . VAL A 1 191 ? 23.909 47.943 107.638 1.00 33.89 ? 219 VAL A CG1 1 ATOM 1419 C CG2 . VAL A 1 191 ? 24.070 45.490 107.637 1.00 30.44 ? 219 VAL A CG2 1 ATOM 1420 N N . PRO A 1 192 ? 24.995 48.788 111.010 1.00 35.11 ? 220 PRO A N 1 ATOM 1421 C CA . PRO A 1 192 ? 24.547 49.879 111.886 1.00 38.71 ? 220 PRO A CA 1 ATOM 1422 C C . PRO A 1 192 ? 23.911 51.054 111.120 1.00 39.54 ? 220 PRO A C 1 ATOM 1423 O O . PRO A 1 192 ? 24.609 51.961 110.681 1.00 34.62 ? 220 PRO A O 1 ATOM 1424 C CB . PRO A 1 192 ? 25.841 50.321 112.584 1.00 35.39 ? 220 PRO A CB 1 ATOM 1425 C CG . PRO A 1 192 ? 26.963 49.772 111.760 1.00 33.41 ? 220 PRO A CG 1 ATOM 1426 C CD . PRO A 1 192 ? 26.418 48.905 110.673 1.00 31.95 ? 220 PRO A CD 1 ATOM 1427 N N . LEU A 1 193 ? 22.591 51.025 110.971 1.00 40.36 ? 221 LEU A N 1 ATOM 1428 C CA . LEU A 1 193 ? 21.868 52.082 110.270 1.00 33.87 ? 221 LEU A CA 1 ATOM 1429 C C . LEU A 1 193 ? 21.960 53.394 111.033 1.00 41.75 ? 221 LEU A C 1 ATOM 1430 O O . LEU A 1 193 ? 21.550 53.470 112.208 1.00 37.74 ? 221 LEU A O 1 ATOM 1431 C CB . LEU A 1 193 ? 20.389 51.717 110.050 1.00 31.19 ? 221 LEU A CB 1 ATOM 1432 C CG . LEU A 1 193 ? 19.963 50.776 108.933 1.00 43.41 ? 221 LEU A CG 1 ATOM 1433 C CD1 . LEU A 1 193 ? 20.924 49.627 108.739 1.00 42.68 ? 221 LEU A CD1 1 ATOM 1434 C CD2 . LEU A 1 193 ? 18.549 50.274 109.188 1.00 39.74 ? 221 LEU A CD2 1 ATOM 1435 N N . PRO A 1 194 ? 22.491 54.430 110.356 1.00 42.76 ? 222 PRO A N 1 ATOM 1436 C CA . PRO A 1 194 ? 22.758 55.779 110.868 1.00 49.08 ? 222 PRO A CA 1 ATOM 1437 C C . PRO A 1 194 ? 21.505 56.344 111.504 1.00 58.26 ? 222 PRO A C 1 ATOM 1438 O O . PRO A 1 194 ? 21.590 57.085 112.487 1.00 70.68 ? 222 PRO A O 1 ATOM 1439 C CB . PRO A 1 194 ? 23.109 56.596 109.622 1.00 51.51 ? 222 PRO A CB 1 ATOM 1440 C CG . PRO A 1 194 ? 23.114 55.669 108.483 1.00 51.41 ? 222 PRO A CG 1 ATOM 1441 C CD . PRO A 1 194 ? 22.856 54.280 108.938 1.00 47.45 ? 222 PRO A CD 1 ATOM 1442 N N . VAL A 1 195 ? 20.363 55.990 110.920 1.00 54.86 ? 223 VAL A N 1 ATOM 1443 C CA . VAL A 1 195 ? 19.049 56.355 111.437 1.00 71.18 ? 223 VAL A CA 1 ATOM 1444 C C . VAL A 1 195 ? 18.942 56.283 112.972 1.00 72.84 ? 223 VAL A C 1 ATOM 1445 O O . VAL A 1 195 ? 19.239 57.249 113.686 1.00 68.29 ? 223 VAL A O 1 ATOM 1446 C CB . VAL A 1 195 ? 17.945 55.468 110.797 1.00 88.67 ? 223 VAL A CB 1 ATOM 1447 N N . ALA B 1 1 ? 13.230 18.704 77.910 1.00 57.99 ? 29 ALA B N 1 ATOM 1448 C CA . ALA B 1 1 ? 14.668 18.549 77.689 1.00 65.62 ? 29 ALA B CA 1 ATOM 1449 C C . ALA B 1 1 ? 15.374 19.856 77.246 1.00 71.77 ? 29 ALA B C 1 ATOM 1450 O O . ALA B 1 1 ? 14.997 20.450 76.240 1.00 55.66 ? 29 ALA B O 1 ATOM 1451 C CB . ALA B 1 1 ? 14.902 17.426 76.673 1.00 75.76 ? 29 ALA B CB 1 ATOM 1452 N N . ASN B 1 2 ? 16.389 20.295 78.002 1.00 84.75 ? 30 ASN B N 1 ATOM 1453 C CA . ASN B 1 2 ? 17.256 21.412 77.599 1.00 94.67 ? 30 ASN B CA 1 ATOM 1454 C C . ASN B 1 2 ? 16.502 22.709 77.187 1.00 41.81 ? 30 ASN B C 1 ATOM 1455 O O . ASN B 1 2 ? 15.641 23.176 77.920 1.00 47.61 ? 30 ASN B O 1 ATOM 1456 C CB . ASN B 1 2 ? 18.162 20.819 76.495 1.00 116.47 ? 30 ASN B CB 1 ATOM 1457 C CG . ASN B 1 2 ? 19.174 21.784 75.919 1.00 122.05 ? 30 ASN B CG 1 ATOM 1458 O OD1 . ASN B 1 2 ? 18.825 22.838 75.383 1.00 127.66 ? 30 ASN B OD1 1 ATOM 1459 N ND2 . ASN B 1 2 ? 20.446 21.430 76.044 1.00 125.24 ? 30 ASN B ND2 1 ATOM 1460 N N . PHE B 1 3 ? 16.858 23.316 76.058 1.00 43.18 ? 31 PHE B N 1 ATOM 1461 C CA . PHE B 1 3 ? 16.000 24.274 75.360 1.00 37.21 ? 31 PHE B CA 1 ATOM 1462 C C . PHE B 1 3 ? 15.525 23.583 74.095 1.00 43.79 ? 31 PHE B C 1 ATOM 1463 O O . PHE B 1 3 ? 16.329 22.991 73.396 1.00 45.80 ? 31 PHE B O 1 ATOM 1464 C CB . PHE B 1 3 ? 16.751 25.535 74.936 1.00 30.64 ? 31 PHE B CB 1 ATOM 1465 C CG . PHE B 1 3 ? 17.211 26.399 76.069 1.00 33.22 ? 31 PHE B CG 1 ATOM 1466 C CD1 . PHE B 1 3 ? 16.779 26.173 77.382 1.00 27.11 ? 31 PHE B CD1 1 ATOM 1467 C CD2 . PHE B 1 3 ? 18.084 27.449 75.817 1.00 23.65 ? 31 PHE B CD2 1 ATOM 1468 C CE1 . PHE B 1 3 ? 17.206 26.983 78.410 1.00 34.63 ? 31 PHE B CE1 1 ATOM 1469 C CE2 . PHE B 1 3 ? 18.519 28.264 76.856 1.00 34.76 ? 31 PHE B CE2 1 ATOM 1470 C CZ . PHE B 1 3 ? 18.071 28.035 78.150 1.00 36.66 ? 31 PHE B CZ 1 ATOM 1471 N N . THR B 1 4 ? 14.242 23.674 73.772 1.00 44.68 ? 32 THR B N 1 ATOM 1472 C CA . THR B 1 4 ? 13.759 23.047 72.549 1.00 45.17 ? 32 THR B CA 1 ATOM 1473 C C . THR B 1 4 ? 14.208 23.856 71.349 1.00 47.97 ? 32 THR B C 1 ATOM 1474 O O . THR B 1 4 ? 14.510 25.040 71.466 1.00 44.38 ? 32 THR B O 1 ATOM 1475 C CB . THR B 1 4 ? 12.235 22.888 72.529 1.00 42.83 ? 32 THR B CB 1 ATOM 1476 O OG1 . THR B 1 4 ? 11.632 24.176 72.636 1.00 45.14 ? 32 THR B OG1 1 ATOM 1477 C CG2 . THR B 1 4 ? 11.789 22.045 73.695 1.00 33.34 ? 32 THR B CG2 1 ATOM 1478 N N . CYS B 1 5 ? 14.285 23.205 70.196 1.00 41.33 ? 33 CYS B N 1 ATOM 1479 C CA . CYS B 1 5 ? 14.661 23.895 68.984 1.00 38.52 ? 33 CYS B CA 1 ATOM 1480 C C . CYS B 1 5 ? 13.875 23.229 67.891 1.00 40.06 ? 33 CYS B C 1 ATOM 1481 O O . CYS B 1 5 ? 13.844 22.012 67.807 1.00 49.97 ? 33 CYS B O 1 ATOM 1482 C CB . CYS B 1 5 ? 16.160 23.783 68.727 1.00 44.92 ? 33 CYS B CB 1 ATOM 1483 S SG . CYS B 1 5 ? 16.713 24.726 67.289 1.00 49.84 ? 33 CYS B SG 1 ATOM 1484 N N . ALA B 1 6 ? 13.194 24.028 67.084 1.00 37.55 ? 34 ALA B N 1 ATOM 1485 C CA . ALA B 1 6 ? 12.247 23.487 66.124 1.00 38.58 ? 34 ALA B CA 1 ATOM 1486 C C . ALA B 1 6 ? 12.677 23.728 64.677 1.00 42.01 ? 34 ALA B C 1 ATOM 1487 O O . ALA B 1 6 ? 11.900 23.553 63.744 1.00 47.06 ? 34 ALA B O 1 ATOM 1488 C CB . ALA B 1 6 ? 10.850 24.039 66.384 1.00 36.43 ? 34 ALA B CB 1 ATOM 1489 N N . VAL B 1 7 ? 13.909 24.165 64.479 1.00 35.90 ? 35 VAL B N 1 ATOM 1490 C CA . VAL B 1 7 ? 14.399 24.304 63.126 1.00 32.11 ? 35 VAL B CA 1 ATOM 1491 C C . VAL B 1 7 ? 14.878 22.955 62.582 1.00 36.41 ? 35 VAL B C 1 ATOM 1492 O O . VAL B 1 7 ? 14.818 21.924 63.263 1.00 34.45 ? 35 VAL B O 1 ATOM 1493 C CB . VAL B 1 7 ? 15.550 25.322 63.049 1.00 46.95 ? 35 VAL B CB 1 ATOM 1494 C CG1 . VAL B 1 7 ? 15.077 26.684 63.501 1.00 45.85 ? 35 VAL B CG1 1 ATOM 1495 C CG2 . VAL B 1 7 ? 16.749 24.836 63.863 1.00 39.56 ? 35 VAL B CG2 1 ATOM 1496 N N . ALA B 1 8 ? 15.324 22.957 61.333 1.00 39.58 ? 36 ALA B N 1 ATOM 1497 C CA . ALA B 1 8 ? 15.787 21.726 60.707 1.00 48.54 ? 36 ALA B CA 1 ATOM 1498 C C . ALA B 1 8 ? 16.999 21.186 61.457 1.00 52.62 ? 36 ALA B C 1 ATOM 1499 O O . ALA B 1 8 ? 17.898 21.953 61.839 1.00 45.57 ? 36 ALA B O 1 ATOM 1500 C CB . ALA B 1 8 ? 16.128 21.959 59.244 1.00 45.13 ? 36 ALA B CB 1 ATOM 1501 N N . SER B 1 9 ? 17.000 19.874 61.680 1.00 49.55 ? 37 SER B N 1 ATOM 1502 C CA . SER B 1 9 ? 18.128 19.185 62.287 1.00 50.87 ? 37 SER B CA 1 ATOM 1503 C C . SER B 1 9 ? 19.423 19.527 61.539 1.00 47.94 ? 37 SER B C 1 ATOM 1504 O O . SER B 1 9 ? 19.438 19.563 60.313 1.00 54.89 ? 37 SER B O 1 ATOM 1505 C CB . SER B 1 9 ? 17.874 17.673 62.255 1.00 53.33 ? 37 SER B CB 1 ATOM 1506 O OG . SER B 1 9 ? 18.996 16.947 62.722 1.00 55.69 ? 37 SER B OG 1 ATOM 1507 N N . GLY B 1 10 ? 20.497 19.787 62.279 1.00 43.51 ? 38 GLY B N 1 ATOM 1508 C CA . GLY B 1 10 ? 21.778 20.144 61.692 1.00 43.16 ? 38 GLY B CA 1 ATOM 1509 C C . GLY B 1 10 ? 22.030 21.638 61.594 1.00 46.96 ? 38 GLY B C 1 ATOM 1510 O O . GLY B 1 10 ? 23.127 22.090 61.215 1.00 39.91 ? 38 GLY B O 1 ATOM 1511 N N . THR B 1 11 ? 21.007 22.422 61.912 1.00 39.97 ? 39 THR B N 1 ATOM 1512 C CA . THR B 1 11 ? 21.169 23.860 61.914 1.00 34.38 ? 39 THR B CA 1 ATOM 1513 C C . THR B 1 11 ? 22.108 24.296 63.021 1.00 36.49 ? 39 THR B C 1 ATOM 1514 O O . THR B 1 11 ? 21.972 23.840 64.166 1.00 37.32 ? 39 THR B O 1 ATOM 1515 C CB . THR B 1 11 ? 19.819 24.582 62.126 1.00 42.91 ? 39 THR B CB 1 ATOM 1516 O OG1 . THR B 1 11 ? 18.905 24.262 61.061 1.00 40.18 ? 39 THR B OG1 1 ATOM 1517 C CG2 . THR B 1 11 ? 20.032 26.090 62.204 1.00 32.90 ? 39 THR B CG2 1 ATOM 1518 N N . THR B 1 12 ? 23.044 25.191 62.704 1.00 30.01 ? 40 THR B N 1 ATOM 1519 C CA . THR B 1 12 ? 23.819 25.812 63.767 1.00 40.24 ? 40 THR B CA 1 ATOM 1520 C C . THR B 1 12 ? 23.642 27.350 63.810 1.00 34.64 ? 40 THR B C 1 ATOM 1521 O O . THR B 1 12 ? 23.459 28.005 62.787 1.00 40.65 ? 40 THR B O 1 ATOM 1522 C CB . THR B 1 12 ? 25.316 25.459 63.687 1.00 37.21 ? 40 THR B CB 1 ATOM 1523 O OG1 . THR B 1 12 ? 25.985 26.356 62.791 1.00 35.28 ? 40 THR B OG1 1 ATOM 1524 C CG2 . THR B 1 12 ? 25.507 24.027 63.240 1.00 34.95 ? 40 THR B CG2 1 ATOM 1525 N N . CYS B 1 13 ? 23.667 27.923 65.001 1.00 29.02 ? 41 CYS B N 1 ATOM 1526 C CA . CYS B 1 13 ? 23.658 29.383 65.116 1.00 41.26 ? 41 CYS B CA 1 ATOM 1527 C C . CYS B 1 13 ? 24.453 29.791 66.344 1.00 45.36 ? 41 CYS B C 1 ATOM 1528 O O . CYS B 1 13 ? 24.913 28.936 67.103 1.00 46.03 ? 41 CYS B O 1 ATOM 1529 C CB . CYS B 1 13 ? 22.230 29.948 65.196 1.00 25.66 ? 41 CYS B CB 1 ATOM 1530 S SG . CYS B 1 13 ? 21.337 29.421 66.679 1.00 38.47 ? 41 CYS B SG 1 ATOM 1531 N N . LYS B 1 14 ? 24.596 31.096 66.553 1.00 43.69 ? 42 LYS B N 1 ATOM 1532 C CA . LYS B 1 14 ? 25.272 31.600 67.739 1.00 42.37 ? 42 LYS B CA 1 ATOM 1533 C C . LYS B 1 14 ? 24.311 31.714 68.919 1.00 38.95 ? 42 LYS B C 1 ATOM 1534 O O . LYS B 1 14 ? 23.235 32.283 68.789 1.00 38.72 ? 42 LYS B O 1 ATOM 1535 C CB . LYS B 1 14 ? 25.893 32.969 67.481 1.00 50.52 ? 42 LYS B CB 1 ATOM 1536 C CG . LYS B 1 14 ? 26.713 33.447 68.673 1.00 64.92 ? 42 LYS B CG 1 ATOM 1537 C CD . LYS B 1 14 ? 27.463 34.747 68.412 1.00 71.78 ? 42 LYS B CD 1 ATOM 1538 C CE . LYS B 1 14 ? 27.543 35.573 69.695 1.00 75.11 ? 42 LYS B CE 1 ATOM 1539 N NZ . LYS B 1 14 ? 27.268 37.020 69.492 1.00 81.66 ? 42 LYS B NZ 1 ATOM 1540 N N . SER B 1 15 ? 24.709 31.164 70.065 1.00 31.26 ? 43 SER B N 1 ATOM 1541 C CA . SER B 1 15 ? 23.959 31.308 71.313 1.00 28.13 ? 43 SER B CA 1 ATOM 1542 C C . SER B 1 15 ? 24.920 31.727 72.422 1.00 33.25 ? 43 SER B C 1 ATOM 1543 O O . SER B 1 15 ? 26.128 31.892 72.188 1.00 33.77 ? 43 SER B O 1 ATOM 1544 C CB . SER B 1 15 ? 23.310 29.984 71.719 1.00 35.90 ? 43 SER B CB 1 ATOM 1545 O OG . SER B 1 15 ? 22.302 29.579 70.828 1.00 43.86 ? 43 SER B OG 1 ATOM 1546 N N . ALA B 1 16 ? 24.396 31.869 73.640 1.00 33.87 ? 44 ALA B N 1 ATOM 1547 C CA . ALA B 1 16 ? 25.240 32.188 74.794 1.00 30.83 ? 44 ALA B CA 1 ATOM 1548 C C . ALA B 1 16 ? 24.645 31.691 76.099 1.00 29.81 ? 44 ALA B C 1 ATOM 1549 O O . ALA B 1 16 ? 23.432 31.481 76.205 1.00 29.82 ? 44 ALA B O 1 ATOM 1550 C CB . ALA B 1 16 ? 25.508 33.696 74.873 1.00 28.93 ? 44 ALA B CB 1 ATOM 1551 N N . ILE B 1 17 ? 25.504 31.521 77.097 1.00 26.40 ? 45 ILE B N 1 ATOM 1552 C CA . ILE B 1 17 ? 25.056 31.314 78.462 1.00 28.68 ? 45 ILE B CA 1 ATOM 1553 C C . ILE B 1 17 ? 25.550 32.510 79.234 1.00 34.66 ? 45 ILE B C 1 ATOM 1554 O O . ILE B 1 17 ? 26.600 33.047 78.909 1.00 30.48 ? 45 ILE B O 1 ATOM 1555 C CB . ILE B 1 17 ? 25.628 29.993 79.118 1.00 30.41 ? 45 ILE B CB 1 ATOM 1556 C CG1 . ILE B 1 17 ? 27.166 30.005 79.195 1.00 26.63 ? 45 ILE B CG1 1 ATOM 1557 C CG2 . ILE B 1 17 ? 25.149 28.770 78.369 1.00 32.22 ? 45 ILE B CG2 1 ATOM 1558 C CD1 . ILE B 1 17 ? 27.750 28.777 79.891 1.00 22.30 ? 45 ILE B CD1 1 ATOM 1559 N N . LEU B 1 18 ? 24.798 32.931 80.246 1.00 32.29 ? 46 LEU B N 1 ATOM 1560 C CA . LEU B 1 18 ? 25.302 33.931 81.158 1.00 33.61 ? 46 LEU B CA 1 ATOM 1561 C C . LEU B 1 18 ? 25.968 33.169 82.272 1.00 30.61 ? 46 LEU B C 1 ATOM 1562 O O . LEU B 1 18 ? 25.310 32.628 83.140 1.00 31.91 ? 46 LEU B O 1 ATOM 1563 C CB . LEU B 1 18 ? 24.192 34.849 81.696 1.00 21.00 ? 46 LEU B CB 1 ATOM 1564 C CG . LEU B 1 18 ? 24.731 35.906 82.670 1.00 29.10 ? 46 LEU B CG 1 ATOM 1565 C CD1 . LEU B 1 18 ? 25.695 36.911 81.978 1.00 23.57 ? 46 LEU B CD1 1 ATOM 1566 C CD2 . LEU B 1 18 ? 23.610 36.608 83.433 1.00 23.37 ? 46 LEU B CD2 1 ATOM 1567 N N . TYR B 1 19 ? 27.286 33.130 82.237 1.00 33.14 ? 47 TYR B N 1 ATOM 1568 C CA . TYR B 1 19 ? 28.030 32.271 83.127 1.00 36.67 ? 47 TYR B CA 1 ATOM 1569 C C . TYR B 1 19 ? 28.420 32.928 84.426 1.00 32.15 ? 47 TYR B C 1 ATOM 1570 O O . TYR B 1 19 ? 28.968 34.016 84.427 1.00 35.51 ? 47 TYR B O 1 ATOM 1571 C CB . TYR B 1 19 ? 29.295 31.801 82.424 1.00 29.85 ? 47 TYR B CB 1 ATOM 1572 C CG . TYR B 1 19 ? 30.096 30.824 83.228 1.00 33.37 ? 47 TYR B CG 1 ATOM 1573 C CD1 . TYR B 1 19 ? 29.570 29.572 83.555 1.00 24.10 ? 47 TYR B CD1 1 ATOM 1574 C CD2 . TYR B 1 19 ? 31.396 31.127 83.636 1.00 32.00 ? 47 TYR B CD2 1 ATOM 1575 C CE1 . TYR B 1 19 ? 30.312 28.650 84.276 1.00 22.11 ? 47 TYR B CE1 1 ATOM 1576 C CE2 . TYR B 1 19 ? 32.154 30.206 84.351 1.00 30.17 ? 47 TYR B CE2 1 ATOM 1577 C CZ . TYR B 1 19 ? 31.604 28.970 84.668 1.00 32.27 ? 47 TYR B CZ 1 ATOM 1578 O OH . TYR B 1 19 ? 32.336 28.056 85.388 1.00 27.82 ? 47 TYR B OH 1 ATOM 1579 N N . THR B 1 20 ? 28.183 32.235 85.531 1.00 28.82 ? 48 THR B N 1 ATOM 1580 C CA . THR B 1 20 ? 28.629 32.717 86.830 1.00 26.32 ? 48 THR B CA 1 ATOM 1581 C C . THR B 1 20 ? 29.916 32.031 87.292 1.00 31.43 ? 48 THR B C 1 ATOM 1582 O O . THR B 1 20 ? 29.935 30.824 87.558 1.00 41.12 ? 48 THR B O 1 ATOM 1583 C CB . THR B 1 20 ? 27.541 32.495 87.893 1.00 28.95 ? 48 THR B CB 1 ATOM 1584 O OG1 . THR B 1 20 ? 26.287 32.969 87.397 1.00 40.72 ? 48 THR B OG1 1 ATOM 1585 C CG2 . THR B 1 20 ? 27.899 33.214 89.170 1.00 21.91 ? 48 THR B CG2 1 ATOM 1586 N N . SER B 1 21 ? 30.986 32.805 87.428 1.00 32.93 ? 49 SER B N 1 ATOM 1587 C CA . SER B 1 21 ? 32.273 32.214 87.769 1.00 30.73 ? 49 SER B CA 1 ATOM 1588 C C . SER B 1 21 ? 32.342 31.700 89.210 1.00 26.61 ? 49 SER B C 1 ATOM 1589 O O . SER B 1 21 ? 32.253 32.469 90.152 1.00 29.16 ? 49 SER B O 1 ATOM 1590 C CB . SER B 1 21 ? 33.376 33.225 87.546 1.00 29.31 ? 49 SER B CB 1 ATOM 1591 O OG . SER B 1 21 ? 34.637 32.637 87.809 1.00 44.05 ? 49 SER B OG 1 ATOM 1592 N N . PRO B 1 22 ? 32.537 30.388 89.379 1.00 33.73 ? 50 PRO B N 1 ATOM 1593 C CA . PRO B 1 22 ? 32.607 29.828 90.736 1.00 27.82 ? 50 PRO B CA 1 ATOM 1594 C C . PRO B 1 22 ? 33.774 30.415 91.538 1.00 35.85 ? 50 PRO B C 1 ATOM 1595 O O . PRO B 1 22 ? 33.664 30.547 92.745 1.00 44.56 ? 50 PRO B O 1 ATOM 1596 C CB . PRO B 1 22 ? 32.851 28.338 90.491 1.00 24.92 ? 50 PRO B CB 1 ATOM 1597 C CG . PRO B 1 22 ? 32.437 28.096 89.057 1.00 30.14 ? 50 PRO B CG 1 ATOM 1598 C CD . PRO B 1 22 ? 32.780 29.368 88.339 1.00 25.30 ? 50 PRO B CD 1 ATOM 1599 N N . ASN B 1 23 ? 34.871 30.762 90.870 1.00 40.10 ? 51 ASN B N 1 ATOM 1600 C CA . ASN B 1 23 ? 36.091 31.228 91.534 1.00 42.16 ? 51 ASN B CA 1 ATOM 1601 C C . ASN B 1 23 ? 36.636 32.498 90.897 1.00 44.04 ? 51 ASN B C 1 ATOM 1602 O O . ASN B 1 23 ? 36.159 32.914 89.849 1.00 44.75 ? 51 ASN B O 1 ATOM 1603 C CB . ASN B 1 23 ? 37.194 30.156 91.443 1.00 49.50 ? 51 ASN B CB 1 ATOM 1604 C CG . ASN B 1 23 ? 36.836 28.877 92.158 1.00 67.58 ? 51 ASN B CG 1 ATOM 1605 O OD1 . ASN B 1 23 ? 35.916 28.855 92.981 1.00 73.82 ? 51 ASN B OD1 1 ATOM 1606 N ND2 . ASN B 1 23 ? 37.582 27.801 91.876 1.00 68.02 ? 51 ASN B ND2 1 ATOM 1607 N N . ALA B 1 24 ? 37.654 33.093 91.516 1.00 47.97 ? 52 ALA B N 1 ATOM 1608 C CA . ALA B 1 24 ? 38.386 34.180 90.874 1.00 44.59 ? 52 ALA B CA 1 ATOM 1609 C C . ALA B 1 24 ? 39.181 33.534 89.766 1.00 47.17 ? 52 ALA B C 1 ATOM 1610 O O . ALA B 1 24 ? 39.842 32.531 89.987 1.00 43.98 ? 52 ALA B O 1 ATOM 1611 C CB . ALA B 1 24 ? 39.314 34.878 91.850 1.00 28.34 ? 52 ALA B CB 1 ATOM 1612 N N . THR B 1 25 ? 39.156 34.130 88.586 1.00 38.23 ? 53 THR B N 1 ATOM 1613 C CA . THR B 1 25 ? 39.817 33.523 87.456 1.00 41.83 ? 53 THR B CA 1 ATOM 1614 C C . THR B 1 25 ? 40.201 34.645 86.509 1.00 44.08 ? 53 THR B C 1 ATOM 1615 O O . THR B 1 25 ? 40.280 35.797 86.929 1.00 50.38 ? 53 THR B O 1 ATOM 1616 C CB . THR B 1 25 ? 38.881 32.485 86.761 1.00 37.35 ? 53 THR B CB 1 ATOM 1617 O OG1 . THR B 1 25 ? 39.559 31.861 85.670 1.00 42.48 ? 53 THR B OG1 1 ATOM 1618 C CG2 . THR B 1 25 ? 37.614 33.144 86.244 1.00 37.68 ? 53 THR B CG2 1 ATOM 1619 N N . THR B 1 26 ? 40.460 34.318 85.247 1.00 36.27 ? 54 THR B N 1 ATOM 1620 C CA . THR B 1 26 ? 40.742 35.331 84.244 1.00 33.58 ? 54 THR B CA 1 ATOM 1621 C C . THR B 1 26 ? 39.955 34.999 82.977 1.00 37.21 ? 54 THR B C 1 ATOM 1622 O O . THR B 1 26 ? 39.447 33.888 82.818 1.00 41.52 ? 54 THR B O 1 ATOM 1623 C CB . THR B 1 26 ? 42.246 35.375 83.901 1.00 36.19 ? 54 THR B CB 1 ATOM 1624 O OG1 . THR B 1 26 ? 42.607 34.180 83.205 1.00 40.20 ? 54 THR B OG1 1 ATOM 1625 C CG2 . THR B 1 26 ? 43.115 35.526 85.178 1.00 23.35 ? 54 THR B CG2 1 ATOM 1626 N N . TYR B 1 27 ? 39.863 35.965 82.073 1.00 32.85 ? 55 TYR B N 1 ATOM 1627 C CA . TYR B 1 27 ? 39.221 35.753 80.782 1.00 38.62 ? 55 TYR B CA 1 ATOM 1628 C C . TYR B 1 27 ? 39.873 34.599 80.005 1.00 43.55 ? 55 TYR B C 1 ATOM 1629 O O . TYR B 1 27 ? 39.194 33.786 79.371 1.00 40.72 ? 55 TYR B O 1 ATOM 1630 C CB . TYR B 1 27 ? 39.261 37.051 79.966 1.00 41.86 ? 55 TYR B CB 1 ATOM 1631 C CG . TYR B 1 27 ? 38.390 38.111 80.581 1.00 35.77 ? 55 TYR B CG 1 ATOM 1632 C CD1 . TYR B 1 27 ? 37.010 38.097 80.406 1.00 39.71 ? 55 TYR B CD1 1 ATOM 1633 C CD2 . TYR B 1 27 ? 38.942 39.088 81.417 1.00 45.33 ? 55 TYR B CD2 1 ATOM 1634 C CE1 . TYR B 1 27 ? 36.202 39.056 81.017 1.00 44.86 ? 55 TYR B CE1 1 ATOM 1635 C CE2 . TYR B 1 27 ? 38.140 40.055 82.036 1.00 35.65 ? 55 TYR B CE2 1 ATOM 1636 C CZ . TYR B 1 27 ? 36.777 40.037 81.822 1.00 42.58 ? 55 TYR B CZ 1 ATOM 1637 O OH . TYR B 1 27 ? 35.991 40.989 82.439 1.00 56.85 ? 55 TYR B OH 1 ATOM 1638 N N . GLY B 1 28 ? 41.198 34.542 80.064 1.00 40.87 ? 56 GLY B N 1 ATOM 1639 C CA . GLY B 1 28 ? 41.952 33.498 79.407 1.00 29.20 ? 56 GLY B CA 1 ATOM 1640 C C . GLY B 1 28 ? 41.565 32.119 79.889 1.00 34.36 ? 56 GLY B C 1 ATOM 1641 O O . GLY B 1 28 ? 41.392 31.202 79.085 1.00 44.41 ? 56 GLY B O 1 ATOM 1642 N N . ASN B 1 29 ? 41.424 31.960 81.202 1.00 35.18 ? 57 ASN B N 1 ATOM 1643 C CA . ASN B 1 29 ? 41.009 30.670 81.755 1.00 42.40 ? 57 ASN B CA 1 ATOM 1644 C C . ASN B 1 29 ? 39.597 30.293 81.288 1.00 43.89 ? 57 ASN B C 1 ATOM 1645 O O . ASN B 1 29 ? 39.312 29.138 80.996 1.00 42.97 ? 57 ASN B O 1 ATOM 1646 C CB . ASN B 1 29 ? 41.059 30.678 83.290 1.00 44.90 ? 57 ASN B CB 1 ATOM 1647 C CG . ASN B 1 29 ? 42.473 30.794 83.842 1.00 47.99 ? 57 ASN B CG 1 ATOM 1648 O OD1 . ASN B 1 29 ? 43.463 30.560 83.144 1.00 43.99 ? 57 ASN B OD1 1 ATOM 1649 N ND2 . ASN B 1 29 ? 42.568 31.150 85.117 1.00 59.28 ? 57 ASN B ND2 1 ATOM 1650 N N . LEU B 1 30 ? 38.725 31.290 81.206 1.00 41.29 ? 58 LEU B N 1 ATOM 1651 C CA . LEU B 1 30 ? 37.369 31.082 80.738 1.00 36.16 ? 58 LEU B CA 1 ATOM 1652 C C . LEU B 1 30 ? 37.366 30.607 79.294 1.00 37.80 ? 58 LEU B C 1 ATOM 1653 O O . LEU B 1 30 ? 36.648 29.672 78.936 1.00 44.01 ? 58 LEU B O 1 ATOM 1654 C CB . LEU B 1 30 ? 36.578 32.386 80.838 1.00 30.25 ? 58 LEU B CB 1 ATOM 1655 C CG . LEU B 1 30 ? 36.280 32.801 82.276 1.00 35.63 ? 58 LEU B CG 1 ATOM 1656 C CD1 . LEU B 1 30 ? 35.487 34.120 82.313 1.00 36.31 ? 58 LEU B CD1 1 ATOM 1657 C CD2 . LEU B 1 30 ? 35.574 31.683 83.032 1.00 41.21 ? 58 LEU B CD2 1 ATOM 1658 N N . VAL B 1 31 ? 38.150 31.280 78.462 1.00 38.30 ? 59 VAL B N 1 ATOM 1659 C CA . VAL B 1 31 ? 38.334 30.876 77.073 1.00 46.71 ? 59 VAL B CA 1 ATOM 1660 C C . VAL B 1 31 ? 38.802 29.433 76.951 1.00 49.13 ? 59 VAL B C 1 ATOM 1661 O O . VAL B 1 31 ? 38.236 28.665 76.180 1.00 55.79 ? 59 VAL B O 1 ATOM 1662 C CB . VAL B 1 31 ? 39.366 31.788 76.355 1.00 45.15 ? 59 VAL B CB 1 ATOM 1663 C CG1 . VAL B 1 31 ? 39.830 31.163 75.033 1.00 29.25 ? 59 VAL B CG1 1 ATOM 1664 C CG2 . VAL B 1 31 ? 38.818 33.219 76.191 1.00 33.21 ? 59 VAL B CG2 1 ATOM 1665 N N . ALA B 1 32 ? 39.784 29.050 77.764 1.00 41.48 ? 60 ALA B N 1 ATOM 1666 C CA . ALA B 1 32 ? 40.330 27.699 77.710 1.00 37.71 ? 60 ALA B CA 1 ATOM 1667 C C . ALA B 1 32 ? 39.315 26.667 78.164 1.00 37.98 ? 60 ALA B C 1 ATOM 1668 O O . ALA B 1 32 ? 39.134 25.638 77.512 1.00 45.78 ? 60 ALA B O 1 ATOM 1669 C CB . ALA B 1 32 ? 41.605 27.588 78.534 1.00 36.77 ? 60 ALA B CB 1 ATOM 1670 N N . ARG B 1 33 ? 38.650 26.942 79.280 1.00 26.29 ? 61 ARG B N 1 ATOM 1671 C CA . ARG B 1 33 ? 37.650 26.009 79.805 1.00 35.31 ? 61 ARG B CA 1 ATOM 1672 C C . ARG B 1 33 ? 36.490 25.797 78.847 1.00 40.09 ? 61 ARG B C 1 ATOM 1673 O O . ARG B 1 33 ? 35.970 24.695 78.715 1.00 41.86 ? 61 ARG B O 1 ATOM 1674 C CB . ARG B 1 33 ? 37.091 26.505 81.148 1.00 35.25 ? 61 ARG B CB 1 ATOM 1675 C CG . ARG B 1 33 ? 35.728 25.878 81.477 1.00 43.04 ? 61 ARG B CG 1 ATOM 1676 C CD . ARG B 1 33 ? 35.166 26.279 82.825 1.00 48.46 ? 61 ARG B CD 1 ATOM 1677 N NE . ARG B 1 33 ? 36.205 26.295 83.838 1.00 52.78 ? 61 ARG B NE 1 ATOM 1678 C CZ . ARG B 1 33 ? 36.085 26.838 85.042 1.00 56.39 ? 61 ARG B CZ 1 ATOM 1679 N NH1 . ARG B 1 33 ? 34.947 27.419 85.413 1.00 44.61 ? 61 ARG B NH1 1 ATOM 1680 N NH2 . ARG B 1 33 ? 37.115 26.790 85.878 1.00 60.27 ? 61 ARG B NH2 1 ATOM 1681 N N . PHE B 1 34 ? 36.068 26.861 78.183 1.00 41.23 ? 62 PHE B N 1 ATOM 1682 C CA . PHE B 1 34 ? 34.918 26.740 77.314 1.00 39.03 ? 62 PHE B CA 1 ATOM 1683 C C . PHE B 1 34 ? 35.357 26.397 75.888 1.00 42.72 ? 62 PHE B C 1 ATOM 1684 O O . PHE B 1 34 ? 34.783 25.512 75.251 1.00 33.72 ? 62 PHE B O 1 ATOM 1685 C CB . PHE B 1 34 ? 33.994 27.960 77.433 1.00 28.13 ? 62 PHE B CB 1 ATOM 1686 C CG . PHE B 1 34 ? 33.099 27.909 78.658 1.00 36.19 ? 62 PHE B CG 1 ATOM 1687 C CD1 . PHE B 1 34 ? 31.877 27.247 78.613 1.00 25.56 ? 62 PHE B CD1 1 ATOM 1688 C CD2 . PHE B 1 34 ? 33.489 28.505 79.859 1.00 34.17 ? 62 PHE B CD2 1 ATOM 1689 C CE1 . PHE B 1 34 ? 31.058 27.171 79.736 1.00 29.61 ? 62 PHE B CE1 1 ATOM 1690 C CE2 . PHE B 1 34 ? 32.665 28.447 80.985 1.00 32.70 ? 62 PHE B CE2 1 ATOM 1691 C CZ . PHE B 1 34 ? 31.445 27.779 80.921 1.00 31.10 ? 62 PHE B CZ 1 ATOM 1692 N N . ASN B 1 35 ? 36.383 27.094 75.407 1.00 33.22 ? 63 ASN B N 1 ATOM 1693 C CA . ASN B 1 35 ? 36.960 26.815 74.095 1.00 39.97 ? 63 ASN B CA 1 ATOM 1694 C C . ASN B 1 35 ? 35.922 26.855 73.002 1.00 33.65 ? 63 ASN B C 1 ATOM 1695 O O . ASN B 1 35 ? 36.023 26.118 72.036 1.00 35.90 ? 63 ASN B O 1 ATOM 1696 C CB . ASN B 1 35 ? 37.686 25.461 74.089 1.00 40.87 ? 63 ASN B CB 1 ATOM 1697 C CG . ASN B 1 35 ? 38.706 25.355 72.977 1.00 52.92 ? 63 ASN B CG 1 ATOM 1698 O OD1 . ASN B 1 35 ? 39.278 26.357 72.554 1.00 59.66 ? 63 ASN B OD1 1 ATOM 1699 N ND2 . ASN B 1 35 ? 38.929 24.139 72.488 1.00 59.94 ? 63 ASN B ND2 1 ATOM 1700 N N . THR B 1 36 ? 34.930 27.728 73.170 1.00 29.57 ? 64 THR B N 1 ATOM 1701 C CA . THR B 1 36 ? 33.814 27.879 72.229 1.00 37.88 ? 64 THR B CA 1 ATOM 1702 C C . THR B 1 36 ? 33.890 29.230 71.506 1.00 40.62 ? 64 THR B C 1 ATOM 1703 O O . THR B 1 36 ? 33.069 29.513 70.645 1.00 40.07 ? 64 THR B O 1 ATOM 1704 C CB . THR B 1 36 ? 32.439 27.892 72.948 1.00 35.72 ? 64 THR B CB 1 ATOM 1705 O OG1 . THR B 1 36 ? 32.463 28.922 73.940 1.00 39.69 ? 64 THR B OG1 1 ATOM 1706 C CG2 . THR B 1 36 ? 32.089 26.558 73.624 1.00 27.19 ? 64 THR B CG2 1 ATOM 1707 N N . THR B 1 37 ? 34.854 30.064 71.891 1.00 42.37 ? 65 THR B N 1 ATOM 1708 C CA . THR B 1 37 ? 34.938 31.452 71.443 1.00 40.68 ? 65 THR B CA 1 ATOM 1709 C C . THR B 1 37 ? 36.367 31.978 71.534 1.00 42.21 ? 65 THR B C 1 ATOM 1710 O O . THR B 1 37 ? 37.184 31.437 72.270 1.00 52.25 ? 65 THR B O 1 ATOM 1711 C CB . THR B 1 37 ? 34.057 32.355 72.329 1.00 48.51 ? 65 THR B CB 1 ATOM 1712 O OG1 . THR B 1 37 ? 34.193 33.719 71.917 1.00 48.47 ? 65 THR B OG1 1 ATOM 1713 C CG2 . THR B 1 37 ? 34.488 32.248 73.787 1.00 45.52 ? 65 THR B CG2 1 ATOM 1714 N N . THR B 1 38 ? 36.673 33.047 70.808 1.00 37.32 ? 66 THR B N 1 ATOM 1715 C CA . THR B 1 38 ? 38.009 33.625 70.887 1.00 29.68 ? 66 THR B CA 1 ATOM 1716 C C . THR B 1 38 ? 38.029 34.663 71.993 1.00 37.32 ? 66 THR B C 1 ATOM 1717 O O . THR B 1 38 ? 36.983 35.134 72.414 1.00 35.50 ? 66 THR B O 1 ATOM 1718 C CB . THR B 1 38 ? 38.429 34.277 69.542 1.00 47.83 ? 66 THR B CB 1 ATOM 1719 O OG1 . THR B 1 38 ? 37.588 35.408 69.253 1.00 42.65 ? 66 THR B OG1 1 ATOM 1720 C CG2 . THR B 1 38 ? 38.301 33.267 68.415 1.00 39.23 ? 66 THR B CG2 1 ATOM 1721 N N . LEU B 1 39 ? 39.211 35.031 72.464 1.00 36.11 ? 67 LEU B N 1 ATOM 1722 C CA . LEU B 1 39 ? 39.277 36.094 73.457 1.00 41.80 ? 67 LEU B CA 1 ATOM 1723 C C . LEU B 1 39 ? 38.638 37.415 72.984 1.00 49.49 ? 67 LEU B C 1 ATOM 1724 O O . LEU B 1 39 ? 37.826 37.988 73.708 1.00 56.68 ? 67 LEU B O 1 ATOM 1725 C CB . LEU B 1 39 ? 40.703 36.324 73.962 1.00 36.41 ? 67 LEU B CB 1 ATOM 1726 C CG . LEU B 1 39 ? 40.698 37.503 74.932 1.00 41.10 ? 67 LEU B CG 1 ATOM 1727 C CD1 . LEU B 1 39 ? 39.891 37.134 76.178 1.00 41.46 ? 67 LEU B CD1 1 ATOM 1728 C CD2 . LEU B 1 39 ? 42.116 37.933 75.289 1.00 49.55 ? 67 LEU B CD2 1 ATOM 1729 N N . PRO B 1 40 ? 38.998 37.905 71.776 1.00 51.81 ? 68 PRO B N 1 ATOM 1730 C CA . PRO B 1 40 ? 38.356 39.175 71.398 1.00 48.76 ? 68 PRO B CA 1 ATOM 1731 C C . PRO B 1 40 ? 36.840 39.076 71.280 1.00 47.62 ? 68 PRO B C 1 ATOM 1732 O O . PRO B 1 40 ? 36.156 40.047 71.594 1.00 49.43 ? 68 PRO B O 1 ATOM 1733 C CB . PRO B 1 40 ? 38.973 39.522 70.028 1.00 45.64 ? 68 PRO B CB 1 ATOM 1734 C CG . PRO B 1 40 ? 39.972 38.486 69.727 1.00 47.16 ? 68 PRO B CG 1 ATOM 1735 C CD . PRO B 1 40 ? 40.102 37.533 70.868 1.00 46.10 ? 68 PRO B CD 1 ATOM 1736 N N . ASP B 1 41 ? 36.322 37.922 70.870 1.00 43.29 ? 69 ASP B N 1 ATOM 1737 C CA . ASP B 1 41 ? 34.877 37.759 70.780 1.00 34.47 ? 69 ASP B CA 1 ATOM 1738 C C . ASP B 1 41 ? 34.219 37.685 72.163 1.00 44.23 ? 69 ASP B C 1 ATOM 1739 O O . ASP B 1 41 ? 33.116 38.197 72.358 1.00 39.71 ? 69 ASP B O 1 ATOM 1740 C CB . ASP B 1 41 ? 34.515 36.561 69.925 1.00 41.82 ? 69 ASP B CB 1 ATOM 1741 C CG . ASP B 1 41 ? 34.804 36.790 68.449 1.00 56.23 ? 69 ASP B CG 1 ATOM 1742 O OD1 . ASP B 1 41 ? 34.984 37.966 68.058 1.00 59.29 ? 69 ASP B OD1 1 ATOM 1743 O OD2 . ASP B 1 41 ? 34.833 35.797 67.677 1.00 56.71 ? 69 ASP B OD2 1 ATOM 1744 N N . LEU B 1 42 ? 34.891 37.043 73.118 1.00 45.01 ? 70 LEU B N 1 ATOM 1745 C CA . LEU B 1 42 ? 34.406 37.024 74.496 1.00 41.51 ? 70 LEU B CA 1 ATOM 1746 C C . LEU B 1 42 ? 34.362 38.457 75.040 1.00 43.90 ? 70 LEU B C 1 ATOM 1747 O O . LEU B 1 42 ? 33.369 38.867 75.605 1.00 45.58 ? 70 LEU B O 1 ATOM 1748 C CB . LEU B 1 42 ? 35.283 36.124 75.377 1.00 33.28 ? 70 LEU B CB 1 ATOM 1749 C CG . LEU B 1 42 ? 34.950 35.931 76.869 1.00 36.68 ? 70 LEU B CG 1 ATOM 1750 C CD1 . LEU B 1 42 ? 33.532 35.482 77.109 1.00 27.43 ? 70 LEU B CD1 1 ATOM 1751 C CD2 . LEU B 1 42 ? 35.892 34.939 77.498 1.00 43.33 ? 70 LEU B CD2 1 ATOM 1752 N N . LEU B 1 43 ? 35.434 39.218 74.826 1.00 46.94 ? 71 LEU B N 1 ATOM 1753 C CA . LEU B 1 43 ? 35.491 40.620 75.258 1.00 46.87 ? 71 LEU B CA 1 ATOM 1754 C C . LEU B 1 43 ? 34.364 41.444 74.670 1.00 39.63 ? 71 LEU B C 1 ATOM 1755 O O . LEU B 1 43 ? 33.755 42.254 75.369 1.00 44.19 ? 71 LEU B O 1 ATOM 1756 C CB . LEU B 1 43 ? 36.820 41.265 74.866 1.00 44.72 ? 71 LEU B CB 1 ATOM 1757 C CG . LEU B 1 43 ? 38.068 40.646 75.487 1.00 53.38 ? 71 LEU B CG 1 ATOM 1758 C CD1 . LEU B 1 43 ? 39.306 41.245 74.870 1.00 51.07 ? 71 LEU B CD1 1 ATOM 1759 C CD2 . LEU B 1 43 ? 38.054 40.865 76.988 1.00 55.24 ? 71 LEU B CD2 1 ATOM 1760 N N . GLY B 1 44 ? 34.096 41.238 73.385 1.00 36.07 ? 72 GLY B N 1 ATOM 1761 C CA . GLY B 1 44 ? 33.035 41.959 72.719 1.00 44.00 ? 72 GLY B CA 1 ATOM 1762 C C . GLY B 1 44 ? 31.659 41.654 73.271 1.00 45.17 ? 72 GLY B C 1 ATOM 1763 O O . GLY B 1 44 ? 30.864 42.556 73.531 1.00 48.08 ? 72 GLY B O 1 ATOM 1764 N N . ALA B 1 45 ? 31.388 40.378 73.490 1.00 47.25 ? 73 ALA B N 1 ATOM 1765 C CA . ALA B 1 45 ? 30.091 39.963 74.015 1.00 41.98 ? 73 ALA B CA 1 ATOM 1766 C C . ALA B 1 45 ? 29.816 40.572 75.382 1.00 40.45 ? 73 ALA B C 1 ATOM 1767 O O . ALA B 1 45 ? 28.672 40.703 75.773 1.00 46.50 ? 73 ALA B O 1 ATOM 1768 C CB . ALA B 1 45 ? 30.006 38.444 74.078 1.00 29.32 ? 73 ALA B CB 1 ATOM 1769 N N . ASN B 1 46 ? 30.869 40.933 76.106 1.00 43.31 ? 74 ASN B N 1 ATOM 1770 C CA . ASN B 1 46 ? 30.711 41.518 77.432 1.00 51.70 ? 74 ASN B CA 1 ATOM 1771 C C . ASN B 1 46 ? 31.015 43.013 77.500 1.00 58.73 ? 74 ASN B C 1 ATOM 1772 O O . ASN B 1 46 ? 31.236 43.545 78.584 1.00 59.12 ? 74 ASN B O 1 ATOM 1773 C CB . ASN B 1 46 ? 31.575 40.767 78.440 1.00 48.19 ? 74 ASN B CB 1 ATOM 1774 C CG . ASN B 1 46 ? 31.100 39.360 78.650 1.00 46.57 ? 74 ASN B CG 1 ATOM 1775 O OD1 . ASN B 1 46 ? 30.318 39.078 79.560 1.00 50.16 ? 74 ASN B OD1 1 ATOM 1776 N ND2 . ASN B 1 46 ? 31.553 38.461 77.789 1.00 35.75 ? 74 ASN B ND2 1 ATOM 1777 N N . GLY B 1 47 ? 31.049 43.671 76.341 1.00 55.43 ? 75 GLY B N 1 ATOM 1778 C CA . GLY B 1 47 ? 31.195 45.112 76.264 1.00 52.93 ? 75 GLY B CA 1 ATOM 1779 C C . GLY B 1 47 ? 32.459 45.622 76.922 1.00 57.64 ? 75 GLY B C 1 ATOM 1780 O O . GLY B 1 47 ? 32.471 46.712 77.489 1.00 52.37 ? 75 GLY B O 1 ATOM 1781 N N . LEU B 1 48 ? 33.530 44.841 76.822 1.00 57.15 ? 76 LEU B N 1 ATOM 1782 C CA . LEU B 1 48 ? 34.781 45.165 77.491 1.00 47.72 ? 76 LEU B CA 1 ATOM 1783 C C . LEU B 1 48 ? 35.791 45.760 76.535 1.00 48.53 ? 76 LEU B C 1 ATOM 1784 O O . LEU B 1 48 ? 35.768 45.452 75.349 1.00 51.82 ? 76 LEU B O 1 ATOM 1785 C CB . LEU B 1 48 ? 35.363 43.905 78.132 1.00 52.72 ? 76 LEU B CB 1 ATOM 1786 C CG . LEU B 1 48 ? 34.505 43.276 79.229 1.00 56.92 ? 76 LEU B CG 1 ATOM 1787 C CD1 . LEU B 1 48 ? 34.961 41.864 79.489 1.00 54.60 ? 76 LEU B CD1 1 ATOM 1788 C CD2 . LEU B 1 48 ? 34.573 44.118 80.512 1.00 52.16 ? 76 LEU B CD2 1 ATOM 1789 N N . PRO B 1 49 ? 36.678 46.626 77.051 1.00 50.05 ? 77 PRO B N 1 ATOM 1790 C CA . PRO B 1 49 ? 37.619 47.248 76.125 1.00 52.27 ? 77 PRO B CA 1 ATOM 1791 C C . PRO B 1 49 ? 38.505 46.206 75.478 1.00 65.35 ? 77 PRO B C 1 ATOM 1792 O O . PRO B 1 49 ? 38.926 45.235 76.107 1.00 72.21 ? 77 PRO B O 1 ATOM 1793 C CB . PRO B 1 49 ? 38.449 48.187 77.007 1.00 51.25 ? 77 PRO B CB 1 ATOM 1794 C CG . PRO B 1 49 ? 37.827 48.197 78.348 1.00 46.49 ? 77 PRO B CG 1 ATOM 1795 C CD . PRO B 1 49 ? 36.820 47.102 78.440 1.00 54.61 ? 77 PRO B CD 1 ATOM 1796 N N . ASP B 1 50 ? 38.799 46.450 74.213 1.00 57.32 ? 78 ASP B N 1 ATOM 1797 C CA . ASP B 1 50 ? 39.615 45.569 73.396 1.00 53.21 ? 78 ASP B CA 1 ATOM 1798 C C . ASP B 1 50 ? 41.002 45.328 73.991 1.00 56.54 ? 78 ASP B C 1 ATOM 1799 O O . ASP B 1 50 ? 41.601 44.274 73.776 1.00 58.62 ? 78 ASP B O 1 ATOM 1800 C CB . ASP B 1 50 ? 39.669 46.155 71.991 1.00 56.37 ? 78 ASP B CB 1 ATOM 1801 C CG . ASP B 1 50 ? 38.283 46.286 71.391 1.00 68.22 ? 78 ASP B CG 1 ATOM 1802 O OD1 . ASP B 1 50 ? 37.350 46.688 72.127 1.00 69.17 ? 78 ASP B OD1 1 ATOM 1803 O OD2 . ASP B 1 50 ? 38.115 45.976 70.198 1.00 79.07 ? 78 ASP B OD2 1 ATOM 1804 N N . GLY B 1 51 ? 41.515 46.311 74.724 1.00 59.78 ? 79 GLY B N 1 ATOM 1805 C CA . GLY B 1 51 ? 42.839 46.210 75.320 1.00 51.75 ? 79 GLY B CA 1 ATOM 1806 C C . GLY B 1 51 ? 42.852 45.372 76.596 1.00 48.33 ? 79 GLY B C 1 ATOM 1807 O O . GLY B 1 51 ? 43.853 45.300 77.303 1.00 49.15 ? 79 GLY B O 1 ATOM 1808 N N . THR B 1 52 ? 41.722 44.757 76.917 1.00 55.41 ? 80 THR B N 1 ATOM 1809 C CA . THR B 1 52 ? 41.649 43.903 78.089 1.00 51.68 ? 80 THR B CA 1 ATOM 1810 C C . THR B 1 52 ? 42.524 42.692 77.840 1.00 48.31 ? 80 THR B C 1 ATOM 1811 O O . THR B 1 52 ? 42.413 42.047 76.800 1.00 54.77 ? 80 THR B O 1 ATOM 1812 C CB . THR B 1 52 ? 40.206 43.459 78.369 1.00 53.36 ? 80 THR B CB 1 ATOM 1813 O OG1 . THR B 1 52 ? 39.371 44.616 78.505 1.00 53.93 ? 80 THR B OG1 1 ATOM 1814 C CG2 . THR B 1 52 ? 40.134 42.638 79.643 1.00 52.19 ? 80 THR B CG2 1 ATOM 1815 N N . LEU B 1 53 ? 43.430 42.420 78.768 1.00 42.47 ? 81 LEU B N 1 ATOM 1816 C CA . LEU B 1 53 ? 44.348 41.298 78.630 1.00 49.15 ? 81 LEU B CA 1 ATOM 1817 C C . LEU B 1 53 ? 43.661 40.010 79.032 1.00 50.40 ? 81 LEU B C 1 ATOM 1818 O O . LEU B 1 53 ? 42.738 40.024 79.847 1.00 41.79 ? 81 LEU B O 1 ATOM 1819 C CB . LEU B 1 53 ? 45.620 41.512 79.464 1.00 49.72 ? 81 LEU B CB 1 ATOM 1820 C CG . LEU B 1 53 ? 46.449 42.751 79.100 1.00 55.81 ? 81 LEU B CG 1 ATOM 1821 C CD1 . LEU B 1 53 ? 47.629 42.901 80.033 1.00 58.95 ? 81 LEU B CD1 1 ATOM 1822 C CD2 . LEU B 1 53 ? 46.926 42.667 77.651 1.00 54.20 ? 81 LEU B CD2 1 ATOM 1823 N N . SER B 1 54 ? 44.127 38.894 78.482 1.00 51.34 ? 82 SER B N 1 ATOM 1824 C CA . SER B 1 54 ? 43.558 37.599 78.829 1.00 51.10 ? 82 SER B CA 1 ATOM 1825 C C . SER B 1 54 ? 43.845 37.260 80.311 1.00 48.82 ? 82 SER B C 1 ATOM 1826 O O . SER B 1 54 ? 43.200 36.385 80.887 1.00 44.20 ? 82 SER B O 1 ATOM 1827 C CB . SER B 1 54 ? 44.102 36.508 77.904 1.00 38.90 ? 82 SER B CB 1 ATOM 1828 O OG . SER B 1 54 ? 45.323 36.007 78.402 1.00 50.39 ? 82 SER B OG 1 ATOM 1829 N N . SER B 1 55 ? 44.799 37.965 80.921 1.00 43.25 ? 83 SER B N 1 ATOM 1830 C CA . SER B 1 55 ? 45.152 37.725 82.319 1.00 46.63 ? 83 SER B CA 1 ATOM 1831 C C . SER B 1 55 ? 44.339 38.591 83.283 1.00 47.90 ? 83 SER B C 1 ATOM 1832 O O . SER B 1 55 ? 44.457 38.459 84.510 1.00 42.10 ? 83 SER B O 1 ATOM 1833 C CB . SER B 1 55 ? 46.637 37.984 82.536 1.00 45.44 ? 83 SER B CB 1 ATOM 1834 O OG . SER B 1 55 ? 46.920 39.353 82.301 1.00 55.45 ? 83 SER B OG 1 ATOM 1835 N N . ALA B 1 56 ? 43.502 39.461 82.719 1.00 47.57 ? 84 ALA B N 1 ATOM 1836 C CA . ALA B 1 56 ? 42.616 40.314 83.506 1.00 47.34 ? 84 ALA B CA 1 ATOM 1837 C C . ALA B 1 56 ? 41.647 39.486 84.334 1.00 54.78 ? 84 ALA B C 1 ATOM 1838 O O . ALA B 1 56 ? 41.044 38.544 83.819 1.00 52.03 ? 84 ALA B O 1 ATOM 1839 C CB . ALA B 1 56 ? 41.848 41.263 82.598 1.00 43.37 ? 84 ALA B CB 1 ATOM 1840 N N . PRO B 1 57 ? 41.471 39.854 85.615 1.00 57.48 ? 85 PRO B N 1 ATOM 1841 C CA . PRO B 1 57 ? 40.698 39.033 86.551 1.00 51.69 ? 85 PRO B CA 1 ATOM 1842 C C . PRO B 1 57 ? 39.186 39.159 86.370 1.00 52.55 ? 85 PRO B C 1 ATOM 1843 O O . PRO B 1 57 ? 38.658 40.233 86.071 1.00 56.99 ? 85 PRO B O 1 ATOM 1844 C CB . PRO B 1 57 ? 41.100 39.606 87.919 1.00 45.38 ? 85 PRO B CB 1 ATOM 1845 C CG . PRO B 1 57 ? 41.351 41.042 87.633 1.00 48.51 ? 85 PRO B CG 1 ATOM 1846 C CD . PRO B 1 57 ? 41.988 41.075 86.261 1.00 51.63 ? 85 PRO B CD 1 ATOM 1847 N N . VAL B 1 58 ? 38.495 38.044 86.547 1.00 48.78 ? 86 VAL B N 1 ATOM 1848 C CA . VAL B 1 58 ? 37.062 38.076 86.741 1.00 43.58 ? 86 VAL B CA 1 ATOM 1849 C C . VAL B 1 58 ? 36.850 37.493 88.132 1.00 45.00 ? 86 VAL B C 1 ATOM 1850 O O . VAL B 1 58 ? 37.409 36.450 88.491 1.00 52.98 ? 86 VAL B O 1 ATOM 1851 C CB . VAL B 1 58 ? 36.277 37.329 85.636 1.00 45.52 ? 86 VAL B CB 1 ATOM 1852 C CG1 . VAL B 1 58 ? 37.203 36.934 84.490 1.00 46.50 ? 86 VAL B CG1 1 ATOM 1853 C CG2 . VAL B 1 58 ? 35.479 36.133 86.191 1.00 44.02 ? 86 VAL B CG2 1 ATOM 1854 N N . ALA B 1 59 ? 36.126 38.236 88.953 1.00 34.51 ? 87 ALA B N 1 ATOM 1855 C CA . ALA B 1 59 ? 35.931 37.842 90.327 1.00 37.65 ? 87 ALA B CA 1 ATOM 1856 C C . ALA B 1 59 ? 34.971 36.656 90.468 1.00 41.36 ? 87 ALA B C 1 ATOM 1857 O O . ALA B 1 59 ? 34.108 36.414 89.620 1.00 33.37 ? 87 ALA B O 1 ATOM 1858 C CB . ALA B 1 59 ? 35.435 39.045 91.141 1.00 38.41 ? 87 ALA B CB 1 ATOM 1859 N N . ALA B 1 60 ? 35.146 35.910 91.549 1.00 43.70 ? 88 ALA B N 1 ATOM 1860 C CA . ALA B 1 60 ? 34.169 34.913 91.953 1.00 39.24 ? 88 ALA B CA 1 ATOM 1861 C C . ALA B 1 60 ? 32.792 35.569 92.066 1.00 40.37 ? 88 ALA B C 1 ATOM 1862 O O . ALA B 1 60 ? 32.666 36.697 92.560 1.00 35.55 ? 88 ALA B O 1 ATOM 1863 C CB . ALA B 1 60 ? 34.562 34.311 93.281 1.00 40.71 ? 88 ALA B CB 1 ATOM 1864 N N . ASN B 1 61 ? 31.782 34.847 91.594 1.00 37.69 ? 89 ASN B N 1 ATOM 1865 C CA . ASN B 1 61 ? 30.390 35.270 91.619 1.00 36.29 ? 89 ASN B CA 1 ATOM 1866 C C . ASN B 1 61 ? 29.999 36.318 90.607 1.00 36.86 ? 89 ASN B C 1 ATOM 1867 O O . ASN B 1 61 ? 28.824 36.665 90.511 1.00 42.31 ? 89 ASN B O 1 ATOM 1868 C CB . ASN B 1 61 ? 29.971 35.731 93.013 1.00 37.17 ? 89 ASN B CB 1 ATOM 1869 C CG . ASN B 1 61 ? 30.193 34.671 94.058 1.00 34.92 ? 89 ASN B CG 1 ATOM 1870 O OD1 . ASN B 1 61 ? 29.441 33.706 94.125 1.00 30.06 ? 89 ASN B OD1 1 ATOM 1871 N ND2 . ASN B 1 61 ? 31.241 34.834 94.864 1.00 32.67 ? 89 ASN B ND2 1 ATOM 1872 N N . SER B 1 62 ? 30.959 36.818 89.839 1.00 37.88 ? 90 SER B N 1 ATOM 1873 C CA . SER B 1 62 ? 30.619 37.786 88.797 1.00 36.75 ? 90 SER B CA 1 ATOM 1874 C C . SER B 1 62 ? 30.169 36.994 87.578 1.00 40.59 ? 90 SER B C 1 ATOM 1875 O O . SER B 1 62 ? 30.509 35.825 87.444 1.00 34.88 ? 90 SER B O 1 ATOM 1876 C CB . SER B 1 62 ? 31.814 38.664 88.446 1.00 38.34 ? 90 SER B CB 1 ATOM 1877 O OG . SER B 1 62 ? 32.726 37.969 87.611 1.00 43.46 ? 90 SER B OG 1 ATOM 1878 N N . THR B 1 63 ? 29.399 37.620 86.701 1.00 40.03 ? 91 THR B N 1 ATOM 1879 C CA . THR B 1 63 ? 28.849 36.925 85.553 1.00 32.91 ? 91 THR B CA 1 ATOM 1880 C C . THR B 1 63 ? 29.557 37.340 84.262 1.00 43.59 ? 91 THR B C 1 ATOM 1881 O O . THR B 1 63 ? 30.030 38.464 84.136 1.00 36.51 ? 91 THR B O 1 ATOM 1882 C CB . THR B 1 63 ? 27.352 37.220 85.394 1.00 35.87 ? 91 THR B CB 1 ATOM 1883 O OG1 . THR B 1 63 ? 27.187 38.622 85.213 1.00 40.94 ? 91 THR B OG1 1 ATOM 1884 C CG2 . THR B 1 63 ? 26.542 36.774 86.631 1.00 34.34 ? 91 THR B CG2 1 ATOM 1885 N N . VAL B 1 64 ? 29.638 36.424 83.303 1.00 39.01 ? 92 VAL B N 1 ATOM 1886 C CA . VAL B 1 64 ? 30.219 36.732 82.010 1.00 26.22 ? 92 VAL B CA 1 ATOM 1887 C C . VAL B 1 64 ? 29.394 36.022 80.951 1.00 35.14 ? 92 VAL B C 1 ATOM 1888 O O . VAL B 1 64 ? 29.010 34.860 81.121 1.00 42.12 ? 92 VAL B O 1 ATOM 1889 C CB . VAL B 1 64 ? 31.699 36.274 81.910 1.00 29.96 ? 92 VAL B CB 1 ATOM 1890 C CG1 . VAL B 1 64 ? 32.288 36.694 80.587 1.00 25.55 ? 92 VAL B CG1 1 ATOM 1891 C CG2 . VAL B 1 64 ? 32.514 36.867 83.015 1.00 33.48 ? 92 VAL B CG2 1 ATOM 1892 N N . LYS B 1 65 ? 29.082 36.743 79.883 1.00 33.65 ? 93 LYS B N 1 ATOM 1893 C CA . LYS B 1 65 ? 28.374 36.186 78.744 1.00 31.33 ? 93 LYS B CA 1 ATOM 1894 C C . LYS B 1 65 ? 29.348 35.327 77.952 1.00 33.05 ? 93 LYS B C 1 ATOM 1895 O O . LYS B 1 65 ? 30.425 35.788 77.587 1.00 27.45 ? 93 LYS B O 1 ATOM 1896 C CB . LYS B 1 65 ? 27.858 37.314 77.860 1.00 33.86 ? 93 LYS B CB 1 ATOM 1897 C CG . LYS B 1 65 ? 26.360 37.327 77.658 1.00 50.16 ? 93 LYS B CG 1 ATOM 1898 C CD . LYS B 1 65 ? 25.905 38.604 76.974 1.00 59.95 ? 93 LYS B CD 1 ATOM 1899 C CE . LYS B 1 65 ? 25.217 38.286 75.646 1.00 62.75 ? 93 LYS B CE 1 ATOM 1900 N NZ . LYS B 1 65 ? 24.908 39.508 74.841 1.00 60.90 ? 93 LYS B NZ 1 ATOM 1901 N N . ILE B 1 66 ? 29.005 34.068 77.719 1.00 32.61 ? 94 ILE B N 1 ATOM 1902 C CA . ILE B 1 66 ? 29.883 33.189 76.953 1.00 24.39 ? 94 ILE B CA 1 ATOM 1903 C C . ILE B 1 66 ? 29.170 32.689 75.720 1.00 28.78 ? 94 ILE B C 1 ATOM 1904 O O . ILE B 1 66 ? 28.248 31.875 75.809 1.00 30.95 ? 94 ILE B O 1 ATOM 1905 C CB . ILE B 1 66 ? 30.419 32.027 77.805 1.00 35.31 ? 94 ILE B CB 1 ATOM 1906 C CG1 . ILE B 1 66 ? 31.184 32.611 78.989 1.00 35.09 ? 94 ILE B CG1 1 ATOM 1907 C CG2 . ILE B 1 66 ? 31.326 31.092 76.973 1.00 22.73 ? 94 ILE B CG2 1 ATOM 1908 C CD1 . ILE B 1 66 ? 31.801 31.608 79.855 1.00 44.76 ? 94 ILE B CD1 1 ATOM 1909 N N . PRO B 1 67 ? 29.585 33.208 74.553 1.00 35.14 ? 95 PRO B N 1 ATOM 1910 C CA . PRO B 1 67 ? 29.012 32.827 73.253 1.00 34.25 ? 95 PRO B CA 1 ATOM 1911 C C . PRO B 1 67 ? 29.583 31.514 72.778 1.00 39.90 ? 95 PRO B C 1 ATOM 1912 O O . PRO B 1 67 ? 30.757 31.245 73.031 1.00 41.36 ? 95 PRO B O 1 ATOM 1913 C CB . PRO B 1 67 ? 29.444 33.967 72.310 1.00 30.25 ? 95 PRO B CB 1 ATOM 1914 C CG . PRO B 1 67 ? 30.476 34.772 73.046 1.00 32.92 ? 95 PRO B CG 1 ATOM 1915 C CD . PRO B 1 67 ? 30.642 34.230 74.442 1.00 34.52 ? 95 PRO B CD 1 ATOM 1916 N N . PHE B 1 68 ? 28.772 30.735 72.073 1.00 35.69 ? 96 PHE B N 1 ATOM 1917 C CA . PHE B 1 68 ? 29.201 29.465 71.508 1.00 37.89 ? 96 PHE B CA 1 ATOM 1918 C C . PHE B 1 68 ? 28.309 29.158 70.327 1.00 34.69 ? 96 PHE B C 1 ATOM 1919 O O . PHE B 1 68 ? 27.258 29.764 70.192 1.00 30.62 ? 96 PHE B O 1 ATOM 1920 C CB . PHE B 1 68 ? 29.090 28.331 72.551 1.00 27.28 ? 96 PHE B CB 1 ATOM 1921 C CG . PHE B 1 68 ? 27.701 28.141 73.102 1.00 27.40 ? 96 PHE B CG 1 ATOM 1922 C CD1 . PHE B 1 68 ? 26.808 27.303 72.488 1.00 23.45 ? 96 PHE B CD1 1 ATOM 1923 C CD2 . PHE B 1 68 ? 27.295 28.823 74.244 1.00 36.69 ? 96 PHE B CD2 1 ATOM 1924 C CE1 . PHE B 1 68 ? 25.539 27.133 72.994 1.00 33.50 ? 96 PHE B CE1 1 ATOM 1925 C CE2 . PHE B 1 68 ? 26.018 28.672 74.756 1.00 32.40 ? 96 PHE B CE2 1 ATOM 1926 C CZ . PHE B 1 68 ? 25.137 27.821 74.136 1.00 32.06 ? 96 PHE B CZ 1 ATOM 1927 N N . ARG B 1 69 ? 28.716 28.190 69.505 1.00 40.01 ? 97 ARG B N 1 ATOM 1928 C CA . ARG B 1 69 ? 27.910 27.696 68.393 1.00 36.60 ? 97 ARG B CA 1 ATOM 1929 C C . ARG B 1 69 ? 26.895 26.691 68.904 1.00 40.53 ? 97 ARG B C 1 ATOM 1930 O O . ARG B 1 69 ? 27.261 25.733 69.561 1.00 32.20 ? 97 ARG B O 1 ATOM 1931 C CB . ARG B 1 69 ? 28.778 27.022 67.323 1.00 29.41 ? 97 ARG B CB 1 ATOM 1932 C CG . ARG B 1 69 ? 29.877 27.906 66.696 1.00 40.71 ? 97 ARG B CG 1 ATOM 1933 C CD . ARG B 1 69 ? 29.318 29.111 65.897 1.00 50.60 ? 97 ARG B CD 1 ATOM 1934 N NE . ARG B 1 69 ? 28.326 28.731 64.893 1.00 50.89 ? 97 ARG B NE 1 ATOM 1935 C CZ . ARG B 1 69 ? 27.599 29.596 64.189 1.00 51.68 ? 97 ARG B CZ 1 ATOM 1936 N NH1 . ARG B 1 69 ? 26.709 29.154 63.304 1.00 40.69 ? 97 ARG B NH1 1 ATOM 1937 N NH2 . ARG B 1 69 ? 27.754 30.903 64.375 1.00 48.22 ? 97 ARG B NH2 1 ATOM 1938 N N . CYS B 1 70 ? 25.618 26.955 68.649 1.00 38.71 ? 98 CYS B N 1 ATOM 1939 C CA . CYS B 1 70 ? 24.558 26.018 68.981 1.00 32.29 ? 98 CYS B CA 1 ATOM 1940 C C . CYS B 1 70 ? 24.197 25.129 67.804 1.00 38.13 ? 98 CYS B C 1 ATOM 1941 O O . CYS B 1 70 ? 24.034 25.608 66.692 1.00 38.25 ? 98 CYS B O 1 ATOM 1942 C CB . CYS B 1 70 ? 23.309 26.778 69.362 1.00 26.72 ? 98 CYS B CB 1 ATOM 1943 S SG . CYS B 1 70 ? 21.920 25.770 69.749 1.00 42.24 ? 98 CYS B SG 1 ATOM 1944 N N . ARG B 1 71 ? 24.027 23.837 68.055 1.00 38.63 ? 99 ARG B N 1 ATOM 1945 C CA . ARG B 1 71 ? 23.534 22.944 67.015 1.00 37.12 ? 99 ARG B CA 1 ATOM 1946 C C . ARG B 1 71 ? 22.206 22.346 67.411 1.00 33.43 ? 99 ARG B C 1 ATOM 1947 O O . ARG B 1 71 ? 22.034 21.864 68.524 1.00 36.78 ? 99 ARG B O 1 ATOM 1948 C CB . ARG B 1 71 ? 24.511 21.820 66.725 1.00 38.56 ? 99 ARG B CB 1 ATOM 1949 C CG . ARG B 1 71 ? 23.930 20.834 65.717 1.00 40.52 ? 99 ARG B CG 1 ATOM 1950 C CD . ARG B 1 71 ? 24.933 19.797 65.263 1.00 41.53 ? 99 ARG B CD 1 ATOM 1951 N NE . ARG B 1 71 ? 24.361 18.955 64.215 1.00 56.39 ? 99 ARG B NE 1 ATOM 1952 C CZ . ARG B 1 71 ? 23.535 17.938 64.444 1.00 59.83 ? 99 ARG B CZ 1 ATOM 1953 N NH1 . ARG B 1 71 ? 23.066 17.231 63.429 1.00 57.89 ? 99 ARG B NH1 1 ATOM 1954 N NH2 . ARG B 1 71 ? 23.177 17.630 65.687 1.00 60.43 ? 99 ARG B NH2 1 ATOM 1955 N N . CYS B 1 72 ? 21.255 22.406 66.499 1.00 30.27 ? 100 CYS B N 1 ATOM 1956 C CA . CYS B 1 72 ? 19.930 21.883 66.779 1.00 37.75 ? 100 CYS B CA 1 ATOM 1957 C C . CYS B 1 72 ? 19.781 20.517 66.180 1.00 40.06 ? 100 CYS B C 1 ATOM 1958 O O . CYS B 1 72 ? 20.156 20.288 65.041 1.00 44.77 ? 100 CYS B O 1 ATOM 1959 C CB . CYS B 1 72 ? 18.854 22.802 66.196 1.00 47.36 ? 100 CYS B CB 1 ATOM 1960 S SG . CYS B 1 72 ? 18.729 24.419 67.003 1.00 48.62 ? 100 CYS B SG 1 ATOM 1961 N N . ASN B 1 73 ? 19.243 19.593 66.948 1.00 45.04 ? 101 ASN B N 1 ATOM 1962 C CA . ASN B 1 73 ? 18.863 18.338 66.363 1.00 54.54 ? 101 ASN B CA 1 ATOM 1963 C C . ASN B 1 73 ? 17.388 18.537 66.083 1.00 62.01 ? 101 ASN B C 1 ATOM 1964 O O . ASN B 1 73 ? 16.905 19.666 66.187 1.00 77.03 ? 101 ASN B O 1 ATOM 1965 C CB . ASN B 1 73 ? 19.256 17.144 67.248 1.00 49.65 ? 101 ASN B CB 1 ATOM 1966 C CG . ASN B 1 73 ? 18.581 17.144 68.622 1.00 47.70 ? 101 ASN B CG 1 ATOM 1967 O OD1 . ASN B 1 73 ? 17.555 17.788 68.857 1.00 43.91 ? 101 ASN B OD1 1 ATOM 1968 N ND2 . ASN B 1 73 ? 19.203 16.436 69.555 1.00 37.41 ? 101 ASN B ND2 1 ATOM 1969 N N . GLY B 1 74 ? 16.662 17.512 65.691 1.00 55.79 ? 102 GLY B N 1 ATOM 1970 C CA . GLY B 1 74 ? 15.265 17.752 65.379 1.00 54.14 ? 102 GLY B CA 1 ATOM 1971 C C . GLY B 1 74 ? 14.449 18.381 66.502 1.00 50.83 ? 102 GLY B C 1 ATOM 1972 O O . GLY B 1 74 ? 13.397 18.965 66.250 1.00 50.43 ? 102 GLY B O 1 ATOM 1973 N N . ASP B 1 75 ? 14.958 18.291 67.732 1.00 44.26 ? 103 ASP B N 1 ATOM 1974 C CA . ASP B 1 75 ? 14.146 18.510 68.921 1.00 53.15 ? 103 ASP B CA 1 ATOM 1975 C C . ASP B 1 75 ? 14.649 19.596 69.867 1.00 55.68 ? 103 ASP B C 1 ATOM 1976 O O . ASP B 1 75 ? 13.865 20.310 70.478 1.00 59.17 ? 103 ASP B O 1 ATOM 1977 C CB . ASP B 1 75 ? 14.116 17.215 69.720 1.00 57.18 ? 103 ASP B CB 1 ATOM 1978 C CG . ASP B 1 75 ? 13.542 16.066 68.932 1.00 68.13 ? 103 ASP B CG 1 ATOM 1979 O OD1 . ASP B 1 75 ? 12.551 16.275 68.195 1.00 67.44 ? 103 ASP B OD1 1 ATOM 1980 O OD2 . ASP B 1 75 ? 14.095 14.951 69.046 1.00 66.90 ? 103 ASP B OD2 1 ATOM 1981 N N . VAL B 1 76 ? 15.964 19.676 70.009 1.00 49.95 ? 104 VAL B N 1 ATOM 1982 C CA . VAL B 1 76 ? 16.572 20.418 71.089 1.00 45.82 ? 104 VAL B CA 1 ATOM 1983 C C . VAL B 1 76 ? 17.870 21.088 70.593 1.00 43.11 ? 104 VAL B C 1 ATOM 1984 O O . VAL B 1 76 ? 18.478 20.635 69.623 1.00 39.52 ? 104 VAL B O 1 ATOM 1985 C CB . VAL B 1 76 ? 16.849 19.441 72.249 1.00 47.71 ? 104 VAL B CB 1 ATOM 1986 C CG1 . VAL B 1 76 ? 18.114 18.650 71.987 1.00 36.15 ? 104 VAL B CG1 1 ATOM 1987 C CG2 . VAL B 1 76 ? 17.018 20.169 73.485 1.00 60.75 ? 104 VAL B CG2 1 ATOM 1988 N N . GLY B 1 77 ? 18.298 22.167 71.235 1.00 33.28 ? 105 GLY B N 1 ATOM 1989 C CA . GLY B 1 77 ? 19.545 22.800 70.842 1.00 24.43 ? 105 GLY B CA 1 ATOM 1990 C C . GLY B 1 77 ? 20.638 22.585 71.856 1.00 36.45 ? 105 GLY B C 1 ATOM 1991 O O . GLY B 1 77 ? 20.394 22.780 73.049 1.00 36.58 ? 105 GLY B O 1 ATOM 1992 N N . GLN B 1 78 ? 21.832 22.197 71.400 1.00 31.72 ? 106 GLN B N 1 ATOM 1993 C CA . GLN B 1 78 ? 22.958 21.918 72.303 1.00 35.10 ? 106 GLN B CA 1 ATOM 1994 C C . GLN B 1 78 ? 24.217 22.589 71.795 1.00 32.53 ? 106 GLN B C 1 ATOM 1995 O O . GLN B 1 78 ? 24.398 22.718 70.587 1.00 30.07 ? 106 GLN B O 1 ATOM 1996 C CB . GLN B 1 78 ? 23.189 20.399 72.406 1.00 32.88 ? 106 GLN B CB 1 ATOM 1997 C CG . GLN B 1 78 ? 21.971 19.613 72.938 1.00 30.57 ? 106 GLN B CG 1 ATOM 1998 C CD . GLN B 1 78 ? 22.047 18.103 72.621 1.00 41.24 ? 106 GLN B CD 1 ATOM 1999 O OE1 . GLN B 1 78 ? 22.483 17.721 71.545 1.00 41.46 ? 106 GLN B OE1 1 ATOM 2000 N NE2 . GLN B 1 78 ? 21.640 17.252 73.576 1.00 33.53 ? 106 GLN B NE2 1 ATOM 2001 N N . SER B 1 79 ? 25.094 23.034 72.696 1.00 34.63 ? 107 SER B N 1 ATOM 2002 C CA . SER B 1 79 ? 26.366 23.600 72.234 1.00 36.41 ? 107 SER B CA 1 ATOM 2003 C C . SER B 1 79 ? 27.081 22.525 71.408 1.00 39.44 ? 107 SER B C 1 ATOM 2004 O O . SER B 1 79 ? 27.173 21.366 71.820 1.00 33.09 ? 107 SER B O 1 ATOM 2005 C CB . SER B 1 79 ? 27.222 24.054 73.408 1.00 33.78 ? 107 SER B CB 1 ATOM 2006 O OG . SER B 1 79 ? 27.440 22.978 74.296 1.00 32.70 ? 107 SER B OG 1 ATOM 2007 N N . ASP B 1 80 ? 27.571 22.915 70.237 1.00 35.22 ? 108 ASP B N 1 ATOM 2008 C CA . ASP B 1 80 ? 27.945 21.962 69.194 1.00 32.71 ? 108 ASP B CA 1 ATOM 2009 C C . ASP B 1 80 ? 29.258 21.223 69.477 1.00 37.66 ? 108 ASP B C 1 ATOM 2010 O O . ASP B 1 80 ? 30.321 21.694 69.107 1.00 36.07 ? 108 ASP B O 1 ATOM 2011 C CB . ASP B 1 80 ? 28.067 22.675 67.849 1.00 32.46 ? 108 ASP B CB 1 ATOM 2012 C CG . ASP B 1 80 ? 28.211 21.708 66.687 1.00 32.71 ? 108 ASP B CG 1 ATOM 2013 O OD1 . ASP B 1 80 ? 27.995 20.494 66.862 1.00 48.72 ? 108 ASP B OD1 1 ATOM 2014 O OD2 . ASP B 1 80 ? 28.557 22.166 65.597 1.00 43.86 ? 108 ASP B OD2 1 ATOM 2015 N N . ARG B 1 81 ? 29.162 20.079 70.145 1.00 36.56 ? 109 ARG B N 1 ATOM 2016 C CA . ARG B 1 81 ? 30.308 19.233 70.489 1.00 40.11 ? 109 ARG B CA 1 ATOM 2017 C C . ARG B 1 81 ? 31.392 19.935 71.288 1.00 45.99 ? 109 ARG B C 1 ATOM 2018 O O . ARG B 1 81 ? 32.510 19.449 71.410 1.00 51.88 ? 109 ARG B O 1 ATOM 2019 C CB . ARG B 1 81 ? 30.875 18.527 69.252 1.00 40.65 ? 109 ARG B CB 1 ATOM 2020 C CG . ARG B 1 81 ? 29.792 17.754 68.471 1.00 63.45 ? 109 ARG B CG 1 ATOM 2021 C CD . ARG B 1 81 ? 29.249 16.522 69.214 1.00 91.09 ? 109 ARG B CD 1 ATOM 2022 N NE . ARG B 1 81 ? 27.947 16.119 68.677 1.00 92.15 ? 109 ARG B NE 1 ATOM 2023 C CZ . ARG B 1 81 ? 27.388 14.924 68.839 1.00 92.70 ? 109 ARG B CZ 1 ATOM 2024 N NH1 . ARG B 1 81 ? 28.012 13.982 69.530 1.00 92.73 ? 109 ARG B NH1 1 ATOM 2025 N NH2 . ARG B 1 81 ? 26.199 14.675 68.307 1.00 94.43 ? 109 ARG B NH2 1 ATOM 2026 N N . LEU B 1 82 ? 31.042 21.091 71.825 1.00 44.05 ? 110 LEU B N 1 ATOM 2027 C CA . LEU B 1 82 ? 31.892 21.805 72.751 1.00 36.33 ? 110 LEU B CA 1 ATOM 2028 C C . LEU B 1 82 ? 30.961 22.349 73.823 1.00 30.61 ? 110 LEU B C 1 ATOM 2029 O O . LEU B 1 82 ? 29.754 22.433 73.615 1.00 29.33 ? 110 LEU B O 1 ATOM 2030 C CB . LEU B 1 82 ? 32.613 22.951 72.047 1.00 42.04 ? 110 LEU B CB 1 ATOM 2031 C CG . LEU B 1 82 ? 33.716 22.644 71.034 1.00 41.39 ? 110 LEU B CG 1 ATOM 2032 C CD1 . LEU B 1 82 ? 34.051 23.918 70.229 1.00 35.57 ? 110 LEU B CD1 1 ATOM 2033 C CD2 . LEU B 1 82 ? 34.967 22.123 71.738 1.00 28.15 ? 110 LEU B CD2 1 ATOM 2034 N N . PRO B 1 83 ? 31.495 22.654 75.005 1.00 28.09 ? 111 PRO B N 1 ATOM 2035 C CA . PRO B 1 83 ? 32.873 22.432 75.436 1.00 32.30 ? 111 PRO B CA 1 ATOM 2036 C C . PRO B 1 83 ? 33.109 20.973 75.815 1.00 42.28 ? 111 PRO B C 1 ATOM 2037 O O . PRO B 1 83 ? 32.173 20.178 75.976 1.00 31.75 ? 111 PRO B O 1 ATOM 2038 C CB . PRO B 1 83 ? 32.991 23.313 76.681 1.00 29.57 ? 111 PRO B CB 1 ATOM 2039 C CG . PRO B 1 83 ? 31.630 23.342 77.236 1.00 30.94 ? 111 PRO B CG 1 ATOM 2040 C CD . PRO B 1 83 ? 30.677 23.275 76.061 1.00 24.14 ? 111 PRO B CD 1 ATOM 2041 N N . ILE B 1 84 ? 34.384 20.629 75.909 1.00 43.17 ? 112 ILE B N 1 ATOM 2042 C CA . ILE B 1 84 ? 34.796 19.331 76.368 1.00 35.14 ? 112 ILE B CA 1 ATOM 2043 C C . ILE B 1 84 ? 35.359 19.476 77.748 1.00 31.89 ? 112 ILE B C 1 ATOM 2044 O O . ILE B 1 84 ? 36.256 20.276 77.970 1.00 37.94 ? 112 ILE B O 1 ATOM 2045 C CB . ILE B 1 84 ? 35.894 18.698 75.481 1.00 43.07 ? 112 ILE B CB 1 ATOM 2046 C CG1 . ILE B 1 84 ? 35.485 18.727 74.017 1.00 41.62 ? 112 ILE B CG1 1 ATOM 2047 C CG2 . ILE B 1 84 ? 36.064 17.236 75.838 1.00 46.99 ? 112 ILE B CG2 1 ATOM 2048 C CD1 . ILE B 1 84 ? 34.228 17.961 73.766 1.00 45.09 ? 112 ILE B CD1 1 ATOM 2049 N N . TYR B 1 85 ? 34.874 18.646 78.662 1.00 29.22 ? 113 TYR B N 1 ATOM 2050 C CA . TYR B 1 85 ? 35.380 18.642 80.022 1.00 34.15 ? 113 TYR B CA 1 ATOM 2051 C C . TYR B 1 85 ? 36.130 17.318 80.326 1.00 37.52 ? 113 TYR B C 1 ATOM 2052 O O . TYR B 1 85 ? 35.644 16.229 80.041 1.00 37.55 ? 113 TYR B O 1 ATOM 2053 C CB . TYR B 1 85 ? 34.237 18.906 81.011 1.00 25.06 ? 113 TYR B CB 1 ATOM 2054 C CG . TYR B 1 85 ? 34.689 18.922 82.443 1.00 24.98 ? 113 TYR B CG 1 ATOM 2055 C CD1 . TYR B 1 85 ? 35.205 20.084 83.022 1.00 24.71 ? 113 TYR B CD1 1 ATOM 2056 C CD2 . TYR B 1 85 ? 34.657 17.755 83.211 1.00 27.78 ? 113 TYR B CD2 1 ATOM 2057 C CE1 . TYR B 1 85 ? 35.656 20.094 84.322 1.00 29.77 ? 113 TYR B CE1 1 ATOM 2058 C CE2 . TYR B 1 85 ? 35.093 17.752 84.527 1.00 25.15 ? 113 TYR B CE2 1 ATOM 2059 C CZ . TYR B 1 85 ? 35.590 18.918 85.071 1.00 36.97 ? 113 TYR B CZ 1 ATOM 2060 O OH . TYR B 1 85 ? 36.028 18.902 86.357 1.00 34.22 ? 113 TYR B OH 1 ATOM 2061 N N . VAL B 1 86 ? 37.351 17.431 80.838 1.00 35.95 ? 114 VAL B N 1 ATOM 2062 C CA . VAL B 1 86 ? 38.121 16.259 81.251 1.00 39.04 ? 114 VAL B CA 1 ATOM 2063 C C . VAL B 1 86 ? 37.909 15.906 82.734 1.00 40.84 ? 114 VAL B C 1 ATOM 2064 O O . VAL B 1 86 ? 38.223 16.707 83.623 1.00 31.27 ? 114 VAL B O 1 ATOM 2065 C CB . VAL B 1 86 ? 39.614 16.432 80.951 1.00 34.85 ? 114 VAL B CB 1 ATOM 2066 C CG1 . VAL B 1 86 ? 40.396 15.209 81.460 1.00 37.99 ? 114 VAL B CG1 1 ATOM 2067 C CG2 . VAL B 1 86 ? 39.818 16.591 79.445 1.00 32.82 ? 114 VAL B CG2 1 ATOM 2068 N N . VAL B 1 87 ? 37.371 14.715 82.993 1.00 37.41 ? 115 VAL B N 1 ATOM 2069 C CA . VAL B 1 87 ? 37.034 14.327 84.359 1.00 35.01 ? 115 VAL B CA 1 ATOM 2070 C C . VAL B 1 87 ? 38.277 14.346 85.231 1.00 36.06 ? 115 VAL B C 1 ATOM 2071 O O . VAL B 1 87 ? 39.284 13.743 84.883 1.00 44.81 ? 115 VAL B O 1 ATOM 2072 C CB . VAL B 1 87 ? 36.383 12.935 84.407 1.00 35.73 ? 115 VAL B CB 1 ATOM 2073 C CG1 . VAL B 1 87 ? 36.002 12.573 85.825 1.00 35.41 ? 115 VAL B CG1 1 ATOM 2074 C CG2 . VAL B 1 87 ? 35.156 12.886 83.521 1.00 26.68 ? 115 VAL B CG2 1 ATOM 2075 N N . GLN B 1 88 ? 38.200 15.061 86.349 1.00 27.39 ? 116 GLN B N 1 ATOM 2076 C CA . GLN B 1 88 ? 39.307 15.192 87.305 1.00 44.49 ? 116 GLN B CA 1 ATOM 2077 C C . GLN B 1 88 ? 39.188 14.260 88.519 1.00 43.77 ? 116 GLN B C 1 ATOM 2078 O O . GLN B 1 88 ? 38.102 13.775 88.811 1.00 44.47 ? 116 GLN B O 1 ATOM 2079 C CB . GLN B 1 88 ? 39.385 16.629 87.832 1.00 47.74 ? 116 GLN B CB 1 ATOM 2080 C CG . GLN B 1 88 ? 39.413 17.678 86.760 1.00 52.62 ? 116 GLN B CG 1 ATOM 2081 C CD . GLN B 1 88 ? 40.709 17.644 86.018 1.00 54.53 ? 116 GLN B CD 1 ATOM 2082 O OE1 . GLN B 1 88 ? 41.740 18.049 86.545 1.00 60.71 ? 116 GLN B OE1 1 ATOM 2083 N NE2 . GLN B 1 88 ? 40.681 17.121 84.796 1.00 50.38 ? 116 GLN B NE2 1 ATOM 2084 N N . PRO B 1 89 ? 40.314 13.995 89.215 1.00 38.18 ? 117 PRO B N 1 ATOM 2085 C CA . PRO B 1 89 ? 40.241 13.304 90.504 1.00 39.02 ? 117 PRO B CA 1 ATOM 2086 C C . PRO B 1 89 ? 39.225 14.000 91.403 1.00 38.40 ? 117 PRO B C 1 ATOM 2087 O O . PRO B 1 89 ? 39.090 15.222 91.332 1.00 42.81 ? 117 PRO B O 1 ATOM 2088 C CB . PRO B 1 89 ? 41.650 13.447 91.083 1.00 37.23 ? 117 PRO B CB 1 ATOM 2089 C CG . PRO B 1 89 ? 42.536 13.670 89.935 1.00 41.79 ? 117 PRO B CG 1 ATOM 2090 C CD . PRO B 1 89 ? 41.708 14.186 88.776 1.00 41.63 ? 117 PRO B CD 1 ATOM 2091 N N . GLN B 1 90 ? 38.538 13.234 92.240 1.00 37.16 ? 118 GLN B N 1 ATOM 2092 C CA . GLN B 1 90 ? 37.517 13.752 93.149 1.00 31.97 ? 118 GLN B CA 1 ATOM 2093 C C . GLN B 1 90 ? 36.244 14.209 92.441 1.00 32.62 ? 118 GLN B C 1 ATOM 2094 O O . GLN B 1 90 ? 35.370 14.768 93.081 1.00 43.98 ? 118 GLN B O 1 ATOM 2095 C CB . GLN B 1 90 ? 38.048 14.901 94.035 1.00 29.25 ? 118 GLN B CB 1 ATOM 2096 C CG . GLN B 1 90 ? 39.461 14.739 94.569 1.00 38.95 ? 118 GLN B CG 1 ATOM 2097 C CD . GLN B 1 90 ? 39.528 13.849 95.803 1.00 46.81 ? 118 GLN B CD 1 ATOM 2098 O OE1 . GLN B 1 90 ? 38.521 13.638 96.466 1.00 39.06 ? 118 GLN B OE1 1 ATOM 2099 N NE2 . GLN B 1 90 ? 40.733 13.357 96.135 1.00 49.66 ? 118 GLN B NE2 1 ATOM 2100 N N . ASP B 1 91 ? 36.109 13.962 91.143 1.00 35.03 ? 119 ASP B N 1 ATOM 2101 C CA . ASP B 1 91 ? 34.931 14.479 90.450 1.00 44.48 ? 119 ASP B CA 1 ATOM 2102 C C . ASP B 1 91 ? 33.772 13.493 90.440 1.00 44.12 ? 119 ASP B C 1 ATOM 2103 O O . ASP B 1 91 ? 33.959 12.281 90.446 1.00 41.39 ? 119 ASP B O 1 ATOM 2104 C CB . ASP B 1 91 ? 35.247 14.841 88.986 1.00 45.86 ? 119 ASP B CB 1 ATOM 2105 C CG . ASP B 1 91 ? 35.688 16.295 88.809 1.00 46.45 ? 119 ASP B CG 1 ATOM 2106 O OD1 . ASP B 1 91 ? 35.627 17.078 89.784 1.00 45.90 ? 119 ASP B OD1 1 ATOM 2107 O OD2 . ASP B 1 91 ? 36.055 16.666 87.675 1.00 27.12 ? 119 ASP B OD2 1 ATOM 2108 N N . GLY B 1 92 ? 32.571 14.050 90.419 1.00 33.78 ? 120 GLY B N 1 ATOM 2109 C CA . GLY B 1 92 ? 31.350 13.314 90.171 1.00 25.55 ? 120 GLY B CA 1 ATOM 2110 C C . GLY B 1 92 ? 30.553 14.058 89.112 1.00 38.28 ? 120 GLY B C 1 ATOM 2111 O O . GLY B 1 92 ? 30.658 15.272 88.975 1.00 45.36 ? 120 GLY B O 1 ATOM 2112 N N . LEU B 1 93 ? 29.771 13.329 88.342 1.00 32.17 ? 121 LEU B N 1 ATOM 2113 C CA . LEU B 1 93 ? 29.005 13.930 87.259 1.00 45.19 ? 121 LEU B CA 1 ATOM 2114 C C . LEU B 1 93 ? 28.110 15.084 87.721 1.00 46.85 ? 121 LEU B C 1 ATOM 2115 O O . LEU B 1 93 ? 28.034 16.133 87.080 1.00 48.90 ? 121 LEU B O 1 ATOM 2116 C CB . LEU B 1 93 ? 28.155 12.850 86.614 1.00 41.00 ? 121 LEU B CB 1 ATOM 2117 C CG . LEU B 1 93 ? 27.933 12.948 85.120 1.00 43.84 ? 121 LEU B CG 1 ATOM 2118 C CD1 . LEU B 1 93 ? 29.202 13.386 84.400 1.00 43.27 ? 121 LEU B CD1 1 ATOM 2119 C CD2 . LEU B 1 93 ? 27.482 11.588 84.654 1.00 36.65 ? 121 LEU B CD2 1 ATOM 2120 N N . ASP B 1 94 ? 27.436 14.880 88.842 1.00 42.78 ? 122 ASP B N 1 ATOM 2121 C CA . ASP B 1 94 ? 26.517 15.871 89.373 1.00 38.33 ? 122 ASP B CA 1 ATOM 2122 C C . ASP B 1 94 ? 27.225 17.128 89.794 1.00 36.43 ? 122 ASP B C 1 ATOM 2123 O O . ASP B 1 94 ? 26.763 18.245 89.536 1.00 46.96 ? 122 ASP B O 1 ATOM 2124 C CB . ASP B 1 94 ? 25.783 15.302 90.580 1.00 43.99 ? 122 ASP B CB 1 ATOM 2125 C CG . ASP B 1 94 ? 24.739 16.251 91.115 1.00 45.75 ? 122 ASP B CG 1 ATOM 2126 O OD1 . ASP B 1 94 ? 23.698 16.452 90.463 1.00 47.14 ? 122 ASP B OD1 1 ATOM 2127 O OD2 . ASP B 1 94 ? 24.966 16.814 92.193 1.00 50.26 ? 122 ASP B OD2 1 ATOM 2128 N N . ALA B 1 95 ? 28.367 16.943 90.432 1.00 32.51 ? 123 ALA B N 1 ATOM 2129 C CA . ALA B 1 95 ? 29.156 18.064 90.905 1.00 30.12 ? 123 ALA B CA 1 ATOM 2130 C C . ALA B 1 95 ? 29.755 18.866 89.715 1.00 31.92 ? 123 ALA B C 1 ATOM 2131 O O . ALA B 1 95 ? 29.943 20.061 89.805 1.00 37.14 ? 123 ALA B O 1 ATOM 2132 C CB . ALA B 1 95 ? 30.240 17.559 91.878 1.00 24.07 ? 123 ALA B CB 1 ATOM 2133 N N . ILE B 1 96 ? 30.051 18.186 88.611 1.00 32.79 ? 124 ILE B N 1 ATOM 2134 C CA . ILE B 1 96 ? 30.525 18.831 87.396 1.00 34.50 ? 124 ILE B CA 1 ATOM 2135 C C . ILE B 1 96 ? 29.433 19.716 86.788 1.00 33.42 ? 124 ILE B C 1 ATOM 2136 O O . ILE B 1 96 ? 29.686 20.846 86.408 1.00 33.48 ? 124 ILE B O 1 ATOM 2137 C CB . ILE B 1 96 ? 30.954 17.772 86.330 1.00 41.61 ? 124 ILE B CB 1 ATOM 2138 C CG1 . ILE B 1 96 ? 32.243 17.076 86.738 1.00 34.14 ? 124 ILE B CG1 1 ATOM 2139 C CG2 . ILE B 1 96 ? 31.179 18.400 84.952 1.00 35.79 ? 124 ILE B CG2 1 ATOM 2140 C CD1 . ILE B 1 96 ? 32.501 15.843 85.909 1.00 32.52 ? 124 ILE B CD1 1 ATOM 2141 N N . ALA B 1 97 ? 28.235 19.164 86.658 1.00 28.90 ? 125 ALA B N 1 ATOM 2142 C CA . ALA B 1 97 ? 27.075 19.891 86.161 1.00 32.37 ? 125 ALA B CA 1 ATOM 2143 C C . ALA B 1 97 ? 26.796 21.162 86.961 1.00 33.40 ? 125 ALA B C 1 ATOM 2144 O O . ALA B 1 97 ? 26.634 22.242 86.392 1.00 41.72 ? 125 ALA B O 1 ATOM 2145 C CB . ALA B 1 97 ? 25.848 18.985 86.190 1.00 34.61 ? 125 ALA B CB 1 ATOM 2146 N N . ARG B 1 98 ? 26.757 21.020 88.282 1.00 25.94 ? 126 ARG B N 1 ATOM 2147 C CA . ARG B 1 98 ? 26.353 22.103 89.191 1.00 27.37 ? 126 ARG B CA 1 ATOM 2148 C C . ARG B 1 98 ? 27.498 23.030 89.574 1.00 37.85 ? 126 ARG B C 1 ATOM 2149 O O . ARG B 1 98 ? 27.315 24.225 89.627 1.00 35.52 ? 126 ARG B O 1 ATOM 2150 C CB . ARG B 1 98 ? 25.740 21.526 90.474 1.00 29.54 ? 126 ARG B CB 1 ATOM 2151 C CG . ARG B 1 98 ? 24.534 20.646 90.255 1.00 29.02 ? 126 ARG B CG 1 ATOM 2152 C CD . ARG B 1 98 ? 23.914 20.102 91.582 1.00 28.05 ? 126 ARG B CD 1 ATOM 2153 N NE . ARG B 1 98 ? 22.455 20.104 91.491 1.00 36.42 ? 126 ARG B NE 1 ATOM 2154 C CZ . ARG B 1 98 ? 21.760 19.148 90.892 1.00 51.14 ? 126 ARG B CZ 1 ATOM 2155 N NH1 . ARG B 1 98 ? 22.398 18.134 90.337 1.00 68.85 ? 126 ARG B NH1 1 ATOM 2156 N NH2 . ARG B 1 98 ? 20.440 19.207 90.820 1.00 48.74 ? 126 ARG B NH2 1 ATOM 2157 N N . ASN B 1 99 ? 28.675 22.481 89.864 1.00 37.32 ? 127 ASN B N 1 ATOM 2158 C CA . ASN B 1 99 ? 29.752 23.317 90.376 1.00 31.47 ? 127 ASN B CA 1 ATOM 2159 C C . ASN B 1 99 ? 30.691 23.882 89.314 1.00 36.46 ? 127 ASN B C 1 ATOM 2160 O O . ASN B 1 99 ? 31.401 24.863 89.573 1.00 33.86 ? 127 ASN B O 1 ATOM 2161 C CB . ASN B 1 99 ? 30.570 22.593 91.433 1.00 33.46 ? 127 ASN B CB 1 ATOM 2162 C CG . ASN B 1 99 ? 29.726 22.055 92.542 1.00 41.02 ? 127 ASN B CG 1 ATOM 2163 O OD1 . ASN B 1 99 ? 28.702 22.628 92.873 1.00 48.01 ? 127 ASN B OD1 1 ATOM 2164 N ND2 . ASN B 1 99 ? 30.169 20.961 93.151 1.00 44.85 ? 127 ASN B ND2 1 ATOM 2165 N N . VAL B 1 100 ? 30.724 23.253 88.141 1.00 35.15 ? 128 VAL B N 1 ATOM 2166 C CA . VAL B 1 100 ? 31.523 23.790 87.040 1.00 40.31 ? 128 VAL B CA 1 ATOM 2167 C C . VAL B 1 100 ? 30.648 24.528 86.033 1.00 30.81 ? 128 VAL B C 1 ATOM 2168 O O . VAL B 1 100 ? 30.998 25.594 85.555 1.00 43.48 ? 128 VAL B O 1 ATOM 2169 C CB . VAL B 1 100 ? 32.367 22.711 86.298 1.00 47.34 ? 128 VAL B CB 1 ATOM 2170 C CG1 . VAL B 1 100 ? 33.289 23.393 85.246 1.00 33.45 ? 128 VAL B CG1 1 ATOM 2171 C CG2 . VAL B 1 100 ? 33.188 21.898 87.284 1.00 36.30 ? 128 VAL B CG2 1 ATOM 2172 N N . PHE B 1 101 ? 29.493 23.969 85.738 1.00 26.64 ? 129 PHE B N 1 ATOM 2173 C CA . PHE B 1 101 ? 28.662 24.525 84.694 1.00 28.33 ? 129 PHE B CA 1 ATOM 2174 C C . PHE B 1 101 ? 27.323 25.125 85.169 1.00 25.75 ? 129 PHE B C 1 ATOM 2175 O O . PHE B 1 101 ? 26.337 25.079 84.430 1.00 31.49 ? 129 PHE B O 1 ATOM 2176 C CB . PHE B 1 101 ? 28.470 23.460 83.590 1.00 35.47 ? 129 PHE B CB 1 ATOM 2177 C CG . PHE B 1 101 ? 29.757 23.082 82.889 1.00 41.72 ? 129 PHE B CG 1 ATOM 2178 C CD1 . PHE B 1 101 ? 30.299 23.913 81.919 1.00 39.57 ? 129 PHE B CD1 1 ATOM 2179 C CD2 . PHE B 1 101 ? 30.449 21.923 83.233 1.00 38.08 ? 129 PHE B CD2 1 ATOM 2180 C CE1 . PHE B 1 101 ? 31.493 23.587 81.269 1.00 32.53 ? 129 PHE B CE1 1 ATOM 2181 C CE2 . PHE B 1 101 ? 31.636 21.584 82.596 1.00 31.32 ? 129 PHE B CE2 1 ATOM 2182 C CZ . PHE B 1 101 ? 32.164 22.414 81.616 1.00 42.82 ? 129 PHE B CZ 1 ATOM 2183 N N . ASN B 1 102 ? 27.280 25.643 86.401 1.00 28.11 ? 130 ASN B N 1 ATOM 2184 C CA . ASN B 1 102 ? 26.142 26.459 86.871 1.00 32.06 ? 130 ASN B CA 1 ATOM 2185 C C . ASN B 1 102 ? 24.799 25.747 86.796 1.00 29.86 ? 130 ASN B C 1 ATOM 2186 O O . ASN B 1 102 ? 23.778 26.409 86.725 1.00 37.49 ? 130 ASN B O 1 ATOM 2187 C CB . ASN B 1 102 ? 25.996 27.761 86.048 1.00 31.07 ? 130 ASN B CB 1 ATOM 2188 C CG . ASN B 1 102 ? 27.111 28.772 86.285 1.00 24.07 ? 130 ASN B CG 1 ATOM 2189 O OD1 . ASN B 1 102 ? 27.115 29.822 85.671 1.00 41.46 ? 130 ASN B OD1 1 ATOM 2190 N ND2 . ASN B 1 102 ? 28.014 28.488 87.198 1.00 36.41 ? 130 ASN B ND2 1 ATOM 2191 N N . ALA B 1 103 ? 24.797 24.416 86.766 1.00 36.41 ? 131 ALA B N 1 ATOM 2192 C CA . ALA B 1 103 ? 23.581 23.625 86.532 1.00 27.51 ? 131 ALA B CA 1 ATOM 2193 C C . ALA B 1 103 ? 22.846 24.012 85.244 1.00 35.53 ? 131 ALA B C 1 ATOM 2194 O O . ALA B 1 103 ? 21.627 23.902 85.162 1.00 39.40 ? 131 ALA B O 1 ATOM 2195 C CB . ALA B 1 103 ? 22.633 23.693 87.747 1.00 27.68 ? 131 ALA B CB 1 ATOM 2196 N N . PHE B 1 104 ? 23.589 24.461 84.234 1.00 36.96 ? 132 PHE B N 1 ATOM 2197 C CA . PHE B 1 104 ? 23.000 24.666 82.909 1.00 34.95 ? 132 PHE B CA 1 ATOM 2198 C C . PHE B 1 104 ? 22.606 23.336 82.297 1.00 37.22 ? 132 PHE B C 1 ATOM 2199 O O . PHE B 1 104 ? 21.722 23.262 81.448 1.00 32.42 ? 132 PHE B O 1 ATOM 2200 C CB . PHE B 1 104 ? 23.933 25.462 81.988 1.00 25.77 ? 132 PHE B CB 1 ATOM 2201 C CG . PHE B 1 104 ? 23.890 26.961 82.245 1.00 32.70 ? 132 PHE B CG 1 ATOM 2202 C CD1 . PHE B 1 104 ? 22.706 27.677 82.086 1.00 32.86 ? 132 PHE B CD1 1 ATOM 2203 C CD2 . PHE B 1 104 ? 25.015 27.638 82.668 1.00 28.75 ? 132 PHE B CD2 1 ATOM 2204 C CE1 . PHE B 1 104 ? 22.666 29.038 82.324 1.00 23.76 ? 132 PHE B CE1 1 ATOM 2205 C CE2 . PHE B 1 104 ? 24.986 29.014 82.915 1.00 31.86 ? 132 PHE B CE2 1 ATOM 2206 C CZ . PHE B 1 104 ? 23.819 29.712 82.750 1.00 25.28 ? 132 PHE B CZ 1 ATOM 2207 N N . VAL B 1 105 ? 23.273 22.281 82.742 1.00 32.06 ? 133 VAL B N 1 ATOM 2208 C CA . VAL B 1 105 ? 22.856 20.932 82.393 1.00 37.63 ? 133 VAL B CA 1 ATOM 2209 C C . VAL B 1 105 ? 22.693 20.117 83.664 1.00 43.00 ? 133 VAL B C 1 ATOM 2210 O O . VAL B 1 105 ? 23.226 20.470 84.709 1.00 49.10 ? 133 VAL B O 1 ATOM 2211 C CB . VAL B 1 105 ? 23.864 20.230 81.459 1.00 33.09 ? 133 VAL B CB 1 ATOM 2212 C CG1 . VAL B 1 105 ? 23.910 20.913 80.119 1.00 31.89 ? 133 VAL B CG1 1 ATOM 2213 C CG2 . VAL B 1 105 ? 25.258 20.132 82.113 1.00 32.09 ? 133 VAL B CG2 1 ATOM 2214 N N . THR B 1 106 ? 21.923 19.046 83.569 1.00 42.42 ? 134 THR B N 1 ATOM 2215 C CA . THR B 1 106 ? 21.842 18.057 84.633 1.00 44.40 ? 134 THR B CA 1 ATOM 2216 C C . THR B 1 106 ? 22.817 16.923 84.337 1.00 43.52 ? 134 THR B C 1 ATOM 2217 O O . THR B 1 106 ? 23.372 16.821 83.225 1.00 35.95 ? 134 THR B O 1 ATOM 2218 C CB . THR B 1 106 ? 20.468 17.444 84.673 1.00 41.14 ? 134 THR B CB 1 ATOM 2219 O OG1 . THR B 1 106 ? 20.320 16.556 83.551 1.00 42.53 ? 134 THR B OG1 1 ATOM 2220 C CG2 . THR B 1 106 ? 19.419 18.552 84.632 1.00 40.56 ? 134 THR B CG2 1 ATOM 2221 N N . TYR B 1 107 ? 23.035 16.069 85.326 1.00 43.97 ? 135 TYR B N 1 ATOM 2222 C CA . TYR B 1 107 ? 23.907 14.917 85.115 1.00 37.10 ? 135 TYR B CA 1 ATOM 2223 C C . TYR B 1 107 ? 23.289 13.897 84.153 1.00 42.72 ? 135 TYR B C 1 ATOM 2224 O O . TYR B 1 107 ? 24.009 13.231 83.391 1.00 44.57 ? 135 TYR B O 1 ATOM 2225 C CB . TYR B 1 107 ? 24.312 14.284 86.450 1.00 44.32 ? 135 TYR B CB 1 ATOM 2226 C CG . TYR B 1 107 ? 23.261 13.463 87.185 1.00 42.90 ? 135 TYR B CG 1 ATOM 2227 C CD1 . TYR B 1 107 ? 22.840 12.230 86.688 1.00 39.26 ? 135 TYR B CD1 1 ATOM 2228 C CD2 . TYR B 1 107 ? 22.749 13.883 88.415 1.00 46.19 ? 135 TYR B CD2 1 ATOM 2229 C CE1 . TYR B 1 107 ? 21.911 11.453 87.357 1.00 41.48 ? 135 TYR B CE1 1 ATOM 2230 C CE2 . TYR B 1 107 ? 21.813 13.100 89.104 1.00 47.60 ? 135 TYR B CE2 1 ATOM 2231 C CZ . TYR B 1 107 ? 21.408 11.883 88.557 1.00 49.87 ? 135 TYR B CZ 1 ATOM 2232 O OH . TYR B 1 107 ? 20.496 11.077 89.187 1.00 58.53 ? 135 TYR B OH 1 ATOM 2233 N N . GLN B 1 108 ? 21.958 13.794 84.156 1.00 40.36 ? 136 GLN B N 1 ATOM 2234 C CA . GLN B 1 108 ? 21.285 12.938 83.176 1.00 36.03 ? 136 GLN B CA 1 ATOM 2235 C C . GLN B 1 108 ? 21.561 13.449 81.773 1.00 32.88 ? 136 GLN B C 1 ATOM 2236 O O . GLN B 1 108 ? 21.777 12.670 80.854 1.00 51.11 ? 136 GLN B O 1 ATOM 2237 C CB . GLN B 1 108 ? 19.777 12.855 83.425 1.00 40.29 ? 136 GLN B CB 1 ATOM 2238 C CG . GLN B 1 108 ? 19.393 12.192 84.735 1.00 35.06 ? 136 GLN B CG 1 ATOM 2239 C CD . GLN B 1 108 ? 19.277 13.168 85.871 1.00 50.09 ? 136 GLN B CD 1 ATOM 2240 O OE1 . GLN B 1 108 ? 19.926 14.213 85.877 1.00 60.50 ? 136 GLN B OE1 1 ATOM 2241 N NE2 . GLN B 1 108 ? 18.464 12.826 86.856 1.00 53.94 ? 136 GLN B NE2 1 ATOM 2242 N N . GLU B 1 109 ? 21.554 14.765 81.596 1.00 42.43 ? 137 GLU B N 1 ATOM 2243 C CA . GLU B 1 109 ? 21.870 15.309 80.282 1.00 42.80 ? 137 GLU B CA 1 ATOM 2244 C C . GLU B 1 109 ? 23.302 15.060 79.841 1.00 31.79 ? 137 GLU B C 1 ATOM 2245 O O . GLU B 1 109 ? 23.523 14.670 78.698 1.00 34.88 ? 137 GLU B O 1 ATOM 2246 C CB . GLU B 1 109 ? 21.526 16.789 80.205 1.00 38.36 ? 137 GLU B CB 1 ATOM 2247 C CG . GLU B 1 109 ? 20.049 17.000 80.068 1.00 42.93 ? 137 GLU B CG 1 ATOM 2248 C CD . GLU B 1 109 ? 19.627 18.423 80.364 1.00 50.64 ? 137 GLU B CD 1 ATOM 2249 O OE1 . GLU B 1 109 ? 20.339 19.129 81.109 1.00 50.19 ? 137 GLU B OE1 1 ATOM 2250 O OE2 . GLU B 1 109 ? 18.588 18.842 79.821 1.00 52.26 ? 137 GLU B OE2 1 ATOM 2251 N N . ILE B 1 110 ? 24.263 15.223 80.749 1.00 26.21 ? 138 ILE B N 1 ATOM 2252 C CA . ILE B 1 110 ? 25.644 14.895 80.429 1.00 30.91 ? 138 ILE B CA 1 ATOM 2253 C C . ILE B 1 110 ? 25.763 13.410 80.038 1.00 38.40 ? 138 ILE B C 1 ATOM 2254 O O . ILE B 1 110 ? 26.324 13.088 78.991 1.00 37.86 ? 138 ILE B O 1 ATOM 2255 C CB . ILE B 1 110 ? 26.611 15.200 81.605 1.00 36.91 ? 138 ILE B CB 1 ATOM 2256 C CG1 . ILE B 1 110 ? 26.545 16.680 82.003 1.00 34.44 ? 138 ILE B CG1 1 ATOM 2257 C CG2 . ILE B 1 110 ? 28.031 14.876 81.194 1.00 34.86 ? 138 ILE B CG2 1 ATOM 2258 C CD1 . ILE B 1 110 ? 27.490 17.096 83.163 1.00 29.06 ? 138 ILE B CD1 1 ATOM 2259 N N . ALA B 1 111 ? 25.196 12.531 80.869 1.00 42.76 ? 139 ALA B N 1 ATOM 2260 C CA . ALA B 1 111 ? 25.214 11.087 80.650 1.00 41.87 ? 139 ALA B CA 1 ATOM 2261 C C . ALA B 1 111 ? 24.666 10.686 79.296 1.00 45.87 ? 139 ALA B C 1 ATOM 2262 O O . ALA B 1 111 ? 25.322 9.964 78.552 1.00 49.87 ? 139 ALA B O 1 ATOM 2263 C CB . ALA B 1 111 ? 24.443 10.355 81.763 1.00 42.28 ? 139 ALA B CB 1 ATOM 2264 N N . ALA B 1 112 ? 23.454 11.142 78.988 1.00 44.45 ? 140 ALA B N 1 ATOM 2265 C CA . ALA B 1 112 ? 22.811 10.814 77.714 1.00 43.17 ? 140 ALA B CA 1 ATOM 2266 C C . ALA B 1 112 ? 23.628 11.320 76.536 1.00 50.95 ? 140 ALA B C 1 ATOM 2267 O O . ALA B 1 112 ? 23.753 10.647 75.511 1.00 63.63 ? 140 ALA B O 1 ATOM 2268 C CB . ALA B 1 112 ? 21.397 11.387 77.663 1.00 36.73 ? 140 ALA B CB 1 ATOM 2269 N N . ALA B 1 113 ? 24.185 12.511 76.683 1.00 48.89 ? 141 ALA B N 1 ATOM 2270 C CA . ALA B 1 113 ? 24.983 13.088 75.615 1.00 57.31 ? 141 ALA B CA 1 ATOM 2271 C C . ALA B 1 113 ? 26.263 12.298 75.415 1.00 52.17 ? 141 ALA B C 1 ATOM 2272 O O . ALA B 1 113 ? 26.802 12.253 74.319 1.00 55.52 ? 141 ALA B O 1 ATOM 2273 C CB . ALA B 1 113 ? 25.291 14.561 75.906 1.00 57.76 ? 141 ALA B CB 1 ATOM 2274 N N . ASN B 1 114 ? 26.763 11.692 76.484 1.00 51.53 ? 142 ASN B N 1 ATOM 2275 C CA . ASN B 1 114 ? 28.022 10.959 76.393 1.00 53.13 ? 142 ASN B CA 1 ATOM 2276 C C . ASN B 1 114 ? 27.864 9.447 76.447 1.00 53.45 ? 142 ASN B C 1 ATOM 2277 O O . ASN B 1 114 ? 28.845 8.727 76.650 1.00 49.32 ? 142 ASN B O 1 ATOM 2278 C CB . ASN B 1 114 ? 29.022 11.433 77.447 1.00 47.47 ? 142 ASN B CB 1 ATOM 2279 C CG . ASN B 1 114 ? 29.478 12.858 77.214 1.00 50.13 ? 142 ASN B CG 1 ATOM 2280 O OD1 . ASN B 1 114 ? 30.448 13.099 76.494 1.00 41.08 ? 142 ASN B OD1 1 ATOM 2281 N ND2 . ASN B 1 114 ? 28.785 13.814 77.837 1.00 54.26 ? 142 ASN B ND2 1 ATOM 2282 N N . ASN B 1 115 ? 26.634 8.972 76.264 1.00 48.50 ? 143 ASN B N 1 ATOM 2283 C CA . ASN B 1 115 ? 26.377 7.535 76.225 1.00 50.84 ? 143 ASN B CA 1 ATOM 2284 C C . ASN B 1 115 ? 26.853 6.828 77.498 1.00 49.45 ? 143 ASN B C 1 ATOM 2285 O O . ASN B 1 115 ? 27.319 5.703 77.451 1.00 51.15 ? 143 ASN B O 1 ATOM 2286 C CB . ASN B 1 115 ? 27.054 6.914 75.004 1.00 55.65 ? 143 ASN B CB 1 ATOM 2287 C CG . ASN B 1 115 ? 26.247 7.100 73.735 1.00 72.88 ? 143 ASN B CG 1 ATOM 2288 O OD1 . ASN B 1 115 ? 26.698 7.761 72.794 1.00 71.47 ? 143 ASN B OD1 1 ATOM 2289 N ND2 . ASN B 1 115 ? 25.045 6.528 73.703 1.00 80.00 ? 143 ASN B ND2 1 ATOM 2290 N N . ILE B 1 116 ? 26.860 7.549 78.611 1.00 49.71 ? 144 ILE B N 1 ATOM 2291 C CA . ILE B 1 116 ? 27.171 6.959 79.898 1.00 49.94 ? 144 ILE B CA 1 ATOM 2292 C C . ILE B 1 116 ? 25.960 6.147 80.315 1.00 58.22 ? 144 ILE B C 1 ATOM 2293 O O . ILE B 1 116 ? 24.871 6.703 80.455 1.00 62.60 ? 144 ILE B O 1 ATOM 2294 C CB . ILE B 1 116 ? 27.487 8.016 80.966 1.00 54.37 ? 144 ILE B CB 1 ATOM 2295 C CG1 . ILE B 1 116 ? 28.555 8.998 80.473 1.00 62.27 ? 144 ILE B CG1 1 ATOM 2296 C CG2 . ILE B 1 116 ? 27.894 7.366 82.275 1.00 48.34 ? 144 ILE B CG2 1 ATOM 2297 C CD1 . ILE B 1 116 ? 29.782 8.333 79.975 1.00 65.68 ? 144 ILE B CD1 1 ATOM 2298 N N . PRO B 1 117 ? 26.136 4.840 80.539 1.00 60.16 ? 145 PRO B N 1 ATOM 2299 C CA . PRO B 1 117 ? 24.992 4.020 80.966 1.00 56.44 ? 145 PRO B CA 1 ATOM 2300 C C . PRO B 1 117 ? 24.629 4.191 82.444 1.00 53.64 ? 145 PRO B C 1 ATOM 2301 O O . PRO B 1 117 ? 23.445 4.199 82.768 1.00 59.67 ? 145 PRO B O 1 ATOM 2302 C CB . PRO B 1 117 ? 25.450 2.581 80.700 1.00 59.65 ? 145 PRO B CB 1 ATOM 2303 C CG . PRO B 1 117 ? 26.889 2.648 80.322 1.00 62.90 ? 145 PRO B CG 1 ATOM 2304 C CD . PRO B 1 117 ? 27.372 4.063 80.373 1.00 63.52 ? 145 PRO B CD 1 ATOM 2305 N N . ASP B 1 118 ? 25.625 4.322 83.316 1.00 45.70 ? 146 ASP B N 1 ATOM 2306 C CA . ASP B 1 118 ? 25.400 4.627 84.728 1.00 50.31 ? 146 ASP B CA 1 ATOM 2307 C C . ASP B 1 118 ? 26.031 5.974 85.131 1.00 54.73 ? 146 ASP B C 1 ATOM 2308 O O . ASP B 1 118 ? 27.236 6.048 85.348 1.00 56.88 ? 146 ASP B O 1 ATOM 2309 C CB . ASP B 1 118 ? 25.969 3.479 85.582 1.00 53.51 ? 146 ASP B CB 1 ATOM 2310 C CG . ASP B 1 118 ? 25.663 3.626 87.064 1.00 62.95 ? 146 ASP B CG 1 ATOM 2311 O OD1 . ASP B 1 118 ? 25.058 4.640 87.476 1.00 67.03 ? 146 ASP B OD1 1 ATOM 2312 O OD2 . ASP B 1 118 ? 26.055 2.723 87.832 1.00 73.75 ? 146 ASP B OD2 1 ATOM 2313 N N . PRO B 1 119 ? 25.211 7.019 85.326 1.00 60.82 ? 147 PRO B N 1 ATOM 2314 C CA . PRO B 1 119 ? 25.763 8.327 85.736 1.00 59.24 ? 147 PRO B CA 1 ATOM 2315 C C . PRO B 1 119 ? 26.627 8.329 86.989 1.00 53.90 ? 147 PRO B C 1 ATOM 2316 O O . PRO B 1 119 ? 27.348 9.305 87.206 1.00 50.71 ? 147 PRO B O 1 ATOM 2317 C CB . PRO B 1 119 ? 24.519 9.196 85.964 1.00 55.12 ? 147 PRO B CB 1 ATOM 2318 C CG . PRO B 1 119 ? 23.326 8.284 85.817 1.00 67.29 ? 147 PRO B CG 1 ATOM 2319 C CD . PRO B 1 119 ? 23.794 6.874 85.691 1.00 64.29 ? 147 PRO B CD 1 ATOM 2320 N N . ASN B 1 120 ? 26.615 7.238 87.745 1.00 47.79 ? 148 ASN B N 1 ATOM 2321 C CA . ASN B 1 120 ? 27.371 7.149 88.983 1.00 49.97 ? 148 ASN B CA 1 ATOM 2322 C C . ASN B 1 120 ? 28.813 6.726 88.734 1.00 50.63 ? 148 ASN B C 1 ATOM 2323 O O . ASN B 1 120 ? 29.650 6.787 89.623 1.00 57.21 ? 148 ASN B O 1 ATOM 2324 C CB . ASN B 1 120 ? 26.683 6.188 89.953 1.00 50.32 ? 148 ASN B CB 1 ATOM 2325 C CG . ASN B 1 120 ? 25.595 6.855 90.755 1.00 52.90 ? 148 ASN B CG 1 ATOM 2326 O OD1 . ASN B 1 120 ? 25.609 8.064 90.971 1.00 57.27 ? 148 ASN B OD1 1 ATOM 2327 N ND2 . ASN B 1 120 ? 24.603 6.075 91.142 1.00 58.82 ? 148 ASN B ND2 1 ATOM 2328 N N . LYS B 1 121 ? 29.098 6.308 87.509 1.00 41.87 ? 149 LYS B N 1 ATOM 2329 C CA . LYS B 1 121 ? 30.435 5.846 87.177 1.00 49.73 ? 149 LYS B CA 1 ATOM 2330 C C . LYS B 1 121 ? 31.050 6.602 86.027 1.00 44.98 ? 149 LYS B C 1 ATOM 2331 O O . LYS B 1 121 ? 30.559 6.536 84.909 1.00 47.30 ? 149 LYS B O 1 ATOM 2332 C CB . LYS B 1 121 ? 30.413 4.361 86.783 1.00 54.79 ? 149 LYS B CB 1 ATOM 2333 C CG . LYS B 1 121 ? 29.542 3.438 87.618 1.00 64.15 ? 149 LYS B CG 1 ATOM 2334 C CD . LYS B 1 121 ? 30.363 2.835 88.775 1.00 69.13 ? 149 LYS B CD 1 ATOM 2335 C CE . LYS B 1 121 ? 29.534 2.072 89.805 1.00 65.93 ? 149 LYS B CE 1 ATOM 2336 N NZ . LYS B 1 121 ? 30.261 0.815 90.146 1.00 70.79 ? 149 LYS B NZ 1 ATOM 2337 N N . ILE B 1 122 ? 32.169 7.259 86.318 1.00 40.90 ? 150 ILE B N 1 ATOM 2338 C CA . ILE B 1 122 ? 32.998 7.957 85.348 1.00 41.10 ? 150 ILE B CA 1 ATOM 2339 C C . ILE B 1 122 ? 34.444 7.798 85.792 1.00 44.97 ? 150 ILE B C 1 ATOM 2340 O O . ILE B 1 122 ? 34.707 7.595 86.970 1.00 47.07 ? 150 ILE B O 1 ATOM 2341 C CB . ILE B 1 122 ? 32.666 9.464 85.243 1.00 41.35 ? 150 ILE B CB 1 ATOM 2342 C CG1 . ILE B 1 122 ? 32.908 10.133 86.600 1.00 27.01 ? 150 ILE B CG1 1 ATOM 2343 C CG2 . ILE B 1 122 ? 31.228 9.679 84.773 1.00 41.49 ? 150 ILE B CG2 1 ATOM 2344 C CD1 . ILE B 1 122 ? 32.556 11.604 86.629 1.00 54.89 ? 150 ILE B CD1 1 ATOM 2345 N N . ASN B 1 123 ? 35.368 7.931 84.849 1.00 41.83 ? 151 ASN B N 1 ATOM 2346 C CA . ASN B 1 123 ? 36.788 7.715 85.082 1.00 39.99 ? 151 ASN B CA 1 ATOM 2347 C C . ASN B 1 123 ? 37.649 8.983 84.994 1.00 40.94 ? 151 ASN B C 1 ATOM 2348 O O . ASN B 1 123 ? 37.402 9.846 84.162 1.00 44.52 ? 151 ASN B O 1 ATOM 2349 C CB . ASN B 1 123 ? 37.322 6.687 84.075 1.00 44.06 ? 151 ASN B CB 1 ATOM 2350 C CG . ASN B 1 123 ? 36.956 5.269 84.441 1.00 62.30 ? 151 ASN B CG 1 ATOM 2351 O OD1 . ASN B 1 123 ? 35.792 4.967 84.698 1.00 68.85 ? 151 ASN B OD1 1 ATOM 2352 N ND2 . ASN B 1 123 ? 37.954 4.386 84.484 1.00 67.22 ? 151 ASN B ND2 1 ATOM 2353 N N . VAL B 1 124 ? 38.676 9.076 85.830 1.00 36.38 ? 152 VAL B N 1 ATOM 2354 C CA . VAL B 1 124 ? 39.637 10.165 85.697 1.00 41.26 ? 152 VAL B CA 1 ATOM 2355 C C . VAL B 1 124 ? 40.164 10.168 84.265 1.00 44.71 ? 152 VAL B C 1 ATOM 2356 O O . VAL B 1 124 ? 40.448 9.099 83.719 1.00 42.81 ? 152 VAL B O 1 ATOM 2357 C CB . VAL B 1 124 ? 40.814 9.995 86.676 1.00 39.79 ? 152 VAL B CB 1 ATOM 2358 C CG1 . VAL B 1 124 ? 41.909 10.981 86.382 1.00 40.93 ? 152 VAL B CG1 1 ATOM 2359 C CG2 . VAL B 1 124 ? 40.348 10.063 88.142 1.00 37.44 ? 152 VAL B CG2 1 ATOM 2360 N N . SER B 1 125 ? 40.266 11.360 83.667 1.00 43.16 ? 153 SER B N 1 ATOM 2361 C CA . SER B 1 125 ? 40.738 11.554 82.277 1.00 40.83 ? 153 SER B CA 1 ATOM 2362 C C . SER B 1 125 ? 39.730 11.181 81.199 1.00 42.54 ? 153 SER B C 1 ATOM 2363 O O . SER B 1 125 ? 40.028 11.274 80.016 1.00 45.34 ? 153 SER B O 1 ATOM 2364 C CB . SER B 1 125 ? 42.077 10.857 82.006 1.00 40.55 ? 153 SER B CB 1 ATOM 2365 O OG . SER B 1 125 ? 43.063 11.345 82.902 1.00 52.32 ? 153 SER B OG 1 ATOM 2366 N N . GLN B 1 126 ? 38.548 10.732 81.596 1.00 37.77 ? 154 GLN B N 1 ATOM 2367 C CA . GLN B 1 126 ? 37.472 10.558 80.632 1.00 28.14 ? 154 GLN B CA 1 ATOM 2368 C C . GLN B 1 126 ? 37.048 11.947 80.125 1.00 39.03 ? 154 GLN B C 1 ATOM 2369 O O . GLN B 1 126 ? 36.997 12.903 80.909 1.00 43.35 ? 154 GLN B O 1 ATOM 2370 C CB . GLN B 1 126 ? 36.316 9.844 81.316 1.00 33.67 ? 154 GLN B CB 1 ATOM 2371 C CG . GLN B 1 126 ? 35.066 9.686 80.490 1.00 38.03 ? 154 GLN B CG 1 ATOM 2372 C CD . GLN B 1 126 ? 33.966 9.018 81.296 1.00 39.78 ? 154 GLN B CD 1 ATOM 2373 O OE1 . GLN B 1 126 ? 34.118 8.796 82.491 1.00 39.61 ? 154 GLN B OE1 1 ATOM 2374 N NE2 . GLN B 1 126 ? 32.874 8.680 80.646 1.00 41.18 ? 154 GLN B NE2 1 ATOM 2375 N N . THR B 1 127 ? 36.768 12.073 78.827 1.00 36.74 ? 155 THR B N 1 ATOM 2376 C CA . THR B 1 127 ? 36.347 13.361 78.259 1.00 45.55 ? 155 THR B CA 1 ATOM 2377 C C . THR B 1 127 ? 34.840 13.431 78.060 1.00 40.84 ? 155 THR B C 1 ATOM 2378 O O . THR B 1 127 ? 34.241 12.518 77.510 1.00 46.46 ? 155 THR B O 1 ATOM 2379 C CB . THR B 1 127 ? 37.020 13.673 76.902 1.00 44.27 ? 155 THR B CB 1 ATOM 2380 O OG1 . THR B 1 127 ? 36.746 12.620 75.983 1.00 44.44 ? 155 THR B OG1 1 ATOM 2381 C CG2 . THR B 1 127 ? 38.510 13.851 77.059 1.00 41.98 ? 155 THR B CG2 1 ATOM 2382 N N . LEU B 1 128 ? 34.245 14.536 78.492 1.00 38.70 ? 156 LEU B N 1 ATOM 2383 C CA . LEU B 1 128 ? 32.808 14.725 78.406 1.00 38.30 ? 156 LEU B CA 1 ATOM 2384 C C . LEU B 1 128 ? 32.451 15.908 77.528 1.00 35.97 ? 156 LEU B C 1 ATOM 2385 O O . LEU B 1 128 ? 33.027 16.976 77.664 1.00 41.68 ? 156 LEU B O 1 ATOM 2386 C CB . LEU B 1 128 ? 32.244 14.973 79.804 1.00 35.04 ? 156 LEU B CB 1 ATOM 2387 C CG . LEU B 1 128 ? 32.549 13.896 80.849 1.00 35.57 ? 156 LEU B CG 1 ATOM 2388 C CD1 . LEU B 1 128 ? 32.120 14.351 82.256 1.00 25.89 ? 156 LEU B CD1 1 ATOM 2389 C CD2 . LEU B 1 128 ? 31.902 12.564 80.458 1.00 31.22 ? 156 LEU B CD2 1 ATOM 2390 N N . TRP B 1 129 ? 31.499 15.701 76.628 1.00 38.10 ? 157 TRP B N 1 ATOM 2391 C CA . TRP B 1 129 ? 30.863 16.781 75.896 1.00 35.59 ? 157 TRP B CA 1 ATOM 2392 C C . TRP B 1 129 ? 29.803 17.359 76.828 1.00 32.88 ? 157 TRP B C 1 ATOM 2393 O O . TRP B 1 129 ? 28.925 16.644 77.292 1.00 46.55 ? 157 TRP B O 1 ATOM 2394 C CB . TRP B 1 129 ? 30.203 16.245 74.623 1.00 31.26 ? 157 TRP B CB 1 ATOM 2395 C CG . TRP B 1 129 ? 29.279 17.230 73.932 1.00 44.29 ? 157 TRP B CG 1 ATOM 2396 C CD1 . TRP B 1 129 ? 29.439 18.588 73.847 1.00 48.21 ? 157 TRP B CD1 1 ATOM 2397 C CD2 . TRP B 1 129 ? 28.041 16.930 73.255 1.00 35.78 ? 157 TRP B CD2 1 ATOM 2398 N NE1 . TRP B 1 129 ? 28.398 19.140 73.146 1.00 45.48 ? 157 TRP B NE1 1 ATOM 2399 C CE2 . TRP B 1 129 ? 27.525 18.151 72.774 1.00 33.86 ? 157 TRP B CE2 1 ATOM 2400 C CE3 . TRP B 1 129 ? 27.325 15.750 73.013 1.00 31.92 ? 157 TRP B CE3 1 ATOM 2401 C CZ2 . TRP B 1 129 ? 26.315 18.232 72.072 1.00 34.38 ? 157 TRP B CZ2 1 ATOM 2402 C CZ3 . TRP B 1 129 ? 26.119 15.829 72.302 1.00 40.70 ? 157 TRP B CZ3 1 ATOM 2403 C CH2 . TRP B 1 129 ? 25.631 17.064 71.836 1.00 35.85 ? 157 TRP B CH2 1 ATOM 2404 N N . ILE B 1 130 ? 29.905 18.641 77.138 1.00 28.89 ? 158 ILE B N 1 ATOM 2405 C CA . ILE B 1 130 ? 28.885 19.301 77.948 1.00 26.19 ? 158 ILE B CA 1 ATOM 2406 C C . ILE B 1 130 ? 27.888 19.979 77.013 1.00 30.05 ? 158 ILE B C 1 ATOM 2407 O O . ILE B 1 130 ? 28.238 20.933 76.336 1.00 35.02 ? 158 ILE B O 1 ATOM 2408 C CB . ILE B 1 130 ? 29.510 20.366 78.862 1.00 33.38 ? 158 ILE B CB 1 ATOM 2409 C CG1 . ILE B 1 130 ? 30.584 19.755 79.778 1.00 37.82 ? 158 ILE B CG1 1 ATOM 2410 C CG2 . ILE B 1 130 ? 28.440 21.073 79.659 1.00 26.09 ? 158 ILE B CG2 1 ATOM 2411 C CD1 . ILE B 1 130 ? 30.091 18.655 80.722 1.00 35.87 ? 158 ILE B CD1 1 ATOM 2412 N N . PRO B 1 131 ? 26.655 19.460 76.930 1.00 27.47 ? 159 PRO B N 1 ATOM 2413 C CA . PRO B 1 131 ? 25.684 20.060 76.002 1.00 26.39 ? 159 PRO B CA 1 ATOM 2414 C C . PRO B 1 131 ? 24.917 21.248 76.606 1.00 31.77 ? 159 PRO B C 1 ATOM 2415 O O . PRO B 1 131 ? 23.756 21.088 76.980 1.00 30.68 ? 159 PRO B O 1 ATOM 2416 C CB . PRO B 1 131 ? 24.711 18.898 75.731 1.00 34.59 ? 159 PRO B CB 1 ATOM 2417 C CG . PRO B 1 131 ? 24.697 18.111 77.005 1.00 26.28 ? 159 PRO B CG 1 ATOM 2418 C CD . PRO B 1 131 ? 26.132 18.246 77.577 1.00 28.40 ? 159 PRO B CD 1 ATOM 2419 N N . LEU B 1 132 ? 25.564 22.407 76.706 1.00 38.24 ? 160 LEU B N 1 ATOM 2420 C CA . LEU B 1 132 ? 24.908 23.642 77.152 1.00 35.66 ? 160 LEU B CA 1 ATOM 2421 C C . LEU B 1 132 ? 23.649 23.876 76.324 1.00 33.98 ? 160 LEU B C 1 ATOM 2422 O O . LEU B 1 132 ? 23.663 23.711 75.103 1.00 36.51 ? 160 LEU B O 1 ATOM 2423 C CB . LEU B 1 132 ? 25.849 24.833 76.992 1.00 35.41 ? 160 LEU B CB 1 ATOM 2424 C CG . LEU B 1 132 ? 27.220 24.650 77.636 1.00 39.31 ? 160 LEU B CG 1 ATOM 2425 C CD1 . LEU B 1 132 ? 28.134 25.788 77.238 1.00 39.30 ? 160 LEU B CD1 1 ATOM 2426 C CD2 . LEU B 1 132 ? 27.106 24.566 79.161 1.00 37.09 ? 160 LEU B CD2 1 ATOM 2427 N N . PRO B 1 133 ? 22.554 24.266 76.986 1.00 29.53 ? 161 PRO B N 1 ATOM 2428 C CA . PRO B 1 133 ? 21.274 24.436 76.292 1.00 27.01 ? 161 PRO B CA 1 ATOM 2429 C C . PRO B 1 133 ? 21.242 25.704 75.410 1.00 36.46 ? 161 PRO B C 1 ATOM 2430 O O . PRO B 1 133 ? 21.742 26.762 75.799 1.00 30.97 ? 161 PRO B O 1 ATOM 2431 C CB . PRO B 1 133 ? 20.275 24.565 77.439 1.00 24.02 ? 161 PRO B CB 1 ATOM 2432 C CG . PRO B 1 133 ? 21.082 25.263 78.546 1.00 23.72 ? 161 PRO B CG 1 ATOM 2433 C CD . PRO B 1 133 ? 22.511 24.759 78.372 1.00 25.97 ? 161 PRO B CD 1 ATOM 2434 N N . CYS B 1 134 ? 20.630 25.599 74.240 1.00 28.22 ? 162 CYS B N 1 ATOM 2435 C CA . CYS B 1 134 ? 20.606 26.708 73.315 1.00 23.03 ? 162 CYS B CA 1 ATOM 2436 C C . CYS B 1 134 ? 19.481 26.469 72.335 1.00 33.30 ? 162 CYS B C 1 ATOM 2437 O O . CYS B 1 134 ? 18.787 25.462 72.427 1.00 34.22 ? 162 CYS B O 1 ATOM 2438 C CB . CYS B 1 134 ? 21.943 26.814 72.595 1.00 26.44 ? 162 CYS B CB 1 ATOM 2439 S SG . CYS B 1 134 ? 22.377 25.299 71.680 1.00 39.12 ? 162 CYS B SG 1 ATOM 2440 N N . SER B 1 135 ? 19.275 27.408 71.422 1.00 36.70 ? 163 SER B N 1 ATOM 2441 C CA . SER B 1 135 ? 18.264 27.234 70.388 1.00 45.87 ? 163 SER B CA 1 ATOM 2442 C C . SER B 1 135 ? 18.586 28.156 69.211 1.00 50.03 ? 163 SER B C 1 ATOM 2443 O O . SER B 1 135 ? 19.362 29.112 69.352 1.00 45.66 ? 163 SER B O 1 ATOM 2444 C CB . SER B 1 135 ? 16.871 27.547 70.945 1.00 40.60 ? 163 SER B CB 1 ATOM 2445 O OG . SER B 1 135 ? 15.864 27.354 69.968 1.00 44.83 ? 163 SER B OG 1 ATOM 2446 N N . CYS B 1 136 ? 18.014 27.846 68.051 1.00 41.98 ? 164 CYS B N 1 ATOM 2447 C CA . CYS B 1 136 ? 18.092 28.731 66.897 1.00 41.51 ? 164 CYS B CA 1 ATOM 2448 C C . CYS B 1 136 ? 16.701 29.165 66.443 1.00 43.68 ? 164 CYS B C 1 ATOM 2449 O O . CYS B 1 136 ? 16.558 29.775 65.381 1.00 40.70 ? 164 CYS B O 1 ATOM 2450 C CB . CYS B 1 136 ? 18.857 28.060 65.752 1.00 39.47 ? 164 CYS B CB 1 ATOM 2451 S SG . CYS B 1 136 ? 20.552 27.591 66.225 1.00 44.03 ? 164 CYS B SG 1 ATOM 2452 N N . ASP B 1 137 ? 15.683 28.854 67.251 1.00 41.33 ? 165 ASP B N 1 ATOM 2453 C CA . ASP B 1 137 ? 14.313 29.269 66.953 1.00 41.60 ? 165 ASP B CA 1 ATOM 2454 C C . ASP B 1 137 ? 14.211 30.781 66.895 1.00 40.96 ? 165 ASP B C 1 ATOM 2455 O O . ASP B 1 137 ? 14.822 31.486 67.692 1.00 37.11 ? 165 ASP B O 1 ATOM 2456 C CB . ASP B 1 137 ? 13.342 28.837 68.052 1.00 39.74 ? 165 ASP B CB 1 ATOM 2457 C CG . ASP B 1 137 ? 13.080 27.367 68.060 1.00 35.01 ? 165 ASP B CG 1 ATOM 2458 O OD1 . ASP B 1 137 ? 13.239 26.739 67.001 1.00 42.28 ? 165 ASP B OD1 1 ATOM 2459 O OD2 . ASP B 1 137 ? 12.678 26.845 69.121 1.00 37.47 ? 165 ASP B OD2 1 ATOM 2460 N N . LYS B 1 138 ? 13.392 31.280 65.981 1.00 51.05 ? 166 LYS B N 1 ATOM 2461 C CA . LYS B 1 138 ? 12.992 32.680 66.023 1.00 49.18 ? 166 LYS B CA 1 ATOM 2462 C C . LYS B 1 138 ? 11.991 32.812 67.159 1.00 44.88 ? 166 LYS B C 1 ATOM 2463 O O . LYS B 1 138 ? 11.461 31.814 67.654 1.00 47.72 ? 166 LYS B O 1 ATOM 2464 C CB . LYS B 1 138 ? 12.340 33.098 64.705 1.00 37.72 ? 166 LYS B CB 1 ATOM 2465 C CG . LYS B 1 138 ? 13.291 33.313 63.537 1.00 39.46 ? 166 LYS B CG 1 ATOM 2466 C CD . LYS B 1 138 ? 12.479 33.373 62.251 1.00 38.09 ? 166 LYS B CD 1 ATOM 2467 C CE . LYS B 1 138 ? 13.336 33.485 61.005 1.00 46.23 ? 166 LYS B CE 1 ATOM 2468 N NZ . LYS B 1 138 ? 13.198 34.815 60.344 1.00 58.85 ? 166 LYS B NZ 1 ATOM 2469 N N . GLU B 1 139 ? 11.762 34.040 67.592 1.00 46.64 ? 167 GLU B N 1 ATOM 2470 C CA . GLU B 1 139 ? 10.728 34.336 68.570 1.00 43.83 ? 167 GLU B CA 1 ATOM 2471 C C . GLU B 1 139 ? 9.581 35.047 67.880 1.00 53.18 ? 167 GLU B C 1 ATOM 2472 O O . GLU B 1 139 ? 9.683 36.232 67.569 1.00 53.24 ? 167 GLU B O 1 ATOM 2473 C CB . GLU B 1 139 ? 11.294 35.183 69.718 1.00 38.41 ? 167 GLU B CB 1 ATOM 2474 C CG . GLU B 1 139 ? 10.298 35.511 70.819 1.00 42.51 ? 167 GLU B CG 1 ATOM 2475 C CD . GLU B 1 139 ? 9.537 34.303 71.340 1.00 51.02 ? 167 GLU B CD 1 ATOM 2476 O OE1 . GLU B 1 139 ? 8.345 34.460 71.715 1.00 47.18 ? 167 GLU B OE1 1 ATOM 2477 O OE2 . GLU B 1 139 ? 10.114 33.196 71.372 1.00 55.46 ? 167 GLU B OE2 1 ATOM 2478 N N . GLU B 1 140 ? 8.510 34.297 67.615 1.00 56.55 ? 168 GLU B N 1 ATOM 2479 C CA . GLU B 1 140 ? 7.316 34.810 66.935 1.00 56.70 ? 168 GLU B CA 1 ATOM 2480 C C . GLU B 1 140 ? 7.674 35.602 65.668 1.00 58.84 ? 168 GLU B C 1 ATOM 2481 O O . GLU B 1 140 ? 7.225 36.739 65.486 1.00 53.24 ? 168 GLU B O 1 ATOM 2482 C CB . GLU B 1 140 ? 6.468 35.669 67.889 1.00 56.11 ? 168 GLU B CB 1 ATOM 2483 C CG . GLU B 1 140 ? 5.829 34.884 69.044 1.00 67.09 ? 168 GLU B CG 1 ATOM 2484 C CD . GLU B 1 140 ? 4.658 34.016 68.628 1.00 86.93 ? 168 GLU B CD 1 ATOM 2485 O OE1 . GLU B 1 140 ? 4.271 34.029 67.440 1.00 92.83 ? 168 GLU B OE1 1 ATOM 2486 O OE2 . GLU B 1 140 ? 4.129 33.294 69.497 1.00 96.72 ? 168 GLU B OE2 1 ATOM 2487 N N . GLY B 1 141 ? 8.496 35.003 64.806 1.00 52.55 ? 169 GLY B N 1 ATOM 2488 C CA . GLY B 1 141 ? 8.856 35.613 63.539 1.00 45.49 ? 169 GLY B CA 1 ATOM 2489 C C . GLY B 1 141 ? 10.057 36.547 63.529 1.00 48.75 ? 169 GLY B C 1 ATOM 2490 O O . GLY B 1 141 ? 10.465 37.019 62.472 1.00 55.49 ? 169 GLY B O 1 ATOM 2491 N N . SER B 1 142 ? 10.617 36.841 64.694 1.00 43.92 ? 170 SER B N 1 ATOM 2492 C CA . SER B 1 142 ? 11.776 37.726 64.764 1.00 47.02 ? 170 SER B CA 1 ATOM 2493 C C . SER B 1 142 ? 13.077 36.968 65.064 1.00 46.38 ? 170 SER B C 1 ATOM 2494 O O . SER B 1 142 ? 13.078 35.919 65.697 1.00 52.46 ? 170 SER B O 1 ATOM 2495 C CB . SER B 1 142 ? 11.563 38.807 65.824 1.00 50.48 ? 170 SER B CB 1 ATOM 2496 O OG . SER B 1 142 ? 11.453 40.084 65.220 1.00 66.26 ? 170 SER B OG 1 ATOM 2497 N N . ASN B 1 143 ? 14.186 37.517 64.607 1.00 35.92 ? 171 ASN B N 1 ATOM 2498 C CA . ASN B 1 143 ? 15.486 36.937 64.876 1.00 32.99 ? 171 ASN B CA 1 ATOM 2499 C C . ASN B 1 143 ? 15.975 37.325 66.258 1.00 43.17 ? 171 ASN B C 1 ATOM 2500 O O . ASN B 1 143 ? 15.945 38.495 66.623 1.00 54.63 ? 171 ASN B O 1 ATOM 2501 C CB . ASN B 1 143 ? 16.488 37.389 63.834 1.00 35.10 ? 171 ASN B CB 1 ATOM 2502 C CG . ASN B 1 143 ? 16.227 36.785 62.482 1.00 45.37 ? 171 ASN B CG 1 ATOM 2503 O OD1 . ASN B 1 143 ? 15.719 35.667 62.369 1.00 47.28 ? 171 ASN B OD1 1 ATOM 2504 N ND2 . ASN B 1 143 ? 16.573 37.526 61.437 1.00 44.35 ? 171 ASN B ND2 1 ATOM 2505 N N . VAL B 1 144 ? 16.430 36.334 67.015 1.00 47.09 ? 172 VAL B N 1 ATOM 2506 C CA . VAL B 1 144 ? 16.909 36.529 68.376 1.00 42.10 ? 172 VAL B CA 1 ATOM 2507 C C . VAL B 1 144 ? 18.186 35.753 68.637 1.00 47.44 ? 172 VAL B C 1 ATOM 2508 O O . VAL B 1 144 ? 18.501 34.807 67.929 1.00 44.21 ? 172 VAL B O 1 ATOM 2509 C CB . VAL B 1 144 ? 15.882 36.047 69.397 1.00 45.74 ? 172 VAL B CB 1 ATOM 2510 C CG1 . VAL B 1 144 ? 14.789 37.114 69.645 1.00 40.06 ? 172 VAL B CG1 1 ATOM 2511 C CG2 . VAL B 1 144 ? 15.305 34.702 68.948 1.00 39.84 ? 172 VAL B CG2 1 ATOM 2512 N N . MET B 1 145 ? 18.941 36.166 69.642 1.00 48.49 ? 173 MET B N 1 ATOM 2513 C CA . MET B 1 145 ? 19.981 35.301 70.157 1.00 44.03 ? 173 MET B CA 1 ATOM 2514 C C . MET B 1 145 ? 19.559 34.748 71.507 1.00 44.98 ? 173 MET B C 1 ATOM 2515 O O . MET B 1 145 ? 19.305 35.490 72.457 1.00 41.99 ? 173 MET B O 1 ATOM 2516 C CB . MET B 1 145 ? 21.318 36.010 70.289 1.00 44.00 ? 173 MET B CB 1 ATOM 2517 C CG . MET B 1 145 ? 22.443 35.006 70.442 1.00 38.16 ? 173 MET B CG 1 ATOM 2518 S SD . MET B 1 145 ? 23.844 35.665 71.294 1.00 58.00 ? 173 MET B SD 1 ATOM 2519 C CE . MET B 1 145 ? 23.055 36.174 72.823 1.00 48.80 ? 173 MET B CE 1 ATOM 2520 N N . HIS B 1 146 ? 19.480 33.430 71.579 1.00 38.96 ? 174 HIS B N 1 ATOM 2521 C CA . HIS B 1 146 ? 19.071 32.767 72.791 1.00 34.19 ? 174 HIS B CA 1 ATOM 2522 C C . HIS B 1 146 ? 20.177 32.828 73.839 1.00 35.42 ? 174 HIS B C 1 ATOM 2523 O O . HIS B 1 146 ? 21.318 32.484 73.564 1.00 38.66 ? 174 HIS B O 1 ATOM 2524 C CB . HIS B 1 146 ? 18.660 31.334 72.484 1.00 33.24 ? 174 HIS B CB 1 ATOM 2525 C CG . HIS B 1 146 ? 17.401 31.228 71.683 1.00 44.79 ? 174 HIS B CG 1 ATOM 2526 N ND1 . HIS B 1 146 ? 16.170 30.996 72.260 1.00 37.23 ? 174 HIS B ND1 1 ATOM 2527 C CD2 . HIS B 1 146 ? 17.177 31.340 70.350 1.00 44.35 ? 174 HIS B CD2 1 ATOM 2528 C CE1 . HIS B 1 146 ? 15.247 30.941 71.313 1.00 37.22 ? 174 HIS B CE1 1 ATOM 2529 N NE2 . HIS B 1 146 ? 15.829 31.153 70.147 1.00 39.44 ? 174 HIS B NE2 1 ATOM 2530 N N . LEU B 1 147 ? 19.819 33.301 75.030 1.00 31.70 ? 175 LEU B N 1 ATOM 2531 C CA . LEU B 1 147 ? 20.726 33.382 76.166 1.00 32.91 ? 175 LEU B CA 1 ATOM 2532 C C . LEU B 1 147 ? 20.195 32.494 77.282 1.00 35.02 ? 175 LEU B C 1 ATOM 2533 O O . LEU B 1 147 ? 19.026 32.594 77.652 1.00 34.04 ? 175 LEU B O 1 ATOM 2534 C CB . LEU B 1 147 ? 20.839 34.817 76.678 1.00 30.67 ? 175 LEU B CB 1 ATOM 2535 C CG . LEU B 1 147 ? 21.685 34.972 77.937 1.00 40.40 ? 175 LEU B CG 1 ATOM 2536 C CD1 . LEU B 1 147 ? 23.117 34.609 77.611 1.00 43.66 ? 175 LEU B CD1 1 ATOM 2537 C CD2 . LEU B 1 147 ? 21.613 36.402 78.490 1.00 38.26 ? 175 LEU B CD2 1 ATOM 2538 N N . ALA B 1 148 ? 21.033 31.587 77.780 1.00 38.86 ? 176 ALA B N 1 ATOM 2539 C CA . ALA B 1 148 ? 20.647 30.738 78.904 1.00 30.75 ? 176 ALA B CA 1 ATOM 2540 C C . ALA B 1 148 ? 20.910 31.460 80.218 1.00 34.00 ? 176 ALA B C 1 ATOM 2541 O O . ALA B 1 148 ? 22.045 31.843 80.510 1.00 33.58 ? 176 ALA B O 1 ATOM 2542 C CB . ALA B 1 148 ? 21.404 29.420 78.859 1.00 27.64 ? 176 ALA B CB 1 ATOM 2543 N N . TYR B 1 149 ? 19.860 31.620 81.018 1.00 37.18 ? 177 TYR B N 1 ATOM 2544 C CA . TYR B 1 149 ? 19.935 32.431 82.221 1.00 25.32 ? 177 TYR B CA 1 ATOM 2545 C C . TYR B 1 149 ? 19.510 31.652 83.449 1.00 25.98 ? 177 TYR B C 1 ATOM 2546 O O . TYR B 1 149 ? 18.393 31.158 83.529 1.00 27.94 ? 177 TYR B O 1 ATOM 2547 C CB . TYR B 1 149 ? 19.030 33.659 82.077 1.00 29.18 ? 177 TYR B CB 1 ATOM 2548 C CG . TYR B 1 149 ? 19.087 34.618 83.262 1.00 30.57 ? 177 TYR B CG 1 ATOM 2549 C CD1 . TYR B 1 149 ? 18.209 34.479 84.338 1.00 37.91 ? 177 TYR B CD1 1 ATOM 2550 C CD2 . TYR B 1 149 ? 20.003 35.660 83.296 1.00 35.74 ? 177 TYR B CD2 1 ATOM 2551 C CE1 . TYR B 1 149 ? 18.245 35.338 85.412 1.00 36.41 ? 177 TYR B CE1 1 ATOM 2552 C CE2 . TYR B 1 149 ? 20.056 36.519 84.365 1.00 40.94 ? 177 TYR B CE2 1 ATOM 2553 C CZ . TYR B 1 149 ? 19.174 36.352 85.421 1.00 38.55 ? 177 TYR B CZ 1 ATOM 2554 O OH . TYR B 1 149 ? 19.222 37.200 86.483 1.00 31.99 ? 177 TYR B OH 1 ATOM 2555 N N . SER B 1 150 ? 20.394 31.597 84.431 1.00 31.29 ? 178 SER B N 1 ATOM 2556 C CA . SER B 1 150 ? 20.079 30.966 85.705 1.00 35.10 ? 178 SER B CA 1 ATOM 2557 C C . SER B 1 150 ? 19.442 31.966 86.676 1.00 40.94 ? 178 SER B C 1 ATOM 2558 O O . SER B 1 150 ? 20.051 32.974 87.035 1.00 35.42 ? 178 SER B O 1 ATOM 2559 C CB . SER B 1 150 ? 21.345 30.373 86.338 1.00 23.00 ? 178 SER B CB 1 ATOM 2560 O OG . SER B 1 150 ? 21.019 29.794 87.583 1.00 30.71 ? 178 SER B OG 1 ATOM 2561 N N . VAL B 1 151 ? 18.214 31.675 87.085 1.00 37.47 ? 179 VAL B N 1 ATOM 2562 C CA . VAL B 1 151 ? 17.459 32.547 87.972 1.00 35.93 ? 179 VAL B CA 1 ATOM 2563 C C . VAL B 1 151 ? 18.090 32.709 89.345 1.00 26.65 ? 179 VAL B C 1 ATOM 2564 O O . VAL B 1 151 ? 18.262 31.740 90.082 1.00 30.01 ? 179 VAL B O 1 ATOM 2565 C CB . VAL B 1 151 ? 16.019 32.008 88.188 1.00 35.20 ? 179 VAL B CB 1 ATOM 2566 C CG1 . VAL B 1 151 ? 15.315 32.784 89.318 1.00 27.70 ? 179 VAL B CG1 1 ATOM 2567 C CG2 . VAL B 1 151 ? 15.248 32.068 86.897 1.00 36.23 ? 179 VAL B CG2 1 ATOM 2568 N N . GLY B 1 152 ? 18.343 33.948 89.741 1.00 32.30 ? 180 GLY B N 1 ATOM 2569 C CA . GLY B 1 152 ? 18.890 34.187 91.065 1.00 21.71 ? 180 GLY B CA 1 ATOM 2570 C C . GLY B 1 152 ? 17.789 34.078 92.109 1.00 35.10 ? 180 GLY B C 1 ATOM 2571 O O . GLY B 1 152 ? 16.605 34.232 91.805 1.00 43.97 ? 180 GLY B O 1 ATOM 2572 N N . LYS B 1 153 ? 18.175 33.803 93.344 1.00 34.53 ? 181 LYS B N 1 ATOM 2573 C CA . LYS B 1 153 ? 17.204 33.705 94.411 1.00 48.57 ? 181 LYS B CA 1 ATOM 2574 C C . LYS B 1 153 ? 16.547 35.079 94.549 1.00 40.27 ? 181 LYS B C 1 ATOM 2575 O O . LYS B 1 153 ? 17.204 36.097 94.463 1.00 39.61 ? 181 LYS B O 1 ATOM 2576 C CB . LYS B 1 153 ? 17.873 33.283 95.722 1.00 56.74 ? 181 LYS B CB 1 ATOM 2577 C CG . LYS B 1 153 ? 16.897 32.964 96.848 1.00 65.56 ? 181 LYS B CG 1 ATOM 2578 C CD . LYS B 1 153 ? 16.974 33.944 98.008 1.00 68.70 ? 181 LYS B CD 1 ATOM 2579 C CE . LYS B 1 153 ? 15.981 33.534 99.097 1.00 66.94 ? 181 LYS B CE 1 ATOM 2580 N NZ . LYS B 1 153 ? 16.260 32.177 99.644 1.00 57.90 ? 181 LYS B NZ 1 ATOM 2581 N N . GLY B 1 154 ? 15.229 35.097 94.657 1.00 42.50 ? 182 GLY B N 1 ATOM 2582 C CA . GLY B 1 154 ? 14.510 36.333 94.864 1.00 36.63 ? 182 GLY B CA 1 ATOM 2583 C C . GLY B 1 154 ? 14.197 37.109 93.610 1.00 42.36 ? 182 GLY B C 1 ATOM 2584 O O . GLY B 1 154 ? 13.563 38.149 93.674 1.00 45.13 ? 182 GLY B O 1 ATOM 2585 N N . GLU B 1 155 ? 14.624 36.601 92.462 1.00 40.97 ? 183 GLU B N 1 ATOM 2586 C CA . GLU B 1 155 ? 14.305 37.249 91.200 1.00 33.35 ? 183 GLU B CA 1 ATOM 2587 C C . GLU B 1 155 ? 12.888 36.917 90.703 1.00 35.79 ? 183 GLU B C 1 ATOM 2588 O O . GLU B 1 155 ? 12.313 35.904 91.081 1.00 51.59 ? 183 GLU B O 1 ATOM 2589 C CB . GLU B 1 155 ? 15.384 36.951 90.140 1.00 28.52 ? 183 GLU B CB 1 ATOM 2590 C CG . GLU B 1 155 ? 16.710 37.700 90.403 1.00 34.08 ? 183 GLU B CG 1 ATOM 2591 C CD . GLU B 1 155 ? 17.818 37.381 89.392 1.00 45.10 ? 183 GLU B CD 1 ATOM 2592 O OE1 . GLU B 1 155 ? 17.658 36.489 88.531 1.00 39.74 ? 183 GLU B OE1 1 ATOM 2593 O OE2 . GLU B 1 155 ? 18.865 38.048 89.455 1.00 62.47 ? 183 GLU B OE2 1 ATOM 2594 N N . ASN B 1 156 ? 12.343 37.787 89.859 1.00 34.16 ? 184 ASN B N 1 ATOM 2595 C CA . ASN B 1 156 ? 11.023 37.615 89.256 1.00 40.23 ? 184 ASN B CA 1 ATOM 2596 C C . ASN B 1 156 ? 11.115 37.783 87.739 1.00 40.71 ? 184 ASN B C 1 ATOM 2597 O O . ASN B 1 156 ? 12.109 38.291 87.222 1.00 48.35 ? 184 ASN B O 1 ATOM 2598 C CB . ASN B 1 156 ? 9.974 38.565 89.874 1.00 41.31 ? 184 ASN B CB 1 ATOM 2599 C CG . ASN B 1 156 ? 10.387 40.031 89.813 1.00 47.17 ? 184 ASN B CG 1 ATOM 2600 O OD1 . ASN B 1 156 ? 10.357 40.648 88.741 1.00 54.38 ? 184 ASN B OD1 1 ATOM 2601 N ND2 . ASN B 1 156 ? 10.745 40.605 90.977 1.00 49.14 ? 184 ASN B ND2 1 ATOM 2602 N N . THR B 1 157 ? 10.084 37.361 87.021 1.00 43.32 ? 185 THR B N 1 ATOM 2603 C CA . THR B 1 157 ? 10.150 37.317 85.566 1.00 35.78 ? 185 THR B CA 1 ATOM 2604 C C . THR B 1 157 ? 10.014 38.715 84.987 1.00 48.03 ? 185 THR B C 1 ATOM 2605 O O . THR B 1 157 ? 10.526 39.003 83.902 1.00 57.34 ? 185 THR B O 1 ATOM 2606 C CB . THR B 1 157 ? 9.046 36.411 84.995 1.00 49.84 ? 185 THR B CB 1 ATOM 2607 O OG1 . THR B 1 157 ? 7.759 36.857 85.445 1.00 62.10 ? 185 THR B OG1 1 ATOM 2608 C CG2 . THR B 1 157 ? 9.258 34.980 85.451 1.00 55.10 ? 185 THR B CG2 1 ATOM 2609 N N . SER B 1 158 ? 9.357 39.600 85.726 1.00 49.11 ? 186 SER B N 1 ATOM 2610 C CA . SER B 1 158 ? 9.214 40.981 85.281 1.00 49.24 ? 186 SER B CA 1 ATOM 2611 C C . SER B 1 158 ? 10.589 41.650 85.138 1.00 42.41 ? 186 SER B C 1 ATOM 2612 O O . SER B 1 158 ? 10.938 42.170 84.083 1.00 47.68 ? 186 SER B O 1 ATOM 2613 C CB . SER B 1 158 ? 8.328 41.765 86.267 1.00 45.88 ? 186 SER B CB 1 ATOM 2614 O OG . SER B 1 158 ? 8.063 43.068 85.774 1.00 49.74 ? 186 SER B OG 1 ATOM 2615 N N . ALA B 1 159 ? 11.379 41.616 86.203 1.00 38.27 ? 187 ALA B N 1 ATOM 2616 C CA . ALA B 1 159 ? 12.695 42.254 86.187 1.00 40.21 ? 187 ALA B CA 1 ATOM 2617 C C . ALA B 1 159 ? 13.684 41.583 85.240 1.00 48.13 ? 187 ALA B C 1 ATOM 2618 O O . ALA B 1 159 ? 14.485 42.258 84.592 1.00 40.32 ? 187 ALA B O 1 ATOM 2619 C CB . ALA B 1 159 ? 13.283 42.275 87.590 1.00 36.19 ? 187 ALA B CB 1 ATOM 2620 N N . ILE B 1 160 ? 13.630 40.251 85.165 1.00 52.27 ? 188 ILE B N 1 ATOM 2621 C CA . ILE B 1 160 ? 14.517 39.527 84.273 1.00 42.92 ? 188 ILE B CA 1 ATOM 2622 C C . ILE B 1 160 ? 14.188 39.915 82.849 1.00 35.84 ? 188 ILE B C 1 ATOM 2623 O O . ILE B 1 160 ? 15.075 40.275 82.090 1.00 38.23 ? 188 ILE B O 1 ATOM 2624 C CB . ILE B 1 160 ? 14.389 38.005 84.452 1.00 43.50 ? 188 ILE B CB 1 ATOM 2625 C CG1 . ILE B 1 160 ? 15.106 37.552 85.715 1.00 29.92 ? 188 ILE B CG1 1 ATOM 2626 C CG2 . ILE B 1 160 ? 14.959 37.255 83.261 1.00 36.81 ? 188 ILE B CG2 1 ATOM 2627 C CD1 . ILE B 1 160 ? 14.772 36.094 86.045 1.00 28.58 ? 188 ILE B CD1 1 ATOM 2628 N N . ALA B 1 161 ? 12.905 39.856 82.501 1.00 41.27 ? 189 ALA B N 1 ATOM 2629 C CA . ALA B 1 161 ? 12.465 40.236 81.163 1.00 43.28 ? 189 ALA B CA 1 ATOM 2630 C C . ALA B 1 161 ? 12.883 41.659 80.844 1.00 44.82 ? 189 ALA B C 1 ATOM 2631 O O . ALA B 1 161 ? 13.477 41.933 79.790 1.00 45.52 ? 189 ALA B O 1 ATOM 2632 C CB . ALA B 1 161 ? 10.959 40.092 81.045 1.00 38.97 ? 189 ALA B CB 1 ATOM 2633 N N . ALA B 1 162 ? 12.617 42.561 81.782 1.00 39.48 ? 190 ALA B N 1 ATOM 2634 C CA . ALA B 1 162 ? 12.948 43.963 81.556 1.00 44.15 ? 190 ALA B CA 1 ATOM 2635 C C . ALA B 1 162 ? 14.449 44.116 81.415 1.00 48.12 ? 190 ALA B C 1 ATOM 2636 O O . ALA B 1 162 ? 14.918 44.834 80.535 1.00 60.92 ? 190 ALA B O 1 ATOM 2637 C CB . ALA B 1 162 ? 12.410 44.847 82.686 1.00 36.88 ? 190 ALA B CB 1 ATOM 2638 N N . LYS B 1 163 ? 15.205 43.428 82.266 1.00 40.48 ? 191 LYS B N 1 ATOM 2639 C CA . LYS B 1 163 ? 16.670 43.485 82.195 1.00 42.20 ? 191 LYS B CA 1 ATOM 2640 C C . LYS B 1 163 ? 17.192 43.122 80.801 1.00 43.65 ? 191 LYS B C 1 ATOM 2641 O O . LYS B 1 163 ? 18.216 43.634 80.351 1.00 51.69 ? 191 LYS B O 1 ATOM 2642 C CB . LYS B 1 163 ? 17.303 42.573 83.248 1.00 48.17 ? 191 LYS B CB 1 ATOM 2643 C CG . LYS B 1 163 ? 18.793 42.344 83.063 1.00 63.36 ? 191 LYS B CG 1 ATOM 2644 C CD . LYS B 1 163 ? 19.432 41.753 84.311 1.00 71.14 ? 191 LYS B CD 1 ATOM 2645 C CE . LYS B 1 163 ? 18.659 40.540 84.801 1.00 63.56 ? 191 LYS B CE 1 ATOM 2646 N NZ . LYS B 1 163 ? 19.320 39.876 85.941 1.00 52.64 ? 191 LYS B NZ 1 ATOM 2647 N N . TYR B 1 164 ? 16.491 42.243 80.103 1.00 42.94 ? 192 TYR B N 1 ATOM 2648 C CA . TYR B 1 164 ? 16.969 41.843 78.784 1.00 52.07 ? 192 TYR B CA 1 ATOM 2649 C C . TYR B 1 164 ? 16.178 42.422 77.632 1.00 54.54 ? 192 TYR B C 1 ATOM 2650 O O . TYR B 1 164 ? 16.437 42.093 76.485 1.00 42.01 ? 192 TYR B O 1 ATOM 2651 C CB . TYR B 1 164 ? 17.088 40.318 78.691 1.00 44.75 ? 192 TYR B CB 1 ATOM 2652 C CG . TYR B 1 164 ? 18.242 39.848 79.536 1.00 42.88 ? 192 TYR B CG 1 ATOM 2653 C CD1 . TYR B 1 164 ? 19.538 40.193 79.190 1.00 34.49 ? 192 TYR B CD1 1 ATOM 2654 C CD2 . TYR B 1 164 ? 18.046 39.108 80.692 1.00 30.28 ? 192 TYR B CD2 1 ATOM 2655 C CE1 . TYR B 1 164 ? 20.605 39.798 79.947 1.00 36.65 ? 192 TYR B CE1 1 ATOM 2656 C CE2 . TYR B 1 164 ? 19.111 38.710 81.450 1.00 33.94 ? 192 TYR B CE2 1 ATOM 2657 C CZ . TYR B 1 164 ? 20.392 39.062 81.069 1.00 40.51 ? 192 TYR B CZ 1 ATOM 2658 O OH . TYR B 1 164 ? 21.478 38.692 81.813 1.00 52.31 ? 192 TYR B OH 1 ATOM 2659 N N . GLY B 1 165 ? 15.293 43.363 77.946 1.00 57.80 ? 193 GLY B N 1 ATOM 2660 C CA . GLY B 1 165 ? 14.531 44.062 76.934 1.00 55.76 ? 193 GLY B CA 1 ATOM 2661 C C . GLY B 1 165 ? 13.576 43.166 76.173 1.00 54.92 ? 193 GLY B C 1 ATOM 2662 O O . GLY B 1 165 ? 13.434 43.273 74.957 1.00 53.98 ? 193 GLY B O 1 ATOM 2663 N N . VAL B 1 166 ? 12.927 42.268 76.905 1.00 40.97 ? 194 VAL B N 1 ATOM 2664 C CA . VAL B 1 166 ? 11.876 41.433 76.339 1.00 41.34 ? 194 VAL B CA 1 ATOM 2665 C C . VAL B 1 166 ? 10.644 41.551 77.231 1.00 47.34 ? 194 VAL B C 1 ATOM 2666 O O . VAL B 1 166 ? 10.732 41.863 78.425 1.00 50.76 ? 194 VAL B O 1 ATOM 2667 C CB . VAL B 1 166 ? 12.301 39.935 76.150 1.00 44.83 ? 194 VAL B CB 1 ATOM 2668 C CG1 . VAL B 1 166 ? 13.614 39.844 75.364 1.00 34.93 ? 194 VAL B CG1 1 ATOM 2669 C CG2 . VAL B 1 166 ? 12.417 39.213 77.497 1.00 35.39 ? 194 VAL B CG2 1 ATOM 2670 N N . THR B 1 167 ? 9.487 41.333 76.636 1.00 46.46 ? 195 THR B N 1 ATOM 2671 C CA . THR B 1 167 ? 8.245 41.342 77.379 1.00 51.53 ? 195 THR B CA 1 ATOM 2672 C C . THR B 1 167 ? 8.209 40.153 78.338 1.00 58.38 ? 195 THR B C 1 ATOM 2673 O O . THR B 1 167 ? 8.715 39.082 78.016 1.00 57.32 ? 195 THR B O 1 ATOM 2674 C CB . THR B 1 167 ? 7.054 41.299 76.399 1.00 55.75 ? 195 THR B CB 1 ATOM 2675 O OG1 . THR B 1 167 ? 6.479 42.604 76.286 1.00 57.64 ? 195 THR B OG1 1 ATOM 2676 C CG2 . THR B 1 167 ? 5.986 40.331 76.861 1.00 52.82 ? 195 THR B CG2 1 ATOM 2677 N N . GLU B 1 168 ? 7.657 40.355 79.531 1.00 57.11 ? 196 GLU B N 1 ATOM 2678 C CA . GLU B 1 168 ? 7.529 39.271 80.493 1.00 51.97 ? 196 GLU B CA 1 ATOM 2679 C C . GLU B 1 168 ? 6.748 38.073 79.942 1.00 59.60 ? 196 GLU B C 1 ATOM 2680 O O . GLU B 1 168 ? 7.080 36.922 80.223 1.00 69.85 ? 196 GLU B O 1 ATOM 2681 C CB . GLU B 1 168 ? 6.891 39.771 81.788 1.00 46.78 ? 196 GLU B CB 1 ATOM 2682 C CG . GLU B 1 168 ? 6.649 38.680 82.825 1.00 48.69 ? 196 GLU B CG 1 ATOM 2683 C CD . GLU B 1 168 ? 6.102 39.199 84.145 1.00 59.02 ? 196 GLU B CD 1 ATOM 2684 O OE1 . GLU B 1 168 ? 6.057 40.435 84.353 1.00 62.42 ? 196 GLU B OE1 1 ATOM 2685 O OE2 . GLU B 1 168 ? 5.729 38.357 84.986 1.00 55.29 ? 196 GLU B OE2 1 ATOM 2686 N N . SER B 1 169 ? 5.713 38.342 79.157 1.00 54.69 ? 197 SER B N 1 ATOM 2687 C CA . SER B 1 169 ? 4.915 37.277 78.550 1.00 60.50 ? 197 SER B CA 1 ATOM 2688 C C . SER B 1 169 ? 5.726 36.455 77.533 1.00 51.95 ? 197 SER B C 1 ATOM 2689 O O . SER B 1 169 ? 5.597 35.232 77.460 1.00 53.52 ? 197 SER B O 1 ATOM 2690 C CB . SER B 1 169 ? 3.623 37.850 77.940 1.00 67.11 ? 197 SER B CB 1 ATOM 2691 O OG . SER B 1 169 ? 3.611 37.781 76.531 1.00 77.53 ? 197 SER B OG 1 ATOM 2692 N N . THR B 1 170 ? 6.551 37.140 76.754 1.00 46.68 ? 198 THR B N 1 ATOM 2693 C CA . THR B 1 170 ? 7.504 36.491 75.863 1.00 53.81 ? 198 THR B CA 1 ATOM 2694 C C . THR B 1 170 ? 8.375 35.513 76.649 1.00 54.34 ? 198 THR B C 1 ATOM 2695 O O . THR B 1 170 ? 8.589 34.368 76.231 1.00 53.31 ? 198 THR B O 1 ATOM 2696 C CB . THR B 1 170 ? 8.382 37.521 75.149 1.00 53.48 ? 198 THR B CB 1 ATOM 2697 O OG1 . THR B 1 170 ? 7.586 38.209 74.178 1.00 62.00 ? 198 THR B OG1 1 ATOM 2698 C CG2 . THR B 1 170 ? 9.559 36.836 74.447 1.00 53.77 ? 198 THR B CG2 1 ATOM 2699 N N . LEU B 1 171 ? 8.875 35.977 77.789 1.00 40.28 ? 199 LEU B N 1 ATOM 2700 C CA . LEU B 1 171 ? 9.685 35.139 78.651 1.00 43.94 ? 199 LEU B CA 1 ATOM 2701 C C . LEU B 1 171 ? 8.883 33.971 79.195 1.00 45.95 ? 199 LEU B C 1 ATOM 2702 O O . LEU B 1 171 ? 9.357 32.836 79.220 1.00 51.09 ? 199 LEU B O 1 ATOM 2703 C CB . LEU B 1 171 ? 10.254 35.954 79.798 1.00 43.56 ? 199 LEU B CB 1 ATOM 2704 C CG . LEU B 1 171 ? 11.261 35.249 80.700 1.00 40.65 ? 199 LEU B CG 1 ATOM 2705 C CD1 . LEU B 1 171 ? 12.518 34.871 79.911 1.00 40.17 ? 199 LEU B CD1 1 ATOM 2706 C CD2 . LEU B 1 171 ? 11.586 36.165 81.885 1.00 36.71 ? 199 LEU B CD2 1 ATOM 2707 N N . LEU B 1 172 ? 7.658 34.252 79.622 1.00 45.21 ? 200 LEU B N 1 ATOM 2708 C CA . LEU B 1 172 ? 6.831 33.234 80.252 1.00 45.71 ? 200 LEU B CA 1 ATOM 2709 C C . LEU B 1 172 ? 6.388 32.131 79.289 1.00 44.57 ? 200 LEU B C 1 ATOM 2710 O O . LEU B 1 172 ? 6.366 30.944 79.648 1.00 44.50 ? 200 LEU B O 1 ATOM 2711 C CB . LEU B 1 172 ? 5.624 33.889 80.916 1.00 58.10 ? 200 LEU B CB 1 ATOM 2712 C CG . LEU B 1 172 ? 5.931 34.742 82.150 1.00 56.04 ? 200 LEU B CG 1 ATOM 2713 C CD1 . LEU B 1 172 ? 4.724 35.570 82.525 1.00 56.74 ? 200 LEU B CD1 1 ATOM 2714 C CD2 . LEU B 1 172 ? 6.328 33.857 83.317 1.00 50.43 ? 200 LEU B CD2 1 ATOM 2715 N N . THR B 1 173 ? 6.036 32.519 78.070 1.00 32.51 ? 201 THR B N 1 ATOM 2716 C CA . THR B 1 173 ? 5.605 31.532 77.104 1.00 49.90 ? 201 THR B CA 1 ATOM 2717 C C . THR B 1 173 ? 6.800 30.758 76.551 1.00 46.71 ? 201 THR B C 1 ATOM 2718 O O . THR B 1 173 ? 6.746 29.535 76.447 1.00 39.07 ? 201 THR B O 1 ATOM 2719 C CB . THR B 1 173 ? 4.762 32.150 75.974 1.00 54.99 ? 201 THR B CB 1 ATOM 2720 O OG1 . THR B 1 173 ? 5.546 33.102 75.245 1.00 68.66 ? 201 THR B OG1 1 ATOM 2721 C CG2 . THR B 1 173 ? 3.538 32.841 76.571 1.00 44.89 ? 201 THR B CG2 1 ATOM 2722 N N . ARG B 1 174 ? 7.889 31.458 76.252 1.00 48.41 ? 202 ARG B N 1 ATOM 2723 C CA . ARG B 1 174 ? 9.075 30.795 75.728 1.00 54.43 ? 202 ARG B CA 1 ATOM 2724 C C . ARG B 1 174 ? 9.492 29.674 76.667 1.00 48.19 ? 202 ARG B C 1 ATOM 2725 O O . ARG B 1 174 ? 9.851 28.585 76.222 1.00 39.67 ? 202 ARG B O 1 ATOM 2726 C CB . ARG B 1 174 ? 10.227 31.795 75.556 1.00 55.65 ? 202 ARG B CB 1 ATOM 2727 C CG . ARG B 1 174 ? 11.476 31.179 74.978 1.00 50.51 ? 202 ARG B CG 1 ATOM 2728 C CD . ARG B 1 174 ? 11.226 30.688 73.565 1.00 49.34 ? 202 ARG B CD 1 ATOM 2729 N NE . ARG B 1 174 ? 12.242 29.730 73.139 1.00 56.44 ? 202 ARG B NE 1 ATOM 2730 C CZ . ARG B 1 174 ? 12.232 29.078 71.977 1.00 56.71 ? 202 ARG B CZ 1 ATOM 2731 N NH1 . ARG B 1 174 ? 11.269 29.297 71.092 1.00 54.05 ? 202 ARG B NH1 1 ATOM 2732 N NH2 . ARG B 1 174 ? 13.203 28.216 71.694 1.00 48.42 ? 202 ARG B NH2 1 ATOM 2733 N N . ASN B 1 175 ? 9.362 29.923 77.966 1.00 45.66 ? 203 ASN B N 1 ATOM 2734 C CA . ASN B 1 175 ? 9.774 28.958 78.973 1.00 37.60 ? 203 ASN B CA 1 ATOM 2735 C C . ASN B 1 175 ? 8.650 28.135 79.558 1.00 46.46 ? 203 ASN B C 1 ATOM 2736 O O . ASN B 1 175 ? 8.838 27.432 80.551 1.00 50.08 ? 203 ASN B O 1 ATOM 2737 C CB . ASN B 1 175 ? 10.558 29.665 80.055 1.00 36.01 ? 203 ASN B CB 1 ATOM 2738 C CG . ASN B 1 175 ? 11.902 30.124 79.563 1.00 43.23 ? 203 ASN B CG 1 ATOM 2739 O OD1 . ASN B 1 175 ? 12.854 29.351 79.562 1.00 50.00 ? 203 ASN B OD1 1 ATOM 2740 N ND2 . ASN B 1 175 ? 11.980 31.367 79.082 1.00 35.71 ? 203 ASN B ND2 1 ATOM 2741 N N . LYS B 1 176 ? 7.487 28.206 78.917 1.00 50.28 ? 204 LYS B N 1 ATOM 2742 C CA . LYS B 1 176 ? 6.312 27.457 79.356 1.00 46.39 ? 204 LYS B CA 1 ATOM 2743 C C . LYS B 1 176 ? 6.031 27.600 80.841 1.00 45.86 ? 204 LYS B C 1 ATOM 2744 O O . LYS B 1 176 ? 5.922 26.620 81.565 1.00 53.10 ? 204 LYS B O 1 ATOM 2745 C CB . LYS B 1 176 ? 6.450 25.987 78.988 1.00 45.88 ? 204 LYS B CB 1 ATOM 2746 C CG . LYS B 1 176 ? 5.984 25.684 77.591 1.00 53.56 ? 204 LYS B CG 1 ATOM 2747 C CD . LYS B 1 176 ? 6.917 24.706 76.909 1.00 59.12 ? 204 LYS B CD 1 ATOM 2748 C CE . LYS B 1 176 ? 6.379 24.305 75.541 1.00 67.55 ? 204 LYS B CE 1 ATOM 2749 N NZ . LYS B 1 176 ? 5.097 24.991 75.201 1.00 68.88 ? 204 LYS B NZ 1 ATOM 2750 N N . ILE B 1 177 ? 5.939 28.838 81.292 1.00 54.97 ? 205 ILE B N 1 ATOM 2751 C CA . ILE B 1 177 ? 5.638 29.117 82.682 1.00 56.63 ? 205 ILE B CA 1 ATOM 2752 C C . ILE B 1 177 ? 4.230 29.674 82.753 1.00 51.99 ? 205 ILE B C 1 ATOM 2753 O O . ILE B 1 177 ? 3.966 30.772 82.250 1.00 52.23 ? 205 ILE B O 1 ATOM 2754 C CB . ILE B 1 177 ? 6.633 30.127 83.268 1.00 54.69 ? 205 ILE B CB 1 ATOM 2755 C CG1 . ILE B 1 177 ? 8.043 29.536 83.286 1.00 55.86 ? 205 ILE B CG1 1 ATOM 2756 C CG2 . ILE B 1 177 ? 6.217 30.550 84.666 1.00 55.56 ? 205 ILE B CG2 1 ATOM 2757 C CD1 . ILE B 1 177 ? 9.119 30.587 83.500 1.00 56.10 ? 205 ILE B CD1 1 ATOM 2758 N N . ASP B 1 178 ? 3.322 28.902 83.332 1.00 59.21 ? 206 ASP B N 1 ATOM 2759 C CA . ASP B 1 178 ? 1.936 29.343 83.471 1.00 70.85 ? 206 ASP B CA 1 ATOM 2760 C C . ASP B 1 178 ? 1.835 30.422 84.540 1.00 68.13 ? 206 ASP B C 1 ATOM 2761 O O . ASP B 1 178 ? 1.207 31.458 84.337 1.00 72.03 ? 206 ASP B O 1 ATOM 2762 C CB . ASP B 1 178 ? 1.024 28.171 83.846 1.00 81.94 ? 206 ASP B CB 1 ATOM 2763 C CG . ASP B 1 178 ? 0.895 27.147 82.729 1.00 96.56 ? 206 ASP B CG 1 ATOM 2764 O OD1 . ASP B 1 178 ? 0.907 27.550 81.543 1.00 103.25 ? 206 ASP B OD1 1 ATOM 2765 O OD2 . ASP B 1 178 ? 0.760 25.941 83.035 1.00 98.21 ? 206 ASP B OD2 1 ATOM 2766 N N . ASP B 1 179 ? 2.508 30.183 85.658 1.00 63.56 ? 207 ASP B N 1 ATOM 2767 C CA . ASP B 1 179 ? 2.428 31.039 86.836 1.00 56.95 ? 207 ASP B CA 1 ATOM 2768 C C . ASP B 1 179 ? 3.782 31.616 87.234 1.00 50.47 ? 207 ASP B C 1 ATOM 2769 O O . ASP B 1 179 ? 4.601 30.919 87.819 1.00 51.02 ? 207 ASP B O 1 ATOM 2770 C CB . ASP B 1 179 ? 1.858 30.231 87.997 1.00 59.43 ? 207 ASP B CB 1 ATOM 2771 C CG . ASP B 1 179 ? 1.664 31.059 89.238 1.00 64.57 ? 207 ASP B CG 1 ATOM 2772 O OD1 . ASP B 1 179 ? 1.738 32.307 89.150 1.00 63.57 ? 207 ASP B OD1 1 ATOM 2773 O OD2 . ASP B 1 179 ? 1.439 30.455 90.307 1.00 67.12 ? 207 ASP B OD2 1 ATOM 2774 N N . PRO B 1 180 ? 3.999 32.908 86.953 1.00 49.72 ? 208 PRO B N 1 ATOM 2775 C CA . PRO B 1 180 ? 5.279 33.555 87.249 1.00 50.10 ? 208 PRO B CA 1 ATOM 2776 C C . PRO B 1 180 ? 5.741 33.314 88.678 1.00 57.32 ? 208 PRO B C 1 ATOM 2777 O O . PRO B 1 180 ? 6.921 33.027 88.874 1.00 63.01 ? 208 PRO B O 1 ATOM 2778 C CB . PRO B 1 180 ? 4.974 35.036 87.038 1.00 52.51 ? 208 PRO B CB 1 ATOM 2779 C CG . PRO B 1 180 ? 3.872 35.045 86.020 1.00 54.89 ? 208 PRO B CG 1 ATOM 2780 C CD . PRO B 1 180 ? 3.033 33.835 86.334 1.00 49.33 ? 208 PRO B CD 1 ATOM 2781 N N . THR B 1 181 ? 4.825 33.361 89.642 1.00 58.49 ? 209 THR B N 1 ATOM 2782 C CA . THR B 1 181 ? 5.174 33.228 91.060 1.00 53.48 ? 209 THR B CA 1 ATOM 2783 C C . THR B 1 181 ? 5.814 31.887 91.363 1.00 52.25 ? 209 THR B C 1 ATOM 2784 O O . THR B 1 181 ? 6.324 31.682 92.461 1.00 55.37 ? 209 THR B O 1 ATOM 2785 C CB . THR B 1 181 ? 3.947 33.390 92.015 1.00 55.12 ? 209 THR B CB 1 ATOM 2786 O OG1 . THR B 1 181 ? 3.057 32.277 91.863 1.00 50.71 ? 209 THR B OG1 1 ATOM 2787 C CG2 . THR B 1 181 ? 3.215 34.701 91.768 1.00 49.50 ? 209 THR B CG2 1 ATOM 2788 N N . LYS B 1 182 ? 5.728 30.949 90.423 1.00 54.73 ? 210 LYS B N 1 ATOM 2789 C CA . LYS B 1 182 ? 6.314 29.624 90.629 1.00 57.53 ? 210 LYS B CA 1 ATOM 2790 C C . LYS B 1 182 ? 7.792 29.547 90.228 1.00 50.17 ? 210 LYS B C 1 ATOM 2791 O O . LYS B 1 182 ? 8.402 28.488 90.318 1.00 49.54 ? 210 LYS B O 1 ATOM 2792 C CB . LYS B 1 182 ? 5.524 28.558 89.872 1.00 62.44 ? 210 LYS B CB 1 ATOM 2793 C CG . LYS B 1 182 ? 4.085 28.366 90.324 1.00 66.83 ? 210 LYS B CG 1 ATOM 2794 C CD . LYS B 1 182 ? 4.033 27.806 91.734 1.00 69.28 ? 210 LYS B CD 1 ATOM 2795 C CE . LYS B 1 182 ? 2.649 27.287 92.065 1.00 73.40 ? 210 LYS B CE 1 ATOM 2796 N NZ . LYS B 1 182 ? 2.383 26.021 91.312 1.00 77.24 ? 210 LYS B NZ 1 ATOM 2797 N N . LEU B 1 183 ? 8.364 30.679 89.825 1.00 43.53 ? 211 LEU B N 1 ATOM 2798 C CA . LEU B 1 183 ? 9.768 30.741 89.413 1.00 46.60 ? 211 LEU B CA 1 ATOM 2799 C C . LEU B 1 183 ? 10.669 30.236 90.532 1.00 48.87 ? 211 LEU B C 1 ATOM 2800 O O . LEU B 1 183 ? 10.529 30.625 91.685 1.00 51.24 ? 211 LEU B O 1 ATOM 2801 C CB . LEU B 1 183 ? 10.157 32.169 88.997 1.00 34.72 ? 211 LEU B CB 1 ATOM 2802 C CG . LEU B 1 183 ? 11.446 32.386 88.188 1.00 47.20 ? 211 LEU B CG 1 ATOM 2803 C CD1 . LEU B 1 183 ? 11.381 31.799 86.782 1.00 41.48 ? 211 LEU B CD1 1 ATOM 2804 C CD2 . LEU B 1 183 ? 11.801 33.879 88.136 1.00 50.23 ? 211 LEU B CD2 1 ATOM 2805 N N . GLN B 1 184 ? 11.540 29.293 90.204 1.00 51.57 ? 212 GLN B N 1 ATOM 2806 C CA . GLN B 1 184 ? 12.466 28.786 91.201 1.00 48.03 ? 212 GLN B CA 1 ATOM 2807 C C . GLN B 1 184 ? 13.872 29.349 91.078 1.00 37.91 ? 212 GLN B C 1 ATOM 2808 O O . GLN B 1 184 ? 14.348 29.647 89.985 1.00 46.63 ? 212 GLN B O 1 ATOM 2809 C CB . GLN B 1 184 ? 12.493 27.260 91.173 1.00 48.85 ? 212 GLN B CB 1 ATOM 2810 C CG . GLN B 1 184 ? 11.239 26.648 91.789 1.00 57.31 ? 212 GLN B CG 1 ATOM 2811 C CD . GLN B 1 184 ? 11.237 25.137 91.772 1.00 63.82 ? 212 GLN B CD 1 ATOM 2812 O OE1 . GLN B 1 184 ? 12.255 24.503 91.479 1.00 64.07 ? 212 GLN B OE1 1 ATOM 2813 N NE2 . GLN B 1 184 ? 10.058 24.551 91.982 1.00 63.74 ? 212 GLN B NE2 1 ATOM 2814 N N . MET B 1 185 ? 14.529 29.491 92.219 1.00 38.00 ? 213 MET B N 1 ATOM 2815 C CA . MET B 1 185 ? 15.950 29.780 92.229 1.00 40.97 ? 213 MET B CA 1 ATOM 2816 C C . MET B 1 185 ? 16.662 28.673 91.462 1.00 41.03 ? 213 MET B C 1 ATOM 2817 O O . MET B 1 185 ? 16.435 27.502 91.718 1.00 40.24 ? 213 MET B O 1 ATOM 2818 C CB . MET B 1 185 ? 16.460 29.792 93.657 1.00 42.31 ? 213 MET B CB 1 ATOM 2819 C CG . MET B 1 185 ? 17.918 30.160 93.784 1.00 53.02 ? 213 MET B CG 1 ATOM 2820 S SD . MET B 1 185 ? 18.517 29.814 95.446 1.00 89.89 ? 213 MET B SD 1 ATOM 2821 C CE . MET B 1 185 ? 20.181 29.263 95.089 1.00 72.05 ? 213 MET B CE 1 ATOM 2822 N N . GLY B 1 186 ? 17.537 29.045 90.534 1.00 44.95 ? 214 GLY B N 1 ATOM 2823 C CA . GLY B 1 186 ? 18.326 28.072 89.798 1.00 41.32 ? 214 GLY B CA 1 ATOM 2824 C C . GLY B 1 186 ? 17.655 27.490 88.566 1.00 42.94 ? 214 GLY B C 1 ATOM 2825 O O . GLY B 1 186 ? 18.264 26.743 87.814 1.00 46.67 ? 214 GLY B O 1 ATOM 2826 N N . GLN B 1 187 ? 16.412 27.874 88.332 1.00 33.78 ? 215 GLN B N 1 ATOM 2827 C CA . GLN B 1 187 ? 15.754 27.545 87.090 1.00 36.05 ? 215 GLN B CA 1 ATOM 2828 C C . GLN B 1 187 ? 16.504 28.164 85.909 1.00 41.52 ? 215 GLN B C 1 ATOM 2829 O O . GLN B 1 187 ? 16.940 29.312 85.959 1.00 43.02 ? 215 GLN B O 1 ATOM 2830 C CB . GLN B 1 187 ? 14.311 28.040 87.140 1.00 31.24 ? 215 GLN B CB 1 ATOM 2831 C CG . GLN B 1 187 ? 13.483 27.756 85.901 1.00 34.04 ? 215 GLN B CG 1 ATOM 2832 C CD . GLN B 1 187 ? 11.990 27.880 86.185 1.00 41.31 ? 215 GLN B CD 1 ATOM 2833 O OE1 . GLN B 1 187 ? 11.585 28.004 87.340 1.00 45.41 ? 215 GLN B OE1 1 ATOM 2834 N NE2 . GLN B 1 187 ? 11.174 27.901 85.132 1.00 36.77 ? 215 GLN B NE2 1 ATOM 2835 N N . ILE B 1 188 ? 16.678 27.380 84.855 1.00 42.05 ? 216 ILE B N 1 ATOM 2836 C CA . ILE B 1 188 ? 17.365 27.839 83.660 1.00 36.82 ? 216 ILE B CA 1 ATOM 2837 C C . ILE B 1 188 ? 16.325 28.376 82.685 1.00 36.30 ? 216 ILE B C 1 ATOM 2838 O O . ILE B 1 188 ? 15.420 27.662 82.292 1.00 41.61 ? 216 ILE B O 1 ATOM 2839 C CB . ILE B 1 188 ? 18.173 26.687 83.006 1.00 33.33 ? 216 ILE B CB 1 ATOM 2840 C CG1 . ILE B 1 188 ? 19.100 26.031 84.040 1.00 30.28 ? 216 ILE B CG1 1 ATOM 2841 C CG2 . ILE B 1 188 ? 18.932 27.191 81.816 1.00 25.29 ? 216 ILE B CG2 1 ATOM 2842 C CD1 . ILE B 1 188 ? 20.123 27.016 84.683 1.00 40.93 ? 216 ILE B CD1 1 ATOM 2843 N N . LEU B 1 189 ? 16.437 29.640 82.311 1.00 33.97 ? 217 LEU B N 1 ATOM 2844 C CA . LEU B 1 189 ? 15.486 30.234 81.386 1.00 34.65 ? 217 LEU B CA 1 ATOM 2845 C C . LEU B 1 189 ? 16.099 30.427 80.008 1.00 34.40 ? 217 LEU B C 1 ATOM 2846 O O . LEU B 1 189 ? 17.289 30.730 79.866 1.00 37.75 ? 217 LEU B O 1 ATOM 2847 C CB . LEU B 1 189 ? 15.013 31.606 81.893 1.00 36.20 ? 217 LEU B CB 1 ATOM 2848 C CG . LEU B 1 189 ? 14.230 31.780 83.189 1.00 38.62 ? 217 LEU B CG 1 ATOM 2849 C CD1 . LEU B 1 189 ? 13.886 33.295 83.385 1.00 25.82 ? 217 LEU B CD1 1 ATOM 2850 C CD2 . LEU B 1 189 ? 12.971 30.942 83.131 1.00 33.98 ? 217 LEU B CD2 1 ATOM 2851 N N . ASP B 1 190 ? 15.266 30.288 78.987 1.00 33.65 ? 218 ASP B N 1 ATOM 2852 C CA . ASP B 1 190 ? 15.676 30.592 77.634 1.00 32.62 ? 218 ASP B CA 1 ATOM 2853 C C . ASP B 1 190 ? 15.194 32.010 77.331 1.00 40.81 ? 218 ASP B C 1 ATOM 2854 O O . ASP B 1 190 ? 14.009 32.238 77.078 1.00 47.98 ? 218 ASP B O 1 ATOM 2855 C CB . ASP B 1 190 ? 15.076 29.554 76.684 1.00 29.94 ? 218 ASP B CB 1 ATOM 2856 C CG . ASP B 1 190 ? 15.340 29.850 75.216 1.00 31.80 ? 218 ASP B CG 1 ATOM 2857 O OD1 . ASP B 1 190 ? 15.985 30.878 74.862 1.00 23.59 ? 218 ASP B OD1 1 ATOM 2858 O OD2 . ASP B 1 190 ? 14.848 29.038 74.406 1.00 37.62 ? 218 ASP B OD2 1 ATOM 2859 N N . VAL B 1 191 ? 16.134 32.953 77.373 1.00 42.80 ? 219 VAL B N 1 ATOM 2860 C CA . VAL B 1 191 ? 15.869 34.366 77.130 1.00 36.78 ? 219 VAL B CA 1 ATOM 2861 C C . VAL B 1 191 ? 16.197 34.745 75.713 1.00 36.51 ? 219 VAL B C 1 ATOM 2862 O O . VAL B 1 191 ? 17.361 34.854 75.359 1.00 43.41 ? 219 VAL B O 1 ATOM 2863 C CB . VAL B 1 191 ? 16.730 35.246 78.012 1.00 32.44 ? 219 VAL B CB 1 ATOM 2864 C CG1 . VAL B 1 191 ? 16.346 36.702 77.805 1.00 29.34 ? 219 VAL B CG1 1 ATOM 2865 C CG2 . VAL B 1 191 ? 16.583 34.829 79.467 1.00 32.85 ? 219 VAL B CG2 1 ATOM 2866 N N . PRO B 1 192 ? 15.171 34.980 74.898 1.00 37.79 ? 220 PRO B N 1 ATOM 2867 C CA . PRO B 1 192 ? 15.427 35.250 73.486 1.00 37.37 ? 220 PRO B CA 1 ATOM 2868 C C . PRO B 1 192 ? 15.772 36.704 73.240 1.00 40.74 ? 220 PRO B C 1 ATOM 2869 O O . PRO B 1 192 ? 14.872 37.520 73.120 1.00 41.78 ? 220 PRO B O 1 ATOM 2870 C CB . PRO B 1 192 ? 14.102 34.864 72.808 1.00 40.62 ? 220 PRO B CB 1 ATOM 2871 C CG . PRO B 1 192 ? 13.066 34.830 73.918 1.00 36.32 ? 220 PRO B CG 1 ATOM 2872 C CD . PRO B 1 192 ? 13.739 35.061 75.233 1.00 33.81 ? 220 PRO B CD 1 ATOM 2873 N N . LEU B 1 193 ? 17.062 37.022 73.194 1.00 41.72 ? 221 LEU B N 1 ATOM 2874 C CA . LEU B 1 193 ? 17.509 38.394 72.961 1.00 43.99 ? 221 LEU B CA 1 ATOM 2875 C C . LEU B 1 193 ? 17.190 38.920 71.570 1.00 52.55 ? 221 LEU B C 1 ATOM 2876 O O . LEU B 1 193 ? 17.673 38.390 70.586 1.00 53.68 ? 221 LEU B O 1 ATOM 2877 C CB . LEU B 1 193 ? 19.012 38.549 73.215 1.00 38.14 ? 221 LEU B CB 1 ATOM 2878 C CG . LEU B 1 193 ? 19.522 38.713 74.646 1.00 40.71 ? 221 LEU B CG 1 ATOM 2879 C CD1 . LEU B 1 193 ? 18.813 37.845 75.642 1.00 40.33 ? 221 LEU B CD1 1 ATOM 2880 C CD2 . LEU B 1 193 ? 21.025 38.491 74.690 1.00 32.87 ? 221 LEU B CD2 1 ATOM 2881 N N . PRO B 1 194 ? 16.440 40.030 71.510 1.00 61.61 ? 222 PRO B N 1 ATOM 2882 C CA . PRO B 1 194 ? 15.878 40.723 70.340 1.00 62.77 ? 222 PRO B CA 1 ATOM 2883 C C . PRO B 1 194 ? 16.786 41.042 69.143 1.00 61.20 ? 222 PRO B C 1 ATOM 2884 O O . PRO B 1 194 ? 16.223 41.108 68.045 1.00 77.94 ? 222 PRO B O 1 ATOM 2885 C CB . PRO B 1 194 ? 15.390 42.058 70.921 1.00 54.69 ? 222 PRO B CB 1 ATOM 2886 C CG . PRO B 1 194 ? 15.513 41.974 72.378 1.00 50.44 ? 222 PRO B CG 1 ATOM 2887 C CD . PRO B 1 194 ? 16.001 40.638 72.776 1.00 54.86 ? 222 PRO B CD 1 ATOM 2888 N N . VAL B 1 195 ? 18.090 41.256 69.325 1.00 47.53 ? 223 VAL B N 1 ATOM 2889 C CA . VAL B 1 195 ? 19.008 41.557 68.201 1.00 61.23 ? 223 VAL B CA 1 ATOM 2890 C C . VAL B 1 195 ? 18.813 42.970 67.633 1.00 70.37 ? 223 VAL B C 1 ATOM 2891 O O . VAL B 1 195 ? 17.906 43.222 66.833 1.00 71.31 ? 223 VAL B O 1 ATOM 2892 C CB . VAL B 1 195 ? 18.904 40.522 67.028 1.00 64.30 ? 223 VAL B CB 1 ATOM 2893 C CG1 . VAL B 1 195 ? 19.689 40.991 65.807 1.00 56.36 ? 223 VAL B CG1 1 ATOM 2894 C CG2 . VAL B 1 195 ? 19.369 39.144 67.477 1.00 65.81 ? 223 VAL B CG2 1 ATOM 2895 N N . ALA C 1 1 ? 10.742 77.606 65.354 1.00 74.29 ? 29 ALA C N 1 ATOM 2896 C CA . ALA C 1 1 ? 9.474 77.013 64.929 1.00 70.81 ? 29 ALA C CA 1 ATOM 2897 C C . ALA C 1 1 ? 9.650 75.526 64.578 1.00 65.09 ? 29 ALA C C 1 ATOM 2898 O O . ALA C 1 1 ? 10.464 75.204 63.714 1.00 56.64 ? 29 ALA C O 1 ATOM 2899 C CB . ALA C 1 1 ? 8.913 77.800 63.739 1.00 68.42 ? 29 ALA C CB 1 ATOM 2900 N N . ASN C 1 2 ? 8.931 74.642 65.290 1.00 69.31 ? 30 ASN C N 1 ATOM 2901 C CA . ASN C 1 2 ? 8.883 73.178 65.040 1.00 66.07 ? 30 ASN C CA 1 ATOM 2902 C C . ASN C 1 2 ? 10.238 72.626 64.584 1.00 63.81 ? 30 ASN C C 1 ATOM 2903 O O . ASN C 1 2 ? 11.251 72.858 65.242 1.00 68.13 ? 30 ASN C O 1 ATOM 2904 C CB . ASN C 1 2 ? 7.764 72.789 64.050 1.00 74.98 ? 30 ASN C CB 1 ATOM 2905 C CG . ASN C 1 2 ? 6.686 71.859 64.685 1.00 70.38 ? 30 ASN C CG 1 ATOM 2906 O OD1 . ASN C 1 2 ? 6.928 71.173 65.688 1.00 75.02 ? 30 ASN C OD1 1 ATOM 2907 N ND2 . ASN C 1 2 ? 5.498 71.848 64.090 1.00 48.06 ? 30 ASN C ND2 1 ATOM 2908 N N . PHE C 1 3 ? 10.253 71.889 63.472 1.00 58.14 ? 31 PHE C N 1 ATOM 2909 C CA . PHE C 1 3 ? 11.508 71.614 62.767 1.00 51.37 ? 31 PHE C CA 1 ATOM 2910 C C . PHE C 1 3 ? 11.539 72.421 61.464 1.00 54.39 ? 31 PHE C C 1 ATOM 2911 O O . PHE C 1 3 ? 10.591 72.386 60.686 1.00 52.41 ? 31 PHE C O 1 ATOM 2912 C CB . PHE C 1 3 ? 11.649 70.135 62.393 1.00 43.15 ? 31 PHE C CB 1 ATOM 2913 C CG . PHE C 1 3 ? 11.734 69.209 63.558 1.00 47.21 ? 31 PHE C CG 1 ATOM 2914 C CD1 . PHE C 1 3 ? 11.863 69.694 64.851 1.00 50.25 ? 31 PHE C CD1 1 ATOM 2915 C CD2 . PHE C 1 3 ? 11.683 67.828 63.356 1.00 52.86 ? 31 PHE C CD2 1 ATOM 2916 C CE1 . PHE C 1 3 ? 11.941 68.809 65.931 1.00 59.04 ? 31 PHE C CE1 1 ATOM 2917 C CE2 . PHE C 1 3 ? 11.756 66.939 64.427 1.00 49.66 ? 31 PHE C CE2 1 ATOM 2918 C CZ . PHE C 1 3 ? 11.887 67.428 65.716 1.00 51.60 ? 31 PHE C CZ 1 ATOM 2919 N N . THR C 1 4 ? 12.651 73.089 61.179 1.00 56.62 ? 32 THR C N 1 ATOM 2920 C CA . THR C 1 4 ? 12.749 73.858 59.944 1.00 56.78 ? 32 THR C CA 1 ATOM 2921 C C . THR C 1 4 ? 12.928 72.952 58.712 1.00 54.50 ? 32 THR C C 1 ATOM 2922 O O . THR C 1 4 ? 13.389 71.808 58.811 1.00 45.55 ? 32 THR C O 1 ATOM 2923 C CB . THR C 1 4 ? 13.874 74.913 60.012 1.00 50.42 ? 32 THR C CB 1 ATOM 2924 O OG1 . THR C 1 4 ? 15.135 74.270 60.246 1.00 48.42 ? 32 THR C OG1 1 ATOM 2925 C CG2 . THR C 1 4 ? 13.584 75.945 61.119 1.00 39.95 ? 32 THR C CG2 1 ATOM 2926 N N . CYS C 1 5 ? 12.529 73.477 57.557 1.00 47.15 ? 33 CYS C N 1 ATOM 2927 C CA . CYS C 1 5 ? 12.619 72.753 56.304 1.00 50.19 ? 33 CYS C CA 1 ATOM 2928 C C . CYS C 1 5 ? 12.871 73.717 55.144 1.00 43.19 ? 33 CYS C C 1 ATOM 2929 O O . CYS C 1 5 ? 12.099 74.646 54.934 1.00 50.80 ? 33 CYS C O 1 ATOM 2930 C CB . CYS C 1 5 ? 11.301 72.011 56.083 1.00 55.17 ? 33 CYS C CB 1 ATOM 2931 S SG . CYS C 1 5 ? 11.242 70.945 54.657 1.00 47.68 ? 33 CYS C SG 1 ATOM 2932 N N . ALA C 1 6 ? 13.902 73.465 54.347 1.00 44.85 ? 34 ALA C N 1 ATOM 2933 C CA . ALA C 1 6 ? 14.318 74.466 53.357 1.00 52.05 ? 34 ALA C CA 1 ATOM 2934 C C . ALA C 1 6 ? 14.072 74.056 51.897 1.00 55.85 ? 34 ALA C C 1 ATOM 2935 O O . ALA C 1 6 ? 14.556 74.710 50.967 1.00 48.91 ? 34 ALA C O 1 ATOM 2936 C CB . ALA C 1 6 ? 15.777 74.844 53.568 1.00 38.98 ? 34 ALA C CB 1 ATOM 2937 N N . VAL C 1 7 ? 13.332 72.972 51.691 1.00 49.62 ? 35 VAL C N 1 ATOM 2938 C CA . VAL C 1 7 ? 13.003 72.568 50.331 1.00 40.33 ? 35 VAL C CA 1 ATOM 2939 C C . VAL C 1 7 ? 11.807 73.376 49.844 1.00 43.16 ? 35 VAL C C 1 ATOM 2940 O O . VAL C 1 7 ? 11.274 74.215 50.571 1.00 48.04 ? 35 VAL C O 1 ATOM 2941 C CB . VAL C 1 7 ? 12.703 71.065 50.238 1.00 40.63 ? 35 VAL C CB 1 ATOM 2942 C CG1 . VAL C 1 7 ? 13.895 70.270 50.758 1.00 35.42 ? 35 VAL C CG1 1 ATOM 2943 C CG2 . VAL C 1 7 ? 11.422 70.716 51.016 1.00 36.25 ? 35 VAL C CG2 1 ATOM 2944 N N . ALA C 1 8 ? 11.403 73.145 48.602 1.00 40.54 ? 36 ALA C N 1 ATOM 2945 C CA . ALA C 1 8 ? 10.300 73.896 48.029 1.00 45.38 ? 36 ALA C CA 1 ATOM 2946 C C . ALA C 1 8 ? 9.027 73.647 48.809 1.00 50.22 ? 36 ALA C C 1 ATOM 2947 O O . ALA C 1 8 ? 8.715 72.519 49.172 1.00 55.34 ? 36 ALA C O 1 ATOM 2948 C CB . ALA C 1 8 ? 10.098 73.539 46.554 1.00 44.58 ? 36 ALA C CB 1 ATOM 2949 N N . SER C 1 9 ? 8.307 74.718 49.088 1.00 48.34 ? 37 SER C N 1 ATOM 2950 C CA . SER C 1 9 ? 7.016 74.622 49.737 1.00 49.67 ? 37 SER C CA 1 ATOM 2951 C C . SER C 1 9 ? 6.098 73.668 48.947 1.00 46.96 ? 37 SER C C 1 ATOM 2952 O O . SER C 1 9 ? 6.066 73.698 47.727 1.00 38.51 ? 37 SER C O 1 ATOM 2953 C CB . SER C 1 9 ? 6.399 76.022 49.836 1.00 47.59 ? 37 SER C CB 1 ATOM 2954 O OG . SER C 1 9 ? 5.068 75.987 50.323 1.00 53.48 ? 37 SER C OG 1 ATOM 2955 N N . GLY C 1 10 ? 5.356 72.823 49.649 1.00 44.39 ? 38 GLY C N 1 ATOM 2956 C CA . GLY C 1 10 ? 4.443 71.907 48.997 1.00 36.50 ? 38 GLY C CA 1 ATOM 2957 C C . GLY C 1 10 ? 5.080 70.553 48.787 1.00 36.00 ? 38 GLY C C 1 ATOM 2958 O O . GLY C 1 10 ? 4.421 69.614 48.370 1.00 42.66 ? 38 GLY C O 1 ATOM 2959 N N . THR C 1 11 ? 6.378 70.470 49.047 1.00 37.06 ? 39 THR C N 1 ATOM 2960 C CA . THR C 1 11 ? 7.073 69.199 49.027 1.00 43.60 ? 39 THR C CA 1 ATOM 2961 C C . THR C 1 11 ? 6.590 68.339 50.194 1.00 51.56 ? 39 THR C C 1 ATOM 2962 O O . THR C 1 11 ? 6.414 68.849 51.295 1.00 50.05 ? 39 THR C O 1 ATOM 2963 C CB . THR C 1 11 ? 8.594 69.399 49.131 1.00 45.67 ? 39 THR C CB 1 ATOM 2964 O OG1 . THR C 1 11 ? 9.055 70.176 48.018 1.00 58.10 ? 39 THR C OG1 1 ATOM 2965 C CG2 . THR C 1 11 ? 9.330 68.065 49.166 1.00 29.66 ? 39 THR C CG2 1 ATOM 2966 N N . THR C 1 12 ? 6.340 67.056 49.942 1.00 51.02 ? 40 THR C N 1 ATOM 2967 C CA . THR C 1 12 ? 6.041 66.092 51.007 1.00 43.11 ? 40 THR C CA 1 ATOM 2968 C C . THR C 1 12 ? 7.037 64.948 51.003 1.00 39.21 ? 40 THR C C 1 ATOM 2969 O O . THR C 1 12 ? 7.609 64.621 49.971 1.00 44.27 ? 40 THR C O 1 ATOM 2970 C CB . THR C 1 12 ? 4.629 65.467 50.931 1.00 37.57 ? 40 THR C CB 1 ATOM 2971 O OG1 . THR C 1 12 ? 4.539 64.629 49.780 1.00 44.13 ? 40 THR C OG1 1 ATOM 2972 C CG2 . THR C 1 12 ? 3.518 66.529 50.922 1.00 34.07 ? 40 THR C CG2 1 ATOM 2973 N N . CYS C 1 13 ? 7.289 64.392 52.179 1.00 33.01 ? 41 CYS C N 1 ATOM 2974 C CA . CYS C 1 13 ? 8.121 63.205 52.319 1.00 33.46 ? 41 CYS C CA 1 ATOM 2975 C C . CYS C 1 13 ? 7.677 62.355 53.523 1.00 41.97 ? 41 CYS C C 1 ATOM 2976 O O . CYS C 1 13 ? 6.736 62.715 54.238 1.00 39.47 ? 41 CYS C O 1 ATOM 2977 C CB . CYS C 1 13 ? 9.587 63.590 52.444 1.00 27.74 ? 41 CYS C CB 1 ATOM 2978 S SG . CYS C 1 13 ? 9.921 64.615 53.857 1.00 49.12 ? 41 CYS C SG 1 ATOM 2979 N N . LYS C 1 14 ? 8.341 61.219 53.729 1.00 45.98 ? 42 LYS C N 1 ATOM 2980 C CA . LYS C 1 14 ? 8.069 60.364 54.891 1.00 42.74 ? 42 LYS C CA 1 ATOM 2981 C C . LYS C 1 14 ? 8.916 60.813 56.077 1.00 48.81 ? 42 LYS C C 1 ATOM 2982 O O . LYS C 1 14 ? 10.120 60.979 55.951 1.00 46.54 ? 42 LYS C O 1 ATOM 2983 C CB . LYS C 1 14 ? 8.387 58.898 54.571 1.00 40.64 ? 42 LYS C CB 1 ATOM 2984 C CG . LYS C 1 14 ? 7.855 58.420 53.216 1.00 60.06 ? 42 LYS C CG 1 ATOM 2985 C CD . LYS C 1 14 ? 8.405 57.053 52.809 1.00 64.67 ? 42 LYS C CD 1 ATOM 2986 C CE . LYS C 1 14 ? 8.055 56.735 51.348 1.00 71.22 ? 42 LYS C CE 1 ATOM 2987 N NZ . LYS C 1 14 ? 8.652 55.453 50.857 1.00 73.04 ? 42 LYS C NZ 1 ATOM 2988 N N . SER C 1 15 ? 8.283 61.042 57.217 1.00 56.19 ? 43 SER C N 1 ATOM 2989 C CA . SER C 1 15 ? 9.011 61.299 58.460 1.00 57.35 ? 43 SER C CA 1 ATOM 2990 C C . SER C 1 15 ? 8.366 60.446 59.553 1.00 61.60 ? 43 SER C C 1 ATOM 2991 O O . SER C 1 15 ? 7.416 59.714 59.281 1.00 62.96 ? 43 SER C O 1 ATOM 2992 C CB . SER C 1 15 ? 8.946 62.774 58.839 1.00 55.80 ? 43 SER C CB 1 ATOM 2993 O OG . SER C 1 15 ? 9.682 63.574 57.935 1.00 69.13 ? 43 SER C OG 1 ATOM 2994 N N . ALA C 1 16 ? 8.864 60.548 60.783 1.00 63.28 ? 44 ALA C N 1 ATOM 2995 C CA . ALA C 1 16 ? 8.289 59.795 61.904 1.00 64.57 ? 44 ALA C CA 1 ATOM 2996 C C . ALA C 1 16 ? 8.516 60.484 63.239 1.00 58.16 ? 44 ALA C C 1 ATOM 2997 O O . ALA C 1 16 ? 9.365 61.370 63.357 1.00 53.42 ? 44 ALA C O 1 ATOM 2998 C CB . ALA C 1 16 ? 8.837 58.350 61.948 1.00 59.51 ? 44 ALA C CB 1 ATOM 2999 N N . ILE C 1 17 ? 7.717 60.091 64.229 1.00 56.23 ? 45 ILE C N 1 ATOM 3000 C CA . ILE C 1 17 ? 7.990 60.412 65.627 1.00 54.49 ? 45 ILE C CA 1 ATOM 3001 C C . ILE C 1 17 ? 8.269 59.126 66.394 1.00 57.98 ? 45 ILE C C 1 ATOM 3002 O O . ILE C 1 17 ? 7.728 58.056 66.061 1.00 48.84 ? 45 ILE C O 1 ATOM 3003 C CB . ILE C 1 17 ? 6.808 61.133 66.307 1.00 55.62 ? 45 ILE C CB 1 ATOM 3004 C CG1 . ILE C 1 17 ? 5.560 60.242 66.313 1.00 58.39 ? 45 ILE C CG1 1 ATOM 3005 C CG2 . ILE C 1 17 ? 6.536 62.499 65.650 1.00 52.82 ? 45 ILE C CG2 1 ATOM 3006 C CD1 . ILE C 1 17 ? 4.366 60.861 67.043 1.00 53.81 ? 45 ILE C CD1 1 ATOM 3007 N N . LEU C 1 18 ? 9.128 59.224 67.406 1.00 61.94 ? 46 LEU C N 1 ATOM 3008 C CA . LEU C 1 18 ? 9.303 58.126 68.347 1.00 58.77 ? 46 LEU C CA 1 ATOM 3009 C C . LEU C 1 18 ? 8.300 58.360 69.454 1.00 62.20 ? 46 LEU C C 1 ATOM 3010 O O . LEU C 1 18 ? 8.493 59.213 70.327 1.00 60.34 ? 46 LEU C O 1 ATOM 3011 C CB . LEU C 1 18 ? 10.719 58.066 68.908 1.00 60.35 ? 46 LEU C CB 1 ATOM 3012 C CG . LEU C 1 18 ? 10.970 56.902 69.863 1.00 57.66 ? 46 LEU C CG 1 ATOM 3013 C CD1 . LEU C 1 18 ? 10.795 55.605 69.103 1.00 57.75 ? 46 LEU C CD1 1 ATOM 3014 C CD2 . LEU C 1 18 ? 12.362 56.985 70.482 1.00 47.64 ? 46 LEU C CD2 1 ATOM 3015 N N . TYR C 1 19 ? 7.202 57.617 69.370 1.00 68.56 ? 47 TYR C N 1 ATOM 3016 C CA . TYR C 1 19 ? 6.064 57.823 70.239 1.00 60.84 ? 47 TYR C CA 1 ATOM 3017 C C . TYR C 1 19 ? 6.160 56.911 71.445 1.00 51.96 ? 47 TYR C C 1 ATOM 3018 O O . TYR C 1 19 ? 6.387 55.703 71.319 1.00 44.77 ? 47 TYR C O 1 ATOM 3019 C CB . TYR C 1 19 ? 4.770 57.546 69.495 1.00 58.43 ? 47 TYR C CB 1 ATOM 3020 C CG . TYR C 1 19 ? 3.546 57.924 70.284 1.00 65.12 ? 47 TYR C CG 1 ATOM 3021 C CD1 . TYR C 1 19 ? 3.268 59.259 70.562 1.00 59.19 ? 47 TYR C CD1 1 ATOM 3022 C CD2 . TYR C 1 19 ? 2.668 56.951 70.758 1.00 69.92 ? 47 TYR C CD2 1 ATOM 3023 C CE1 . TYR C 1 19 ? 2.148 59.618 71.279 1.00 65.73 ? 47 TYR C CE1 1 ATOM 3024 C CE2 . TYR C 1 19 ? 1.538 57.302 71.481 1.00 65.26 ? 47 TYR C CE2 1 ATOM 3025 C CZ . TYR C 1 19 ? 1.288 58.634 71.737 1.00 63.63 ? 47 TYR C CZ 1 ATOM 3026 O OH . TYR C 1 19 ? 0.180 58.991 72.452 1.00 65.33 ? 47 TYR C OH 1 ATOM 3027 N N . THR C 1 20 ? 6.000 57.510 72.614 1.00 51.90 ? 48 THR C N 1 ATOM 3028 C CA . THR C 1 20 ? 5.942 56.760 73.856 1.00 58.03 ? 48 THR C CA 1 ATOM 3029 C C . THR C 1 20 ? 4.472 56.639 74.274 1.00 53.71 ? 48 THR C C 1 ATOM 3030 O O . THR C 1 20 ? 3.793 57.641 74.493 1.00 39.18 ? 48 THR C O 1 ATOM 3031 C CB . THR C 1 20 ? 6.784 57.450 74.934 1.00 52.97 ? 48 THR C CB 1 ATOM 3032 O OG1 . THR C 1 20 ? 6.140 58.669 75.320 1.00 62.10 ? 48 THR C OG1 1 ATOM 3033 C CG2 . THR C 1 20 ? 8.187 57.764 74.372 1.00 37.65 ? 48 THR C CG2 1 ATOM 3034 N N . SER C 1 21 ? 3.967 55.412 74.329 1.00 61.05 ? 49 SER C N 1 ATOM 3035 C CA . SER C 1 21 ? 2.555 55.199 74.651 1.00 63.31 ? 49 SER C CA 1 ATOM 3036 C C . SER C 1 21 ? 2.278 55.442 76.134 1.00 58.48 ? 49 SER C C 1 ATOM 3037 O O . SER C 1 21 ? 2.868 54.788 76.999 1.00 59.86 ? 49 SER C O 1 ATOM 3038 C CB . SER C 1 21 ? 2.109 53.792 74.252 1.00 61.23 ? 49 SER C CB 1 ATOM 3039 O OG . SER C 1 21 ? 0.719 53.624 74.473 1.00 68.53 ? 49 SER C OG 1 ATOM 3040 N N . PRO C 1 22 ? 1.391 56.400 76.433 1.00 60.31 ? 50 PRO C N 1 ATOM 3041 C CA . PRO C 1 22 ? 1.068 56.733 77.824 1.00 67.85 ? 50 PRO C CA 1 ATOM 3042 C C . PRO C 1 22 ? 0.497 55.533 78.576 1.00 71.25 ? 50 PRO C C 1 ATOM 3043 O O . PRO C 1 22 ? 0.779 55.353 79.757 1.00 71.93 ? 50 PRO C O 1 ATOM 3044 C CB . PRO C 1 22 ? -0.013 57.815 77.682 1.00 68.10 ? 50 PRO C CB 1 ATOM 3045 C CG . PRO C 1 22 ? 0.153 58.361 76.294 1.00 62.88 ? 50 PRO C CG 1 ATOM 3046 C CD . PRO C 1 22 ? 0.592 57.184 75.477 1.00 61.44 ? 50 PRO C CD 1 ATOM 3047 N N . ASN C 1 23 ? -0.266 54.707 77.866 1.00 76.83 ? 51 ASN C N 1 ATOM 3048 C CA . ASN C 1 23 ? -0.962 53.567 78.444 1.00 75.27 ? 51 ASN C CA 1 ATOM 3049 C C . ASN C 1 23 ? -0.722 52.316 77.610 1.00 70.48 ? 51 ASN C C 1 ATOM 3050 O O . ASN C 1 23 ? -0.096 52.385 76.548 1.00 68.40 ? 51 ASN C O 1 ATOM 3051 C CB . ASN C 1 23 ? -2.462 53.862 78.511 1.00 76.49 ? 51 ASN C CB 1 ATOM 3052 C CG . ASN C 1 23 ? -2.782 55.076 79.384 1.00 89.29 ? 51 ASN C CG 1 ATOM 3053 O OD1 . ASN C 1 23 ? -3.561 55.955 78.999 1.00 92.31 ? 51 ASN C OD1 1 ATOM 3054 N ND2 . ASN C 1 23 ? -2.173 55.129 80.564 1.00 92.81 ? 51 ASN C ND2 1 ATOM 3055 N N . ALA C 1 24 ? -1.201 51.173 78.093 1.00 59.53 ? 52 ALA C N 1 ATOM 3056 C CA . ALA C 1 24 ? -1.206 49.958 77.284 1.00 58.51 ? 52 ALA C CA 1 ATOM 3057 C C . ALA C 1 24 ? -2.243 50.099 76.173 1.00 56.59 ? 52 ALA C C 1 ATOM 3058 O O . ALA C 1 24 ? -3.316 50.661 76.392 1.00 52.10 ? 52 ALA C O 1 ATOM 3059 C CB . ALA C 1 24 ? -1.520 48.734 78.140 1.00 48.68 ? 52 ALA C CB 1 ATOM 3060 N N . THR C 1 25 ? -1.889 49.627 74.979 1.00 56.58 ? 53 THR C N 1 ATOM 3061 C CA . THR C 1 25 ? -2.770 49.645 73.809 1.00 63.59 ? 53 THR C CA 1 ATOM 3062 C C . THR C 1 25 ? -2.366 48.517 72.884 1.00 62.34 ? 53 THR C C 1 ATOM 3063 O O . THR C 1 25 ? -1.731 47.552 73.295 1.00 65.91 ? 53 THR C O 1 ATOM 3064 C CB . THR C 1 25 ? -2.702 50.969 72.989 1.00 51.34 ? 53 THR C CB 1 ATOM 3065 O OG1 . THR C 1 25 ? -1.338 51.397 72.875 1.00 53.27 ? 53 THR C OG1 1 ATOM 3066 C CG2 . THR C 1 25 ? -3.536 52.062 73.632 1.00 48.82 ? 53 THR C CG2 1 ATOM 3067 N N . THR C 1 26 ? -2.734 48.659 71.619 1.00 59.41 ? 54 THR C N 1 ATOM 3068 C CA . THR C 1 26 ? -2.371 47.704 70.591 1.00 50.33 ? 54 THR C CA 1 ATOM 3069 C C . THR C 1 26 ? -1.857 48.464 69.372 1.00 59.17 ? 54 THR C C 1 ATOM 3070 O O . THR C 1 26 ? -1.988 49.696 69.287 1.00 64.10 ? 54 THR C O 1 ATOM 3071 C CB . THR C 1 26 ? -3.578 46.870 70.150 1.00 55.91 ? 54 THR C CB 1 ATOM 3072 O OG1 . THR C 1 26 ? -4.548 47.748 69.577 1.00 57.49 ? 54 THR C OG1 1 ATOM 3073 C CG2 . THR C 1 26 ? -4.224 46.131 71.330 1.00 57.28 ? 54 THR C CG2 1 ATOM 3074 N N . TYR C 1 27 ? -1.245 47.730 68.447 1.00 51.48 ? 55 TYR C N 1 ATOM 3075 C CA . TYR C 1 27 ? -0.789 48.307 67.198 1.00 52.54 ? 55 TYR C CA 1 ATOM 3076 C C . TYR C 1 27 ? -1.964 48.895 66.443 1.00 57.49 ? 55 TYR C C 1 ATOM 3077 O O . TYR C 1 27 ? -1.883 49.998 65.916 1.00 65.20 ? 55 TYR C O 1 ATOM 3078 C CB . TYR C 1 27 ? -0.072 47.260 66.354 1.00 55.66 ? 55 TYR C CB 1 ATOM 3079 C CG . TYR C 1 27 ? 1.266 46.878 66.930 1.00 59.17 ? 55 TYR C CG 1 ATOM 3080 C CD1 . TYR C 1 27 ? 2.327 47.769 66.909 1.00 57.03 ? 55 TYR C CD1 1 ATOM 3081 C CD2 . TYR C 1 27 ? 1.465 45.628 67.512 1.00 56.43 ? 55 TYR C CD2 1 ATOM 3082 C CE1 . TYR C 1 27 ? 3.554 47.424 67.440 1.00 63.12 ? 55 TYR C CE1 1 ATOM 3083 C CE2 . TYR C 1 27 ? 2.688 45.273 68.047 1.00 46.51 ? 55 TYR C CE2 1 ATOM 3084 C CZ . TYR C 1 27 ? 3.728 46.173 68.008 1.00 61.59 ? 55 TYR C CZ 1 ATOM 3085 O OH . TYR C 1 27 ? 4.947 45.827 68.541 1.00 67.50 ? 55 TYR C OH 1 ATOM 3086 N N . GLY C 1 28 ? -3.064 48.151 66.417 1.00 54.37 ? 56 GLY C N 1 ATOM 3087 C CA . GLY C 1 28 ? -4.281 48.592 65.765 1.00 54.88 ? 56 GLY C CA 1 ATOM 3088 C C . GLY C 1 28 ? -4.808 49.900 66.322 1.00 55.81 ? 56 GLY C C 1 ATOM 3089 O O . GLY C 1 28 ? -5.238 50.781 65.576 1.00 57.17 ? 56 GLY C O 1 ATOM 3090 N N . ASN C 1 29 ? -4.779 50.022 67.643 1.00 54.64 ? 57 ASN C N 1 ATOM 3091 C CA . ASN C 1 29 ? -5.207 51.245 68.311 1.00 67.08 ? 57 ASN C CA 1 ATOM 3092 C C . ASN C 1 29 ? -4.324 52.453 67.956 1.00 60.03 ? 57 ASN C C 1 ATOM 3093 O O . ASN C 1 29 ? -4.820 53.578 67.826 1.00 54.54 ? 57 ASN C O 1 ATOM 3094 C CB . ASN C 1 29 ? -5.235 51.032 69.829 1.00 81.29 ? 57 ASN C CB 1 ATOM 3095 C CG . ASN C 1 29 ? -5.476 52.317 70.599 1.00 95.33 ? 57 ASN C CG 1 ATOM 3096 O OD1 . ASN C 1 29 ? -4.545 53.085 70.862 1.00 101.06 ? 57 ASN C OD1 1 ATOM 3097 N ND2 . ASN C 1 29 ? -6.730 52.555 70.976 1.00 99.84 ? 57 ASN C ND2 1 ATOM 3098 N N . LEU C 1 30 ? -3.019 52.216 67.835 1.00 51.29 ? 58 LEU C N 1 ATOM 3099 C CA . LEU C 1 30 ? -2.071 53.253 67.442 1.00 45.56 ? 58 LEU C CA 1 ATOM 3100 C C . LEU C 1 30 ? -2.325 53.718 66.020 1.00 46.46 ? 58 LEU C C 1 ATOM 3101 O O . LEU C 1 30 ? -2.315 54.907 65.746 1.00 53.75 ? 58 LEU C O 1 ATOM 3102 C CB . LEU C 1 30 ? -0.631 52.751 67.583 1.00 56.62 ? 58 LEU C CB 1 ATOM 3103 C CG . LEU C 1 30 ? -0.079 52.728 69.008 1.00 57.40 ? 58 LEU C CG 1 ATOM 3104 C CD1 . LEU C 1 30 ? 1.314 52.148 69.014 1.00 56.54 ? 58 LEU C CD1 1 ATOM 3105 C CD2 . LEU C 1 30 ? -0.061 54.150 69.572 1.00 52.85 ? 58 LEU C CD2 1 ATOM 3106 N N . VAL C 1 31 ? -2.551 52.766 65.122 1.00 50.23 ? 59 VAL C N 1 ATOM 3107 C CA . VAL C 1 31 ? -2.930 53.071 63.750 1.00 58.14 ? 59 VAL C CA 1 ATOM 3108 C C . VAL C 1 31 ? -4.158 53.998 63.724 1.00 59.81 ? 59 VAL C C 1 ATOM 3109 O O . VAL C 1 31 ? -4.219 54.938 62.929 1.00 69.18 ? 59 VAL C O 1 ATOM 3110 C CB . VAL C 1 31 ? -3.217 51.775 62.941 1.00 50.27 ? 59 VAL C CB 1 ATOM 3111 C CG1 . VAL C 1 31 ? -3.801 52.106 61.565 1.00 42.37 ? 59 VAL C CG1 1 ATOM 3112 C CG2 . VAL C 1 31 ? -1.951 50.936 62.795 1.00 54.85 ? 59 VAL C CG2 1 ATOM 3113 N N . ALA C 1 32 ? -5.127 53.736 64.597 1.00 53.14 ? 60 ALA C N 1 ATOM 3114 C CA . ALA C 1 32 ? -6.357 54.543 64.670 1.00 60.35 ? 60 ALA C CA 1 ATOM 3115 C C . ALA C 1 32 ? -6.189 55.955 65.245 1.00 54.41 ? 60 ALA C C 1 ATOM 3116 O O . ALA C 1 32 ? -6.799 56.902 64.752 1.00 57.04 ? 60 ALA C O 1 ATOM 3117 C CB . ALA C 1 32 ? -7.460 53.792 65.428 1.00 56.65 ? 60 ALA C CB 1 ATOM 3118 N N . ARG C 1 33 ? -5.426 56.085 66.323 1.00 53.00 ? 61 ARG C N 1 ATOM 3119 C CA . ARG C 1 33 ? -5.231 57.380 66.966 1.00 65.94 ? 61 ARG C CA 1 ATOM 3120 C C . ARG C 1 33 ? -4.482 58.354 66.035 1.00 66.21 ? 61 ARG C C 1 ATOM 3121 O O . ARG C 1 33 ? -4.724 59.567 66.044 1.00 66.96 ? 61 ARG C O 1 ATOM 3122 C CB . ARG C 1 33 ? -4.467 57.213 68.284 1.00 77.70 ? 61 ARG C CB 1 ATOM 3123 C CG . ARG C 1 33 ? -4.098 58.522 68.967 1.00 85.94 ? 61 ARG C CG 1 ATOM 3124 C CD . ARG C 1 33 ? -3.316 58.275 70.241 1.00 95.00 ? 61 ARG C CD 1 ATOM 3125 N NE . ARG C 1 33 ? -3.745 57.056 70.920 1.00 106.43 ? 61 ARG C NE 1 ATOM 3126 C CZ . ARG C 1 33 ? -3.064 56.475 71.903 1.00 112.21 ? 61 ARG C CZ 1 ATOM 3127 N NH1 . ARG C 1 33 ? -1.934 57.021 72.338 1.00 112.27 ? 61 ARG C NH1 1 ATOM 3128 N NH2 . ARG C 1 33 ? -3.517 55.358 72.461 1.00 110.46 ? 61 ARG C NH2 1 ATOM 3129 N N . PHE C 1 34 ? -3.550 57.817 65.255 1.00 57.51 ? 62 PHE C N 1 ATOM 3130 C CA . PHE C 1 34 ? -2.748 58.645 64.353 1.00 59.25 ? 62 PHE C CA 1 ATOM 3131 C C . PHE C 1 34 ? -3.306 58.782 62.931 1.00 59.10 ? 62 PHE C C 1 ATOM 3132 O O . PHE C 1 34 ? -3.379 59.889 62.402 1.00 61.92 ? 62 PHE C O 1 ATOM 3133 C CB . PHE C 1 34 ? -1.280 58.206 64.369 1.00 55.28 ? 62 PHE C CB 1 ATOM 3134 C CG . PHE C 1 34 ? -0.525 58.741 65.545 1.00 66.56 ? 62 PHE C CG 1 ATOM 3135 C CD1 . PHE C 1 34 ? -0.466 58.033 66.734 1.00 72.78 ? 62 PHE C CD1 1 ATOM 3136 C CD2 . PHE C 1 34 ? 0.084 59.986 65.481 1.00 62.24 ? 62 PHE C CD2 1 ATOM 3137 C CE1 . PHE C 1 34 ? 0.212 58.549 67.828 1.00 73.48 ? 62 PHE C CE1 1 ATOM 3138 C CE2 . PHE C 1 34 ? 0.759 60.501 66.569 1.00 59.13 ? 62 PHE C CE2 1 ATOM 3139 C CZ . PHE C 1 34 ? 0.826 59.784 67.739 1.00 67.48 ? 62 PHE C CZ 1 ATOM 3140 N N . ASN C 1 35 ? -3.712 57.665 62.334 1.00 56.26 ? 63 ASN C N 1 ATOM 3141 C CA . ASN C 1 35 ? -4.322 57.664 61.005 1.00 56.29 ? 63 ASN C CA 1 ATOM 3142 C C . ASN C 1 35 ? -3.427 58.304 59.941 1.00 57.94 ? 63 ASN C C 1 ATOM 3143 O O . ASN C 1 35 ? -3.904 58.939 58.995 1.00 57.86 ? 63 ASN C O 1 ATOM 3144 C CB . ASN C 1 35 ? -5.701 58.343 61.047 1.00 53.10 ? 63 ASN C CB 1 ATOM 3145 C CG . ASN C 1 35 ? -6.574 57.963 59.870 1.00 57.91 ? 63 ASN C CG 1 ATOM 3146 O OD1 . ASN C 1 35 ? -6.435 56.879 59.314 1.00 60.70 ? 63 ASN C OD1 1 ATOM 3147 N ND2 . ASN C 1 35 ? -7.488 58.850 59.492 1.00 62.11 ? 63 ASN C ND2 1 ATOM 3148 N N . THR C 1 36 ? -2.125 58.107 60.108 1.00 52.51 ? 64 THR C N 1 ATOM 3149 C CA . THR C 1 36 ? -1.129 58.675 59.219 1.00 50.64 ? 64 THR C CA 1 ATOM 3150 C C . THR C 1 36 ? -0.457 57.551 58.448 1.00 52.96 ? 64 THR C C 1 ATOM 3151 O O . THR C 1 36 ? 0.303 57.791 57.518 1.00 54.57 ? 64 THR C O 1 ATOM 3152 C CB . THR C 1 36 ? -0.038 59.427 60.013 1.00 50.03 ? 64 THR C CB 1 ATOM 3153 O OG1 . THR C 1 36 ? 0.583 58.539 60.953 1.00 58.00 ? 64 THR C OG1 1 ATOM 3154 C CG2 . THR C 1 36 ? -0.625 60.621 60.771 1.00 40.40 ? 64 THR C CG2 1 ATOM 3155 N N . THR C 1 37 ? -0.755 56.314 58.827 1.00 53.85 ? 65 THR C N 1 ATOM 3156 C CA . THR C 1 37 ? -0.060 55.170 58.262 1.00 51.77 ? 65 THR C CA 1 ATOM 3157 C C . THR C 1 37 ? -0.899 53.903 58.366 1.00 63.09 ? 65 THR C C 1 ATOM 3158 O O . THR C 1 37 ? -1.791 53.803 59.211 1.00 69.53 ? 65 THR C O 1 ATOM 3159 C CB . THR C 1 37 ? 1.266 54.918 59.007 1.00 53.30 ? 65 THR C CB 1 ATOM 3160 O OG1 . THR C 1 37 ? 1.916 53.766 58.455 1.00 67.49 ? 65 THR C OG1 1 ATOM 3161 C CG2 . THR C 1 37 ? 1.012 54.673 60.480 1.00 48.32 ? 65 THR C CG2 1 ATOM 3162 N N . THR C 1 38 ? -0.596 52.923 57.520 1.00 54.98 ? 66 THR C N 1 ATOM 3163 C CA . THR C 1 38 ? -1.284 51.653 57.589 1.00 45.00 ? 66 THR C CA 1 ATOM 3164 C C . THR C 1 38 ? -0.515 50.779 58.563 1.00 55.42 ? 66 THR C C 1 ATOM 3165 O O . THR C 1 38 ? 0.646 51.061 58.873 1.00 59.88 ? 66 THR C O 1 ATOM 3166 C CB . THR C 1 38 ? -1.347 50.930 56.218 1.00 50.70 ? 66 THR C CB 1 ATOM 3167 O OG1 . THR C 1 38 ? -0.037 50.482 55.835 1.00 59.29 ? 66 THR C OG1 1 ATOM 3168 C CG2 . THR C 1 38 ? -1.918 51.837 55.149 1.00 45.60 ? 66 THR C CG2 1 ATOM 3169 N N . LEU C 1 39 ? -1.156 49.714 59.030 1.00 56.03 ? 67 LEU C N 1 ATOM 3170 C CA . LEU C 1 39 ? -0.505 48.760 59.918 1.00 54.71 ? 67 LEU C CA 1 ATOM 3171 C C . LEU C 1 39 ? 0.778 48.148 59.341 1.00 58.79 ? 67 LEU C C 1 ATOM 3172 O O . LEU C 1 39 ? 1.820 48.189 60.008 1.00 58.53 ? 67 LEU C O 1 ATOM 3173 C CB . LEU C 1 39 ? -1.498 47.683 60.394 1.00 53.50 ? 67 LEU C CB 1 ATOM 3174 C CG . LEU C 1 39 ? -0.970 46.516 61.234 1.00 54.93 ? 67 LEU C CG 1 ATOM 3175 C CD1 . LEU C 1 39 ? -0.409 47.004 62.557 1.00 48.26 ? 67 LEU C CD1 1 ATOM 3176 C CD2 . LEU C 1 39 ? -2.102 45.550 61.489 1.00 53.87 ? 67 LEU C CD2 1 ATOM 3177 N N . PRO C 1 40 ? 0.731 47.615 58.098 1.00 60.95 ? 68 PRO C N 1 ATOM 3178 C CA . PRO C 1 40 ? 1.980 47.003 57.611 1.00 55.82 ? 68 PRO C CA 1 ATOM 3179 C C . PRO C 1 40 ? 3.120 48.006 57.530 1.00 58.26 ? 68 PRO C C 1 ATOM 3180 O O . PRO C 1 40 ? 4.283 47.614 57.707 1.00 57.38 ? 68 PRO C O 1 ATOM 3181 C CB . PRO C 1 40 ? 1.630 46.475 56.213 1.00 54.24 ? 68 PRO C CB 1 ATOM 3182 C CG . PRO C 1 40 ? 0.194 46.776 55.976 1.00 49.51 ? 68 PRO C CG 1 ATOM 3183 C CD . PRO C 1 40 ? -0.415 47.386 57.193 1.00 55.46 ? 68 PRO C CD 1 ATOM 3184 N N . ASP C 1 41 ? 2.795 49.276 57.281 1.00 55.68 ? 69 ASP C N 1 ATOM 3185 C CA . ASP C 1 41 ? 3.814 50.326 57.260 1.00 50.84 ? 69 ASP C CA 1 ATOM 3186 C C . ASP C 1 41 ? 4.321 50.631 58.665 1.00 50.48 ? 69 ASP C C 1 ATOM 3187 O O . ASP C 1 41 ? 5.527 50.832 58.866 1.00 47.28 ? 69 ASP C O 1 ATOM 3188 C CB . ASP C 1 41 ? 3.294 51.591 56.568 1.00 52.83 ? 69 ASP C CB 1 ATOM 3189 C CG . ASP C 1 41 ? 3.089 51.393 55.067 1.00 59.29 ? 69 ASP C CG 1 ATOM 3190 O OD1 . ASP C 1 41 ? 3.648 50.424 54.505 1.00 53.59 ? 69 ASP C OD1 1 ATOM 3191 O OD2 . ASP C 1 41 ? 2.345 52.191 54.453 1.00 65.66 ? 69 ASP C OD2 1 ATOM 3192 N N . LEU C 1 42 ? 3.410 50.649 59.637 1.00 47.78 ? 70 LEU C N 1 ATOM 3193 C CA . LEU C 1 42 ? 3.803 50.793 61.046 1.00 55.70 ? 70 LEU C CA 1 ATOM 3194 C C . LEU C 1 42 ? 4.688 49.619 61.484 1.00 48.94 ? 70 LEU C C 1 ATOM 3195 O O . LEU C 1 42 ? 5.742 49.800 62.103 1.00 45.41 ? 70 LEU C O 1 ATOM 3196 C CB . LEU C 1 42 ? 2.572 50.887 61.951 1.00 58.76 ? 70 LEU C CB 1 ATOM 3197 C CG . LEU C 1 42 ? 2.824 51.055 63.456 1.00 57.42 ? 70 LEU C CG 1 ATOM 3198 C CD1 . LEU C 1 42 ? 3.732 52.222 63.719 1.00 55.09 ? 70 LEU C CD1 1 ATOM 3199 C CD2 . LEU C 1 42 ? 1.512 51.231 64.212 1.00 55.13 ? 70 LEU C CD2 1 ATOM 3200 N N . LEU C 1 43 ? 4.249 48.414 61.146 1.00 47.45 ? 71 LEU C N 1 ATOM 3201 C CA . LEU C 1 43 ? 5.017 47.218 61.460 1.00 62.77 ? 71 LEU C CA 1 ATOM 3202 C C . LEU C 1 43 ? 6.386 47.250 60.762 1.00 64.16 ? 71 LEU C C 1 ATOM 3203 O O . LEU C 1 43 ? 7.412 46.987 61.378 1.00 60.36 ? 71 LEU C O 1 ATOM 3204 C CB . LEU C 1 43 ? 4.230 45.963 61.049 1.00 67.97 ? 71 LEU C CB 1 ATOM 3205 C CG . LEU C 1 43 ? 2.855 45.741 61.696 1.00 60.62 ? 71 LEU C CG 1 ATOM 3206 C CD1 . LEU C 1 43 ? 2.102 44.564 61.049 1.00 48.25 ? 71 LEU C CD1 1 ATOM 3207 C CD2 . LEU C 1 43 ? 2.986 45.552 63.205 1.00 62.78 ? 71 LEU C CD2 1 ATOM 3208 N N . GLY C 1 44 ? 6.396 47.606 59.482 1.00 63.33 ? 72 GLY C N 1 ATOM 3209 C CA . GLY C 1 44 ? 7.635 47.664 58.728 1.00 63.71 ? 72 GLY C CA 1 ATOM 3210 C C . GLY C 1 44 ? 8.585 48.713 59.261 1.00 67.45 ? 72 GLY C C 1 ATOM 3211 O O . GLY C 1 44 ? 9.785 48.479 59.371 1.00 69.72 ? 72 GLY C O 1 ATOM 3212 N N . ALA C 1 45 ? 8.039 49.879 59.590 1.00 70.55 ? 73 ALA C N 1 ATOM 3213 C CA . ALA C 1 45 ? 8.826 50.974 60.144 1.00 64.58 ? 73 ALA C CA 1 ATOM 3214 C C . ALA C 1 45 ? 9.479 50.618 61.474 1.00 65.79 ? 73 ALA C C 1 ATOM 3215 O O . ALA C 1 45 ? 10.500 51.191 61.828 1.00 64.77 ? 73 ALA C O 1 ATOM 3216 C CB . ALA C 1 45 ? 7.962 52.221 60.303 1.00 62.01 ? 73 ALA C CB 1 ATOM 3217 N N . ASN C 1 46 ? 8.900 49.674 62.211 1.00 67.82 ? 74 ASN C N 1 ATOM 3218 C CA . ASN C 1 46 ? 9.473 49.290 63.499 1.00 65.47 ? 74 ASN C CA 1 ATOM 3219 C C . ASN C 1 46 ? 10.189 47.947 63.477 1.00 72.37 ? 74 ASN C C 1 ATOM 3220 O O . ASN C 1 46 ? 10.448 47.368 64.532 1.00 82.56 ? 74 ASN C O 1 ATOM 3221 C CB . ASN C 1 46 ? 8.409 49.299 64.603 1.00 52.74 ? 74 ASN C CB 1 ATOM 3222 C CG . ASN C 1 46 ? 7.948 50.699 64.950 1.00 52.42 ? 74 ASN C CG 1 ATOM 3223 O OD1 . ASN C 1 46 ? 8.479 51.328 65.862 1.00 59.61 ? 74 ASN C OD1 1 ATOM 3224 N ND2 . ASN C 1 46 ? 6.959 51.200 64.219 1.00 48.73 ? 74 ASN C ND2 1 ATOM 3225 N N . GLY C 1 47 ? 10.525 47.465 62.282 1.00 69.25 ? 75 GLY C N 1 ATOM 3226 C CA . GLY C 1 47 ? 11.268 46.222 62.133 1.00 68.48 ? 75 GLY C CA 1 ATOM 3227 C C . GLY C 1 47 ? 10.548 45.016 62.720 1.00 70.55 ? 75 GLY C C 1 ATOM 3228 O O . GLY C 1 47 ? 11.166 44.104 63.262 1.00 77.26 ? 75 GLY C O 1 ATOM 3229 N N . LEU C 1 48 ? 9.228 45.018 62.607 1.00 70.71 ? 76 LEU C N 1 ATOM 3230 C CA . LEU C 1 48 ? 8.394 43.954 63.146 1.00 69.04 ? 76 LEU C CA 1 ATOM 3231 C C . LEU C 1 48 ? 7.901 43.039 62.014 1.00 68.75 ? 76 LEU C C 1 ATOM 3232 O O . LEU C 1 48 ? 7.786 43.472 60.855 1.00 61.92 ? 76 LEU C O 1 ATOM 3233 C CB . LEU C 1 48 ? 7.210 44.558 63.916 1.00 67.35 ? 76 LEU C CB 1 ATOM 3234 C CG . LEU C 1 48 ? 7.537 45.477 65.103 1.00 61.64 ? 76 LEU C CG 1 ATOM 3235 C CD1 . LEU C 1 48 ? 6.311 46.274 65.519 1.00 55.67 ? 76 LEU C CD1 1 ATOM 3236 C CD2 . LEU C 1 48 ? 8.097 44.710 66.293 1.00 58.68 ? 76 LEU C CD2 1 ATOM 3237 N N . PRO C 1 49 ? 7.641 41.761 62.335 1.00 73.31 ? 77 PRO C N 1 ATOM 3238 C CA . PRO C 1 49 ? 7.193 40.792 61.321 1.00 73.41 ? 77 PRO C CA 1 ATOM 3239 C C . PRO C 1 49 ? 5.870 41.166 60.654 1.00 77.28 ? 77 PRO C C 1 ATOM 3240 O O . PRO C 1 49 ? 5.022 41.840 61.243 1.00 70.44 ? 77 PRO C O 1 ATOM 3241 C CB . PRO C 1 49 ? 7.038 39.473 62.100 1.00 65.86 ? 77 PRO C CB 1 ATOM 3242 C CG . PRO C 1 49 ? 7.626 39.694 63.435 1.00 68.85 ? 77 PRO C CG 1 ATOM 3243 C CD . PRO C 1 49 ? 7.878 41.151 63.656 1.00 72.56 ? 77 PRO C CD 1 ATOM 3244 N N . ASP C 1 50 ? 5.722 40.714 59.412 1.00 81.70 ? 78 ASP C N 1 ATOM 3245 C CA . ASP C 1 50 ? 4.544 40.988 58.600 1.00 86.07 ? 78 ASP C CA 1 ATOM 3246 C C . ASP C 1 50 ? 3.259 40.525 59.292 1.00 80.36 ? 78 ASP C C 1 ATOM 3247 O O . ASP C 1 50 ? 2.208 41.160 59.178 1.00 78.63 ? 78 ASP C O 1 ATOM 3248 C CB . ASP C 1 50 ? 4.651 40.261 57.248 1.00 94.30 ? 78 ASP C CB 1 ATOM 3249 C CG . ASP C 1 50 ? 5.961 40.535 56.526 1.00 105.25 ? 78 ASP C CG 1 ATOM 3250 O OD1 . ASP C 1 50 ? 5.921 41.084 55.405 1.00 109.84 ? 78 ASP C OD1 1 ATOM 3251 O OD2 . ASP C 1 50 ? 7.034 40.252 57.101 1.00 111.48 ? 78 ASP C OD2 1 ATOM 3252 N N . GLY C 1 51 ? 3.355 39.394 59.986 1.00 72.03 ? 79 GLY C N 1 ATOM 3253 C CA . GLY C 1 51 ? 2.200 38.756 60.582 1.00 64.43 ? 79 GLY C CA 1 ATOM 3254 C C . GLY C 1 51 ? 1.738 39.250 61.939 1.00 62.16 ? 79 GLY C C 1 ATOM 3255 O O . GLY C 1 51 ? 0.794 38.687 62.493 1.00 65.87 ? 79 GLY C O 1 ATOM 3256 N N . THR C 1 52 ? 2.362 40.299 62.473 1.00 53.86 ? 80 THR C N 1 ATOM 3257 C CA . THR C 1 52 ? 1.959 40.810 63.782 1.00 47.74 ? 80 THR C CA 1 ATOM 3258 C C . THR C 1 52 ? 0.515 41.281 63.716 1.00 53.31 ? 80 THR C C 1 ATOM 3259 O O . THR C 1 52 ? 0.147 42.040 62.817 1.00 52.80 ? 80 THR C O 1 ATOM 3260 C CB . THR C 1 52 ? 2.833 41.973 64.235 1.00 49.83 ? 80 THR C CB 1 ATOM 3261 O OG1 . THR C 1 52 ? 4.206 41.567 64.234 1.00 57.65 ? 80 THR C OG1 1 ATOM 3262 C CG2 . THR C 1 52 ? 2.441 42.433 65.640 1.00 48.70 ? 80 THR C CG2 1 ATOM 3263 N N . LEU C 1 53 ? -0.305 40.818 64.657 1.00 50.73 ? 81 LEU C N 1 ATOM 3264 C CA . LEU C 1 53 ? -1.730 41.143 64.617 1.00 58.59 ? 81 LEU C CA 1 ATOM 3265 C C . LEU C 1 53 ? -1.943 42.592 65.028 1.00 52.05 ? 81 LEU C C 1 ATOM 3266 O O . LEU C 1 53 ? -1.152 43.150 65.782 1.00 50.57 ? 81 LEU C O 1 ATOM 3267 C CB . LEU C 1 53 ? -2.543 40.228 65.545 1.00 51.60 ? 81 LEU C CB 1 ATOM 3268 C CG . LEU C 1 53 ? -2.490 38.700 65.382 1.00 49.96 ? 81 LEU C CG 1 ATOM 3269 C CD1 . LEU C 1 53 ? -3.358 38.027 66.445 1.00 53.13 ? 81 LEU C CD1 1 ATOM 3270 C CD2 . LEU C 1 53 ? -2.896 38.245 63.984 1.00 45.63 ? 81 LEU C CD2 1 ATOM 3271 N N . SER C 1 54 ? -3.010 43.200 64.530 1.00 49.07 ? 82 SER C N 1 ATOM 3272 C CA . SER C 1 54 ? -3.316 44.562 64.921 1.00 52.73 ? 82 SER C CA 1 ATOM 3273 C C . SER C 1 54 ? -3.703 44.571 66.395 1.00 52.33 ? 82 SER C C 1 ATOM 3274 O O . SER C 1 54 ? -3.603 45.597 67.064 1.00 52.24 ? 82 SER C O 1 ATOM 3275 C CB . SER C 1 54 ? -4.439 45.149 64.057 1.00 55.98 ? 82 SER C CB 1 ATOM 3276 O OG . SER C 1 54 ? -5.721 44.815 64.549 1.00 64.53 ? 82 SER C OG 1 ATOM 3277 N N . SER C 1 55 ? -4.094 43.403 66.904 1.00 53.26 ? 83 SER C N 1 ATOM 3278 C CA . SER C 1 55 ? -4.506 43.260 68.303 1.00 53.58 ? 83 SER C CA 1 ATOM 3279 C C . SER C 1 55 ? -3.335 42.915 69.237 1.00 61.00 ? 83 SER C C 1 ATOM 3280 O O . SER C 1 55 ? -3.531 42.759 70.438 1.00 70.18 ? 83 SER C O 1 ATOM 3281 C CB . SER C 1 55 ? -5.594 42.194 68.427 1.00 51.04 ? 83 SER C CB 1 ATOM 3282 O OG . SER C 1 55 ? -5.104 40.910 68.063 1.00 59.10 ? 83 SER C OG 1 ATOM 3283 N N . ALA C 1 56 ? -2.133 42.767 68.681 1.00 53.63 ? 84 ALA C N 1 ATOM 3284 C CA . ALA C 1 56 ? -0.935 42.551 69.487 1.00 55.18 ? 84 ALA C CA 1 ATOM 3285 C C . ALA C 1 56 ? -0.690 43.751 70.415 1.00 65.28 ? 84 ALA C C 1 ATOM 3286 O O . ALA C 1 56 ? -0.864 44.897 70.003 1.00 65.54 ? 84 ALA C O 1 ATOM 3287 C CB . ALA C 1 56 ? 0.282 42.298 68.595 1.00 46.01 ? 84 ALA C CB 1 ATOM 3288 N N . PRO C 1 57 ? -0.310 43.486 71.681 1.00 64.64 ? 85 PRO C N 1 ATOM 3289 C CA . PRO C 1 57 ? -0.190 44.512 72.735 1.00 59.73 ? 85 PRO C CA 1 ATOM 3290 C C . PRO C 1 57 ? 1.058 45.402 72.647 1.00 58.87 ? 85 PRO C C 1 ATOM 3291 O O . PRO C 1 57 ? 2.115 44.944 72.204 1.00 66.65 ? 85 PRO C O 1 ATOM 3292 C CB . PRO C 1 57 ? -0.131 43.670 74.017 1.00 59.96 ? 85 PRO C CB 1 ATOM 3293 C CG . PRO C 1 57 ? 0.497 42.387 73.586 1.00 59.30 ? 85 PRO C CG 1 ATOM 3294 C CD . PRO C 1 57 ? -0.026 42.130 72.194 1.00 55.34 ? 85 PRO C CD 1 ATOM 3295 N N . VAL C 1 58 ? 0.920 46.674 73.019 1.00 54.25 ? 86 VAL C N 1 ATOM 3296 C CA . VAL C 1 58 ? 2.082 47.537 73.259 1.00 59.69 ? 86 VAL C CA 1 ATOM 3297 C C . VAL C 1 58 ? 2.045 48.029 74.696 1.00 54.49 ? 86 VAL C C 1 ATOM 3298 O O . VAL C 1 58 ? 1.025 48.585 75.139 1.00 45.98 ? 86 VAL C O 1 ATOM 3299 C CB . VAL C 1 58 ? 2.153 48.768 72.313 1.00 45.30 ? 86 VAL C CB 1 ATOM 3300 C CG1 . VAL C 1 58 ? 2.860 48.399 71.032 1.00 48.99 ? 86 VAL C CG1 1 ATOM 3301 C CG2 . VAL C 1 58 ? 0.779 49.286 72.019 1.00 56.29 ? 86 VAL C CG2 1 ATOM 3302 N N . ALA C 1 59 ? 3.150 47.822 75.415 1.00 54.96 ? 87 ALA C N 1 ATOM 3303 C CA . ALA C 1 59 ? 3.221 48.156 76.840 1.00 55.48 ? 87 ALA C CA 1 ATOM 3304 C C . ALA C 1 59 ? 3.284 49.660 77.065 1.00 59.36 ? 87 ALA C C 1 ATOM 3305 O O . ALA C 1 59 ? 3.849 50.386 76.250 1.00 65.02 ? 87 ALA C O 1 ATOM 3306 C CB . ALA C 1 59 ? 4.427 47.475 77.475 1.00 46.34 ? 87 ALA C CB 1 ATOM 3307 N N . ALA C 1 60 ? 2.719 50.117 78.181 1.00 58.49 ? 88 ALA C N 1 ATOM 3308 C CA . ALA C 1 60 ? 2.838 51.517 78.586 1.00 55.92 ? 88 ALA C CA 1 ATOM 3309 C C . ALA C 1 60 ? 4.306 51.898 78.684 1.00 65.55 ? 88 ALA C C 1 ATOM 3310 O O . ALA C 1 60 ? 5.115 51.119 79.184 1.00 64.69 ? 88 ALA C O 1 ATOM 3311 C CB . ALA C 1 60 ? 2.137 51.752 79.908 1.00 47.18 ? 88 ALA C CB 1 ATOM 3312 N N . ASN C 1 61 ? 4.639 53.088 78.182 1.00 74.00 ? 89 ASN C N 1 ATOM 3313 C CA . ASN C 1 61 ? 6.016 53.602 78.178 1.00 73.89 ? 89 ASN C CA 1 ATOM 3314 C C . ASN C 1 61 ? 6.964 52.910 77.191 1.00 63.57 ? 89 ASN C C 1 ATOM 3315 O O . ASN C 1 61 ? 8.158 53.207 77.161 1.00 63.66 ? 89 ASN C O 1 ATOM 3316 C CB . ASN C 1 61 ? 6.622 53.673 79.590 1.00 79.16 ? 89 ASN C CB 1 ATOM 3317 C CG . ASN C 1 61 ? 5.841 54.598 80.508 1.00 83.33 ? 89 ASN C CG 1 ATOM 3318 O OD1 . ASN C 1 61 ? 4.721 55.005 80.190 1.00 82.12 ? 89 ASN C OD1 1 ATOM 3319 N ND2 . ASN C 1 61 ? 6.436 54.946 81.648 1.00 87.67 ? 89 ASN C ND2 1 ATOM 3320 N N . SER C 1 62 ? 6.454 51.970 76.402 1.00 60.42 ? 90 SER C N 1 ATOM 3321 C CA . SER C 1 62 ? 7.290 51.382 75.362 1.00 59.88 ? 90 SER C CA 1 ATOM 3322 C C . SER C 1 62 ? 7.252 52.342 74.176 1.00 64.39 ? 90 SER C C 1 ATOM 3323 O O . SER C 1 62 ? 6.325 53.144 74.057 1.00 68.26 ? 90 SER C O 1 ATOM 3324 C CB . SER C 1 62 ? 6.787 49.999 74.951 1.00 50.78 ? 90 SER C CB 1 ATOM 3325 O OG . SER C 1 62 ? 5.665 50.106 74.097 1.00 48.43 ? 90 SER C OG 1 ATOM 3326 N N . THR C 1 63 ? 8.260 52.283 73.313 1.00 65.72 ? 91 THR C N 1 ATOM 3327 C CA . THR C 1 63 ? 8.340 53.238 72.214 1.00 68.55 ? 91 THR C CA 1 ATOM 3328 C C . THR C 1 63 ? 8.010 52.590 70.877 1.00 69.22 ? 91 THR C C 1 ATOM 3329 O O . THR C 1 63 ? 8.342 51.430 70.645 1.00 70.02 ? 91 THR C O 1 ATOM 3330 C CB . THR C 1 63 ? 9.744 53.863 72.115 1.00 57.36 ? 91 THR C CB 1 ATOM 3331 O OG1 . THR C 1 63 ? 10.708 52.843 71.826 1.00 56.86 ? 91 THR C OG1 1 ATOM 3332 C CG2 . THR C 1 63 ? 10.102 54.565 73.413 1.00 51.02 ? 91 THR C CG2 1 ATOM 3333 N N . VAL C 1 64 ? 7.375 53.355 69.992 1.00 68.36 ? 92 VAL C N 1 ATOM 3334 C CA . VAL C 1 64 ? 7.077 52.887 68.640 1.00 63.36 ? 92 VAL C CA 1 ATOM 3335 C C . VAL C 1 64 ? 7.330 54.002 67.635 1.00 64.09 ? 92 VAL C C 1 ATOM 3336 O O . VAL C 1 64 ? 6.907 55.146 67.852 1.00 55.44 ? 92 VAL C O 1 ATOM 3337 C CB . VAL C 1 64 ? 5.611 52.457 68.484 1.00 57.00 ? 92 VAL C CB 1 ATOM 3338 C CG1 . VAL C 1 64 ? 5.360 51.951 67.052 1.00 51.50 ? 92 VAL C CG1 1 ATOM 3339 C CG2 . VAL C 1 64 ? 5.245 51.394 69.506 1.00 57.59 ? 92 VAL C CG2 1 ATOM 3340 N N . LYS C 1 65 ? 8.028 53.670 66.547 1.00 62.04 ? 93 LYS C N 1 ATOM 3341 C CA . LYS C 1 65 ? 8.235 54.618 65.458 1.00 61.18 ? 93 LYS C CA 1 ATOM 3342 C C . LYS C 1 65 ? 6.934 54.715 64.671 1.00 58.26 ? 93 LYS C C 1 ATOM 3343 O O . LYS C 1 65 ? 6.375 53.699 64.264 1.00 51.02 ? 93 LYS C O 1 ATOM 3344 C CB . LYS C 1 65 ? 9.386 54.165 64.562 1.00 57.47 ? 93 LYS C CB 1 ATOM 3345 C CG . LYS C 1 65 ? 10.753 54.551 65.112 1.00 59.11 ? 93 LYS C CG 1 ATOM 3346 C CD . LYS C 1 65 ? 11.893 53.828 64.407 1.00 61.18 ? 93 LYS C CD 1 ATOM 3347 C CE . LYS C 1 65 ? 11.850 54.058 62.909 1.00 74.73 ? 93 LYS C CE 1 ATOM 3348 N NZ . LYS C 1 65 ? 13.084 53.576 62.217 1.00 81.51 ? 93 LYS C NZ 1 ATOM 3349 N N . ILE C 1 66 ? 6.431 55.935 64.500 1.00 57.29 ? 94 ILE C N 1 ATOM 3350 C CA . ILE C 1 66 ? 5.181 56.147 63.769 1.00 54.36 ? 94 ILE C CA 1 ATOM 3351 C C . ILE C 1 66 ? 5.410 56.997 62.522 1.00 53.67 ? 94 ILE C C 1 ATOM 3352 O O . ILE C 1 66 ? 5.606 58.209 62.607 1.00 54.96 ? 94 ILE C O 1 ATOM 3353 C CB . ILE C 1 66 ? 4.101 56.794 64.656 1.00 51.00 ? 94 ILE C CB 1 ATOM 3354 C CG1 . ILE C 1 66 ? 3.827 55.909 65.867 1.00 54.59 ? 94 ILE C CG1 1 ATOM 3355 C CG2 . ILE C 1 66 ? 2.809 57.026 63.873 1.00 44.59 ? 94 ILE C CG2 1 ATOM 3356 C CD1 . ILE C 1 66 ? 2.739 56.426 66.754 1.00 52.45 ? 94 ILE C CD1 1 ATOM 3357 N N . PRO C 1 67 ? 5.345 56.362 61.349 1.00 50.73 ? 95 PRO C N 1 ATOM 3358 C CA . PRO C 1 67 ? 5.576 57.080 60.097 1.00 43.50 ? 95 PRO C CA 1 ATOM 3359 C C . PRO C 1 67 ? 4.383 57.925 59.737 1.00 45.27 ? 95 PRO C C 1 ATOM 3360 O O . PRO C 1 67 ? 3.242 57.613 60.083 1.00 41.55 ? 95 PRO C O 1 ATOM 3361 C CB . PRO C 1 67 ? 5.740 55.966 59.057 1.00 47.67 ? 95 PRO C CB 1 ATOM 3362 C CG . PRO C 1 67 ? 5.266 54.697 59.702 1.00 49.48 ? 95 PRO C CG 1 ATOM 3363 C CD . PRO C 1 67 ? 4.895 54.978 61.135 1.00 49.57 ? 95 PRO C CD 1 ATOM 3364 N N . PHE C 1 68 ? 4.648 59.025 59.050 1.00 46.32 ? 96 PHE C N 1 ATOM 3365 C CA . PHE C 1 68 ? 3.567 59.855 58.550 1.00 41.67 ? 96 PHE C CA 1 ATOM 3366 C C . PHE C 1 68 ? 4.056 60.622 57.338 1.00 44.51 ? 96 PHE C C 1 ATOM 3367 O O . PHE C 1 68 ? 5.255 60.692 57.063 1.00 46.03 ? 96 PHE C O 1 ATOM 3368 C CB . PHE C 1 68 ? 3.055 60.809 59.653 1.00 29.78 ? 96 PHE C CB 1 ATOM 3369 C CG . PHE C 1 68 ? 4.120 61.739 60.221 1.00 42.19 ? 96 PHE C CG 1 ATOM 3370 C CD1 . PHE C 1 68 ? 4.394 62.982 59.633 1.00 42.12 ? 96 PHE C CD1 1 ATOM 3371 C CD2 . PHE C 1 68 ? 4.834 61.378 61.350 1.00 42.66 ? 96 PHE C CD2 1 ATOM 3372 C CE1 . PHE C 1 68 ? 5.372 63.825 60.162 1.00 48.90 ? 96 PHE C CE1 1 ATOM 3373 C CE2 . PHE C 1 68 ? 5.820 62.221 61.889 1.00 48.89 ? 96 PHE C CE2 1 ATOM 3374 C CZ . PHE C 1 68 ? 6.090 63.444 61.289 1.00 54.99 ? 96 PHE C CZ 1 ATOM 3375 N N . ARG C 1 69 ? 3.099 61.184 56.628 1.00 45.20 ? 97 ARG C N 1 ATOM 3376 C CA . ARG C 1 69 ? 3.315 62.039 55.475 1.00 45.31 ? 97 ARG C CA 1 ATOM 3377 C C . ARG C 1 69 ? 3.673 63.407 56.060 1.00 47.37 ? 97 ARG C C 1 ATOM 3378 O O . ARG C 1 69 ? 2.910 63.983 56.824 1.00 40.44 ? 97 ARG C O 1 ATOM 3379 C CB . ARG C 1 69 ? 2.004 62.067 54.653 1.00 40.16 ? 97 ARG C CB 1 ATOM 3380 C CG . ARG C 1 69 ? 1.871 62.795 53.313 1.00 61.61 ? 97 ARG C CG 1 ATOM 3381 C CD . ARG C 1 69 ? 0.345 63.057 53.043 1.00 126.25 ? 97 ARG C CD 1 ATOM 3382 N NE . ARG C 1 69 ? -0.404 61.829 53.325 1.00 135.63 ? 97 ARG C NE 1 ATOM 3383 C CZ . ARG C 1 69 ? -1.733 61.714 53.370 1.00 145.62 ? 97 ARG C CZ 1 ATOM 3384 N NH1 . ARG C 1 69 ? -2.526 62.765 53.128 1.00 147.45 ? 97 ARG C NH1 1 ATOM 3385 N NH2 . ARG C 1 69 ? -2.267 60.524 53.665 1.00 153.91 ? 97 ARG C NH2 1 ATOM 3386 N N . CYS C 1 70 ? 4.878 63.881 55.772 1.00 38.53 ? 98 CYS C N 1 ATOM 3387 C CA . CYS C 1 70 ? 5.319 65.217 56.181 1.00 38.19 ? 98 CYS C CA 1 ATOM 3388 C C . CYS C 1 70 ? 5.131 66.256 55.057 1.00 42.58 ? 98 CYS C C 1 ATOM 3389 O O . CYS C 1 70 ? 5.452 65.975 53.921 1.00 44.40 ? 98 CYS C O 1 ATOM 3390 C CB . CYS C 1 70 ? 6.797 65.159 56.549 1.00 37.64 ? 98 CYS C CB 1 ATOM 3391 S SG . CYS C 1 70 ? 7.594 66.786 56.936 1.00 47.82 ? 98 CYS C SG 1 ATOM 3392 N N . ARG C 1 71 ? 4.634 67.453 55.360 1.00 38.51 ? 99 ARG C N 1 ATOM 3393 C CA . ARG C 1 71 ? 4.566 68.513 54.337 1.00 40.08 ? 99 ARG C CA 1 ATOM 3394 C C . ARG C 1 71 ? 5.349 69.776 54.708 1.00 42.43 ? 99 ARG C C 1 ATOM 3395 O O . ARG C 1 71 ? 5.174 70.333 55.791 1.00 49.93 ? 99 ARG C O 1 ATOM 3396 C CB . ARG C 1 71 ? 3.106 68.908 54.055 1.00 40.42 ? 99 ARG C CB 1 ATOM 3397 C CG . ARG C 1 71 ? 2.969 70.050 53.066 1.00 37.88 ? 99 ARG C CG 1 ATOM 3398 C CD . ARG C 1 71 ? 1.523 70.284 52.640 1.00 46.04 ? 99 ARG C CD 1 ATOM 3399 N NE . ARG C 1 71 ? 1.480 71.281 51.570 1.00 56.80 ? 99 ARG C NE 1 ATOM 3400 C CZ . ARG C 1 71 ? 1.571 72.597 51.753 1.00 57.69 ? 99 ARG C CZ 1 ATOM 3401 N NH1 . ARG C 1 71 ? 1.685 73.102 52.977 1.00 50.81 ? 99 ARG C NH1 1 ATOM 3402 N NH2 . ARG C 1 71 ? 1.538 73.411 50.705 1.00 57.75 ? 99 ARG C NH2 1 ATOM 3403 N N . CYS C 1 72 ? 6.183 70.259 53.800 1.00 42.27 ? 100 CYS C N 1 ATOM 3404 C CA . CYS C 1 72 ? 6.958 71.472 54.074 1.00 43.59 ? 100 CYS C CA 1 ATOM 3405 C C . CYS C 1 72 ? 6.321 72.698 53.463 1.00 45.77 ? 100 CYS C C 1 ATOM 3406 O O . CYS C 1 72 ? 5.918 72.702 52.301 1.00 52.08 ? 100 CYS C O 1 ATOM 3407 C CB . CYS C 1 72 ? 8.380 71.345 53.530 1.00 41.59 ? 100 CYS C CB 1 ATOM 3408 S SG . CYS C 1 72 ? 9.375 70.114 54.397 1.00 53.38 ? 100 CYS C SG 1 ATOM 3409 N N . ASN C 1 73 ? 6.221 73.754 54.250 1.00 46.61 ? 101 ASN C N 1 ATOM 3410 C CA . ASN C 1 73 ? 5.863 75.035 53.682 1.00 51.58 ? 101 ASN C CA 1 ATOM 3411 C C . ASN C 1 73 ? 7.208 75.701 53.474 1.00 63.81 ? 101 ASN C C 1 ATOM 3412 O O . ASN C 1 73 ? 8.241 75.051 53.689 1.00 81.06 ? 101 ASN C O 1 ATOM 3413 C CB . ASN C 1 73 ? 4.847 75.800 54.542 1.00 52.89 ? 101 ASN C CB 1 ATOM 3414 C CG . ASN C 1 73 ? 5.363 76.139 55.933 1.00 59.87 ? 101 ASN C CG 1 ATOM 3415 O OD1 . ASN C 1 73 ? 6.570 76.141 56.195 1.00 61.42 ? 101 ASN C OD1 1 ATOM 3416 N ND2 . ASN C 1 73 ? 4.429 76.368 56.855 1.00 50.06 ? 101 ASN C ND2 1 ATOM 3417 N N . GLY C 1 74 ? 7.240 76.946 53.039 1.00 58.33 ? 102 GLY C N 1 ATOM 3418 C CA . GLY C 1 74 ? 8.527 77.554 52.743 1.00 59.24 ? 102 GLY C CA 1 ATOM 3419 C C . GLY C 1 74 ? 9.568 77.442 53.842 1.00 56.43 ? 102 GLY C C 1 ATOM 3420 O O . GLY C 1 74 ? 10.766 77.483 53.572 1.00 55.61 ? 102 GLY C O 1 ATOM 3421 N N . ASP C 1 75 ? 9.099 77.211 55.068 1.00 59.10 ? 103 ASP C N 1 ATOM 3422 C CA . ASP C 1 75 ? 9.910 77.387 56.262 1.00 60.41 ? 103 ASP C CA 1 ATOM 3423 C C . ASP C 1 75 ? 10.043 76.172 57.175 1.00 59.19 ? 103 ASP C C 1 ATOM 3424 O O . ASP C 1 75 ? 11.118 75.930 57.746 1.00 56.70 ? 103 ASP C O 1 ATOM 3425 C CB . ASP C 1 75 ? 9.291 78.524 57.055 1.00 66.77 ? 103 ASP C CB 1 ATOM 3426 C CG . ASP C 1 75 ? 9.333 79.824 56.296 1.00 78.69 ? 103 ASP C CG 1 ATOM 3427 O OD1 . ASP C 1 75 ? 10.392 80.114 55.701 1.00 77.19 ? 103 ASP C OD1 1 ATOM 3428 O OD2 . ASP C 1 75 ? 8.295 80.521 56.238 1.00 86.25 ? 103 ASP C OD2 1 ATOM 3429 N N . VAL C 1 76 ? 8.959 75.411 57.314 1.00 57.36 ? 104 VAL C N 1 ATOM 3430 C CA . VAL C 1 76 ? 8.854 74.406 58.367 1.00 49.55 ? 104 VAL C CA 1 ATOM 3431 C C . VAL C 1 76 ? 8.188 73.145 57.837 1.00 51.01 ? 104 VAL C C 1 ATOM 3432 O O . VAL C 1 76 ? 7.376 73.211 56.915 1.00 52.17 ? 104 VAL C O 1 ATOM 3433 C CB . VAL C 1 76 ? 8.033 74.986 59.562 1.00 67.01 ? 104 VAL C CB 1 ATOM 3434 C CG1 . VAL C 1 76 ? 6.563 75.135 59.212 1.00 57.32 ? 104 VAL C CG1 1 ATOM 3435 C CG2 . VAL C 1 76 ? 8.182 74.147 60.793 1.00 69.42 ? 104 VAL C CG2 1 ATOM 3436 N N . GLY C 1 77 ? 8.519 71.996 58.427 1.00 50.63 ? 105 GLY C N 1 ATOM 3437 C CA . GLY C 1 77 ? 7.877 70.744 58.062 1.00 49.34 ? 105 GLY C CA 1 ATOM 3438 C C . GLY C 1 77 ? 6.905 70.261 59.133 1.00 49.00 ? 105 GLY C C 1 ATOM 3439 O O . GLY C 1 77 ? 7.257 70.172 60.302 1.00 52.94 ? 105 GLY C O 1 ATOM 3440 N N . GLN C 1 78 ? 5.684 69.935 58.717 1.00 42.90 ? 106 GLN C N 1 ATOM 3441 C CA . GLN C 1 78 ? 4.624 69.507 59.618 1.00 44.68 ? 106 GLN C CA 1 ATOM 3442 C C . GLN C 1 78 ? 3.927 68.287 59.006 1.00 48.20 ? 106 GLN C C 1 ATOM 3443 O O . GLN C 1 78 ? 3.876 68.130 57.776 1.00 42.17 ? 106 GLN C O 1 ATOM 3444 C CB . GLN C 1 78 ? 3.602 70.637 59.833 1.00 41.04 ? 106 GLN C CB 1 ATOM 3445 C CG . GLN C 1 78 ? 4.184 71.940 60.378 1.00 49.84 ? 106 GLN C CG 1 ATOM 3446 C CD . GLN C 1 78 ? 3.249 73.130 60.168 1.00 50.56 ? 106 GLN C CD 1 ATOM 3447 O OE1 . GLN C 1 78 ? 2.564 73.220 59.157 1.00 48.63 ? 106 GLN C OE1 1 ATOM 3448 N NE2 . GLN C 1 78 ? 3.238 74.055 61.118 1.00 51.38 ? 106 GLN C NE2 1 ATOM 3449 N N . SER C 1 79 ? 3.413 67.414 59.860 1.00 42.61 ? 107 SER C N 1 ATOM 3450 C CA . SER C 1 79 ? 2.669 66.270 59.384 1.00 42.51 ? 107 SER C CA 1 ATOM 3451 C C . SER C 1 79 ? 1.474 66.814 58.602 1.00 49.54 ? 107 SER C C 1 ATOM 3452 O O . SER C 1 79 ? 0.823 67.762 59.031 1.00 53.03 ? 107 SER C O 1 ATOM 3453 C CB . SER C 1 79 ? 2.250 65.371 60.552 1.00 48.93 ? 107 SER C CB 1 ATOM 3454 O OG . SER C 1 79 ? 1.456 66.056 61.510 1.00 46.03 ? 107 SER C OG 1 ATOM 3455 N N . ASP C 1 80 ? 1.223 66.241 57.430 1.00 45.22 ? 108 ASP C N 1 ATOM 3456 C CA . ASP C 1 80 ? 0.373 66.875 56.430 1.00 37.58 ? 108 ASP C CA 1 ATOM 3457 C C . ASP C 1 80 ? -1.114 66.750 56.735 1.00 45.05 ? 108 ASP C C 1 ATOM 3458 O O . ASP C 1 80 ? -1.744 65.807 56.304 1.00 50.39 ? 108 ASP C O 1 ATOM 3459 C CB . ASP C 1 80 ? 0.713 66.283 55.063 1.00 42.78 ? 108 ASP C CB 1 ATOM 3460 C CG . ASP C 1 80 ? 0.094 67.041 53.918 1.00 41.90 ? 108 ASP C CG 1 ATOM 3461 O OD1 . ASP C 1 80 ? -0.514 68.109 54.133 1.00 47.76 ? 108 ASP C OD1 1 ATOM 3462 O OD2 . ASP C 1 80 ? 0.256 66.575 52.778 1.00 52.84 ? 108 ASP C OD2 1 ATOM 3463 N N . ARG C 1 81 ? -1.653 67.717 57.480 1.00 58.79 ? 109 ARG C N 1 ATOM 3464 C CA . ARG C 1 81 ? -3.070 67.767 57.900 1.00 65.55 ? 109 ARG C CA 1 ATOM 3465 C C . ARG C 1 81 ? -3.600 66.538 58.669 1.00 62.08 ? 109 ARG C C 1 ATOM 3466 O O . ARG C 1 81 ? -4.811 66.334 58.796 1.00 60.07 ? 109 ARG C O 1 ATOM 3467 C CB . ARG C 1 81 ? -3.994 68.180 56.740 1.00 77.23 ? 109 ARG C CB 1 ATOM 3468 C CG . ARG C 1 81 ? -3.686 69.574 56.171 1.00 91.55 ? 109 ARG C CG 1 ATOM 3469 C CD . ARG C 1 81 ? -4.096 70.667 57.167 1.00 106.48 ? 109 ARG C CD 1 ATOM 3470 N NE . ARG C 1 81 ? -3.462 71.959 56.904 1.00 118.02 ? 109 ARG C NE 1 ATOM 3471 C CZ . ARG C 1 81 ? -3.895 73.119 57.392 1.00 128.70 ? 109 ARG C CZ 1 ATOM 3472 N NH1 . ARG C 1 81 ? -3.252 74.245 57.105 1.00 132.55 ? 109 ARG C NH1 1 ATOM 3473 N NH2 . ARG C 1 81 ? -4.963 73.154 58.178 1.00 131.06 ? 109 ARG C NH2 1 ATOM 3474 N N . LEU C 1 82 ? -2.669 65.736 59.174 1.00 53.82 ? 110 LEU C N 1 ATOM 3475 C CA . LEU C 1 82 ? -2.943 64.635 60.094 1.00 52.11 ? 110 LEU C CA 1 ATOM 3476 C C . LEU C 1 82 ? -1.830 64.656 61.144 1.00 54.25 ? 110 LEU C C 1 ATOM 3477 O O . LEU C 1 82 ? -0.737 65.145 60.863 1.00 52.40 ? 110 LEU C O 1 ATOM 3478 C CB . LEU C 1 82 ? -2.912 63.301 59.337 1.00 51.56 ? 110 LEU C CB 1 ATOM 3479 C CG . LEU C 1 82 ? -4.053 63.019 58.349 1.00 50.20 ? 110 LEU C CG 1 ATOM 3480 C CD1 . LEU C 1 82 ? -3.682 61.863 57.432 1.00 48.01 ? 110 LEU C CD1 1 ATOM 3481 C CD2 . LEU C 1 82 ? -5.352 62.715 59.096 1.00 34.83 ? 110 LEU C CD2 1 ATOM 3482 N N . PRO C 1 83 ? -2.077 64.110 62.351 1.00 62.76 ? 111 PRO C N 1 ATOM 3483 C CA . PRO C 1 83 ? -3.308 63.505 62.870 1.00 54.93 ? 111 PRO C CA 1 ATOM 3484 C C . PRO C 1 83 ? -4.342 64.524 63.335 1.00 52.51 ? 111 PRO C C 1 ATOM 3485 O O . PRO C 1 83 ? -4.032 65.695 63.557 1.00 58.52 ? 111 PRO C O 1 ATOM 3486 C CB . PRO C 1 83 ? -2.803 62.699 64.066 1.00 52.63 ? 111 PRO C CB 1 ATOM 3487 C CG . PRO C 1 83 ? -1.637 63.467 64.558 1.00 45.19 ? 111 PRO C CG 1 ATOM 3488 C CD . PRO C 1 83 ? -0.985 64.061 63.344 1.00 53.77 ? 111 PRO C CD 1 ATOM 3489 N N . ILE C 1 84 ? -5.576 64.058 63.483 1.00 60.75 ? 112 ILE C N 1 ATOM 3490 C CA . ILE C 1 84 ? -6.666 64.882 63.973 1.00 65.26 ? 112 ILE C CA 1 ATOM 3491 C C . ILE C 1 84 ? -6.995 64.469 65.386 1.00 65.97 ? 112 ILE C C 1 ATOM 3492 O O . ILE C 1 84 ? -7.010 63.282 65.705 1.00 69.11 ? 112 ILE C O 1 ATOM 3493 C CB . ILE C 1 84 ? -7.934 64.753 63.106 1.00 68.32 ? 112 ILE C CB 1 ATOM 3494 C CG1 . ILE C 1 84 ? -8.194 63.290 62.733 1.00 75.16 ? 112 ILE C CG1 1 ATOM 3495 C CG2 . ILE C 1 84 ? -7.808 65.621 61.863 1.00 70.94 ? 112 ILE C CG2 1 ATOM 3496 C CD1 . ILE C 1 84 ? -9.275 62.602 63.568 1.00 78.23 ? 112 ILE C CD1 1 ATOM 3497 N N . TYR C 1 85 ? -7.183 65.456 66.250 1.00 62.86 ? 113 TYR C N 1 ATOM 3498 C CA . TYR C 1 85 ? -7.597 65.184 67.608 1.00 61.71 ? 113 TYR C CA 1 ATOM 3499 C C . TYR C 1 85 ? -8.953 65.819 67.864 1.00 66.43 ? 113 TYR C C 1 ATOM 3500 O O . TYR C 1 85 ? -9.134 67.013 67.611 1.00 74.69 ? 113 TYR C O 1 ATOM 3501 C CB . TYR C 1 85 ? -6.579 65.704 68.615 1.00 57.52 ? 113 TYR C CB 1 ATOM 3502 C CG . TYR C 1 85 ? -6.937 65.348 70.043 1.00 61.38 ? 113 TYR C CG 1 ATOM 3503 C CD1 . TYR C 1 85 ? -6.540 64.130 70.592 1.00 62.90 ? 113 TYR C CD1 1 ATOM 3504 C CD2 . TYR C 1 85 ? -7.698 66.205 70.830 1.00 54.08 ? 113 TYR C CD2 1 ATOM 3505 C CE1 . TYR C 1 85 ? -6.865 63.782 71.891 1.00 53.53 ? 113 TYR C CE1 1 ATOM 3506 C CE2 . TYR C 1 85 ? -8.037 65.858 72.135 1.00 62.42 ? 113 TYR C CE2 1 ATOM 3507 C CZ . TYR C 1 85 ? -7.613 64.643 72.655 1.00 59.12 ? 113 TYR C CZ 1 ATOM 3508 O OH . TYR C 1 85 ? -7.933 64.286 73.940 1.00 63.82 ? 113 TYR C OH 1 ATOM 3509 N N . VAL C 1 86 ? -9.906 65.032 68.360 1.00 60.15 ? 114 VAL C N 1 ATOM 3510 C CA . VAL C 1 86 ? -11.202 65.585 68.770 1.00 61.72 ? 114 VAL C CA 1 ATOM 3511 C C . VAL C 1 86 ? -11.214 66.011 70.242 1.00 61.99 ? 114 VAL C C 1 ATOM 3512 O O . VAL C 1 86 ? -10.909 65.217 71.130 1.00 56.11 ? 114 VAL C O 1 ATOM 3513 C CB . VAL C 1 86 ? -12.388 64.634 68.477 1.00 58.95 ? 114 VAL C CB 1 ATOM 3514 C CG1 . VAL C 1 86 ? -13.679 65.423 68.368 1.00 55.93 ? 114 VAL C CG1 1 ATOM 3515 C CG2 . VAL C 1 86 ? -12.134 63.815 67.215 1.00 52.56 ? 114 VAL C CG2 1 ATOM 3516 N N . VAL C 1 87 ? -11.515 67.287 70.477 1.00 67.13 ? 115 VAL C N 1 ATOM 3517 C CA . VAL C 1 87 ? -11.533 67.852 71.826 1.00 79.06 ? 115 VAL C CA 1 ATOM 3518 C C . VAL C 1 87 ? -12.512 67.132 72.754 1.00 91.19 ? 115 VAL C C 1 ATOM 3519 O O . VAL C 1 87 ? -13.694 66.986 72.440 1.00 91.52 ? 115 VAL C O 1 ATOM 3520 C CB . VAL C 1 87 ? -11.914 69.354 71.813 1.00 67.56 ? 115 VAL C CB 1 ATOM 3521 C CG1 . VAL C 1 87 ? -11.925 69.900 73.227 1.00 59.07 ? 115 VAL C CG1 1 ATOM 3522 C CG2 . VAL C 1 87 ? -10.964 70.152 70.926 1.00 60.44 ? 115 VAL C CG2 1 ATOM 3523 N N . GLN C 1 88 ? -12.020 66.733 73.922 1.00 94.67 ? 116 GLN C N 1 ATOM 3524 C CA . GLN C 1 88 ? -12.833 66.011 74.889 1.00 93.06 ? 116 GLN C CA 1 ATOM 3525 C C . GLN C 1 88 ? -13.415 67.052 75.847 1.00 100.51 ? 116 GLN C C 1 ATOM 3526 O O . GLN C 1 88 ? -12.911 68.173 75.902 1.00 100.03 ? 116 GLN C O 1 ATOM 3527 C CB . GLN C 1 88 ? -11.987 64.971 75.630 1.00 86.47 ? 116 GLN C CB 1 ATOM 3528 C CG . GLN C 1 88 ? -11.123 64.098 74.732 1.00 85.85 ? 116 GLN C CG 1 ATOM 3529 C CD . GLN C 1 88 ? -11.900 63.080 73.923 1.00 92.77 ? 116 GLN C CD 1 ATOM 3530 O OE1 . GLN C 1 88 ? -13.122 62.964 74.044 1.00 95.14 ? 116 GLN C OE1 1 ATOM 3531 N NE2 . GLN C 1 88 ? -11.189 62.337 73.077 1.00 94.09 ? 116 GLN C NE2 1 ATOM 3532 N N . PRO C 1 89 ? -14.479 66.691 76.592 1.00 106.59 ? 117 PRO C N 1 ATOM 3533 C CA . PRO C 1 89 ? -15.142 67.605 77.535 1.00 106.09 ? 117 PRO C CA 1 ATOM 3534 C C . PRO C 1 89 ? -14.224 68.519 78.364 1.00 105.18 ? 117 PRO C C 1 ATOM 3535 O O . PRO C 1 89 ? -14.442 69.733 78.373 1.00 103.91 ? 117 PRO C O 1 ATOM 3536 C CB . PRO C 1 89 ? -15.898 66.645 78.461 1.00 104.55 ? 117 PRO C CB 1 ATOM 3537 C CG . PRO C 1 89 ? -16.181 65.437 77.614 1.00 102.27 ? 117 PRO C CG 1 ATOM 3538 C CD . PRO C 1 89 ? -15.213 65.416 76.463 1.00 104.50 ? 117 PRO C CD 1 ATOM 3539 N N . GLN C 1 90 ? -13.219 67.962 79.031 1.00 104.04 ? 118 GLN C N 1 ATOM 3540 C CA . GLN C 1 90 ? -12.338 68.772 79.878 1.00 110.09 ? 118 GLN C CA 1 ATOM 3541 C C . GLN C 1 90 ? -10.890 68.823 79.395 1.00 109.82 ? 118 GLN C C 1 ATOM 3542 O O . GLN C 1 90 ? -9.960 68.526 80.144 1.00 111.54 ? 118 GLN C O 1 ATOM 3543 C CB . GLN C 1 90 ? -12.422 68.343 81.347 1.00 115.07 ? 118 GLN C CB 1 ATOM 3544 C CG . GLN C 1 90 ? -13.425 69.162 82.169 1.00 120.06 ? 118 GLN C CG 1 ATOM 3545 C CD . GLN C 1 90 ? -12.920 70.561 82.516 1.00 125.49 ? 118 GLN C CD 1 ATOM 3546 O OE1 . GLN C 1 90 ? -11.715 70.822 82.507 1.00 128.12 ? 118 GLN C OE1 1 ATOM 3547 N NE2 . GLN C 1 90 ? -13.846 71.465 82.826 1.00 125.23 ? 118 GLN C NE2 1 ATOM 3548 N N . ASP C 1 91 ? -10.715 69.152 78.121 1.00 103.79 ? 119 ASP C N 1 ATOM 3549 C CA . ASP C 1 91 ? -9.390 69.235 77.529 1.00 93.19 ? 119 ASP C CA 1 ATOM 3550 C C . ASP C 1 91 ? -8.830 70.654 77.447 1.00 82.27 ? 119 ASP C C 1 ATOM 3551 O O . ASP C 1 91 ? -9.571 71.636 77.324 1.00 77.38 ? 119 ASP C O 1 ATOM 3552 C CB . ASP C 1 91 ? -9.414 68.636 76.128 1.00 94.47 ? 119 ASP C CB 1 ATOM 3553 C CG . ASP C 1 91 ? -9.098 67.163 76.131 1.00 96.91 ? 119 ASP C CG 1 ATOM 3554 O OD1 . ASP C 1 91 ? -8.672 66.648 77.187 1.00 103.90 ? 119 ASP C OD1 1 ATOM 3555 O OD2 . ASP C 1 91 ? -9.268 66.520 75.077 1.00 90.37 ? 119 ASP C OD2 1 ATOM 3556 N N . GLY C 1 92 ? -7.504 70.739 77.506 1.00 72.15 ? 120 GLY C N 1 ATOM 3557 C CA . GLY C 1 92 ? -6.794 71.964 77.201 1.00 68.35 ? 120 GLY C CA 1 ATOM 3558 C C . GLY C 1 92 ? -5.721 71.629 76.180 1.00 70.86 ? 120 GLY C C 1 ATOM 3559 O O . GLY C 1 92 ? -5.187 70.512 76.184 1.00 72.73 ? 120 GLY C O 1 ATOM 3560 N N . LEU C 1 93 ? -5.413 72.588 75.306 1.00 67.05 ? 121 LEU C N 1 ATOM 3561 C CA . LEU C 1 93 ? -4.450 72.384 74.218 1.00 68.61 ? 121 LEU C CA 1 ATOM 3562 C C . LEU C 1 93 ? -3.138 71.877 74.772 1.00 68.08 ? 121 LEU C C 1 ATOM 3563 O O . LEU C 1 93 ? -2.522 70.948 74.235 1.00 57.57 ? 121 LEU C O 1 ATOM 3564 C CB . LEU C 1 93 ? -4.189 73.695 73.468 1.00 64.70 ? 121 LEU C CB 1 ATOM 3565 C CG . LEU C 1 93 ? -5.389 74.554 73.069 1.00 66.57 ? 121 LEU C CG 1 ATOM 3566 C CD1 . LEU C 1 93 ? -5.431 75.799 73.949 1.00 74.59 ? 121 LEU C CD1 1 ATOM 3567 C CD2 . LEU C 1 93 ? -5.327 74.954 71.599 1.00 59.53 ? 121 LEU C CD2 1 ATOM 3568 N N . ASP C 1 94 ? -2.733 72.497 75.873 1.00 74.71 ? 122 ASP C N 1 ATOM 3569 C CA . ASP C 1 94 ? -1.464 72.206 76.508 1.00 72.38 ? 122 ASP C CA 1 ATOM 3570 C C . ASP C 1 94 ? -1.485 70.783 77.060 1.00 65.58 ? 122 ASP C C 1 ATOM 3571 O O . ASP C 1 94 ? -0.491 70.051 76.952 1.00 65.59 ? 122 ASP C O 1 ATOM 3572 C CB . ASP C 1 94 ? -1.207 73.231 77.611 1.00 78.84 ? 122 ASP C CB 1 ATOM 3573 C CG . ASP C 1 94 ? 0.229 73.246 78.072 1.00 86.55 ? 122 ASP C CG 1 ATOM 3574 O OD1 . ASP C 1 94 ? 0.841 72.168 78.187 1.00 87.38 ? 122 ASP C OD1 1 ATOM 3575 O OD2 . ASP C 1 94 ? 0.768 74.350 78.301 1.00 89.76 ? 122 ASP C OD2 1 ATOM 3576 N N . ALA C 1 95 ? -2.626 70.377 77.618 1.00 58.80 ? 123 ALA C N 1 ATOM 3577 C CA . ALA C 1 95 ? -2.746 69.032 78.172 1.00 60.72 ? 123 ALA C CA 1 ATOM 3578 C C . ALA C 1 95 ? -2.745 67.994 77.060 1.00 64.66 ? 123 ALA C C 1 ATOM 3579 O O . ALA C 1 95 ? -2.174 66.912 77.200 1.00 61.93 ? 123 ALA C O 1 ATOM 3580 C CB . ALA C 1 95 ? -4.003 68.912 79.022 1.00 60.07 ? 123 ALA C CB 1 ATOM 3581 N N . ILE C 1 96 ? -3.373 68.342 75.943 1.00 68.69 ? 124 ILE C N 1 ATOM 3582 C CA . ILE C 1 96 ? -3.371 67.486 74.756 1.00 69.87 ? 124 ILE C CA 1 ATOM 3583 C C . ILE C 1 96 ? -1.950 67.422 74.192 1.00 61.89 ? 124 ILE C C 1 ATOM 3584 O O . ILE C 1 96 ? -1.402 66.338 73.926 1.00 58.15 ? 124 ILE C O 1 ATOM 3585 C CB . ILE C 1 96 ? -4.335 68.041 73.683 1.00 66.11 ? 124 ILE C CB 1 ATOM 3586 C CG1 . ILE C 1 96 ? -5.781 67.936 74.170 1.00 65.11 ? 124 ILE C CG1 1 ATOM 3587 C CG2 . ILE C 1 96 ? -4.164 67.299 72.377 1.00 67.10 ? 124 ILE C CG2 1 ATOM 3588 C CD1 . ILE C 1 96 ? -6.755 68.826 73.422 1.00 64.55 ? 124 ILE C CD1 1 ATOM 3589 N N . ALA C 1 97 ? -1.357 68.606 74.051 1.00 51.35 ? 125 ALA C N 1 ATOM 3590 C CA . ALA C 1 97 ? 0.011 68.751 73.583 1.00 55.23 ? 125 ALA C CA 1 ATOM 3591 C C . ALA C 1 97 ? 0.945 67.868 74.388 1.00 63.61 ? 125 ALA C C 1 ATOM 3592 O O . ALA C 1 97 ? 1.733 67.108 73.818 1.00 62.94 ? 125 ALA C O 1 ATOM 3593 C CB . ALA C 1 97 ? 0.449 70.207 73.676 1.00 50.98 ? 125 ALA C CB 1 ATOM 3594 N N . ARG C 1 98 ? 0.833 67.952 75.713 1.00 70.19 ? 126 ARG C N 1 ATOM 3595 C CA . ARG C 1 98 ? 1.749 67.234 76.595 1.00 62.22 ? 126 ARG C CA 1 ATOM 3596 C C . ARG C 1 98 ? 1.355 65.781 76.904 1.00 63.09 ? 126 ARG C C 1 ATOM 3597 O O . ARG C 1 98 ? 2.212 64.885 76.896 1.00 56.49 ? 126 ARG C O 1 ATOM 3598 C CB . ARG C 1 98 ? 1.946 68.013 77.890 1.00 53.18 ? 126 ARG C CB 1 ATOM 3599 C CG . ARG C 1 98 ? 2.473 69.398 77.647 1.00 51.98 ? 126 ARG C CG 1 ATOM 3600 C CD . ARG C 1 98 ? 2.943 70.065 78.921 1.00 52.88 ? 126 ARG C CD 1 ATOM 3601 N NE . ARG C 1 98 ? 4.170 70.802 78.645 1.00 53.09 ? 126 ARG C NE 1 ATOM 3602 C CZ . ARG C 1 98 ? 4.198 72.058 78.215 1.00 58.11 ? 126 ARG C CZ 1 ATOM 3603 N NH1 . ARG C 1 98 ? 3.063 72.721 78.060 1.00 65.75 ? 126 ARG C NH1 1 ATOM 3604 N NH2 . ARG C 1 98 ? 5.355 72.664 77.970 1.00 42.18 ? 126 ARG C NH2 1 ATOM 3605 N N . ASN C 1 99 ? 0.070 65.534 77.150 1.00 63.27 ? 127 ASN C N 1 ATOM 3606 C CA . ASN C 1 99 ? -0.342 64.206 77.612 1.00 70.45 ? 127 ASN C CA 1 ATOM 3607 C C . ASN C 1 99 ? -0.698 63.212 76.519 1.00 74.74 ? 127 ASN C C 1 ATOM 3608 O O . ASN C 1 99 ? -0.600 62.006 76.723 1.00 77.40 ? 127 ASN C O 1 ATOM 3609 C CB . ASN C 1 99 ? -1.531 64.292 78.578 1.00 66.11 ? 127 ASN C CB 1 ATOM 3610 C CG . ASN C 1 99 ? -1.261 65.176 79.767 1.00 62.56 ? 127 ASN C CG 1 ATOM 3611 O OD1 . ASN C 1 99 ? -0.143 65.226 80.283 1.00 62.17 ? 127 ASN C OD1 1 ATOM 3612 N ND2 . ASN C 1 99 ? -2.285 65.897 80.204 1.00 61.85 ? 127 ASN C ND2 1 ATOM 3613 N N . VAL C 1 100 ? -1.087 63.707 75.352 1.00 73.64 ? 128 VAL C N 1 ATOM 3614 C CA . VAL C 1 100 ? -1.458 62.808 74.272 1.00 61.39 ? 128 VAL C CA 1 ATOM 3615 C C . VAL C 1 100 ? -0.360 62.646 73.247 1.00 58.60 ? 128 VAL C C 1 ATOM 3616 O O . VAL C 1 100 ? -0.080 61.533 72.806 1.00 60.96 ? 128 VAL C O 1 ATOM 3617 C CB . VAL C 1 100 ? -2.750 63.265 73.571 1.00 62.97 ? 128 VAL C CB 1 ATOM 3618 C CG1 . VAL C 1 100 ? -3.187 62.236 72.543 1.00 61.61 ? 128 VAL C CG1 1 ATOM 3619 C CG2 . VAL C 1 100 ? -3.846 63.498 74.593 1.00 65.40 ? 128 VAL C CG2 1 ATOM 3620 N N . PHE C 1 101 ? 0.282 63.751 72.886 1.00 55.82 ? 129 PHE C N 1 ATOM 3621 C CA . PHE C 1 101 ? 1.264 63.706 71.812 1.00 52.76 ? 129 PHE C CA 1 ATOM 3622 C C . PHE C 1 101 ? 2.709 63.985 72.259 1.00 58.25 ? 129 PHE C C 1 ATOM 3623 O O . PHE C 1 101 ? 3.506 64.512 71.482 1.00 63.21 ? 129 PHE C O 1 ATOM 3624 C CB . PHE C 1 101 ? 0.835 64.623 70.658 1.00 48.43 ? 129 PHE C CB 1 ATOM 3625 C CG . PHE C 1 101 ? -0.468 64.216 70.006 1.00 46.01 ? 129 PHE C CG 1 ATOM 3626 C CD1 . PHE C 1 101 ? -0.526 63.118 69.160 1.00 44.71 ? 129 PHE C CD1 1 ATOM 3627 C CD2 . PHE C 1 101 ? -1.631 64.935 70.233 1.00 45.73 ? 129 PHE C CD2 1 ATOM 3628 C CE1 . PHE C 1 101 ? -1.724 62.741 68.566 1.00 42.97 ? 129 PHE C CE1 1 ATOM 3629 C CE2 . PHE C 1 101 ? -2.835 64.561 69.635 1.00 38.27 ? 129 PHE C CE2 1 ATOM 3630 C CZ . PHE C 1 101 ? -2.876 63.477 68.800 1.00 39.95 ? 129 PHE C CZ 1 ATOM 3631 N N . ASN C 1 102 ? 3.031 63.626 73.505 1.00 51.35 ? 130 ASN C N 1 ATOM 3632 C CA . ASN C 1 102 ? 4.415 63.587 73.999 1.00 45.38 ? 130 ASN C CA 1 ATOM 3633 C C . ASN C 1 102 ? 5.152 64.943 73.978 1.00 44.16 ? 130 ASN C C 1 ATOM 3634 O O . ASN C 1 102 ? 6.385 64.988 73.900 1.00 41.78 ? 130 ASN C O 1 ATOM 3635 C CB . ASN C 1 102 ? 5.250 62.568 73.191 1.00 49.20 ? 130 ASN C CB 1 ATOM 3636 C CG . ASN C 1 102 ? 4.779 61.121 73.373 1.00 51.74 ? 130 ASN C CG 1 ATOM 3637 O OD1 . ASN C 1 102 ? 5.401 60.194 72.865 1.00 59.27 ? 130 ASN C OD1 1 ATOM 3638 N ND2 . ASN C 1 102 ? 3.655 60.936 74.042 1.00 52.15 ? 130 ASN C ND2 1 ATOM 3639 N N . ALA C 1 103 ? 4.400 66.041 74.010 1.00 48.01 ? 131 ALA C N 1 ATOM 3640 C CA . ALA C 1 103 ? 4.974 67.379 73.838 1.00 51.85 ? 131 ALA C CA 1 ATOM 3641 C C . ALA C 1 103 ? 5.842 67.519 72.572 1.00 60.14 ? 131 ALA C C 1 ATOM 3642 O O . ALA C 1 103 ? 6.784 68.304 72.551 1.00 62.02 ? 131 ALA C O 1 ATOM 3643 C CB . ALA C 1 103 ? 5.763 67.794 75.075 1.00 38.92 ? 131 ALA C CB 1 ATOM 3644 N N . PHE C 1 104 ? 5.538 66.740 71.534 1.00 62.37 ? 132 PHE C N 1 ATOM 3645 C CA . PHE C 1 104 ? 6.165 66.927 70.221 1.00 57.41 ? 132 PHE C CA 1 ATOM 3646 C C . PHE C 1 104 ? 5.723 68.246 69.591 1.00 53.40 ? 132 PHE C C 1 ATOM 3647 O O . PHE C 1 104 ? 6.385 68.774 68.699 1.00 55.34 ? 132 PHE C O 1 ATOM 3648 C CB . PHE C 1 104 ? 5.881 65.753 69.279 1.00 51.30 ? 132 PHE C CB 1 ATOM 3649 C CG . PHE C 1 104 ? 6.783 64.559 69.494 1.00 51.91 ? 132 PHE C CG 1 ATOM 3650 C CD1 . PHE C 1 104 ? 8.159 64.678 69.363 1.00 46.66 ? 132 PHE C CD1 1 ATOM 3651 C CD2 . PHE C 1 104 ? 6.250 63.309 69.792 1.00 53.96 ? 132 PHE C CD2 1 ATOM 3652 C CE1 . PHE C 1 104 ? 8.989 63.583 69.555 1.00 51.48 ? 132 PHE C CE1 1 ATOM 3653 C CE2 . PHE C 1 104 ? 7.075 62.203 69.978 1.00 54.62 ? 132 PHE C CE2 1 ATOM 3654 C CZ . PHE C 1 104 ? 8.444 62.338 69.860 1.00 51.80 ? 132 PHE C CZ 1 ATOM 3655 N N . VAL C 1 105 ? 4.584 68.759 70.043 1.00 48.85 ? 133 VAL C N 1 ATOM 3656 C CA . VAL C 1 105 ? 4.147 70.094 69.668 1.00 48.53 ? 133 VAL C CA 1 ATOM 3657 C C . VAL C 1 105 ? 3.858 70.920 70.926 1.00 56.57 ? 133 VAL C C 1 ATOM 3658 O O . VAL C 1 105 ? 3.585 70.363 71.988 1.00 46.65 ? 133 VAL C O 1 ATOM 3659 C CB . VAL C 1 105 ? 2.868 70.040 68.784 1.00 55.91 ? 133 VAL C CB 1 ATOM 3660 C CG1 . VAL C 1 105 ? 3.124 69.204 67.529 1.00 51.25 ? 133 VAL C CG1 1 ATOM 3661 C CG2 . VAL C 1 105 ? 1.685 69.472 69.553 1.00 44.51 ? 133 VAL C CG2 1 ATOM 3662 N N . THR C 1 106 ? 3.915 72.244 70.817 1.00 66.69 ? 134 THR C N 1 ATOM 3663 C CA . THR C 1 106 ? 3.475 73.095 71.921 1.00 64.94 ? 134 THR C CA 1 ATOM 3664 C C . THR C 1 106 ? 2.058 73.527 71.628 1.00 63.56 ? 134 THR C C 1 ATOM 3665 O O . THR C 1 106 ? 1.618 73.463 70.478 1.00 68.33 ? 134 THR C O 1 ATOM 3666 C CB . THR C 1 106 ? 4.331 74.372 72.063 1.00 64.62 ? 134 THR C CB 1 ATOM 3667 O OG1 . THR C 1 106 ? 3.998 75.311 71.024 1.00 61.75 ? 134 THR C OG1 1 ATOM 3668 C CG2 . THR C 1 106 ? 5.823 74.035 72.040 1.00 57.56 ? 134 THR C CG2 1 ATOM 3669 N N . TYR C 1 107 ? 1.361 74.021 72.647 1.00 58.17 ? 135 TYR C N 1 ATOM 3670 C CA . TYR C 1 107 ? -0.024 74.431 72.469 1.00 53.34 ? 135 TYR C CA 1 ATOM 3671 C C . TYR C 1 107 ? -0.105 75.650 71.569 1.00 55.79 ? 135 TYR C C 1 ATOM 3672 O O . TYR C 1 107 ? -1.124 75.889 70.915 1.00 58.18 ? 135 TYR C O 1 ATOM 3673 C CB . TYR C 1 107 ? -0.731 74.672 73.807 1.00 66.31 ? 135 TYR C CB 1 ATOM 3674 C CG . TYR C 1 107 ? -0.404 75.982 74.486 1.00 74.84 ? 135 TYR C CG 1 ATOM 3675 C CD1 . TYR C 1 107 ? -1.186 77.114 74.260 1.00 69.38 ? 135 TYR C CD1 1 ATOM 3676 C CD2 . TYR C 1 107 ? 0.666 76.087 75.371 1.00 80.03 ? 135 TYR C CD2 1 ATOM 3677 C CE1 . TYR C 1 107 ? -0.907 78.313 74.878 1.00 72.53 ? 135 TYR C CE1 1 ATOM 3678 C CE2 . TYR C 1 107 ? 0.954 77.291 75.999 1.00 82.27 ? 135 TYR C CE2 1 ATOM 3679 C CZ . TYR C 1 107 ? 0.160 78.400 75.748 1.00 79.40 ? 135 TYR C CZ 1 ATOM 3680 O OH . TYR C 1 107 ? 0.432 79.603 76.367 1.00 83.44 ? 135 TYR C OH 1 ATOM 3681 N N . GLN C 1 108 ? 0.963 76.439 71.570 1.00 60.70 ? 136 GLN C N 1 ATOM 3682 C CA . GLN C 1 108 ? 1.091 77.560 70.650 1.00 65.14 ? 136 GLN C CA 1 ATOM 3683 C C . GLN C 1 108 ? 1.146 77.065 69.203 1.00 61.17 ? 136 GLN C C 1 ATOM 3684 O O . GLN C 1 108 ? 0.556 77.666 68.310 1.00 47.69 ? 136 GLN C O 1 ATOM 3685 C CB . GLN C 1 108 ? 2.340 78.389 70.970 1.00 75.71 ? 136 GLN C CB 1 ATOM 3686 C CG . GLN C 1 108 ? 2.337 79.061 72.347 1.00 81.08 ? 136 GLN C CG 1 ATOM 3687 C CD . GLN C 1 108 ? 2.954 78.200 73.449 1.00 84.38 ? 136 GLN C CD 1 ATOM 3688 O OE1 . GLN C 1 108 ? 2.919 76.966 73.405 1.00 81.78 ? 136 GLN C OE1 1 ATOM 3689 N NE2 . GLN C 1 108 ? 3.541 78.861 74.440 1.00 86.24 ? 136 GLN C NE2 1 ATOM 3690 N N . GLU C 1 109 ? 1.875 75.973 68.980 1.00 70.83 ? 137 GLU C N 1 ATOM 3691 C CA . GLU C 1 109 ? 1.986 75.380 67.650 1.00 61.84 ? 137 GLU C CA 1 ATOM 3692 C C . GLU C 1 109 ? 0.639 74.837 67.171 1.00 67.14 ? 137 GLU C C 1 ATOM 3693 O O . GLU C 1 109 ? 0.277 75.010 66.004 1.00 73.62 ? 137 GLU C O 1 ATOM 3694 C CB . GLU C 1 109 ? 3.089 74.323 67.611 1.00 49.98 ? 137 GLU C CB 1 ATOM 3695 C CG . GLU C 1 109 ? 4.474 74.937 67.654 1.00 44.36 ? 137 GLU C CG 1 ATOM 3696 C CD . GLU C 1 109 ? 5.561 73.914 67.882 1.00 57.26 ? 137 GLU C CD 1 ATOM 3697 O OE1 . GLU C 1 109 ? 5.256 72.824 68.402 1.00 57.17 ? 137 GLU C OE1 1 ATOM 3698 O OE2 . GLU C 1 109 ? 6.725 74.198 67.528 1.00 66.38 ? 137 GLU C OE2 1 ATOM 3699 N N . ILE C 1 110 ? -0.105 74.190 68.070 1.00 62.73 ? 138 ILE C N 1 ATOM 3700 C CA . ILE C 1 110 ? -1.522 73.913 67.820 1.00 58.70 ? 138 ILE C CA 1 ATOM 3701 C C . ILE C 1 110 ? -2.148 75.309 67.811 1.00 66.04 ? 138 ILE C C 1 ATOM 3702 O O . ILE C 1 110 ? -1.460 76.280 68.067 1.00 78.31 ? 138 ILE C O 1 ATOM 3703 C CB . ILE C 1 110 ? -2.154 72.987 68.903 1.00 58.20 ? 138 ILE C CB 1 ATOM 3704 C CG1 . ILE C 1 110 ? -1.312 71.730 69.098 1.00 54.86 ? 138 ILE C CG1 1 ATOM 3705 C CG2 . ILE C 1 110 ? -3.598 72.599 68.565 1.00 54.50 ? 138 ILE C CG2 1 ATOM 3706 C CD1 . ILE C 1 110 ? -1.892 70.754 70.088 1.00 50.79 ? 138 ILE C CD1 1 ATOM 3707 N N . ALA C 1 111 ? -3.428 75.446 67.517 1.00 67.57 ? 139 ALA C N 1 ATOM 3708 C CA . ALA C 1 111 ? -4.047 76.774 67.483 1.00 64.42 ? 139 ALA C CA 1 ATOM 3709 C C . ALA C 1 111 ? -3.525 77.612 66.325 1.00 59.70 ? 139 ALA C C 1 ATOM 3710 O O . ALA C 1 111 ? -4.309 78.065 65.500 1.00 67.38 ? 139 ALA C O 1 ATOM 3711 C CB . ALA C 1 111 ? -3.869 77.527 68.825 1.00 58.82 ? 139 ALA C CB 1 ATOM 3712 N N . ALA C 1 112 ? -2.217 77.833 66.254 1.00 59.77 ? 140 ALA C N 1 ATOM 3713 C CA . ALA C 1 112 ? -1.671 78.556 65.106 1.00 65.47 ? 140 ALA C CA 1 ATOM 3714 C C . ALA C 1 112 ? -1.973 77.710 63.874 1.00 67.06 ? 140 ALA C C 1 ATOM 3715 O O . ALA C 1 112 ? -2.347 78.219 62.818 1.00 74.48 ? 140 ALA C O 1 ATOM 3716 C CB . ALA C 1 112 ? -0.169 78.802 65.256 1.00 59.07 ? 140 ALA C CB 1 ATOM 3717 N N . ALA C 1 113 ? -1.810 76.403 64.042 1.00 57.46 ? 141 ALA C N 1 ATOM 3718 C CA . ALA C 1 113 ? -2.076 75.430 62.998 1.00 54.10 ? 141 ALA C CA 1 ATOM 3719 C C . ALA C 1 113 ? -3.564 75.344 62.710 1.00 63.53 ? 141 ALA C C 1 ATOM 3720 O O . ALA C 1 113 ? -3.973 75.039 61.592 1.00 72.14 ? 141 ALA C O 1 ATOM 3721 C CB . ALA C 1 113 ? -1.538 74.081 63.394 1.00 57.68 ? 141 ALA C CB 1 ATOM 3722 N N . ASN C 1 114 ? -4.381 75.612 63.720 1.00 61.35 ? 142 ASN C N 1 ATOM 3723 C CA . ASN C 1 114 ? -5.820 75.490 63.536 1.00 67.03 ? 142 ASN C CA 1 ATOM 3724 C C . ASN C 1 114 ? -6.549 76.833 63.391 1.00 79.31 ? 142 ASN C C 1 ATOM 3725 O O . ASN C 1 114 ? -7.779 76.888 63.460 1.00 72.84 ? 142 ASN C O 1 ATOM 3726 C CB . ASN C 1 114 ? -6.425 74.617 64.637 1.00 60.71 ? 142 ASN C CB 1 ATOM 3727 C CG . ASN C 1 114 ? -5.973 73.159 64.534 1.00 65.57 ? 142 ASN C CG 1 ATOM 3728 O OD1 . ASN C 1 114 ? -6.611 72.344 63.862 1.00 61.75 ? 142 ASN C OD1 1 ATOM 3729 N ND2 . ASN C 1 114 ? -4.857 72.834 65.184 1.00 69.19 ? 142 ASN C ND2 1 ATOM 3730 N N . ASN C 1 115 ? -5.776 77.903 63.178 1.00 91.08 ? 143 ASN C N 1 ATOM 3731 C CA . ASN C 1 115 ? -6.299 79.243 62.853 1.00 101.47 ? 143 ASN C CA 1 ATOM 3732 C C . ASN C 1 115 ? -7.366 79.864 63.743 1.00 114.48 ? 143 ASN C C 1 ATOM 3733 O O . ASN C 1 115 ? -7.169 80.959 64.270 1.00 119.76 ? 143 ASN C O 1 ATOM 3734 C CB . ASN C 1 115 ? -6.734 79.352 61.381 1.00 107.43 ? 143 ASN C CB 1 ATOM 3735 C CG . ASN C 1 115 ? -5.616 79.832 60.471 1.00 114.67 ? 143 ASN C CG 1 ATOM 3736 O OD1 . ASN C 1 115 ? -4.990 80.862 60.729 1.00 117.23 ? 143 ASN C OD1 1 ATOM 3737 N ND2 . ASN C 1 115 ? -5.368 79.094 59.395 1.00 116.38 ? 143 ASN C ND2 1 ATOM 3738 N N . ILE C 1 116 ? -8.478 79.157 63.925 1.00 125.71 ? 144 ILE C N 1 ATOM 3739 C CA . ILE C 1 116 ? -9.616 79.684 64.678 1.00 133.33 ? 144 ILE C CA 1 ATOM 3740 C C . ILE C 1 116 ? -9.263 80.053 66.130 1.00 135.17 ? 144 ILE C C 1 ATOM 3741 O O . ILE C 1 116 ? -9.746 81.072 66.639 1.00 137.64 ? 144 ILE C O 1 ATOM 3742 C CB . ILE C 1 116 ? -10.817 78.684 64.662 1.00 133.44 ? 144 ILE C CB 1 ATOM 3743 C CG1 . ILE C 1 116 ? -11.172 78.287 63.225 1.00 131.31 ? 144 ILE C CG1 1 ATOM 3744 C CG2 . ILE C 1 116 ? -12.031 79.276 65.362 1.00 134.51 ? 144 ILE C CG2 1 ATOM 3745 C CD1 . ILE C 1 116 ? -12.335 77.316 63.118 1.00 127.85 ? 144 ILE C CD1 1 ATOM 3746 N N . PRO C 1 117 ? -8.408 79.256 66.804 1.00 129.75 ? 145 PRO C N 1 ATOM 3747 C CA . PRO C 1 117 ? -8.115 79.767 68.145 1.00 126.05 ? 145 PRO C CA 1 ATOM 3748 C C . PRO C 1 117 ? -7.062 80.874 68.196 1.00 121.28 ? 145 PRO C C 1 ATOM 3749 O O . PRO C 1 117 ? -5.980 80.766 67.618 1.00 118.87 ? 145 PRO C O 1 ATOM 3750 C CB . PRO C 1 117 ? -7.620 78.532 68.916 1.00 123.70 ? 145 PRO C CB 1 ATOM 3751 C CG . PRO C 1 117 ? -7.489 77.432 67.934 1.00 122.64 ? 145 PRO C CG 1 ATOM 3752 C CD . PRO C 1 117 ? -7.825 77.922 66.569 1.00 125.61 ? 145 PRO C CD 1 ATOM 3753 N N . ASP C 1 118 ? -7.418 81.946 68.890 1.00 116.00 ? 146 ASP C N 1 ATOM 3754 C CA . ASP C 1 118 ? -6.468 82.963 69.312 1.00 110.81 ? 146 ASP C CA 1 ATOM 3755 C C . ASP C 1 118 ? -6.359 82.964 70.836 1.00 112.04 ? 146 ASP C C 1 ATOM 3756 O O . ASP C 1 118 ? -5.256 83.112 71.373 1.00 111.86 ? 146 ASP C O 1 ATOM 3757 C CB . ASP C 1 118 ? -6.856 84.349 68.798 1.00 107.86 ? 146 ASP C CB 1 ATOM 3758 C CG . ASP C 1 118 ? -6.213 84.674 67.464 1.00 107.17 ? 146 ASP C CG 1 ATOM 3759 O OD1 . ASP C 1 118 ? -5.148 85.334 67.466 1.00 101.01 ? 146 ASP C OD1 1 ATOM 3760 O OD2 . ASP C 1 118 ? -6.761 84.270 66.417 1.00 109.92 ? 146 ASP C OD2 1 ATOM 3761 N N . PRO C 1 119 ? -7.495 82.806 71.552 1.00 112.14 ? 147 PRO C N 1 ATOM 3762 C CA . PRO C 1 119 ? -7.294 82.611 72.990 1.00 109.95 ? 147 PRO C CA 1 ATOM 3763 C C . PRO C 1 119 ? -7.179 81.143 73.416 1.00 107.23 ? 147 PRO C C 1 ATOM 3764 O O . PRO C 1 119 ? -7.084 80.250 72.576 1.00 98.61 ? 147 PRO C O 1 ATOM 3765 C CB . PRO C 1 119 ? -8.551 83.232 73.614 1.00 111.17 ? 147 PRO C CB 1 ATOM 3766 C CG . PRO C 1 119 ? -9.499 83.504 72.492 1.00 115.04 ? 147 PRO C CG 1 ATOM 3767 C CD . PRO C 1 119 ? -8.928 82.936 71.235 1.00 114.98 ? 147 PRO C CD 1 ATOM 3768 N N . ASN C 1 120 ? -7.207 80.922 74.732 1.00 113.22 ? 148 ASN C N 1 ATOM 3769 C CA . ASN C 1 120 ? -7.088 79.597 75.359 1.00 111.27 ? 148 ASN C CA 1 ATOM 3770 C C . ASN C 1 120 ? -8.450 78.905 75.462 1.00 107.75 ? 148 ASN C C 1 ATOM 3771 O O . ASN C 1 120 ? -8.725 78.197 76.417 1.00 104.10 ? 148 ASN C O 1 ATOM 3772 C CB . ASN C 1 120 ? -6.429 79.752 76.757 1.00 106.92 ? 148 ASN C CB 1 ATOM 3773 C CG . ASN C 1 120 ? -5.503 78.591 77.134 1.00 107.11 ? 148 ASN C CG 1 ATOM 3774 O OD1 . ASN C 1 120 ? -5.596 77.505 76.572 1.00 109.72 ? 148 ASN C OD1 1 ATOM 3775 N ND2 . ASN C 1 120 ? -4.622 78.821 78.113 1.00 103.79 ? 148 ASN C ND2 1 ATOM 3776 N N . LYS C 1 121 ? -9.304 79.119 74.464 1.00 109.45 ? 149 LYS C N 1 ATOM 3777 C CA . LYS C 1 121 ? -10.689 78.632 74.537 1.00 106.10 ? 149 LYS C CA 1 ATOM 3778 C C . LYS C 1 121 ? -11.091 77.770 73.339 1.00 96.46 ? 149 LYS C C 1 ATOM 3779 O O . LYS C 1 121 ? -11.099 78.252 72.203 1.00 90.26 ? 149 LYS C O 1 ATOM 3780 C CB . LYS C 1 121 ? -11.643 79.829 74.587 1.00 111.14 ? 149 LYS C CB 1 ATOM 3781 C CG . LYS C 1 121 ? -11.001 81.139 75.022 1.00 117.73 ? 149 LYS C CG 1 ATOM 3782 C CD . LYS C 1 121 ? -10.673 81.185 76.489 1.00 124.56 ? 149 LYS C CD 1 ATOM 3783 C CE . LYS C 1 121 ? -9.805 82.400 76.771 1.00 128.90 ? 149 LYS C CE 1 ATOM 3784 N NZ . LYS C 1 121 ? -8.826 82.104 77.845 1.00 132.17 ? 149 LYS C NZ 1 ATOM 3785 N N . ILE C 1 122 ? -11.513 76.532 73.597 1.00 94.59 ? 150 ILE C N 1 ATOM 3786 C CA . ILE C 1 122 ? -11.888 75.589 72.529 1.00 89.72 ? 150 ILE C CA 1 ATOM 3787 C C . ILE C 1 122 ? -13.186 74.840 72.827 1.00 87.75 ? 150 ILE C C 1 ATOM 3788 O O . ILE C 1 122 ? -13.597 74.751 73.978 1.00 94.14 ? 150 ILE C O 1 ATOM 3789 C CB . ILE C 1 122 ? -10.792 74.524 72.312 1.00 84.28 ? 150 ILE C CB 1 ATOM 3790 C CG1 . ILE C 1 122 ? -10.647 73.649 73.567 1.00 70.04 ? 150 ILE C CG1 1 ATOM 3791 C CG2 . ILE C 1 122 ? -9.485 75.182 71.985 1.00 88.25 ? 150 ILE C CG2 1 ATOM 3792 C CD1 . ILE C 1 122 ? -9.541 72.605 73.487 1.00 55.98 ? 150 ILE C CD1 1 ATOM 3793 N N . ASN C 1 123 ? -13.824 74.299 71.788 1.00 85.34 ? 151 ASN C N 1 ATOM 3794 C CA . ASN C 1 123 ? -15.124 73.638 71.936 1.00 82.92 ? 151 ASN C CA 1 ATOM 3795 C C . ASN C 1 123 ? -15.032 72.124 71.854 1.00 87.31 ? 151 ASN C C 1 ATOM 3796 O O . ASN C 1 123 ? -14.267 71.576 71.064 1.00 88.75 ? 151 ASN C O 1 ATOM 3797 C CB . ASN C 1 123 ? -16.122 74.133 70.877 1.00 87.13 ? 151 ASN C CB 1 ATOM 3798 C CG . ASN C 1 123 ? -16.753 75.461 71.238 1.00 90.67 ? 151 ASN C CG 1 ATOM 3799 O OD1 . ASN C 1 123 ? -16.605 76.452 70.524 1.00 88.83 ? 151 ASN C OD1 1 ATOM 3800 N ND2 . ASN C 1 123 ? -17.486 75.480 72.346 1.00 91.73 ? 151 ASN C ND2 1 ATOM 3801 N N . VAL C 1 124 ? -15.804 71.452 72.700 1.00 86.88 ? 152 VAL C N 1 ATOM 3802 C CA . VAL C 1 124 ? -15.894 70.002 72.655 1.00 87.80 ? 152 VAL C CA 1 ATOM 3803 C C . VAL C 1 124 ? -16.386 69.610 71.258 1.00 88.44 ? 152 VAL C C 1 ATOM 3804 O O . VAL C 1 124 ? -17.237 70.304 70.670 1.00 86.24 ? 152 VAL C O 1 ATOM 3805 C CB . VAL C 1 124 ? -16.841 69.452 73.747 1.00 91.64 ? 152 VAL C CB 1 ATOM 3806 C CG1 . VAL C 1 124 ? -16.844 67.926 73.729 1.00 88.42 ? 152 VAL C CG1 1 ATOM 3807 C CG2 . VAL C 1 124 ? -16.409 69.946 75.124 1.00 90.58 ? 152 VAL C CG2 1 ATOM 3808 N N . SER C 1 125 ? -15.830 68.515 70.741 1.00 84.43 ? 153 SER C N 1 ATOM 3809 C CA . SER C 1 125 ? -16.128 67.983 69.407 1.00 85.34 ? 153 SER C CA 1 ATOM 3810 C C . SER C 1 125 ? -15.435 68.735 68.268 1.00 85.21 ? 153 SER C C 1 ATOM 3811 O O . SER C 1 125 ? -15.558 68.355 67.103 1.00 87.95 ? 153 SER C O 1 ATOM 3812 C CB . SER C 1 125 ? -17.639 67.885 69.147 1.00 85.15 ? 153 SER C CB 1 ATOM 3813 O OG . SER C 1 125 ? -18.079 66.540 69.196 1.00 91.46 ? 153 SER C OG 1 ATOM 3814 N N . GLN C 1 126 ? -14.701 69.791 68.598 1.00 81.54 ? 154 GLN C N 1 ATOM 3815 C CA . GLN C 1 126 ? -13.887 70.463 67.597 1.00 77.24 ? 154 GLN C CA 1 ATOM 3816 C C . GLN C 1 126 ? -12.717 69.581 67.166 1.00 80.93 ? 154 GLN C C 1 ATOM 3817 O O . GLN C 1 126 ? -12.082 68.916 67.989 1.00 77.65 ? 154 GLN C O 1 ATOM 3818 C CB . GLN C 1 126 ? -13.370 71.790 68.139 1.00 72.62 ? 154 GLN C CB 1 ATOM 3819 C CG . GLN C 1 126 ? -12.436 72.506 67.204 1.00 75.86 ? 154 GLN C CG 1 ATOM 3820 C CD . GLN C 1 126 ? -11.904 73.780 67.802 1.00 84.01 ? 154 GLN C CD 1 ATOM 3821 O OE1 . GLN C 1 126 ? -12.165 74.087 68.964 1.00 86.95 ? 154 GLN C OE1 1 ATOM 3822 N NE2 . GLN C 1 126 ? -11.140 74.528 67.015 1.00 86.65 ? 154 GLN C NE2 1 ATOM 3823 N N . THR C 1 127 ? -12.426 69.599 65.869 1.00 84.23 ? 155 THR C N 1 ATOM 3824 C CA . THR C 1 127 ? -11.328 68.819 65.314 1.00 73.99 ? 155 THR C CA 1 ATOM 3825 C C . THR C 1 127 ? -10.098 69.693 65.195 1.00 63.89 ? 155 THR C C 1 ATOM 3826 O O . THR C 1 127 ? -10.171 70.799 64.668 1.00 73.35 ? 155 THR C O 1 ATOM 3827 C CB . THR C 1 127 ? -11.678 68.263 63.926 1.00 71.24 ? 155 THR C CB 1 ATOM 3828 O OG1 . THR C 1 127 ? -12.127 69.337 63.088 1.00 73.19 ? 155 THR C OG1 1 ATOM 3829 C CG2 . THR C 1 127 ? -12.783 67.224 64.031 1.00 69.90 ? 155 THR C CG2 1 ATOM 3830 N N . LEU C 1 128 ? -8.975 69.197 65.705 1.00 54.16 ? 156 LEU C N 1 ATOM 3831 C CA . LEU C 1 128 ? -7.720 69.928 65.645 1.00 54.90 ? 156 LEU C CA 1 ATOM 3832 C C . LEU C 1 128 ? -6.690 69.143 64.842 1.00 54.59 ? 156 LEU C C 1 ATOM 3833 O O . LEU C 1 128 ? -6.552 67.933 65.018 1.00 55.37 ? 156 LEU C O 1 ATOM 3834 C CB . LEU C 1 128 ? -7.172 70.181 67.047 1.00 58.36 ? 156 LEU C CB 1 ATOM 3835 C CG . LEU C 1 128 ? -8.088 70.938 68.013 1.00 60.84 ? 156 LEU C CG 1 ATOM 3836 C CD1 . LEU C 1 128 ? -7.461 70.952 69.393 1.00 64.86 ? 156 LEU C CD1 1 ATOM 3837 C CD2 . LEU C 1 128 ? -8.385 72.350 67.527 1.00 47.79 ? 156 LEU C CD2 1 ATOM 3838 N N . TRP C 1 129 ? -5.990 69.845 63.954 1.00 52.41 ? 157 TRP C N 1 ATOM 3839 C CA . TRP C 1 129 ? -4.828 69.313 63.259 1.00 55.15 ? 157 TRP C CA 1 ATOM 3840 C C . TRP C 1 129 ? -3.619 69.405 64.182 1.00 53.16 ? 157 TRP C C 1 ATOM 3841 O O . TRP C 1 129 ? -3.296 70.473 64.703 1.00 54.61 ? 157 TRP C O 1 ATOM 3842 C CB . TRP C 1 129 ? -4.556 70.106 61.965 1.00 59.30 ? 157 TRP C CB 1 ATOM 3843 C CG . TRP C 1 129 ? -3.210 69.798 61.326 1.00 50.22 ? 157 TRP C CG 1 ATOM 3844 C CD1 . TRP C 1 129 ? -2.552 68.590 61.321 1.00 47.14 ? 157 TRP C CD1 1 ATOM 3845 C CD2 . TRP C 1 129 ? -2.360 70.713 60.631 1.00 49.96 ? 157 TRP C CD2 1 ATOM 3846 N NE1 . TRP C 1 129 ? -1.354 68.701 60.661 1.00 41.83 ? 157 TRP C NE1 1 ATOM 3847 C CE2 . TRP C 1 129 ? -1.210 69.995 60.224 1.00 45.59 ? 157 TRP C CE2 1 ATOM 3848 C CE3 . TRP C 1 129 ? -2.457 72.073 60.304 1.00 47.58 ? 157 TRP C CE3 1 ATOM 3849 C CZ2 . TRP C 1 129 ? -0.174 70.588 59.511 1.00 44.63 ? 157 TRP C CZ2 1 ATOM 3850 C CZ3 . TRP C 1 129 ? -1.424 72.663 59.598 1.00 46.04 ? 157 TRP C CZ3 1 ATOM 3851 C CH2 . TRP C 1 129 ? -0.296 71.920 59.205 1.00 47.69 ? 157 TRP C CH2 1 ATOM 3852 N N . ILE C 1 130 ? -2.972 68.268 64.398 1.00 54.67 ? 158 ILE C N 1 ATOM 3853 C CA . ILE C 1 130 ? -1.756 68.210 65.196 1.00 55.40 ? 158 ILE C CA 1 ATOM 3854 C C . ILE C 1 130 ? -0.527 68.250 64.285 1.00 56.60 ? 158 ILE C C 1 ATOM 3855 O O . ILE C 1 130 ? -0.234 67.284 63.584 1.00 51.71 ? 158 ILE C O 1 ATOM 3856 C CB . ILE C 1 130 ? -1.736 66.926 66.039 1.00 50.55 ? 158 ILE C CB 1 ATOM 3857 C CG1 . ILE C 1 130 ? -2.996 66.852 66.909 1.00 51.84 ? 158 ILE C CG1 1 ATOM 3858 C CG2 . ILE C 1 130 ? -0.477 66.845 66.883 1.00 47.06 ? 158 ILE C CG2 1 ATOM 3859 C CD1 . ILE C 1 130 ? -3.158 68.017 67.861 1.00 51.31 ? 158 ILE C CD1 1 ATOM 3860 N N . PRO C 1 131 ? 0.193 69.380 64.290 1.00 56.83 ? 159 PRO C N 1 ATOM 3861 C CA . PRO C 1 131 ? 1.338 69.537 63.388 1.00 54.20 ? 159 PRO C CA 1 ATOM 3862 C C . PRO C 1 131 ? 2.628 68.968 63.961 1.00 46.90 ? 159 PRO C C 1 ATOM 3863 O O . PRO C 1 131 ? 3.513 69.731 64.363 1.00 45.71 ? 159 PRO C O 1 ATOM 3864 C CB . PRO C 1 131 ? 1.454 71.057 63.253 1.00 50.75 ? 159 PRO C CB 1 ATOM 3865 C CG . PRO C 1 131 ? 0.986 71.569 64.551 1.00 50.11 ? 159 PRO C CG 1 ATOM 3866 C CD . PRO C 1 131 ? -0.093 70.618 65.034 1.00 53.04 ? 159 PRO C CD 1 ATOM 3867 N N . LEU C 1 132 ? 2.736 67.644 63.988 1.00 37.79 ? 160 LEU C N 1 ATOM 3868 C CA . LEU C 1 132 ? 3.976 67.002 64.406 1.00 46.06 ? 160 LEU C CA 1 ATOM 3869 C C . LEU C 1 132 ? 5.139 67.548 63.581 1.00 55.95 ? 160 LEU C C 1 ATOM 3870 O O . LEU C 1 132 ? 5.016 67.731 62.365 1.00 51.73 ? 160 LEU C O 1 ATOM 3871 C CB . LEU C 1 132 ? 3.897 65.482 64.248 1.00 39.33 ? 160 LEU C CB 1 ATOM 3872 C CG . LEU C 1 132 ? 2.716 64.783 64.916 1.00 55.60 ? 160 LEU C CG 1 ATOM 3873 C CD1 . LEU C 1 132 ? 2.684 63.295 64.543 1.00 46.55 ? 160 LEU C CD1 1 ATOM 3874 C CD2 . LEU C 1 132 ? 2.780 64.980 66.425 1.00 61.08 ? 160 LEU C CD2 1 ATOM 3875 N N . PRO C 1 133 ? 6.273 67.807 64.244 1.00 56.17 ? 161 PRO C N 1 ATOM 3876 C CA . PRO C 1 133 ? 7.461 68.348 63.580 1.00 50.13 ? 161 PRO C CA 1 ATOM 3877 C C . PRO C 1 133 ? 8.139 67.323 62.676 1.00 51.86 ? 161 PRO C C 1 ATOM 3878 O O . PRO C 1 133 ? 8.282 66.152 63.035 1.00 53.76 ? 161 PRO C O 1 ATOM 3879 C CB . PRO C 1 133 ? 8.389 68.670 64.748 1.00 53.92 ? 161 PRO C CB 1 ATOM 3880 C CG . PRO C 1 133 ? 8.016 67.666 65.813 1.00 51.97 ? 161 PRO C CG 1 ATOM 3881 C CD . PRO C 1 133 ? 6.538 67.415 65.643 1.00 52.78 ? 161 PRO C CD 1 ATOM 3882 N N . CYS C 1 134 ? 8.574 67.771 61.511 1.00 44.19 ? 162 CYS C N 1 ATOM 3883 C CA . CYS C 1 134 ? 9.244 66.893 60.560 1.00 47.24 ? 162 CYS C CA 1 ATOM 3884 C C . CYS C 1 134 ? 10.017 67.776 59.598 1.00 51.64 ? 162 CYS C C 1 ATOM 3885 O O . CYS C 1 134 ? 9.983 68.998 59.706 1.00 47.75 ? 162 CYS C O 1 ATOM 3886 C CB . CYS C 1 134 ? 8.234 66.032 59.795 1.00 29.48 ? 162 CYS C CB 1 ATOM 3887 S SG . CYS C 1 134 ? 7.009 67.001 58.879 1.00 45.88 ? 162 CYS C SG 1 ATOM 3888 N N . SER C 1 135 ? 10.713 67.153 58.662 1.00 54.13 ? 163 SER C N 1 ATOM 3889 C CA . SER C 1 135 ? 11.451 67.885 57.645 1.00 53.46 ? 163 SER C CA 1 ATOM 3890 C C . SER C 1 135 ? 11.688 66.973 56.460 1.00 53.24 ? 163 SER C C 1 ATOM 3891 O O . SER C 1 135 ? 11.607 65.749 56.581 1.00 45.36 ? 163 SER C O 1 ATOM 3892 C CB . SER C 1 135 ? 12.795 68.368 58.193 1.00 52.76 ? 163 SER C CB 1 ATOM 3893 O OG . SER C 1 135 ? 13.535 69.031 57.187 1.00 50.63 ? 163 SER C OG 1 ATOM 3894 N N . CYS C 1 136 ? 11.982 67.571 55.315 1.00 53.25 ? 164 CYS C N 1 ATOM 3895 C CA . CYS C 1 136 ? 12.376 66.800 54.155 1.00 45.98 ? 164 CYS C CA 1 ATOM 3896 C C . CYS C 1 136 ? 13.793 67.192 53.740 1.00 47.31 ? 164 CYS C C 1 ATOM 3897 O O . CYS C 1 136 ? 14.283 66.764 52.697 1.00 46.98 ? 164 CYS C O 1 ATOM 3898 C CB . CYS C 1 136 ? 11.383 67.019 53.005 1.00 45.76 ? 164 CYS C CB 1 ATOM 3899 S SG . CYS C 1 136 ? 9.624 66.577 53.347 1.00 56.04 ? 164 CYS C SG 1 ATOM 3900 N N . ASP C 1 137 ? 14.457 67.991 54.575 1.00 45.65 ? 165 ASP C N 1 ATOM 3901 C CA . ASP C 1 137 ? 15.817 68.434 54.277 1.00 46.51 ? 165 ASP C CA 1 ATOM 3902 C C . ASP C 1 137 ? 16.734 67.261 54.203 1.00 49.34 ? 165 ASP C C 1 ATOM 3903 O O . ASP C 1 137 ? 16.613 66.311 54.978 1.00 48.88 ? 165 ASP C O 1 ATOM 3904 C CB . ASP C 1 137 ? 16.365 69.355 55.364 1.00 43.30 ? 165 ASP C CB 1 ATOM 3905 C CG . ASP C 1 137 ? 15.740 70.723 55.331 1.00 49.67 ? 165 ASP C CG 1 ATOM 3906 O OD1 . ASP C 1 137 ? 15.284 71.144 54.245 1.00 42.81 ? 165 ASP C OD1 1 ATOM 3907 O OD2 . ASP C 1 137 ? 15.699 71.374 56.398 1.00 54.72 ? 165 ASP C OD2 1 ATOM 3908 N N . LYS C 1 138 ? 17.679 67.346 53.280 1.00 59.48 ? 166 LYS C N 1 ATOM 3909 C CA . LYS C 1 138 ? 18.796 66.431 53.277 1.00 58.19 ? 166 LYS C CA 1 ATOM 3910 C C . LYS C 1 138 ? 19.712 66.820 54.416 1.00 55.33 ? 166 LYS C C 1 ATOM 3911 O O . LYS C 1 138 ? 19.653 67.942 54.920 1.00 49.08 ? 166 LYS C O 1 ATOM 3912 C CB . LYS C 1 138 ? 19.559 66.538 51.976 1.00 51.67 ? 166 LYS C CB 1 ATOM 3913 C CG . LYS C 1 138 ? 18.894 65.878 50.812 1.00 48.64 ? 166 LYS C CG 1 ATOM 3914 C CD . LYS C 1 138 ? 19.640 66.277 49.551 1.00 51.59 ? 166 LYS C CD 1 ATOM 3915 C CE . LYS C 1 138 ? 19.037 65.646 48.327 1.00 54.92 ? 166 LYS C CE 1 ATOM 3916 N NZ . LYS C 1 138 ? 19.955 64.575 47.817 1.00 55.08 ? 166 LYS C NZ 1 ATOM 3917 N N . GLU C 1 139 ? 20.553 65.884 54.826 1.00 60.58 ? 167 GLU C N 1 ATOM 3918 C CA . GLU C 1 139 ? 21.558 66.186 55.825 1.00 68.99 ? 167 GLU C CA 1 ATOM 3919 C C . GLU C 1 139 ? 22.926 66.172 55.174 1.00 65.72 ? 167 GLU C C 1 ATOM 3920 O O . GLU C 1 139 ? 23.444 65.112 54.831 1.00 60.72 ? 167 GLU C O 1 ATOM 3921 C CB . GLU C 1 139 ? 21.493 65.204 57.001 1.00 66.62 ? 167 GLU C CB 1 ATOM 3922 C CG . GLU C 1 139 ? 22.411 65.565 58.164 1.00 57.51 ? 167 GLU C CG 1 ATOM 3923 C CD . GLU C 1 139 ? 22.234 67.003 58.636 1.00 64.30 ? 167 GLU C CD 1 ATOM 3924 O OE1 . GLU C 1 139 ? 23.225 67.606 59.097 1.00 64.18 ? 167 GLU C OE1 1 ATOM 3925 O OE2 . GLU C 1 139 ? 21.107 67.539 58.560 1.00 71.85 ? 167 GLU C OE2 1 ATOM 3926 N N . GLU C 1 140 ? 23.476 67.362 54.971 1.00 71.23 ? 168 GLU C N 1 ATOM 3927 C CA . GLU C 1 140 ? 24.784 67.522 54.343 1.00 82.07 ? 168 GLU C CA 1 ATOM 3928 C C . GLU C 1 140 ? 24.912 66.720 53.035 1.00 80.38 ? 168 GLU C C 1 ATOM 3929 O O . GLU C 1 140 ? 25.867 65.967 52.843 1.00 74.70 ? 168 GLU C O 1 ATOM 3930 C CB . GLU C 1 140 ? 25.889 67.132 55.329 1.00 86.39 ? 168 GLU C CB 1 ATOM 3931 C CG . GLU C 1 140 ? 26.275 68.237 56.305 1.00 94.46 ? 168 GLU C CG 1 ATOM 3932 C CD . GLU C 1 140 ? 26.603 69.554 55.619 1.00 107.48 ? 168 GLU C CD 1 ATOM 3933 O OE1 . GLU C 1 140 ? 27.762 69.732 55.192 1.00 111.28 ? 168 GLU C OE1 1 ATOM 3934 O OE2 . GLU C 1 140 ? 25.704 70.417 55.510 1.00 111.40 ? 168 GLU C OE2 1 ATOM 3935 N N . GLY C 1 141 ? 23.932 66.880 52.150 1.00 79.39 ? 169 GLY C N 1 ATOM 3936 C CA . GLY C 1 141 ? 23.950 66.232 50.849 1.00 69.28 ? 169 GLY C CA 1 ATOM 3937 C C . GLY C 1 141 ? 23.371 64.827 50.838 1.00 71.41 ? 169 GLY C C 1 ATOM 3938 O O . GLY C 1 141 ? 23.185 64.240 49.771 1.00 78.60 ? 169 GLY C O 1 ATOM 3939 N N . SER C 1 142 ? 23.062 64.288 52.015 1.00 63.06 ? 170 SER C N 1 ATOM 3940 C CA . SER C 1 142 ? 22.589 62.912 52.108 1.00 62.12 ? 170 SER C CA 1 ATOM 3941 C C . SER C 1 142 ? 21.097 62.815 52.405 1.00 66.02 ? 170 SER C C 1 ATOM 3942 O O . SER C 1 142 ? 20.543 63.652 53.118 1.00 72.49 ? 170 SER C O 1 ATOM 3943 C CB . SER C 1 142 ? 23.360 62.169 53.200 1.00 66.41 ? 170 SER C CB 1 ATOM 3944 O OG . SER C 1 142 ? 24.756 62.272 52.995 1.00 80.40 ? 170 SER C OG 1 ATOM 3945 N N . ASN C 1 143 ? 20.468 61.757 51.898 1.00 57.84 ? 171 ASN C N 1 ATOM 3946 C CA . ASN C 1 143 ? 19.053 61.517 52.134 1.00 53.96 ? 171 ASN C CA 1 ATOM 3947 C C . ASN C 1 143 ? 18.847 60.861 53.491 1.00 61.80 ? 171 ASN C C 1 ATOM 3948 O O . ASN C 1 143 ? 19.450 59.830 53.790 1.00 59.17 ? 171 ASN C O 1 ATOM 3949 C CB . ASN C 1 143 ? 18.459 60.636 51.031 1.00 48.42 ? 171 ASN C CB 1 ATOM 3950 C CG . ASN C 1 143 ? 18.347 61.357 49.704 1.00 52.45 ? 171 ASN C CG 1 ATOM 3951 O OD1 . ASN C 1 143 ? 18.357 62.591 49.646 1.00 59.93 ? 171 ASN C OD1 1 ATOM 3952 N ND2 . ASN C 1 143 ? 18.257 60.591 48.622 1.00 51.87 ? 171 ASN C ND2 1 ATOM 3953 N N . VAL C 1 144 ? 17.951 61.433 54.287 1.00 65.93 ? 172 VAL C N 1 ATOM 3954 C CA . VAL C 1 144 ? 17.714 60.956 55.638 1.00 63.17 ? 172 VAL C CA 1 ATOM 3955 C C . VAL C 1 144 ? 16.207 60.872 55.885 1.00 59.07 ? 172 VAL C C 1 ATOM 3956 O O . VAL C 1 144 ? 15.430 61.502 55.176 1.00 54.84 ? 172 VAL C O 1 ATOM 3957 C CB . VAL C 1 144 ? 18.352 61.919 56.675 1.00 68.72 ? 172 VAL C CB 1 ATOM 3958 C CG1 . VAL C 1 144 ? 19.874 61.764 56.692 1.00 62.58 ? 172 VAL C CG1 1 ATOM 3959 C CG2 . VAL C 1 144 ? 17.990 63.364 56.358 1.00 65.98 ? 172 VAL C CG2 1 ATOM 3960 N N . MET C 1 145 ? 15.782 60.067 56.854 1.00 53.36 ? 173 MET C N 1 ATOM 3961 C CA . MET C 1 145 ? 14.413 60.194 57.353 1.00 44.82 ? 173 MET C CA 1 ATOM 3962 C C . MET C 1 145 ? 14.471 60.866 58.701 1.00 49.99 ? 173 MET C C 1 ATOM 3963 O O . MET C 1 145 ? 15.086 60.347 59.631 1.00 60.67 ? 173 MET C O 1 ATOM 3964 C CB . MET C 1 145 ? 13.693 58.851 57.479 1.00 44.88 ? 173 MET C CB 1 ATOM 3965 C CG . MET C 1 145 ? 12.168 59.018 57.663 1.00 39.40 ? 173 MET C CG 1 ATOM 3966 S SD . MET C 1 145 ? 11.319 57.644 58.469 1.00 89.16 ? 173 MET C SD 1 ATOM 3967 C CE . MET C 1 145 ? 12.695 56.549 58.828 1.00 112.20 ? 173 MET C CE 1 ATOM 3968 N N . HIS C 1 146 ? 13.828 62.022 58.814 1.00 39.51 ? 174 HIS C N 1 ATOM 3969 C CA . HIS C 1 146 ? 13.836 62.744 60.066 1.00 46.96 ? 174 HIS C CA 1 ATOM 3970 C C . HIS C 1 146 ? 12.964 62.019 61.091 1.00 56.01 ? 174 HIS C C 1 ATOM 3971 O O . HIS C 1 146 ? 11.835 61.614 60.793 1.00 59.60 ? 174 HIS C O 1 ATOM 3972 C CB . HIS C 1 146 ? 13.390 64.198 59.869 1.00 52.51 ? 174 HIS C CB 1 ATOM 3973 C CG . HIS C 1 146 ? 14.360 65.017 59.070 1.00 61.55 ? 174 HIS C CG 1 ATOM 3974 N ND1 . HIS C 1 146 ? 15.352 65.769 59.652 1.00 60.32 ? 174 HIS C ND1 1 ATOM 3975 C CD2 . HIS C 1 146 ? 14.486 65.190 57.731 1.00 67.21 ? 174 HIS C CD2 1 ATOM 3976 C CE1 . HIS C 1 146 ? 16.057 66.370 58.707 1.00 69.09 ? 174 HIS C CE1 1 ATOM 3977 N NE2 . HIS C 1 146 ? 15.551 66.036 57.536 1.00 69.46 ? 174 HIS C NE2 1 ATOM 3978 N N . LEU C 1 147 ? 13.527 61.803 62.278 1.00 60.87 ? 175 LEU C N 1 ATOM 3979 C CA . LEU C 1 147 ? 12.806 61.188 63.389 1.00 53.93 ? 175 LEU C CA 1 ATOM 3980 C C . LEU C 1 147 ? 12.732 62.176 64.539 1.00 52.67 ? 175 LEU C C 1 ATOM 3981 O O . LEU C 1 147 ? 13.757 62.628 65.034 1.00 54.59 ? 175 LEU C O 1 ATOM 3982 C CB . LEU C 1 147 ? 13.527 59.926 63.849 1.00 52.80 ? 175 LEU C CB 1 ATOM 3983 C CG . LEU C 1 147 ? 12.960 59.214 65.076 1.00 57.66 ? 175 LEU C CG 1 ATOM 3984 C CD1 . LEU C 1 147 ? 11.588 58.604 64.777 1.00 58.60 ? 175 LEU C CD1 1 ATOM 3985 C CD2 . LEU C 1 147 ? 13.948 58.158 65.570 1.00 57.55 ? 175 LEU C CD2 1 ATOM 3986 N N . ALA C 1 148 ? 11.523 62.492 64.985 1.00 54.79 ? 176 ALA C N 1 ATOM 3987 C CA . ALA C 1 148 ? 11.363 63.385 66.119 1.00 57.60 ? 176 ALA C CA 1 ATOM 3988 C C . ALA C 1 148 ? 11.538 62.595 67.425 1.00 59.92 ? 176 ALA C C 1 ATOM 3989 O O . ALA C 1 148 ? 10.911 61.560 67.613 1.00 60.93 ? 176 ALA C O 1 ATOM 3990 C CB . ALA C 1 148 ? 10.013 64.065 66.062 1.00 54.71 ? 176 ALA C CB 1 ATOM 3991 N N . TYR C 1 149 ? 12.425 63.069 68.299 1.00 59.96 ? 177 TYR C N 1 ATOM 3992 C CA . TYR C 1 149 ? 12.812 62.333 69.497 1.00 64.22 ? 177 TYR C CA 1 ATOM 3993 C C . TYR C 1 149 ? 12.649 63.199 70.736 1.00 71.14 ? 177 TYR C C 1 ATOM 3994 O O . TYR C 1 149 ? 13.203 64.297 70.812 1.00 69.74 ? 177 TYR C O 1 ATOM 3995 C CB . TYR C 1 149 ? 14.276 61.896 69.381 1.00 72.31 ? 177 TYR C CB 1 ATOM 3996 C CG . TYR C 1 149 ? 14.778 60.957 70.464 1.00 76.90 ? 177 TYR C CG 1 ATOM 3997 C CD1 . TYR C 1 149 ? 15.173 61.428 71.714 1.00 83.00 ? 177 TYR C CD1 1 ATOM 3998 C CD2 . TYR C 1 149 ? 14.886 59.595 70.218 1.00 77.06 ? 177 TYR C CD2 1 ATOM 3999 C CE1 . TYR C 1 149 ? 15.640 60.558 72.695 1.00 83.75 ? 177 TYR C CE1 1 ATOM 4000 C CE2 . TYR C 1 149 ? 15.350 58.720 71.187 1.00 81.48 ? 177 TYR C CE2 1 ATOM 4001 C CZ . TYR C 1 149 ? 15.727 59.203 72.422 1.00 83.02 ? 177 TYR C CZ 1 ATOM 4002 O OH . TYR C 1 149 ? 16.187 58.319 73.374 1.00 78.82 ? 177 TYR C OH 1 ATOM 4003 N N . SER C 1 150 ? 11.881 62.709 71.705 1.00 73.17 ? 178 SER C N 1 ATOM 4004 C CA . SER C 1 150 ? 11.788 63.372 72.996 1.00 69.40 ? 178 SER C CA 1 ATOM 4005 C C . SER C 1 150 ? 12.884 62.771 73.863 1.00 68.88 ? 178 SER C C 1 ATOM 4006 O O . SER C 1 150 ? 12.878 61.572 74.144 1.00 54.19 ? 178 SER C O 1 ATOM 4007 C CB . SER C 1 150 ? 10.421 63.164 73.635 1.00 68.79 ? 178 SER C CB 1 ATOM 4008 O OG . SER C 1 150 ? 10.325 63.841 74.878 1.00 63.59 ? 178 SER C OG 1 ATOM 4009 N N . VAL C 1 151 ? 13.820 63.620 74.274 1.00 74.49 ? 179 VAL C N 1 ATOM 4010 C CA . VAL C 1 151 ? 15.011 63.207 75.016 1.00 79.28 ? 179 VAL C CA 1 ATOM 4011 C C . VAL C 1 151 ? 14.710 62.559 76.367 1.00 71.76 ? 179 VAL C C 1 ATOM 4012 O O . VAL C 1 151 ? 14.022 63.158 77.202 1.00 62.62 ? 179 VAL C O 1 ATOM 4013 C CB . VAL C 1 151 ? 15.919 64.429 75.287 1.00 84.25 ? 179 VAL C CB 1 ATOM 4014 C CG1 . VAL C 1 151 ? 17.062 64.052 76.222 1.00 85.06 ? 179 VAL C CG1 1 ATOM 4015 C CG2 . VAL C 1 151 ? 16.443 65.012 73.979 1.00 84.85 ? 179 VAL C CG2 1 ATOM 4016 N N . GLY C 1 152 ? 15.209 61.336 76.568 1.00 70.56 ? 180 GLY C N 1 ATOM 4017 C CA . GLY C 1 152 ? 15.096 60.674 77.858 1.00 82.82 ? 180 GLY C CA 1 ATOM 4018 C C . GLY C 1 152 ? 16.259 61.077 78.745 1.00 92.77 ? 180 GLY C C 1 ATOM 4019 O O . GLY C 1 152 ? 17.355 61.314 78.241 1.00 90.33 ? 180 GLY C O 1 ATOM 4020 N N . LYS C 1 153 ? 16.037 61.128 80.059 1.00 100.80 ? 181 LYS C N 1 ATOM 4021 C CA . LYS C 1 153 ? 17.091 61.517 81.004 1.00 98.41 ? 181 LYS C CA 1 ATOM 4022 C C . LYS C 1 153 ? 18.150 60.428 81.151 1.00 91.31 ? 181 LYS C C 1 ATOM 4023 O O . LYS C 1 153 ? 17.828 59.281 81.458 1.00 88.06 ? 181 LYS C O 1 ATOM 4024 C CB . LYS C 1 153 ? 16.494 61.864 82.369 1.00 95.14 ? 181 LYS C CB 1 ATOM 4025 C CG . LYS C 1 153 ? 17.298 62.888 83.187 1.00 97.93 ? 181 LYS C CG 1 ATOM 4026 C CD . LYS C 1 153 ? 17.212 64.304 82.603 1.00 100.33 ? 181 LYS C CD 1 ATOM 4027 C CE . LYS C 1 153 ? 18.558 65.021 82.597 1.00 99.17 ? 181 LYS C CE 1 ATOM 4028 N NZ . LYS C 1 153 ? 19.664 64.173 82.083 1.00 96.09 ? 181 LYS C NZ 1 ATOM 4029 N N . ASN C 1 156 ? 21.891 63.731 78.242 1.00 126.94 ? 184 ASN C N 1 ATOM 4030 C CA . ASN C 1 156 ? 23.008 63.284 77.418 1.00 129.96 ? 184 ASN C CA 1 ATOM 4031 C C . ASN C 1 156 ? 22.665 63.339 75.930 1.00 132.41 ? 184 ASN C C 1 ATOM 4032 O O . ASN C 1 156 ? 21.496 63.281 75.559 1.00 138.81 ? 184 ASN C O 1 ATOM 4033 C CB . ASN C 1 156 ? 23.441 61.875 77.845 1.00 129.17 ? 184 ASN C CB 1 ATOM 4034 C CG . ASN C 1 156 ? 23.768 60.974 76.672 1.00 128.40 ? 184 ASN C CG 1 ATOM 4035 O OD1 . ASN C 1 156 ? 24.831 61.089 76.061 1.00 127.81 ? 184 ASN C OD1 1 ATOM 4036 N ND2 . ASN C 1 156 ? 22.845 60.080 76.341 1.00 127.53 ? 184 ASN C ND2 1 ATOM 4037 N N . THR C 1 157 ? 23.683 63.436 75.080 1.00 125.75 ? 185 THR C N 1 ATOM 4038 C CA . THR C 1 157 ? 23.471 63.589 73.645 1.00 117.17 ? 185 THR C CA 1 ATOM 4039 C C . THR C 1 157 ? 24.273 62.555 72.874 1.00 115.95 ? 185 THR C C 1 ATOM 4040 O O . THR C 1 157 ? 23.912 62.168 71.763 1.00 118.31 ? 185 THR C O 1 ATOM 4041 C CB . THR C 1 157 ? 23.887 64.988 73.160 1.00 111.42 ? 185 THR C CB 1 ATOM 4042 O OG1 . THR C 1 157 ? 25.237 65.246 73.563 1.00 112.55 ? 185 THR C OG1 1 ATOM 4043 C CG2 . THR C 1 157 ? 22.984 66.049 73.751 1.00 108.25 ? 185 THR C CG2 1 ATOM 4044 N N . SER C 1 158 ? 25.362 62.106 73.484 1.00 109.84 ? 186 SER C N 1 ATOM 4045 C CA . SER C 1 158 ? 26.244 61.131 72.867 1.00 104.42 ? 186 SER C CA 1 ATOM 4046 C C . SER C 1 158 ? 25.529 59.812 72.594 1.00 100.91 ? 186 SER C C 1 ATOM 4047 O O . SER C 1 158 ? 25.542 59.309 71.469 1.00 99.66 ? 186 SER C O 1 ATOM 4048 C CB . SER C 1 158 ? 27.467 60.893 73.758 1.00 103.47 ? 186 SER C CB 1 ATOM 4049 O OG . SER C 1 158 ? 28.411 60.046 73.125 1.00 101.51 ? 186 SER C OG 1 ATOM 4050 N N . ALA C 1 159 ? 24.899 59.255 73.621 1.00 98.32 ? 187 ALA C N 1 ATOM 4051 C CA . ALA C 1 159 ? 24.264 57.951 73.486 1.00 97.12 ? 187 ALA C CA 1 ATOM 4052 C C . ALA C 1 159 ? 23.089 57.990 72.517 1.00 91.75 ? 187 ALA C C 1 ATOM 4053 O O . ALA C 1 159 ? 22.847 57.023 71.800 1.00 90.23 ? 187 ALA C O 1 ATOM 4054 C CB . ALA C 1 159 ? 23.825 57.418 74.848 1.00 95.77 ? 187 ALA C CB 1 ATOM 4055 N N . ILE C 1 160 ? 22.376 59.114 72.487 1.00 89.02 ? 188 ILE C N 1 ATOM 4056 C CA . ILE C 1 160 ? 21.245 59.281 71.577 1.00 84.80 ? 188 ILE C CA 1 ATOM 4057 C C . ILE C 1 160 ? 21.730 59.251 70.135 1.00 85.85 ? 188 ILE C C 1 ATOM 4058 O O . ILE C 1 160 ? 21.190 58.520 69.298 1.00 81.71 ? 188 ILE C O 1 ATOM 4059 C CB . ILE C 1 160 ? 20.507 60.603 71.830 1.00 75.44 ? 188 ILE C CB 1 ATOM 4060 C CG1 . ILE C 1 160 ? 19.743 60.542 73.157 1.00 67.69 ? 188 ILE C CG1 1 ATOM 4061 C CG2 . ILE C 1 160 ? 19.573 60.922 70.669 1.00 74.61 ? 188 ILE C CG2 1 ATOM 4062 C CD1 . ILE C 1 160 ? 19.201 61.880 73.619 1.00 62.71 ? 188 ILE C CD1 1 ATOM 4063 N N . ALA C 1 161 ? 22.753 60.058 69.862 1.00 84.61 ? 189 ALA C N 1 ATOM 4064 C CA . ALA C 1 161 ? 23.401 60.086 68.557 1.00 85.78 ? 189 ALA C CA 1 ATOM 4065 C C . ALA C 1 161 ? 23.948 58.700 68.212 1.00 87.74 ? 189 ALA C C 1 ATOM 4066 O O . ALA C 1 161 ? 23.822 58.235 67.081 1.00 84.86 ? 189 ALA C O 1 ATOM 4067 C CB . ALA C 1 161 ? 24.507 61.129 68.535 1.00 81.18 ? 189 ALA C CB 1 ATOM 4068 N N . ALA C 1 162 ? 24.584 58.061 69.190 1.00 91.10 ? 190 ALA C N 1 ATOM 4069 C CA . ALA C 1 162 ? 25.139 56.725 69.005 1.00 94.85 ? 190 ALA C CA 1 ATOM 4070 C C . ALA C 1 162 ? 24.032 55.702 68.772 1.00 89.87 ? 190 ALA C C 1 ATOM 4071 O O . ALA C 1 162 ? 24.140 54.837 67.898 1.00 84.08 ? 190 ALA C O 1 ATOM 4072 C CB . ALA C 1 162 ? 25.988 56.327 70.203 1.00 98.26 ? 190 ALA C CB 1 ATOM 4073 N N . LYS C 1 163 ? 22.966 55.821 69.560 1.00 94.43 ? 191 LYS C N 1 ATOM 4074 C CA . LYS C 1 163 ? 21.819 54.922 69.470 1.00 98.97 ? 191 LYS C CA 1 ATOM 4075 C C . LYS C 1 163 ? 21.272 54.881 68.049 1.00 103.75 ? 191 LYS C C 1 ATOM 4076 O O . LYS C 1 163 ? 20.862 53.827 67.558 1.00 105.34 ? 191 LYS C O 1 ATOM 4077 C CB . LYS C 1 163 ? 20.722 55.366 70.452 1.00 94.19 ? 191 LYS C CB 1 ATOM 4078 C CG . LYS C 1 163 ? 19.374 54.698 70.260 1.00 91.36 ? 191 LYS C CG 1 ATOM 4079 C CD . LYS C 1 163 ? 18.452 54.930 71.451 1.00 87.65 ? 191 LYS C CD 1 ATOM 4080 C CE . LYS C 1 163 ? 17.075 54.327 71.182 1.00 86.40 ? 191 LYS C CE 1 ATOM 4081 N NZ . LYS C 1 163 ? 16.148 54.419 72.342 1.00 81.80 ? 191 LYS C NZ 1 ATOM 4082 N N . TYR C 1 164 ? 21.314 56.034 67.385 1.00 100.81 ? 192 TYR C N 1 ATOM 4083 C CA . TYR C 1 164 ? 20.802 56.178 66.025 1.00 94.00 ? 192 TYR C CA 1 ATOM 4084 C C . TYR C 1 164 ? 21.870 56.318 64.936 1.00 93.76 ? 192 TYR C C 1 ATOM 4085 O O . TYR C 1 164 ? 21.570 56.754 63.824 1.00 89.06 ? 192 TYR C O 1 ATOM 4086 C CB . TYR C 1 164 ? 19.805 57.330 65.959 1.00 85.81 ? 192 TYR C CB 1 ATOM 4087 C CG . TYR C 1 164 ? 18.525 57.052 66.702 1.00 78.03 ? 192 TYR C CG 1 ATOM 4088 C CD1 . TYR C 1 164 ? 17.626 56.100 66.244 1.00 72.50 ? 192 TYR C CD1 1 ATOM 4089 C CD2 . TYR C 1 164 ? 18.224 57.730 67.872 1.00 74.36 ? 192 TYR C CD2 1 ATOM 4090 C CE1 . TYR C 1 164 ? 16.451 55.847 66.927 1.00 74.01 ? 192 TYR C CE1 1 ATOM 4091 C CE2 . TYR C 1 164 ? 17.057 57.482 68.562 1.00 71.20 ? 192 TYR C CE2 1 ATOM 4092 C CZ . TYR C 1 164 ? 16.172 56.542 68.087 1.00 72.91 ? 192 TYR C CZ 1 ATOM 4093 O OH . TYR C 1 164 ? 15.009 56.297 68.780 1.00 75.24 ? 192 TYR C OH 1 ATOM 4094 N N . GLY C 1 165 ? 23.115 55.995 65.271 1.00 93.41 ? 193 GLY C N 1 ATOM 4095 C CA . GLY C 1 165 ? 24.176 55.977 64.282 1.00 92.10 ? 193 GLY C CA 1 ATOM 4096 C C . GLY C 1 165 ? 24.401 57.315 63.606 1.00 85.99 ? 193 GLY C C 1 ATOM 4097 O O . GLY C 1 165 ? 24.587 57.389 62.396 1.00 88.62 ? 193 GLY C O 1 ATOM 4098 N N . VAL C 1 166 ? 24.368 58.384 64.383 1.00 83.85 ? 194 VAL C N 1 ATOM 4099 C CA . VAL C 1 166 ? 24.615 59.700 63.825 1.00 86.33 ? 194 VAL C CA 1 ATOM 4100 C C . VAL C 1 166 ? 25.715 60.378 64.628 1.00 87.86 ? 194 VAL C C 1 ATOM 4101 O O . VAL C 1 166 ? 25.885 60.110 65.822 1.00 89.54 ? 194 VAL C O 1 ATOM 4102 C CB . VAL C 1 166 ? 23.319 60.554 63.773 1.00 82.34 ? 194 VAL C CB 1 ATOM 4103 C CG1 . VAL C 1 166 ? 23.384 61.733 64.735 1.00 80.70 ? 194 VAL C CG1 1 ATOM 4104 C CG2 . VAL C 1 166 ? 23.053 61.031 62.346 1.00 80.45 ? 194 VAL C CG2 1 ATOM 4105 N N . THR C 1 167 ? 26.468 61.248 63.968 1.00 84.03 ? 195 THR C N 1 ATOM 4106 C CA . THR C 1 167 ? 27.539 61.958 64.634 1.00 87.72 ? 195 THR C CA 1 ATOM 4107 C C . THR C 1 167 ? 26.920 62.925 65.646 1.00 93.48 ? 195 THR C C 1 ATOM 4108 O O . THR C 1 167 ? 25.908 63.560 65.366 1.00 93.96 ? 195 THR C O 1 ATOM 4109 C CB . THR C 1 167 ? 28.414 62.684 63.592 1.00 88.93 ? 195 THR C CB 1 ATOM 4110 O OG1 . THR C 1 167 ? 29.559 61.879 63.285 1.00 93.51 ? 195 THR C OG1 1 ATOM 4111 C CG2 . THR C 1 167 ? 28.856 64.049 64.082 1.00 84.59 ? 195 THR C CG2 1 ATOM 4112 N N . GLU C 1 168 ? 27.513 63.010 66.833 1.00 95.18 ? 196 GLU C N 1 ATOM 4113 C CA . GLU C 1 168 ? 26.995 63.891 67.885 1.00 95.84 ? 196 GLU C CA 1 ATOM 4114 C C . GLU C 1 168 ? 26.955 65.351 67.428 1.00 85.37 ? 196 GLU C C 1 ATOM 4115 O O . GLU C 1 168 ? 26.038 66.108 67.773 1.00 74.13 ? 196 GLU C O 1 ATOM 4116 C CB . GLU C 1 168 ? 27.791 63.726 69.190 1.00 99.09 ? 196 GLU C CB 1 ATOM 4117 C CG . GLU C 1 168 ? 27.294 64.589 70.349 1.00 100.32 ? 196 GLU C CG 1 ATOM 4118 C CD . GLU C 1 168 ? 28.002 64.283 71.661 1.00 102.93 ? 196 GLU C CD 1 ATOM 4119 O OE1 . GLU C 1 168 ? 28.751 63.285 71.712 1.00 101.47 ? 196 GLU C OE1 1 ATOM 4120 O OE2 . GLU C 1 168 ? 27.802 65.032 72.644 1.00 104.20 ? 196 GLU C OE2 1 ATOM 4121 N N . SER C 1 169 ? 27.958 65.734 66.648 1.00 82.37 ? 197 SER C N 1 ATOM 4122 C CA . SER C 1 169 ? 28.010 67.071 66.074 1.00 82.03 ? 197 SER C CA 1 ATOM 4123 C C . SER C 1 169 ? 26.869 67.313 65.077 1.00 81.30 ? 197 SER C C 1 ATOM 4124 O O . SER C 1 169 ? 26.298 68.403 65.044 1.00 79.00 ? 197 SER C O 1 ATOM 4125 C CB . SER C 1 169 ? 29.369 67.336 65.427 1.00 75.52 ? 197 SER C CB 1 ATOM 4126 O OG . SER C 1 169 ? 29.409 68.641 64.893 1.00 75.15 ? 197 SER C OG 1 ATOM 4127 N N . THR C 1 170 ? 26.541 66.290 64.283 1.00 76.63 ? 198 THR C N 1 ATOM 4128 C CA . THR C 1 170 ? 25.401 66.336 63.366 1.00 79.36 ? 198 THR C CA 1 ATOM 4129 C C . THR C 1 170 ? 24.122 66.769 64.083 1.00 79.22 ? 198 THR C C 1 ATOM 4130 O O . THR C 1 170 ? 23.412 67.675 63.636 1.00 77.12 ? 198 THR C O 1 ATOM 4131 C CB . THR C 1 170 ? 25.131 64.951 62.730 1.00 84.50 ? 198 THR C CB 1 ATOM 4132 O OG1 . THR C 1 170 ? 26.215 64.574 61.874 1.00 87.89 ? 198 THR C OG1 1 ATOM 4133 C CG2 . THR C 1 170 ? 23.823 64.954 61.951 1.00 84.29 ? 198 THR C CG2 1 ATOM 4134 N N . LEU C 1 171 ? 23.849 66.118 65.209 1.00 74.34 ? 199 LEU C N 1 ATOM 4135 C CA . LEU C 1 171 ? 22.668 66.398 66.010 1.00 72.84 ? 199 LEU C CA 1 ATOM 4136 C C . LEU C 1 171 ? 22.647 67.812 66.608 1.00 81.17 ? 199 LEU C C 1 ATOM 4137 O O . LEU C 1 171 ? 21.623 68.502 66.548 1.00 82.68 ? 199 LEU C O 1 ATOM 4138 C CB . LEU C 1 171 ? 22.564 65.366 67.123 1.00 66.52 ? 199 LEU C CB 1 ATOM 4139 C CG . LEU C 1 171 ? 21.297 65.404 67.965 1.00 73.15 ? 199 LEU C CG 1 ATOM 4140 C CD1 . LEU C 1 171 ? 20.087 65.085 67.105 1.00 79.41 ? 199 LEU C CD1 1 ATOM 4141 C CD2 . LEU C 1 171 ? 21.417 64.438 69.142 1.00 72.19 ? 199 LEU C CD2 1 ATOM 4142 N N . LEU C 1 172 ? 23.777 68.247 67.164 1.00 79.07 ? 200 LEU C N 1 ATOM 4143 C CA . LEU C 1 172 ? 23.854 69.552 67.824 1.00 68.87 ? 200 LEU C CA 1 ATOM 4144 C C . LEU C 1 172 ? 23.672 70.695 66.845 1.00 66.99 ? 200 LEU C C 1 ATOM 4145 O O . LEU C 1 172 ? 23.099 71.728 67.191 1.00 63.57 ? 200 LEU C O 1 ATOM 4146 C CB . LEU C 1 172 ? 25.167 69.730 68.591 1.00 72.46 ? 200 LEU C CB 1 ATOM 4147 C CG . LEU C 1 172 ? 25.366 68.915 69.868 1.00 72.87 ? 200 LEU C CG 1 ATOM 4148 C CD1 . LEU C 1 172 ? 26.804 69.030 70.355 1.00 75.12 ? 200 LEU C CD1 1 ATOM 4149 C CD2 . LEU C 1 172 ? 24.396 69.388 70.939 1.00 62.02 ? 200 LEU C CD2 1 ATOM 4150 N N . THR C 1 173 ? 24.197 70.529 65.637 1.00 65.67 ? 201 THR C N 1 ATOM 4151 C CA . THR C 1 173 ? 24.039 71.555 64.615 1.00 77.08 ? 201 THR C CA 1 ATOM 4152 C C . THR C 1 173 ? 22.626 71.546 64.031 1.00 78.19 ? 201 THR C C 1 ATOM 4153 O O . THR C 1 173 ? 22.013 72.607 63.857 1.00 75.18 ? 201 THR C O 1 ATOM 4154 C CB . THR C 1 173 ? 25.070 71.402 63.485 1.00 84.67 ? 201 THR C CB 1 ATOM 4155 O OG1 . THR C 1 173 ? 24.894 70.130 62.848 1.00 91.47 ? 201 THR C OG1 1 ATOM 4156 C CG2 . THR C 1 173 ? 26.476 71.486 64.045 1.00 85.57 ? 201 THR C CG2 1 ATOM 4157 N N . ARG C 1 174 ? 22.114 70.348 63.741 1.00 74.39 ? 202 ARG C N 1 ATOM 4158 C CA . ARG C 1 174 ? 20.762 70.188 63.204 1.00 65.03 ? 202 ARG C CA 1 ATOM 4159 C C . ARG C 1 174 ? 19.761 70.794 64.176 1.00 64.07 ? 202 ARG C C 1 ATOM 4160 O O . ARG C 1 174 ? 18.781 71.427 63.779 1.00 65.35 ? 202 ARG C O 1 ATOM 4161 C CB . ARG C 1 174 ? 20.453 68.708 62.946 1.00 64.45 ? 202 ARG C CB 1 ATOM 4162 C CG . ARG C 1 174 ? 19.079 68.444 62.334 1.00 66.65 ? 202 ARG C CG 1 ATOM 4163 C CD . ARG C 1 174 ? 18.944 69.043 60.931 1.00 63.35 ? 202 ARG C CD 1 ATOM 4164 N NE . ARG C 1 174 ? 17.538 69.188 60.555 1.00 54.53 ? 202 ARG C NE 1 ATOM 4165 C CZ . ARG C 1 174 ? 17.112 69.822 59.469 1.00 56.23 ? 202 ARG C CZ 1 ATOM 4166 N NH1 . ARG C 1 174 ? 17.988 70.400 58.651 1.00 50.02 ? 202 ARG C NH1 1 ATOM 4167 N NH2 . ARG C 1 174 ? 15.807 69.915 59.220 1.00 55.22 ? 202 ARG C NH2 1 ATOM 4168 N N . ASN C 1 175 ? 20.024 70.618 65.461 1.00 61.41 ? 203 ASN C N 1 ATOM 4169 C CA . ASN C 1 175 ? 19.146 71.184 66.472 1.00 65.38 ? 203 ASN C CA 1 ATOM 4170 C C . ASN C 1 175 ? 19.696 72.493 67.065 1.00 75.62 ? 203 ASN C C 1 ATOM 4171 O O . ASN C 1 175 ? 19.181 73.003 68.065 1.00 74.93 ? 203 ASN C O 1 ATOM 4172 C CB . ASN C 1 175 ? 18.829 70.136 67.534 1.00 59.87 ? 203 ASN C CB 1 ATOM 4173 C CG . ASN C 1 175 ? 17.952 69.014 66.989 1.00 55.89 ? 203 ASN C CG 1 ATOM 4174 O OD1 . ASN C 1 175 ? 16.727 69.153 66.910 1.00 53.56 ? 203 ASN C OD1 1 ATOM 4175 N ND2 . ASN C 1 175 ? 18.577 67.909 66.590 1.00 41.93 ? 203 ASN C ND2 1 ATOM 4176 N N . LYS C 1 176 ? 20.738 73.018 66.411 1.00 83.32 ? 204 LYS C N 1 ATOM 4177 C CA . LYS C 1 176 ? 21.411 74.286 66.747 1.00 86.25 ? 204 LYS C CA 1 ATOM 4178 C C . LYS C 1 176 ? 21.715 74.504 68.234 1.00 85.53 ? 204 LYS C C 1 ATOM 4179 O O . LYS C 1 176 ? 21.352 75.534 68.804 1.00 86.17 ? 204 LYS C O 1 ATOM 4180 C CB . LYS C 1 176 ? 20.638 75.488 66.187 1.00 90.35 ? 204 LYS C CB 1 ATOM 4181 C CG . LYS C 1 176 ? 21.510 76.395 65.312 1.00 100.82 ? 204 LYS C CG 1 ATOM 4182 C CD . LYS C 1 176 ? 21.195 77.884 65.476 1.00 102.64 ? 204 LYS C CD 1 ATOM 4183 C CE . LYS C 1 176 ? 22.168 78.741 64.666 1.00 100.23 ? 204 LYS C CE 1 ATOM 4184 N NZ . LYS C 1 176 ? 21.845 80.197 64.724 1.00 99.27 ? 204 LYS C NZ 1 ATOM 4185 N N . ILE C 1 177 ? 22.402 73.548 68.852 1.00 83.68 ? 205 ILE C N 1 ATOM 4186 C CA . ILE C 1 177 ? 22.732 73.660 70.270 1.00 83.33 ? 205 ILE C CA 1 ATOM 4187 C C . ILE C 1 177 ? 24.227 73.908 70.508 1.00 85.31 ? 205 ILE C C 1 ATOM 4188 O O . ILE C 1 177 ? 25.091 73.294 69.873 1.00 85.41 ? 205 ILE C O 1 ATOM 4189 C CB . ILE C 1 177 ? 22.296 72.388 71.013 1.00 75.35 ? 205 ILE C CB 1 ATOM 4190 C CG1 . ILE C 1 177 ? 20.781 72.204 70.878 1.00 73.52 ? 205 ILE C CG1 1 ATOM 4191 C CG2 . ILE C 1 177 ? 22.746 72.438 72.470 1.00 67.92 ? 205 ILE C CG2 1 ATOM 4192 C CD1 . ILE C 1 177 ? 20.287 70.807 71.229 1.00 73.18 ? 205 ILE C CD1 1 ATOM 4193 N N . ASP C 1 179 ? 26.097 73.573 73.026 1.00 90.36 ? 207 ASP C N 1 ATOM 4194 C CA . ASP C 1 179 ? 26.418 73.173 74.388 1.00 89.98 ? 207 ASP C CA 1 ATOM 4195 C C . ASP C 1 179 ? 25.416 72.136 74.909 1.00 86.60 ? 207 ASP C C 1 ATOM 4196 O O . ASP C 1 179 ? 24.315 72.496 75.330 1.00 92.31 ? 207 ASP C O 1 ATOM 4197 C CB . ASP C 1 179 ? 26.418 74.409 75.293 1.00 98.16 ? 207 ASP C CB 1 ATOM 4198 C CG . ASP C 1 179 ? 26.887 74.110 76.707 1.00 107.55 ? 207 ASP C CG 1 ATOM 4199 O OD1 . ASP C 1 179 ? 27.469 73.029 76.940 1.00 111.76 ? 207 ASP C OD1 1 ATOM 4200 O OD2 . ASP C 1 179 ? 26.659 74.959 77.593 1.00 111.14 ? 207 ASP C OD2 1 ATOM 4201 N N . PRO C 1 180 ? 25.805 70.846 74.892 1.00 78.62 ? 208 PRO C N 1 ATOM 4202 C CA . PRO C 1 180 ? 25.012 69.694 75.362 1.00 75.41 ? 208 PRO C CA 1 ATOM 4203 C C . PRO C 1 180 ? 24.470 69.798 76.788 1.00 83.00 ? 208 PRO C C 1 ATOM 4204 O O . PRO C 1 180 ? 23.358 69.351 77.040 1.00 89.63 ? 208 PRO C O 1 ATOM 4205 C CB . PRO C 1 180 ? 26.007 68.534 75.286 1.00 69.41 ? 208 PRO C CB 1 ATOM 4206 C CG . PRO C 1 180 ? 26.916 68.913 74.182 1.00 74.00 ? 208 PRO C CG 1 ATOM 4207 C CD . PRO C 1 180 ? 27.064 70.415 74.260 1.00 75.52 ? 208 PRO C CD 1 ATOM 4208 N N . THR C 1 181 ? 25.240 70.366 77.705 1.00 84.52 ? 209 THR C N 1 ATOM 4209 C CA . THR C 1 181 ? 24.871 70.360 79.120 1.00 86.39 ? 209 THR C CA 1 ATOM 4210 C C . THR C 1 181 ? 23.547 71.054 79.453 1.00 92.70 ? 209 THR C C 1 ATOM 4211 O O . THR C 1 181 ? 22.954 70.794 80.502 1.00 93.68 ? 209 THR C O 1 ATOM 4212 C CB . THR C 1 181 ? 25.981 71.001 79.961 1.00 74.78 ? 209 THR C CB 1 ATOM 4213 O OG1 . THR C 1 181 ? 26.155 72.362 79.534 1.00 72.84 ? 209 THR C OG1 1 ATOM 4214 C CG2 . THR C 1 181 ? 27.290 70.247 79.764 1.00 64.76 ? 209 THR C CG2 1 ATOM 4215 N N . LYS C 1 182 ? 23.067 71.907 78.554 1.00 96.52 ? 210 LYS C N 1 ATOM 4216 C CA . LYS C 1 182 ? 21.811 72.616 78.784 1.00 106.00 ? 210 LYS C CA 1 ATOM 4217 C C . LYS C 1 182 ? 20.625 71.781 78.311 1.00 110.10 ? 210 LYS C C 1 ATOM 4218 O O . LYS C 1 182 ? 19.489 72.265 78.258 1.00 108.84 ? 210 LYS C O 1 ATOM 4219 C CB . LYS C 1 182 ? 21.813 73.986 78.101 1.00 111.04 ? 210 LYS C CB 1 ATOM 4220 C CG . LYS C 1 182 ? 22.873 74.937 78.636 1.00 114.90 ? 210 LYS C CG 1 ATOM 4221 C CD . LYS C 1 182 ? 22.578 75.327 80.085 1.00 113.78 ? 210 LYS C CD 1 ATOM 4222 C CE . LYS C 1 182 ? 23.457 76.481 80.551 1.00 111.77 ? 210 LYS C CE 1 ATOM 4223 N NZ . LYS C 1 182 ? 24.911 76.162 80.457 1.00 110.72 ? 210 LYS C NZ 1 ATOM 4224 N N . LEU C 1 183 ? 20.913 70.543 77.919 1.00 108.97 ? 211 LEU C N 1 ATOM 4225 C CA . LEU C 1 183 ? 19.885 69.614 77.471 1.00 103.60 ? 211 LEU C CA 1 ATOM 4226 C C . LEU C 1 183 ? 18.856 69.290 78.546 1.00 107.99 ? 211 LEU C C 1 ATOM 4227 O O . LEU C 1 183 ? 19.204 68.855 79.646 1.00 111.22 ? 211 LEU C O 1 ATOM 4228 C CB . LEU C 1 183 ? 20.509 68.314 76.975 1.00 94.78 ? 211 LEU C CB 1 ATOM 4229 C CG . LEU C 1 183 ? 19.543 67.491 76.126 1.00 92.09 ? 211 LEU C CG 1 ATOM 4230 C CD1 . LEU C 1 183 ? 19.231 68.213 74.816 1.00 87.70 ? 211 LEU C CD1 1 ATOM 4231 C CD2 . LEU C 1 183 ? 20.096 66.098 75.870 1.00 90.24 ? 211 LEU C CD2 1 ATOM 4232 N N . GLN C 1 184 ? 17.587 69.492 78.211 1.00 108.26 ? 212 GLN C N 1 ATOM 4233 C CA . GLN C 1 184 ? 16.489 69.124 79.089 1.00 108.77 ? 212 GLN C CA 1 ATOM 4234 C C . GLN C 1 184 ? 15.927 67.777 78.654 1.00 112.62 ? 212 GLN C C 1 ATOM 4235 O O . GLN C 1 184 ? 15.922 67.457 77.464 1.00 116.26 ? 212 GLN C O 1 ATOM 4236 C CB . GLN C 1 184 ? 15.396 70.196 79.078 1.00 107.31 ? 212 GLN C CB 1 ATOM 4237 C CG . GLN C 1 184 ? 15.711 71.432 79.894 1.00 106.89 ? 212 GLN C CG 1 ATOM 4238 C CD . GLN C 1 184 ? 14.617 72.484 79.799 1.00 107.70 ? 212 GLN C CD 1 ATOM 4239 O OE1 . GLN C 1 184 ? 13.628 72.309 79.084 1.00 106.26 ? 212 GLN C OE1 1 ATOM 4240 N NE2 . GLN C 1 184 ? 14.772 73.567 80.554 1.00 109.39 ? 212 GLN C NE2 1 ATOM 4241 N N . MET C 1 185 ? 15.475 66.984 79.619 1.00 112.40 ? 213 MET C N 1 ATOM 4242 C CA . MET C 1 185 ? 14.758 65.754 79.311 1.00 111.48 ? 213 MET C CA 1 ATOM 4243 C C . MET C 1 185 ? 13.480 66.135 78.562 1.00 110.22 ? 213 MET C C 1 ATOM 4244 O O . MET C 1 185 ? 12.788 67.079 78.951 1.00 112.14 ? 213 MET C O 1 ATOM 4245 C CB . MET C 1 185 ? 14.423 64.991 80.594 1.00 106.10 ? 213 MET C CB 1 ATOM 4246 C CG . MET C 1 185 ? 13.850 63.600 80.354 1.00 109.82 ? 213 MET C CG 1 ATOM 4247 S SD . MET C 1 185 ? 13.172 62.770 81.809 1.00 140.76 ? 213 MET C SD 1 ATOM 4248 C CE . MET C 1 185 ? 11.513 63.446 81.848 1.00 61.17 ? 213 MET C CE 1 ATOM 4249 N N . GLY C 1 186 ? 13.190 65.441 77.464 1.00 101.55 ? 214 GLY C N 1 ATOM 4250 C CA . GLY C 1 186 ? 11.959 65.696 76.734 1.00 98.86 ? 214 GLY C CA 1 ATOM 4251 C C . GLY C 1 186 ? 12.012 66.853 75.751 1.00 93.45 ? 214 GLY C C 1 ATOM 4252 O O . GLY C 1 186 ? 11.020 67.166 75.083 1.00 89.15 ? 214 GLY C O 1 ATOM 4253 N N . GLN C 1 187 ? 13.165 67.507 75.673 1.00 86.64 ? 215 GLN C N 1 ATOM 4254 C CA . GLN C 1 187 ? 13.380 68.501 74.642 1.00 82.73 ? 215 GLN C CA 1 ATOM 4255 C C . GLN C 1 187 ? 13.243 67.765 73.326 1.00 73.34 ? 215 GLN C C 1 ATOM 4256 O O . GLN C 1 187 ? 13.749 66.653 73.184 1.00 72.37 ? 215 GLN C O 1 ATOM 4257 C CB . GLN C 1 187 ? 14.765 69.125 74.765 1.00 81.21 ? 215 GLN C CB 1 ATOM 4258 C CG . GLN C 1 187 ? 14.995 70.265 73.798 1.00 81.39 ? 215 GLN C CG 1 ATOM 4259 C CD . GLN C 1 187 ? 16.217 71.084 74.152 1.00 86.39 ? 215 GLN C CD 1 ATOM 4260 O OE1 . GLN C 1 187 ? 16.861 70.853 75.177 1.00 83.55 ? 215 GLN C OE1 1 ATOM 4261 N NE2 . GLN C 1 187 ? 16.534 72.061 73.312 1.00 92.47 ? 215 GLN C NE2 1 ATOM 4262 N N . ILE C 1 188 ? 12.562 68.363 72.361 1.00 61.81 ? 216 ILE C N 1 ATOM 4263 C CA . ILE C 1 188 ? 12.335 67.655 71.109 1.00 56.43 ? 216 ILE C CA 1 ATOM 4264 C C . ILE C 1 188 ? 13.472 67.856 70.116 1.00 54.65 ? 216 ILE C C 1 ATOM 4265 O O . ILE C 1 188 ? 13.787 68.971 69.726 1.00 57.65 ? 216 ILE C O 1 ATOM 4266 C CB . ILE C 1 188 ? 11.030 68.097 70.435 1.00 50.36 ? 216 ILE C CB 1 ATOM 4267 C CG1 . ILE C 1 188 ? 9.862 68.006 71.422 1.00 52.88 ? 216 ILE C CG1 1 ATOM 4268 C CG2 . ILE C 1 188 ? 10.797 67.263 69.186 1.00 47.21 ? 216 ILE C CG2 1 ATOM 4269 C CD1 . ILE C 1 188 ? 9.639 66.617 71.984 1.00 52.93 ? 216 ILE C CD1 1 ATOM 4270 N N . LEU C 1 189 ? 14.087 66.756 69.711 1.00 48.99 ? 217 LEU C N 1 ATOM 4271 C CA . LEU C 1 189 ? 15.173 66.808 68.762 1.00 53.27 ? 217 LEU C CA 1 ATOM 4272 C C . LEU C 1 189 ? 14.758 66.340 67.371 1.00 64.09 ? 217 LEU C C 1 ATOM 4273 O O . LEU C 1 189 ? 13.905 65.461 67.216 1.00 71.58 ? 217 LEU C O 1 ATOM 4274 C CB . LEU C 1 189 ? 16.320 65.923 69.236 1.00 58.87 ? 217 LEU C CB 1 ATOM 4275 C CG . LEU C 1 189 ? 16.996 66.270 70.555 1.00 57.72 ? 217 LEU C CG 1 ATOM 4276 C CD1 . LEU C 1 189 ? 18.185 65.335 70.748 1.00 50.47 ? 217 LEU C CD1 1 ATOM 4277 C CD2 . LEU C 1 189 ? 17.413 67.741 70.579 1.00 60.88 ? 217 LEU C CD2 1 ATOM 4278 N N . ASP C 1 190 ? 15.374 66.944 66.362 1.00 52.27 ? 218 ASP C N 1 ATOM 4279 C CA . ASP C 1 190 ? 15.247 66.491 64.991 1.00 51.62 ? 218 ASP C CA 1 ATOM 4280 C C . ASP C 1 190 ? 16.447 65.591 64.717 1.00 58.74 ? 218 ASP C C 1 ATOM 4281 O O . ASP C 1 190 ? 17.563 66.074 64.535 1.00 61.32 ? 218 ASP C O 1 ATOM 4282 C CB . ASP C 1 190 ? 15.228 67.707 64.060 1.00 58.87 ? 218 ASP C CB 1 ATOM 4283 C CG . ASP C 1 190 ? 15.235 67.342 62.585 1.00 54.76 ? 218 ASP C CG 1 ATOM 4284 O OD1 . ASP C 1 190 ? 15.280 66.145 62.220 1.00 53.84 ? 218 ASP C OD1 1 ATOM 4285 O OD2 . ASP C 1 190 ? 15.221 68.287 61.778 1.00 59.89 ? 218 ASP C OD2 1 ATOM 4286 N N . VAL C 1 191 ? 16.214 64.281 64.702 1.00 56.97 ? 219 VAL C N 1 ATOM 4287 C CA . VAL C 1 191 ? 17.275 63.294 64.483 1.00 53.98 ? 219 VAL C CA 1 ATOM 4288 C C . VAL C 1 191 ? 17.304 62.802 63.029 1.00 57.07 ? 219 VAL C C 1 ATOM 4289 O O . VAL C 1 191 ? 16.445 62.019 62.620 1.00 63.22 ? 219 VAL C O 1 ATOM 4290 C CB . VAL C 1 191 ? 17.044 62.077 65.395 1.00 50.85 ? 219 VAL C CB 1 ATOM 4291 C CG1 . VAL C 1 191 ? 18.177 61.057 65.258 1.00 45.50 ? 219 VAL C CG1 1 ATOM 4292 C CG2 . VAL C 1 191 ? 16.848 62.527 66.844 1.00 53.08 ? 219 VAL C CG2 1 ATOM 4293 N N . PRO C 1 192 ? 18.302 63.236 62.246 1.00 59.16 ? 220 PRO C N 1 ATOM 4294 C CA . PRO C 1 192 ? 18.297 62.867 60.823 1.00 61.28 ? 220 PRO C CA 1 ATOM 4295 C C . PRO C 1 192 ? 18.906 61.492 60.544 1.00 60.73 ? 220 PRO C C 1 ATOM 4296 O O . PRO C 1 192 ? 20.109 61.359 60.305 1.00 60.90 ? 220 PRO C O 1 ATOM 4297 C CB . PRO C 1 192 ? 19.115 63.986 60.164 1.00 68.10 ? 220 PRO C CB 1 ATOM 4298 C CG . PRO C 1 192 ? 19.881 64.668 61.293 1.00 70.98 ? 220 PRO C CG 1 ATOM 4299 C CD . PRO C 1 192 ? 19.463 64.066 62.606 1.00 66.56 ? 220 PRO C CD 1 ATOM 4300 N N . LEU C 1 193 ? 18.035 60.487 60.540 1.00 64.16 ? 221 LEU C N 1 ATOM 4301 C CA . LEU C 1 193 ? 18.397 59.087 60.359 1.00 62.19 ? 221 LEU C CA 1 ATOM 4302 C C . LEU C 1 193 ? 18.883 58.784 58.954 1.00 73.19 ? 221 LEU C C 1 ATOM 4303 O O . LEU C 1 193 ? 18.108 58.902 58.004 1.00 71.80 ? 221 LEU C O 1 ATOM 4304 C CB . LEU C 1 193 ? 17.176 58.216 60.612 1.00 59.43 ? 221 LEU C CB 1 ATOM 4305 C CG . LEU C 1 193 ? 16.502 58.290 61.975 1.00 61.64 ? 221 LEU C CG 1 ATOM 4306 C CD1 . LEU C 1 193 ? 15.416 57.211 62.079 1.00 49.52 ? 221 LEU C CD1 1 ATOM 4307 C CD2 . LEU C 1 193 ? 17.514 58.219 63.101 1.00 65.88 ? 221 LEU C CD2 1 ATOM 4308 N N . PRO C 1 194 ? 20.151 58.367 58.812 1.00 81.26 ? 222 PRO C N 1 ATOM 4309 C CA . PRO C 1 194 ? 20.657 58.010 57.480 1.00 81.71 ? 222 PRO C CA 1 ATOM 4310 C C . PRO C 1 194 ? 19.756 56.966 56.823 1.00 74.97 ? 222 PRO C C 1 ATOM 4311 O O . PRO C 1 194 ? 19.407 55.993 57.477 1.00 77.61 ? 222 PRO C O 1 ATOM 4312 C CB . PRO C 1 194 ? 22.051 57.425 57.756 1.00 79.85 ? 222 PRO C CB 1 ATOM 4313 C CG . PRO C 1 194 ? 22.341 57.666 59.202 1.00 83.19 ? 222 PRO C CG 1 ATOM 4314 C CD . PRO C 1 194 ? 21.210 58.416 59.831 1.00 84.00 ? 222 PRO C CD 1 ATOM 4315 N N . VAL C 1 195 ? 19.369 57.184 55.569 1.00 72.36 ? 223 VAL C N 1 ATOM 4316 C CA . VAL C 1 195 ? 18.527 56.241 54.831 1.00 69.36 ? 223 VAL C CA 1 ATOM 4317 C C . VAL C 1 195 ? 19.222 54.900 54.585 1.00 75.28 ? 223 VAL C C 1 ATOM 4318 O O . VAL C 1 195 ? 20.081 54.776 53.705 1.00 78.78 ? 223 VAL C O 1 ATOM 4319 C CB . VAL C 1 195 ? 18.058 56.832 53.482 1.00 65.33 ? 223 VAL C CB 1 HETATM 4320 C C1 . NAG D 2 . ? 29.253 45.672 93.925 1.00 53.32 ? 301 NAG A C1 1 HETATM 4321 C C2 . NAG D 2 . ? 30.176 45.993 92.743 1.00 52.30 ? 301 NAG A C2 1 HETATM 4322 C C3 . NAG D 2 . ? 29.570 47.082 91.860 1.00 54.97 ? 301 NAG A C3 1 HETATM 4323 C C4 . NAG D 2 . ? 28.239 46.558 91.335 1.00 61.49 ? 301 NAG A C4 1 HETATM 4324 C C5 . NAG D 2 . ? 27.339 46.294 92.538 1.00 63.37 ? 301 NAG A C5 1 HETATM 4325 C C6 . NAG D 2 . ? 25.928 45.830 92.141 1.00 63.81 ? 301 NAG A C6 1 HETATM 4326 C C7 . NAG D 2 . ? 32.440 45.392 93.226 1.00 61.43 ? 301 NAG A C7 1 HETATM 4327 C C8 . NAG D 2 . ? 33.727 45.755 93.909 1.00 55.49 ? 301 NAG A C8 1 HETATM 4328 N N2 . NAG D 2 . ? 31.505 46.337 93.201 1.00 55.14 ? 301 NAG A N2 1 HETATM 4329 O O3 . NAG D 2 . ? 30.457 47.441 90.818 1.00 66.23 ? 301 NAG A O3 1 HETATM 4330 O O4 . NAG D 2 . ? 27.618 47.460 90.443 1.00 67.84 ? 301 NAG A O4 1 HETATM 4331 O O5 . NAG D 2 . ? 27.956 45.360 93.415 1.00 62.52 ? 301 NAG A O5 1 HETATM 4332 O O6 . NAG D 2 . ? 25.905 44.555 91.519 1.00 67.29 ? 301 NAG A O6 1 HETATM 4333 O O7 . NAG D 2 . ? 32.269 44.272 92.727 1.00 55.22 ? 301 NAG A O7 1 HETATM 4334 C C1 . NAG E 2 . ? 10.944 31.214 95.882 1.00 37.23 ? 302 NAG A C1 1 HETATM 4335 C C2 . NAG E 2 . ? 12.105 30.609 95.090 1.00 41.99 ? 302 NAG A C2 1 HETATM 4336 C C3 . NAG E 2 . ? 11.917 29.132 94.778 1.00 41.65 ? 302 NAG A C3 1 HETATM 4337 C C4 . NAG E 2 . ? 11.474 28.339 96.009 1.00 45.12 ? 302 NAG A C4 1 HETATM 4338 C C5 . NAG E 2 . ? 10.326 29.046 96.713 1.00 45.36 ? 302 NAG A C5 1 HETATM 4339 C C6 . NAG E 2 . ? 10.061 28.359 98.043 1.00 45.41 ? 302 NAG A C6 1 HETATM 4340 C C7 . NAG E 2 . ? 13.234 32.309 93.790 1.00 35.55 ? 302 NAG A C7 1 HETATM 4341 C C8 . NAG E 2 . ? 13.196 33.137 92.547 1.00 31.84 ? 302 NAG A C8 1 HETATM 4342 N N2 . NAG E 2 . ? 12.304 31.370 93.871 1.00 42.82 ? 302 NAG A N2 1 HETATM 4343 O O3 . NAG E 2 . ? 13.183 28.658 94.393 1.00 44.33 ? 302 NAG A O3 1 HETATM 4344 O O4 . NAG E 2 . ? 11.095 27.008 95.671 1.00 54.41 ? 302 NAG A O4 1 HETATM 4345 O O5 . NAG E 2 . ? 10.617 30.409 96.985 1.00 48.09 ? 302 NAG A O5 1 HETATM 4346 O O6 . NAG E 2 . ? 8.890 28.879 98.623 1.00 50.14 ? 302 NAG A O6 1 HETATM 4347 O O7 . NAG E 2 . ? 14.076 32.502 94.668 1.00 33.75 ? 302 NAG A O7 1 HETATM 4348 C C1 . NAG F 2 . ? 39.996 24.130 71.505 1.00 61.39 ? 301 NAG B C1 1 HETATM 4349 C C2 . NAG F 2 . ? 41.079 23.250 72.151 1.00 60.51 ? 301 NAG B C2 1 HETATM 4350 C C3 . NAG F 2 . ? 42.175 22.966 71.138 1.00 71.43 ? 301 NAG B C3 1 HETATM 4351 C C4 . NAG F 2 . ? 41.565 22.214 69.974 1.00 75.35 ? 301 NAG B C4 1 HETATM 4352 C C5 . NAG F 2 . ? 40.462 23.057 69.340 1.00 74.28 ? 301 NAG B C5 1 HETATM 4353 C C7 . NAG F 2 . ? 41.276 23.421 74.581 1.00 70.61 ? 301 NAG B C7 1 HETATM 4354 C C8 . NAG F 2 . ? 40.697 22.037 74.701 1.00 68.09 ? 301 NAG B C8 1 HETATM 4355 N N2 . NAG F 2 . ? 41.638 23.838 73.357 1.00 63.24 ? 301 NAG B N2 1 HETATM 4356 O O3 . NAG F 2 . ? 43.231 22.223 71.703 1.00 71.48 ? 301 NAG B O3 1 HETATM 4357 O O4 . NAG F 2 . ? 42.593 21.943 69.048 1.00 84.34 ? 301 NAG B O4 1 HETATM 4358 O O5 . NAG F 2 . ? 39.526 23.562 70.288 1.00 73.75 ? 301 NAG B O5 1 HETATM 4359 O O7 . NAG F 2 . ? 41.392 24.117 75.592 1.00 64.89 ? 301 NAG B O7 1 HETATM 4360 C C1 . NAG G 2 . ? 11.231 41.985 90.857 1.00 57.04 ? 302 NAG B C1 1 HETATM 4361 C C2 . NAG G 2 . ? 10.145 42.797 91.558 1.00 66.65 ? 302 NAG B C2 1 HETATM 4362 C C3 . NAG G 2 . ? 10.535 44.258 91.678 1.00 70.81 ? 302 NAG B C3 1 HETATM 4363 C C4 . NAG G 2 . ? 11.924 44.458 92.248 1.00 77.74 ? 302 NAG B C4 1 HETATM 4364 C C5 . NAG G 2 . ? 12.993 43.426 91.879 1.00 70.47 ? 302 NAG B C5 1 HETATM 4365 C C6 . NAG G 2 . ? 13.899 43.266 93.112 1.00 67.88 ? 302 NAG B C6 1 HETATM 4366 C C7 . NAG G 2 . ? 7.932 41.915 91.237 1.00 65.48 ? 302 NAG B C7 1 HETATM 4367 C C8 . NAG G 2 . ? 6.732 41.802 90.340 1.00 63.78 ? 302 NAG B C8 1 HETATM 4368 N N2 . NAG G 2 . ? 8.895 42.730 90.832 1.00 65.51 ? 302 NAG B N2 1 HETATM 4369 O O3 . NAG G 2 . ? 9.633 44.929 92.535 1.00 75.53 ? 302 NAG B O3 1 HETATM 4370 O O4 . NAG G 2 . ? 12.328 45.723 91.772 1.00 84.90 ? 302 NAG B O4 1 HETATM 4371 O O5 . NAG G 2 . ? 12.483 42.150 91.521 1.00 63.20 ? 302 NAG B O5 1 HETATM 4372 O O6 . NAG G 2 . ? 15.288 43.213 92.832 1.00 61.88 ? 302 NAG B O6 1 HETATM 4373 O O7 . NAG G 2 . ? 8.012 41.272 92.283 1.00 62.05 ? 302 NAG B O7 1 HETATM 4374 O O . HOH H 3 . ? 7.082 27.136 104.786 1.00 51.91 ? 401 HOH A O 1 HETATM 4375 O O . HOH H 3 . ? 6.292 44.566 101.371 1.00 48.82 ? 402 HOH A O 1 HETATM 4376 O O . HOH H 3 . ? 20.937 33.363 105.744 1.00 46.22 ? 403 HOH A O 1 HETATM 4377 O O . HOH H 3 . ? 30.951 49.462 116.017 1.00 36.03 ? 404 HOH A O 1 HETATM 4378 O O . HOH H 3 . ? 32.486 49.898 113.141 1.00 45.03 ? 405 HOH A O 1 HETATM 4379 O O . HOH H 3 . ? 6.888 34.976 118.592 1.00 39.42 ? 406 HOH A O 1 HETATM 4380 O O . HOH H 3 . ? 19.360 48.597 117.279 1.00 31.50 ? 407 HOH A O 1 HETATM 4381 O O . HOH H 3 . ? 9.965 43.193 120.259 1.00 46.83 ? 408 HOH A O 1 HETATM 4382 O O . HOH H 3 . ? 19.398 59.365 112.280 1.00 46.06 ? 409 HOH A O 1 HETATM 4383 O O . HOH H 3 . ? 22.918 53.218 118.749 1.00 47.04 ? 410 HOH A O 1 HETATM 4384 O O . HOH H 3 . ? 31.473 46.772 128.031 1.00 49.33 ? 411 HOH A O 1 HETATM 4385 O O . HOH H 3 . ? 22.773 35.052 116.136 1.00 33.65 ? 412 HOH A O 1 HETATM 4386 O O . HOH H 3 . ? 32.675 42.116 99.300 1.00 37.00 ? 413 HOH A O 1 HETATM 4387 O O . HOH H 3 . ? 13.819 43.546 128.945 1.00 43.61 ? 414 HOH A O 1 HETATM 4388 O O . HOH H 3 . ? 31.830 40.290 97.559 1.00 38.12 ? 415 HOH A O 1 HETATM 4389 O O . HOH H 3 . ? 22.547 25.781 112.597 1.00 41.46 ? 416 HOH A O 1 HETATM 4390 O O . HOH H 3 . ? 17.396 36.870 104.941 1.00 27.96 ? 417 HOH A O 1 HETATM 4391 O O . HOH H 3 . ? 27.497 49.925 116.283 1.00 36.52 ? 418 HOH A O 1 HETATM 4392 O O . HOH H 3 . ? 10.101 37.278 95.182 1.00 46.34 ? 419 HOH A O 1 HETATM 4393 O O . HOH H 3 . ? 19.924 43.399 114.659 1.00 28.84 ? 420 HOH A O 1 HETATM 4394 O O . HOH H 3 . ? 28.509 34.990 116.148 1.00 40.83 ? 421 HOH A O 1 HETATM 4395 O O . HOH H 3 . ? 30.252 38.081 109.516 1.00 43.37 ? 422 HOH A O 1 HETATM 4396 O O . HOH H 3 . ? 5.167 34.267 96.027 1.00 38.00 ? 423 HOH A O 1 HETATM 4397 O O . HOH H 3 . ? 16.333 50.027 128.197 1.00 48.32 ? 424 HOH A O 1 HETATM 4398 O O . HOH H 3 . ? 42.078 42.307 111.653 1.00 64.91 ? 425 HOH A O 1 HETATM 4399 O O . HOH H 3 . ? 30.305 51.979 99.949 1.00 60.21 ? 426 HOH A O 1 HETATM 4400 O O . HOH H 3 . ? 18.624 39.544 104.748 1.00 33.22 ? 427 HOH A O 1 HETATM 4401 O O . HOH H 3 . ? 12.199 41.856 98.230 1.00 34.54 ? 428 HOH A O 1 HETATM 4402 O O . HOH H 3 . ? 27.404 34.588 109.304 1.00 34.91 ? 429 HOH A O 1 HETATM 4403 O O . HOH H 3 . ? 23.298 33.770 121.437 1.00 53.58 ? 430 HOH A O 1 HETATM 4404 O O . HOH H 3 . ? 18.892 39.888 102.127 1.00 28.89 ? 431 HOH A O 1 HETATM 4405 O O . HOH H 3 . ? 21.688 18.827 114.599 1.00 56.34 ? 432 HOH A O 1 HETATM 4406 O O . HOH H 3 . ? 6.577 28.435 106.408 1.00 43.81 ? 433 HOH A O 1 HETATM 4407 O O . HOH H 3 . ? 10.534 43.788 99.107 1.00 60.58 ? 434 HOH A O 1 HETATM 4408 O O . HOH H 3 . ? 19.614 19.907 114.644 1.00 50.69 ? 435 HOH A O 1 HETATM 4409 O O . HOH H 3 . ? 18.741 41.532 100.203 1.00 43.41 ? 436 HOH A O 1 HETATM 4410 O O . HOH H 3 . ? 18.252 34.526 103.628 1.00 33.42 ? 437 HOH A O 1 HETATM 4411 O O . HOH I 3 . ? 10.114 43.798 79.724 1.00 57.46 ? 401 HOH B O 1 HETATM 4412 O O . HOH I 3 . ? 19.667 38.266 91.734 1.00 54.57 ? 402 HOH B O 1 HETATM 4413 O O . HOH I 3 . ? 32.881 39.106 85.359 1.00 47.65 ? 403 HOH B O 1 HETATM 4414 O O . HOH I 3 . ? 14.558 14.751 66.544 1.00 71.64 ? 404 HOH B O 1 HETATM 4415 O O . HOH I 3 . ? 23.556 40.157 81.564 1.00 49.80 ? 405 HOH B O 1 HETATM 4416 O O . HOH I 3 . ? 20.943 17.924 75.968 1.00 36.99 ? 406 HOH B O 1 HETATM 4417 O O . HOH I 3 . ? 38.300 32.750 94.026 1.00 46.61 ? 407 HOH B O 1 HETATM 4418 O O . HOH I 3 . ? 20.713 16.228 90.950 1.00 58.60 ? 408 HOH B O 1 HETATM 4419 O O . HOH I 3 . ? 45.072 33.928 82.351 1.00 50.72 ? 409 HOH B O 1 HETATM 4420 O O . HOH I 3 . ? 22.510 17.473 87.782 1.00 40.80 ? 410 HOH B O 1 HETATM 4421 O O . HOH I 3 . ? 24.736 10.565 91.048 1.00 53.04 ? 411 HOH B O 1 HETATM 4422 O O . HOH I 3 . ? 22.014 15.441 76.632 1.00 44.21 ? 412 HOH B O 1 HETATM 4423 O O . HOH I 3 . ? 37.896 23.261 77.360 1.00 44.72 ? 413 HOH B O 1 HETATM 4424 O O . HOH I 3 . ? 29.250 10.217 88.879 1.00 48.35 ? 414 HOH B O 1 HETATM 4425 O O . HOH I 3 . ? 46.366 34.416 80.318 1.00 48.97 ? 415 HOH B O 1 HETATM 4426 O O . HOH I 3 . ? 31.643 27.413 69.712 1.00 50.70 ? 416 HOH B O 1 HETATM 4427 O O . HOH I 3 . ? 36.010 22.806 75.901 1.00 38.81 ? 417 HOH B O 1 HETATM 4428 O O . HOH I 3 . ? 43.952 40.930 74.854 1.00 46.02 ? 418 HOH B O 1 HETATM 4429 O O . HOH I 3 . ? 19.736 16.114 87.844 1.00 43.82 ? 419 HOH B O 1 HETATM 4430 O O . HOH I 3 . ? 21.696 29.749 74.960 1.00 47.41 ? 420 HOH B O 1 HETATM 4431 O O . HOH I 3 . ? 27.861 40.035 82.921 1.00 45.20 ? 421 HOH B O 1 HETATM 4432 O O . HOH I 3 . ? 15.262 44.740 85.578 1.00 54.58 ? 422 HOH B O 1 HETATM 4433 O O . HOH I 3 . ? 35.109 40.715 88.015 1.00 64.50 ? 423 HOH B O 1 HETATM 4434 O O . HOH I 3 . ? 28.395 40.071 87.908 1.00 56.68 ? 424 HOH B O 1 HETATM 4435 O O . HOH I 3 . ? 21.899 39.657 84.595 1.00 48.68 ? 425 HOH B O 1 HETATM 4436 O O . HOH I 3 . ? 45.599 39.406 75.977 1.00 42.81 ? 426 HOH B O 1 HETATM 4437 O O . HOH I 3 . ? 12.422 29.340 63.948 1.00 40.38 ? 427 HOH B O 1 HETATM 4438 O O . HOH I 3 . ? 33.052 40.531 82.638 1.00 52.70 ? 428 HOH B O 1 HETATM 4439 O O . HOH I 3 . ? 35.731 29.976 87.015 1.00 56.54 ? 429 HOH B O 1 HETATM 4440 O O . HOH I 3 . ? 22.594 34.636 86.945 1.00 38.65 ? 430 HOH B O 1 HETATM 4441 O O . HOH I 3 . ? 22.280 20.031 87.586 1.00 44.95 ? 431 HOH B O 1 HETATM 4442 O O . HOH I 3 . ? 26.443 12.004 90.114 1.00 40.58 ? 432 HOH B O 1 HETATM 4443 O O . HOH I 3 . ? 41.911 36.694 89.667 1.00 59.97 ? 433 HOH B O 1 HETATM 4444 O O . HOH I 3 . ? 2.613 40.955 76.990 1.00 46.41 ? 434 HOH B O 1 HETATM 4445 O O . HOH I 3 . ? 13.006 25.158 78.881 1.00 54.24 ? 435 HOH B O 1 HETATM 4446 O O . HOH I 3 . ? 21.776 13.859 74.482 1.00 55.76 ? 436 HOH B O 1 HETATM 4447 O O . HOH I 3 . ? 0.522 39.692 76.406 1.00 52.07 ? 437 HOH B O 1 HETATM 4448 O O . HOH I 3 . ? 3.002 35.588 95.120 1.00 43.38 ? 438 HOH B O 1 HETATM 4449 O O . HOH J 3 . ? 10.620 46.399 58.514 1.00 60.23 ? 301 HOH C O 1 HETATM 4450 O O . HOH J 3 . ? -0.321 36.716 61.650 1.00 57.25 ? 302 HOH C O 1 HETATM 4451 O O . HOH J 3 . ? 7.875 74.780 69.716 1.00 61.29 ? 303 HOH C O 1 HETATM 4452 O O . HOH J 3 . ? -0.541 70.210 55.634 1.00 51.17 ? 304 HOH C O 1 HETATM 4453 O O . HOH J 3 . ? -0.542 41.781 60.263 1.00 50.55 ? 305 HOH C O 1 HETATM 4454 O O . HOH J 3 . ? 16.850 71.205 52.085 1.00 40.67 ? 306 HOH C O 1 HETATM 4455 O O . HOH J 3 . ? 15.879 74.280 57.656 1.00 56.80 ? 307 HOH C O 1 HETATM 4456 O O . HOH J 3 . ? -3.916 41.900 62.210 1.00 58.51 ? 308 HOH C O 1 HETATM 4457 O O . HOH J 3 . ? 17.202 59.251 75.938 1.00 59.69 ? 309 HOH C 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 . ALA A 1 ? 0.7776 0.5925 0.6722 -0.0106 -0.0018 -0.0407 29 ALA A N 2 C CA . ALA A 1 ? 0.9244 0.7335 0.8150 -0.0154 0.0022 -0.0416 29 ALA A CA 3 C C . ALA A 1 ? 0.8728 0.6923 0.7747 -0.0191 0.0045 -0.0403 29 ALA A C 4 O O . ALA A 1 ? 0.6220 0.4463 0.5307 -0.0189 0.0035 -0.0390 29 ALA A O 5 C CB . ALA A 1 ? 1.0376 0.8324 0.9175 -0.0161 0.0028 -0.0427 29 ALA A CB 6 N N . ASN A 2 ? 0.9198 0.7429 0.8237 -0.0221 0.0073 -0.0408 30 ASN A N 7 C CA . ASN A 2 ? 0.7127 0.5438 0.6254 -0.0259 0.0098 -0.0400 30 ASN A CA 8 C C . ASN A 2 ? 0.5941 0.4375 0.5193 -0.0247 0.0078 -0.0378 30 ASN A C 9 O O . ASN A 2 ? 0.5575 0.4081 0.4873 -0.0218 0.0053 -0.0367 30 ASN A O 10 C CB . ASN A 2 ? 0.9324 0.7536 0.8386 -0.0287 0.0122 -0.0411 30 ASN A CB 11 C CG . ASN A 2 ? 0.9270 0.7529 0.8384 -0.0332 0.0158 -0.0414 30 ASN A CG 12 O OD1 . ASN A 2 ? 0.8171 0.6497 0.7368 -0.0338 0.0158 -0.0403 30 ASN A OD1 13 N ND2 . ASN A 2 ? 0.6710 0.4927 0.5768 -0.0365 0.0189 -0.0429 30 ASN A ND2 14 N N . PHE A 3 ? 0.5866 0.4327 0.5173 -0.0268 0.0089 -0.0371 31 PHE A N 15 C CA . PHE A 3 ? 0.4738 0.3286 0.4143 -0.0254 0.0065 -0.0350 31 PHE A CA 16 C C . PHE A 3 ? 0.5642 0.4113 0.5006 -0.0242 0.0051 -0.0352 31 PHE A C 17 O O . PHE A 3 ? 0.5688 0.4067 0.4983 -0.0258 0.0070 -0.0366 31 PHE A O 18 C CB . PHE A 3 ? 0.4683 0.3322 0.4188 -0.0281 0.0081 -0.0340 31 PHE A CB 19 C CG . PHE A 3 ? 0.5090 0.3825 0.4655 -0.0291 0.0090 -0.0334 31 PHE A CG 20 C CD1 . PHE A 3 ? 0.4795 0.3544 0.4335 -0.0273 0.0080 -0.0336 31 PHE A CD1 21 C CD2 . PHE A 3 ? 0.3803 0.2616 0.3448 -0.0316 0.0107 -0.0328 31 PHE A CD2 22 C CE1 . PHE A 3 ? 0.4793 0.3627 0.4384 -0.0282 0.0088 -0.0332 31 PHE A CE1 23 C CE2 . PHE A 3 ? 0.3829 0.2729 0.3527 -0.0325 0.0114 -0.0323 31 PHE A CE2 24 C CZ . PHE A 3 ? 0.5672 0.4582 0.5342 -0.0309 0.0105 -0.0325 31 PHE A CZ 25 N N . THR A 4 ? 0.5189 0.3700 0.4593 -0.0214 0.0016 -0.0337 32 THR A N 26 C CA . THR A 4 ? 0.5389 0.3837 0.4762 -0.0200 -0.0003 -0.0337 32 THR A CA 27 C C . THR A 4 ? 0.6699 0.5163 0.6126 -0.0222 0.0005 -0.0330 32 THR A C 28 O O . THR A 4 ? 0.5041 0.3599 0.4561 -0.0237 0.0011 -0.0318 32 THR A O 29 C CB . THR A 4 ? 0.4925 0.3421 0.4328 -0.0164 -0.0045 -0.0324 32 THR A CB 30 O OG1 . THR A 4 ? 0.6682 0.5093 0.5986 -0.0137 -0.0057 -0.0339 32 THR A OG1 31 C CG2 . THR A 4 ? 0.5553 0.4071 0.5006 -0.0158 -0.0070 -0.0310 32 THR A CG2 32 N N . CYS A 5 ? 0.6335 0.4707 0.5702 -0.0221 0.0004 -0.0339 33 CYS A N 33 C CA . CYS A 5 ? 0.5612 0.3989 0.5021 -0.0235 0.0008 -0.0335 33 CYS A CA 34 C C . CYS A 5 ? 0.6020 0.4311 0.5370 -0.0217 -0.0015 -0.0339 33 CYS A C 35 O O . CYS A 5 ? 0.6611 0.4797 0.5857 -0.0211 -0.0010 -0.0354 33 CYS A O 36 C CB . CYS A 5 ? 0.5166 0.3513 0.4553 -0.0268 0.0050 -0.0350 33 CYS A CB 37 S SG . CYS A 5 ? 0.7091 0.5454 0.6535 -0.0282 0.0057 -0.0348 33 CYS A SG 38 N N . ALA A 6 ? 0.5649 0.3981 0.5062 -0.0209 -0.0042 -0.0324 34 ALA A N 39 C CA . ALA A 6 ? 0.6017 0.4282 0.5386 -0.0189 -0.0071 -0.0325 34 ALA A CA 40 C C . ALA A 6 ? 0.6689 0.4907 0.6054 -0.0200 -0.0067 -0.0329 34 ALA A C 41 O O . ALA A 6 ? 0.6001 0.4166 0.5333 -0.0185 -0.0093 -0.0329 34 ALA A O 42 C CB . ALA A 6 ? 0.4776 0.3120 0.4213 -0.0168 -0.0113 -0.0305 34 ALA A CB 43 N N . VAL A 7 ? 0.5109 0.3347 0.4504 -0.0225 -0.0034 -0.0334 35 VAL A N 44 C CA . VAL A 7 ? 0.5750 0.3950 0.5143 -0.0235 -0.0027 -0.0340 35 VAL A CA 45 C C . VAL A 7 ? 0.6743 0.4824 0.6023 -0.0241 -0.0002 -0.0363 35 VAL A C 46 O O . VAL A 7 ? 0.6234 0.4260 0.5438 -0.0240 0.0009 -0.0373 35 VAL A O 47 C CB . VAL A 7 ? 0.7336 0.5612 0.6811 -0.0256 -0.0004 -0.0337 35 VAL A CB 48 C CG1 . VAL A 7 ? 0.4061 0.2454 0.3646 -0.0252 -0.0029 -0.0312 35 VAL A CG1 49 C CG2 . VAL A 7 ? 0.6845 0.5119 0.6292 -0.0277 0.0039 -0.0352 35 VAL A CG2 50 N N . ALA A 8 ? 0.6551 0.4589 0.5818 -0.0247 0.0006 -0.0372 36 ALA A N 51 C CA . ALA A 8 ? 0.6144 0.4065 0.5299 -0.0254 0.0029 -0.0393 36 ALA A CA 52 C C . ALA A 8 ? 0.6624 0.4528 0.5734 -0.0279 0.0074 -0.0407 36 ALA A C 53 O O . ALA A 8 ? 0.6367 0.4345 0.5540 -0.0299 0.0100 -0.0408 36 ALA A O 54 C CB . ALA A 8 ? 0.5207 0.3099 0.4365 -0.0258 0.0034 -0.0401 36 ALA A CB 55 N N . SER A 9 ? 0.5395 0.3198 0.4392 -0.0278 0.0081 -0.0419 37 SER A N 56 C CA . SER A 9 ? 0.6062 0.3827 0.4996 -0.0304 0.0122 -0.0434 37 SER A CA 57 C C . SER A 9 ? 0.5822 0.3597 0.4769 -0.0333 0.0164 -0.0447 37 SER A C 58 O O . SER A 9 ? 0.5284 0.3026 0.4220 -0.0330 0.0164 -0.0454 37 SER A O 59 C CB . SER A 9 ? 0.6069 0.3702 0.4867 -0.0298 0.0120 -0.0444 37 SER A CB 60 O OG . SER A 9 ? 0.8368 0.5956 0.7098 -0.0328 0.0161 -0.0458 37 SER A OG 61 N N . GLY A 10 ? 0.6061 0.3887 0.5033 -0.0361 0.0199 -0.0453 38 GLY A N 62 C CA . GLY A 10 ? 0.5808 0.3663 0.4805 -0.0389 0.0239 -0.0468 38 GLY A CA 63 C C . GLY A 10 ? 0.6190 0.4172 0.5320 -0.0386 0.0234 -0.0458 38 GLY A C 64 O O . GLY A 10 ? 0.7214 0.5242 0.6383 -0.0406 0.0266 -0.0469 38 GLY A O 65 N N . THR A 11 ? 0.6335 0.4374 0.5536 -0.0361 0.0194 -0.0437 39 THR A N 66 C CA . THR A 11 ? 0.6138 0.4293 0.5462 -0.0358 0.0185 -0.0425 39 THR A CA 67 C C . THR A 11 ? 0.6411 0.4642 0.5779 -0.0382 0.0216 -0.0429 39 THR A C 68 O O . THR A 11 ? 0.5917 0.4142 0.5253 -0.0391 0.0222 -0.0429 39 THR A O 69 C CB . THR A 11 ? 0.5554 0.3759 0.4940 -0.0332 0.0138 -0.0400 39 THR A CB 70 O OG1 . THR A 11 ? 0.5521 0.3665 0.4877 -0.0311 0.0107 -0.0396 39 THR A OG1 71 C CG2 . THR A 11 ? 0.4379 0.2703 0.3887 -0.0332 0.0130 -0.0385 39 THR A CG2 72 N N . THR A 12 ? 0.6112 0.4414 0.5552 -0.0392 0.0233 -0.0434 40 THR A N 73 C CA . THR A 12 ? 0.6066 0.4450 0.5559 -0.0414 0.0259 -0.0438 40 THR A CA 74 C C . THR A 12 ? 0.5853 0.4349 0.5466 -0.0402 0.0237 -0.0420 40 THR A C 75 O O . THR A 12 ? 0.5852 0.4361 0.5508 -0.0386 0.0220 -0.0415 40 THR A O 76 C CB . THR A 12 ? 0.6811 0.5178 0.6272 -0.0442 0.0306 -0.0464 40 THR A CB 77 O OG1 . THR A 12 ? 0.6946 0.5264 0.6326 -0.0469 0.0335 -0.0477 40 THR A OG1 78 C CG2 . THR A 12 ? 0.6533 0.5009 0.6094 -0.0450 0.0322 -0.0469 40 THR A CG2 79 N N . CYS A 13 ? 0.4368 0.2938 0.4029 -0.0409 0.0237 -0.0411 41 CYS A N 80 C CA . CYS A 13 ? 0.4631 0.3310 0.4402 -0.0401 0.0220 -0.0393 41 CYS A CA 81 C C . CYS A 13 ? 0.5211 0.3963 0.5016 -0.0423 0.0243 -0.0398 41 CYS A C 82 O O . CYS A 13 ? 0.5430 0.4147 0.5173 -0.0444 0.0271 -0.0413 41 CYS A O 83 C CB . CYS A 13 ? 0.4145 0.2843 0.3949 -0.0377 0.0174 -0.0366 41 CYS A CB 84 S SG . CYS A 13 ? 0.4671 0.3353 0.4427 -0.0372 0.0161 -0.0356 41 CYS A SG 85 N N . LYS A 14 ? 0.4640 0.3492 0.4541 -0.0418 0.0230 -0.0384 42 LYS A N 86 C CA . LYS A 14 ? 0.4807 0.3736 0.4748 -0.0435 0.0246 -0.0385 42 LYS A CA 87 C C . LYS A 14 ? 0.4844 0.3804 0.4797 -0.0427 0.0222 -0.0364 42 LYS A C 88 O O . LYS A 14 ? 0.3763 0.2751 0.3759 -0.0406 0.0188 -0.0341 42 LYS A O 89 C CB . LYS A 14 ? 0.4477 0.3499 0.4514 -0.0434 0.0247 -0.0383 42 LYS A CB 90 C CG . LYS A 14 ? 0.7158 0.6253 0.7227 -0.0458 0.0274 -0.0395 42 LYS A CG 91 C CD . LYS A 14 ? 0.8748 0.7927 0.8903 -0.0456 0.0279 -0.0399 42 LYS A CD 92 C CE . LYS A 14 ? 0.8796 0.8063 0.9037 -0.0442 0.0249 -0.0374 42 LYS A CE 93 N NZ . LYS A 14 ? 0.8544 0.7806 0.8822 -0.0415 0.0212 -0.0353 42 LYS A NZ 94 N N . SER A 15 ? 0.4728 0.3683 0.4641 -0.0443 0.0240 -0.0373 43 SER A N 95 C CA . SER A 15 ? 0.3332 0.2319 0.3253 -0.0435 0.0222 -0.0357 43 SER A CA 96 C C . SER A 15 ? 0.4421 0.3475 0.4370 -0.0457 0.0243 -0.0365 43 SER A C 97 O O . SER A 15 ? 0.4565 0.3644 0.4533 -0.0478 0.0270 -0.0381 43 SER A O 98 C CB . SER A 15 ? 0.4740 0.3634 0.4563 -0.0429 0.0218 -0.0362 43 SER A CB 99 O OG . SER A 15 ? 0.5205 0.4040 0.5000 -0.0406 0.0194 -0.0355 43 SER A OG 100 N N . ALA A 16 ? 0.4404 0.3488 0.4355 -0.0452 0.0230 -0.0354 44 ALA A N 101 C CA . ALA A 16 ? 0.4651 0.3791 0.4620 -0.0472 0.0248 -0.0362 44 ALA A CA 102 C C . ALA A 16 ? 0.4154 0.3277 0.4076 -0.0467 0.0240 -0.0359 44 ALA A C 103 O O . ALA A 16 ? 0.4684 0.3783 0.4588 -0.0441 0.0214 -0.0345 44 ALA A O 104 C CB . ALA A 16 ? 0.2688 0.1945 0.2766 -0.0470 0.0238 -0.0347 44 ALA A CB 105 N N . ILE A 17 ? 0.3807 0.2944 0.3711 -0.0490 0.0262 -0.0373 45 ILE A N 106 C CA . ILE A 17 ? 0.3613 0.2765 0.3498 -0.0483 0.0251 -0.0368 45 ILE A CA 107 C C . ILE A 17 ? 0.3389 0.2654 0.3358 -0.0492 0.0252 -0.0361 45 ILE A C 108 O O . ILE A 17 ? 0.4772 0.4080 0.4781 -0.0515 0.0271 -0.0371 45 ILE A O 109 C CB . ILE A 17 ? 0.3928 0.2991 0.3708 -0.0502 0.0272 -0.0391 45 ILE A CB 110 C CG1 . ILE A 17 ? 0.4406 0.3478 0.4184 -0.0543 0.0309 -0.0412 45 ILE A CG1 111 C CG2 . ILE A 17 ? 0.3903 0.2847 0.3590 -0.0489 0.0268 -0.0396 45 ILE A CG2 112 C CD1 . ILE A 17 ? 0.3177 0.2162 0.2850 -0.0571 0.0332 -0.0434 45 ILE A CD1 113 N N . LEU A 18 ? 0.3314 0.2630 0.3307 -0.0475 0.0231 -0.0346 46 LEU A N 114 C CA . LEU A 18 ? 0.4121 0.3533 0.4176 -0.0486 0.0233 -0.0342 46 LEU A CA 115 C C . LEU A 18 ? 0.4674 0.4047 0.4659 -0.0506 0.0253 -0.0363 46 LEU A C 116 O O . LEU A 18 ? 0.4625 0.3963 0.4557 -0.0491 0.0243 -0.0363 46 LEU A O 117 C CB . LEU A 18 ? 0.3326 0.2815 0.3439 -0.0460 0.0203 -0.0315 46 LEU A CB 118 C CG . LEU A 18 ? 0.4749 0.4340 0.4927 -0.0469 0.0203 -0.0309 46 LEU A CG 119 C CD1 . LEU A 18 ? 0.3658 0.3307 0.3910 -0.0484 0.0211 -0.0308 46 LEU A CD1 120 C CD2 . LEU A 18 ? 0.4031 0.3689 0.4249 -0.0445 0.0175 -0.0284 46 LEU A CD2 121 N N . TYR A 19 ? 0.4879 0.4256 0.4863 -0.0539 0.0281 -0.0382 47 TYR A N 122 C CA . TYR A 19 ? 0.3906 0.3229 0.3812 -0.0565 0.0302 -0.0405 47 TYR A CA 123 C C . TYR A 19 ? 0.4119 0.3518 0.4058 -0.0573 0.0299 -0.0405 47 TYR A C 124 O O . TYR A 19 ? 0.4415 0.3910 0.4438 -0.0581 0.0300 -0.0399 47 TYR A O 125 C CB . TYR A 19 ? 0.3385 0.2671 0.3266 -0.0603 0.0335 -0.0427 47 TYR A CB 126 C CG . TYR A 19 ? 0.4864 0.4084 0.4658 -0.0636 0.0358 -0.0451 47 TYR A CG 127 C CD1 . TYR A 19 ? 0.4889 0.3994 0.4575 -0.0629 0.0355 -0.0457 47 TYR A CD1 128 C CD2 . TYR A 19 ? 0.4095 0.3361 0.3910 -0.0675 0.0383 -0.0467 47 TYR A CD2 129 C CE1 . TYR A 19 ? 0.4839 0.3871 0.4437 -0.0660 0.0375 -0.0477 47 TYR A CE1 130 C CE2 . TYR A 19 ? 0.3781 0.2980 0.3511 -0.0710 0.0403 -0.0488 47 TYR A CE2 131 C CZ . TYR A 19 ? 0.5043 0.4121 0.4663 -0.0703 0.0399 -0.0493 47 TYR A CZ 132 O OH . TYR A 19 ? 0.5921 0.4921 0.5450 -0.0737 0.0417 -0.0512 47 TYR A OH 133 N N . THR A 20 ? 0.4389 0.3741 0.4259 -0.0569 0.0295 -0.0411 48 THR A N 134 C CA . THR A 20 ? 0.3547 0.2956 0.3431 -0.0579 0.0295 -0.0415 48 THR A CA 135 C C . THR A 20 ? 0.4295 0.3654 0.4120 -0.0622 0.0324 -0.0442 48 THR A C 136 O O . THR A 20 ? 0.4776 0.4026 0.4501 -0.0630 0.0333 -0.0456 48 THR A O 137 C CB . THR A 20 ? 0.4534 0.3925 0.4377 -0.0549 0.0273 -0.0408 48 THR A CB 138 O OG1 . THR A 20 ? 0.4141 0.3585 0.4041 -0.0511 0.0247 -0.0383 48 THR A OG1 139 C CG2 . THR A 20 ? 0.3461 0.2909 0.3314 -0.0561 0.0275 -0.0415 48 THR A CG2 140 N N . SER A 21 ? 0.2806 0.2243 0.2691 -0.0651 0.0339 -0.0449 49 SER A N 141 C CA . SER A 21 ? 0.3288 0.2690 0.3127 -0.0698 0.0368 -0.0475 49 SER A CA 142 C C . SER A 21 ? 0.4487 0.3854 0.4259 -0.0710 0.0367 -0.0487 49 SER A C 143 O O . SER A 21 ? 0.4389 0.3834 0.4207 -0.0703 0.0355 -0.0482 49 SER A O 144 C CB . SER A 21 ? 0.3752 0.3259 0.3683 -0.0723 0.0382 -0.0480 49 SER A CB 145 O OG . SER A 21 ? 0.4153 0.3635 0.4045 -0.0772 0.0412 -0.0506 49 SER A OG 146 N N . PRO A 22 ? 0.4462 0.3708 0.4122 -0.0728 0.0380 -0.0504 50 PRO A N 147 C CA . PRO A 22 ? 0.4163 0.3363 0.3751 -0.0737 0.0376 -0.0516 50 PRO A CA 148 C C . PRO A 22 ? 0.5495 0.4771 0.5122 -0.0776 0.0390 -0.0530 50 PRO A C 149 O O . PRO A 22 ? 0.6832 0.6131 0.6452 -0.0771 0.0378 -0.0531 50 PRO A O 150 C CB . PRO A 22 ? 0.4341 0.3394 0.3804 -0.0757 0.0391 -0.0533 50 PRO A CB 151 C CG . PRO A 22 ? 0.4001 0.3017 0.3466 -0.0738 0.0391 -0.0523 50 PRO A CG 152 C CD . PRO A 22 ? 0.4338 0.3480 0.3929 -0.0740 0.0396 -0.0512 50 PRO A CD 153 N N . ASN A 23 ? 0.4880 0.4202 0.4556 -0.0813 0.0413 -0.0539 51 ASN A N 154 C CA . ASN A 23 ? 0.5521 0.4920 0.5238 -0.0852 0.0426 -0.0553 51 ASN A CA 155 C C . ASN A 23 ? 0.5535 0.5062 0.5375 -0.0853 0.0430 -0.0546 51 ASN A C 156 O O . ASN A 23 ? 0.6276 0.5823 0.6163 -0.0826 0.0424 -0.0531 51 ASN A O 157 C CB . ASN A 23 ? 0.5882 0.5206 0.5521 -0.0910 0.0457 -0.0579 51 ASN A CB 158 C CG . ASN A 23 ? 0.8054 0.7243 0.7563 -0.0913 0.0453 -0.0587 51 ASN A CG 159 O OD1 . ASN A 23 ? 0.8147 0.7324 0.7634 -0.0880 0.0428 -0.0580 51 ASN A OD1 160 N ND2 . ASN A 23 ? 0.9352 0.8435 0.8770 -0.0952 0.0476 -0.0604 51 ASN A ND2 161 N N . ALA A 24 ? 0.5194 0.4806 0.5084 -0.0883 0.0437 -0.0557 52 ALA A N 162 C CA . ALA A 24 ? 0.4367 0.4099 0.4367 -0.0889 0.0443 -0.0557 52 ALA A CA 163 C C . ALA A 24 ? 0.5315 0.5012 0.5299 -0.0920 0.0473 -0.0572 52 ALA A C 164 O O . ALA A 24 ? 0.5952 0.5569 0.5853 -0.0961 0.0496 -0.0592 52 ALA A O 165 C CB . ALA A 24 ? 0.3256 0.3079 0.3301 -0.0918 0.0444 -0.0569 52 ALA A CB 166 N N . THR A 25 ? 0.4256 0.4006 0.4313 -0.0900 0.0473 -0.0563 53 THR A N 167 C CA . THR A 25 ? 0.4460 0.4183 0.4505 -0.0925 0.0502 -0.0578 53 THR A CA 168 C C . THR A 25 ? 0.4726 0.4559 0.4885 -0.0906 0.0499 -0.0573 53 THR A C 169 O O . THR A 25 ? 0.5042 0.4973 0.5283 -0.0885 0.0478 -0.0562 53 THR A O 170 C CB . THR A 25 ? 0.5498 0.5090 0.5452 -0.0911 0.0505 -0.0573 53 THR A CB 171 O OG1 . THR A 25 ? 0.6145 0.5716 0.6090 -0.0936 0.0534 -0.0587 53 THR A OG1 172 C CG2 . THR A 25 ? 0.6348 0.5941 0.6334 -0.0854 0.0474 -0.0545 53 THR A CG2 173 N N . THR A 26 ? 0.3984 0.3797 0.4145 -0.0911 0.0518 -0.0580 54 THR A N 174 C CA . THR A 26 ? 0.3519 0.3427 0.3781 -0.0888 0.0514 -0.0577 54 THR A CA 175 C C . THR A 26 ? 0.3665 0.3508 0.3907 -0.0861 0.0513 -0.0567 54 THR A C 176 O O . THR A 26 ? 0.4960 0.4691 0.5110 -0.0870 0.0524 -0.0570 54 THR A O 177 C CB . THR A 26 ? 0.4795 0.4776 0.5097 -0.0930 0.0546 -0.0605 54 THR A CB 178 O OG1 . THR A 26 ? 0.5254 0.5150 0.5478 -0.0963 0.0579 -0.0623 54 THR A OG1 179 C CG2 . THR A 26 ? 0.3490 0.3527 0.3800 -0.0966 0.0549 -0.0619 54 THR A CG2 180 N N . TYR A 27 ? 0.5258 0.5170 0.5585 -0.0828 0.0500 -0.0557 55 TYR A N 181 C CA . TYR A 27 ? 0.5129 0.4985 0.5443 -0.0803 0.0498 -0.0550 55 TYR A CA 182 C C . TYR A 27 ? 0.5401 0.5198 0.5656 -0.0837 0.0536 -0.0575 55 TYR A C 183 O O . TYR A 27 ? 0.5822 0.5518 0.6007 -0.0830 0.0540 -0.0571 55 TYR A O 184 C CB . TYR A 27 ? 0.5373 0.5313 0.5788 -0.0764 0.0477 -0.0538 55 TYR A CB 185 C CG . TYR A 27 ? 0.5436 0.5388 0.5882 -0.0723 0.0436 -0.0505 55 TYR A CG 186 C CD1 . TYR A 27 ? 0.4338 0.4363 0.4829 -0.0719 0.0417 -0.0494 55 TYR A CD1 187 C CD2 . TYR A 27 ? 0.5379 0.5268 0.5805 -0.0689 0.0416 -0.0485 55 TYR A CD2 188 C CE1 . TYR A 27 ? 0.3455 0.3492 0.3970 -0.0684 0.0382 -0.0464 55 TYR A CE1 189 C CE2 . TYR A 27 ? 0.4388 0.4289 0.4840 -0.0656 0.0381 -0.0455 55 TYR A CE2 190 C CZ . TYR A 27 ? 0.4583 0.4559 0.5079 -0.0654 0.0364 -0.0444 55 TYR A CZ 191 O OH . TYR A 27 ? 0.5193 0.5185 0.5713 -0.0623 0.0330 -0.0414 55 TYR A OH 192 N N . GLY A 28 ? 0.5747 0.5606 0.6025 -0.0876 0.0565 -0.0601 56 GLY A N 193 C CA . GLY A 28 ? 0.4208 0.4021 0.4431 -0.0916 0.0605 -0.0626 56 GLY A CA 194 C C . GLY A 28 ? 0.5174 0.4854 0.5271 -0.0943 0.0618 -0.0627 56 GLY A C 195 O O . GLY A 28 ? 0.6052 0.5647 0.6082 -0.0951 0.0636 -0.0634 56 GLY A O 196 N N . ASN A 29 ? 0.5517 0.5174 0.5576 -0.0956 0.0607 -0.0622 57 ASN A N 197 C CA . ASN A 29 ? 0.5220 0.4742 0.5154 -0.0976 0.0613 -0.0623 57 ASN A CA 198 C C . ASN A 29 ? 0.5519 0.4940 0.5399 -0.0934 0.0591 -0.0602 57 ASN A C 199 O O . ASN A 29 ? 0.6084 0.5386 0.5861 -0.0947 0.0603 -0.0606 57 ASN A O 200 C CB . ASN A 29 ? 0.6220 0.5743 0.6130 -0.0993 0.0603 -0.0623 57 ASN A CB 201 C CG . ASN A 29 ? 0.7244 0.6810 0.7153 -0.1052 0.0632 -0.0648 57 ASN A CG 202 O OD1 . ASN A 29 ? 0.7782 0.7438 0.7750 -0.1060 0.0624 -0.0651 57 ASN A OD1 203 N ND2 . ASN A 29 ? 0.8381 0.7884 0.8221 -0.1096 0.0667 -0.0667 57 ASN A ND2 204 N N . LEU A 30 ? 0.4702 0.4171 0.4648 -0.0884 0.0557 -0.0580 58 LEU A N 205 C CA . LEU A 30 ? 0.5375 0.4766 0.5285 -0.0841 0.0532 -0.0559 58 LEU A CA 206 C C . LEU A 30 ? 0.5092 0.4439 0.4984 -0.0838 0.0548 -0.0565 58 LEU A C 207 O O . LEU A 30 ? 0.6236 0.5470 0.6040 -0.0832 0.0548 -0.0562 58 LEU A O 208 C CB . LEU A 30 ? 0.5408 0.4876 0.5405 -0.0794 0.0494 -0.0534 58 LEU A CB 209 C CG . LEU A 30 ? 0.4570 0.4060 0.4566 -0.0790 0.0474 -0.0524 58 LEU A CG 210 C CD1 . LEU A 30 ? 0.3607 0.3185 0.3694 -0.0749 0.0440 -0.0499 58 LEU A CD1 211 C CD2 . LEU A 30 ? 0.5353 0.4722 0.5240 -0.0784 0.0467 -0.0521 58 LEU A CD2 212 N N . VAL A 31 ? 0.4852 0.4287 0.4825 -0.0841 0.0561 -0.0574 59 VAL A N 213 C CA . VAL A 31 ? 0.5582 0.4985 0.5542 -0.0840 0.0579 -0.0584 59 VAL A CA 214 C C . VAL A 31 ? 0.6922 0.6222 0.6770 -0.0882 0.0613 -0.0602 59 VAL A C 215 O O . VAL A 31 ? 0.6981 0.6192 0.6766 -0.0874 0.0618 -0.0602 59 VAL A O 216 C CB . VAL A 31 ? 0.4282 0.3803 0.4341 -0.0843 0.0594 -0.0599 59 VAL A CB 217 C CG1 . VAL A 31 ? 0.4469 0.3953 0.4503 -0.0848 0.0619 -0.0614 59 VAL A CG1 218 C CG2 . VAL A 31 ? 0.4239 0.3849 0.4402 -0.0798 0.0559 -0.0579 59 VAL A CG2 219 N N . ALA A 32 ? 0.7022 0.6334 0.6844 -0.0929 0.0635 -0.0618 60 ALA A N 220 C CA . ALA A 32 ? 0.7640 0.6853 0.7350 -0.0977 0.0667 -0.0635 60 ALA A CA 221 C C . ALA A 32 ? 0.7808 0.6877 0.7400 -0.0969 0.0651 -0.0623 60 ALA A C 222 O O . ALA A 32 ? 0.9087 0.8049 0.8588 -0.0978 0.0665 -0.0627 60 ALA A O 223 C CB . ALA A 32 ? 0.7814 0.7083 0.7532 -0.1032 0.0693 -0.0656 60 ALA A CB 224 N N . ARG A 33 ? 0.6301 0.5368 0.5893 -0.0950 0.0622 -0.0609 61 ARG A N 225 C CA . ARG A 33 ? 0.7549 0.6486 0.7031 -0.0937 0.0605 -0.0600 61 ARG A CA 226 C C . ARG A 33 ? 0.7378 0.6250 0.6838 -0.0892 0.0585 -0.0585 61 ARG A C 227 O O . ARG A 33 ? 0.8115 0.6861 0.7468 -0.0892 0.0586 -0.0585 61 ARG A O 228 C CB . ARG A 33 ? 0.8666 0.7630 0.8167 -0.0916 0.0575 -0.0587 61 ARG A CB 229 C CG . ARG A 33 ? 1.1727 1.0571 1.1130 -0.0888 0.0549 -0.0576 61 ARG A CG 230 C CD . ARG A 33 ? 1.0747 0.9636 1.0180 -0.0864 0.0520 -0.0564 61 ARG A CD 231 N NE . ARG A 33 ? 1.0481 0.9460 0.9966 -0.0900 0.0534 -0.0576 61 ARG A NE 232 C CZ . ARG A 33 ? 1.0869 0.9928 1.0414 -0.0885 0.0514 -0.0568 61 ARG A CZ 233 N NH1 . ARG A 33 ? 1.0035 0.9102 0.9598 -0.0835 0.0480 -0.0548 61 ARG A NH1 234 N NH2 . ARG A 33 ? 1.1789 1.0927 1.1377 -0.0921 0.0529 -0.0581 61 ARG A NH2 235 N N . PHE A 34 ? 0.6096 0.5054 0.5657 -0.0854 0.0567 -0.0572 62 PHE A N 236 C CA . PHE A 34 ? 0.5864 0.4771 0.5413 -0.0810 0.0544 -0.0556 62 PHE A CA 237 C C . PHE A 34 ? 0.6334 0.5211 0.5868 -0.0818 0.0567 -0.0567 62 PHE A C 238 O O . PHE A 34 ? 0.6229 0.4995 0.5676 -0.0811 0.0566 -0.0566 62 PHE A O 239 C CB . PHE A 34 ? 0.4261 0.3257 0.3912 -0.0763 0.0507 -0.0534 62 PHE A CB 240 C CG . PHE A 34 ? 0.4686 0.3666 0.4316 -0.0743 0.0479 -0.0519 62 PHE A CG 241 C CD1 . PHE A 34 ? 0.4766 0.3663 0.4339 -0.0709 0.0453 -0.0505 62 PHE A CD1 242 C CD2 . PHE A 34 ? 0.3926 0.2973 0.3589 -0.0758 0.0479 -0.0522 62 PHE A CD2 243 C CE1 . PHE A 34 ? 0.4387 0.3272 0.3939 -0.0688 0.0427 -0.0494 62 PHE A CE1 244 C CE2 . PHE A 34 ? 0.4775 0.3805 0.4414 -0.0738 0.0454 -0.0510 62 PHE A CE2 245 C CZ . PHE A 34 ? 0.4317 0.3268 0.3900 -0.0702 0.0429 -0.0497 62 PHE A CZ 246 N N . ASN A 35 ? 0.5808 0.4783 0.5423 -0.0834 0.0588 -0.0579 63 ASN A N 247 C CA . ASN A 35 ? 0.7005 0.5969 0.6615 -0.0842 0.0613 -0.0593 63 ASN A CA 248 C C . ASN A 35 ? 0.6479 0.5396 0.6086 -0.0795 0.0587 -0.0577 63 ASN A C 249 O O . ASN A 35 ? 0.7841 0.6680 0.7385 -0.0799 0.0601 -0.0585 63 ASN A O 250 C CB . ASN A 35 ? 0.7594 0.6467 0.7094 -0.0892 0.0652 -0.0613 63 ASN A CB 251 C CG . ASN A 35 ? 0.8318 0.7224 0.7835 -0.0914 0.0688 -0.0633 63 ASN A CG 252 O OD1 . ASN A 35 ? 0.7790 0.6813 0.7414 -0.0904 0.0691 -0.0639 63 ASN A OD1 253 N ND2 . ASN A 35 ? 0.8756 0.7560 0.8168 -0.0944 0.0716 -0.0645 63 ASN A ND2 254 N N . THR A 36 ? 0.5864 0.4827 0.5539 -0.0753 0.0549 -0.0555 64 THR A N 255 C CA . THR A 36 ? 0.6300 0.5221 0.5975 -0.0709 0.0519 -0.0539 64 THR A CA 256 C C . THR A 36 ? 0.5654 0.4669 0.5437 -0.0683 0.0507 -0.0533 64 THR A C 257 O O . THR A 36 ? 0.6471 0.5460 0.6263 -0.0650 0.0485 -0.0522 64 THR A O 258 C CB . THR A 36 ? 0.5653 0.4549 0.5316 -0.0679 0.0480 -0.0515 64 THR A CB 259 O OG1 . THR A 36 ? 0.5289 0.4292 0.5041 -0.0672 0.0466 -0.0505 64 THR A OG1 260 C CG2 . THR A 36 ? 0.4130 0.2918 0.3677 -0.0697 0.0487 -0.0520 64 THR A CG2 261 N N . THR A 37 ? 0.4749 0.3872 0.4612 -0.0698 0.0520 -0.0542 65 THR A N 262 C CA . THR A 37 ? 0.5664 0.4886 0.5635 -0.0671 0.0505 -0.0536 65 THR A CA 263 C C . THR A 37 ? 0.5373 0.4689 0.5398 -0.0702 0.0537 -0.0559 65 THR A C 264 O O . THR A 37 ? 0.5654 0.4966 0.5640 -0.0741 0.0563 -0.0573 65 THR A O 265 C CB . THR A 37 ? 0.6109 0.5383 0.6145 -0.0640 0.0463 -0.0508 65 THR A CB 266 O OG1 . THR A 37 ? 0.7741 0.7106 0.7877 -0.0616 0.0449 -0.0503 65 THR A OG1 267 C CG2 . THR A 37 ? 0.5382 0.4699 0.5425 -0.0661 0.0466 -0.0507 65 THR A CG2 268 N N . THR A 38 ? 0.5182 0.4582 0.5295 -0.0683 0.0533 -0.0563 66 THR A N 269 C CA . THR A 38 ? 0.5883 0.5387 0.6059 -0.0706 0.0559 -0.0585 66 THR A CA 270 C C . THR A 38 ? 0.6372 0.5968 0.6624 -0.0699 0.0536 -0.0571 66 THR A C 271 O O . THR A 38 ? 0.6372 0.5961 0.6641 -0.0670 0.0500 -0.0545 66 THR A O 272 C CB . THR A 38 ? 0.6811 0.6368 0.7049 -0.0684 0.0564 -0.0598 66 THR A CB 273 O OG1 . THR A 38 ? 0.5262 0.4863 0.5576 -0.0639 0.0523 -0.0576 66 THR A OG1 274 C CG2 . THR A 38 ? 0.5296 0.4760 0.5461 -0.0684 0.0582 -0.0610 66 THR A CG2 275 N N . LEU A 39 ? 0.6969 0.6656 0.7267 -0.0726 0.0558 -0.0591 67 LEU A N 276 C CA . LEU A 39 ? 0.6880 0.6664 0.7256 -0.0720 0.0538 -0.0581 67 LEU A CA 277 C C . LEU A 39 ? 0.6813 0.6651 0.7272 -0.0672 0.0499 -0.0559 67 LEU A C 278 O O . LEU A 39 ? 0.7817 0.7669 0.8297 -0.0655 0.0468 -0.0535 67 LEU A O 279 C CB . LEU A 39 ? 0.7647 0.7526 0.8065 -0.0755 0.0568 -0.0608 67 LEU A CB 280 C CG . LEU A 39 ? 0.8397 0.8390 0.8907 -0.0745 0.0546 -0.0601 67 LEU A CG 281 C CD1 . LEU A 39 ? 0.8346 0.8315 0.8825 -0.0752 0.0527 -0.0581 67 LEU A CD1 282 C CD2 . LEU A 39 ? 0.8559 0.8654 0.9118 -0.0776 0.0576 -0.0631 67 LEU A CD2 283 N N . PRO A 40 ? 0.7065 0.6932 0.7569 -0.0648 0.0499 -0.0568 68 PRO A N 284 C CA . PRO A 40 ? 0.6623 0.6536 0.7202 -0.0604 0.0459 -0.0546 68 PRO A CA 285 C C . PRO A 40 ? 0.6531 0.6365 0.7077 -0.0577 0.0424 -0.0513 68 PRO A C 286 O O . PRO A 40 ? 0.5989 0.5860 0.6585 -0.0553 0.0389 -0.0489 68 PRO A O 287 C CB . PRO A 40 ? 0.6727 0.6666 0.7344 -0.0584 0.0467 -0.0564 68 PRO A CB 288 C CG . PRO A 40 ? 0.6822 0.6734 0.7387 -0.0617 0.0512 -0.0595 68 PRO A CG 289 C CD . PRO A 40 ? 0.5953 0.5826 0.6451 -0.0661 0.0534 -0.0599 68 PRO A CD 290 N N . ASP A 41 ? 0.6736 0.6465 0.7199 -0.0583 0.0433 -0.0514 69 ASP A N 291 C CA . ASP A 41 ? 0.6191 0.5851 0.6622 -0.0560 0.0400 -0.0485 69 ASP A CA 292 C C . ASP A 41 ? 0.5181 0.4847 0.5598 -0.0570 0.0387 -0.0467 69 ASP A C 293 O O . ASP A 41 ? 0.3726 0.3395 0.4164 -0.0546 0.0353 -0.0440 69 ASP A O 294 C CB . ASP A 41 ? 0.6327 0.5874 0.6671 -0.0561 0.0411 -0.0490 69 ASP A CB 295 C CG . ASP A 41 ? 0.7841 0.7375 0.8201 -0.0541 0.0413 -0.0501 69 ASP A CG 296 O OD1 . ASP A 41 ? 0.6723 0.6325 0.7162 -0.0517 0.0396 -0.0497 69 ASP A OD1 297 O OD2 . ASP A 41 ? 0.8914 0.8368 0.9205 -0.0548 0.0432 -0.0514 69 ASP A OD2 298 N N . LEU A 42 ? 0.4606 0.4276 0.4988 -0.0605 0.0414 -0.0484 70 LEU A N 299 C CA . LEU A 42 ? 0.5365 0.5041 0.5731 -0.0613 0.0403 -0.0471 70 LEU A CA 300 C C . LEU A 42 ? 0.5708 0.5489 0.6165 -0.0597 0.0378 -0.0454 70 LEU A C 301 O O . LEU A 42 ? 0.6566 0.6352 0.7032 -0.0581 0.0350 -0.0429 70 LEU A O 302 C CB . LEU A 42 ? 0.5148 0.4806 0.5457 -0.0657 0.0437 -0.0494 70 LEU A CB 303 C CG . LEU A 42 ? 0.5961 0.5607 0.6236 -0.0666 0.0427 -0.0483 70 LEU A CG 304 C CD1 . LEU A 42 ? 0.3806 0.3372 0.4030 -0.0639 0.0400 -0.0461 70 LEU A CD1 305 C CD2 . LEU A 42 ? 0.3150 0.2758 0.3354 -0.0712 0.0461 -0.0508 70 LEU A CD2 306 N N . LEU A 43 ? 0.6131 0.5997 0.6657 -0.0601 0.0388 -0.0469 71 LEU A N 307 C CA . LEU A 43 ? 0.5431 0.5397 0.6043 -0.0586 0.0364 -0.0456 71 LEU A CA 308 C C . LEU A 43 ? 0.5208 0.5174 0.5859 -0.0546 0.0324 -0.0425 71 LEU A C 309 O O . LEU A 43 ? 0.4823 0.4830 0.5508 -0.0534 0.0297 -0.0401 71 LEU A O 310 C CB . LEU A 43 ? 0.6735 0.6786 0.7409 -0.0594 0.0383 -0.0481 71 LEU A CB 311 C CG . LEU A 43 ? 0.7467 0.7536 0.8113 -0.0638 0.0422 -0.0512 71 LEU A CG 312 C CD1 . LEU A 43 ? 0.8012 0.8165 0.8719 -0.0645 0.0442 -0.0539 71 LEU A CD1 313 C CD2 . LEU A 43 ? 0.6666 0.6767 0.7308 -0.0658 0.0418 -0.0506 71 LEU A CD2 314 N N . GLY A 44 ? 0.5020 0.4938 0.5663 -0.0528 0.0321 -0.0426 72 GLY A N 315 C CA . GLY A 44 ? 0.4191 0.4097 0.4863 -0.0494 0.0284 -0.0398 72 GLY A CA 316 C C . GLY A 44 ? 0.5015 0.4868 0.5646 -0.0488 0.0262 -0.0371 72 GLY A C 317 O O . GLY A 44 ? 0.4999 0.4875 0.5666 -0.0468 0.0228 -0.0342 72 GLY A O 318 N N . ALA A 45 ? 0.5258 0.5036 0.5810 -0.0504 0.0280 -0.0380 73 ALA A N 319 C CA . ALA A 45 ? 0.5300 0.5030 0.5808 -0.0497 0.0261 -0.0359 73 ALA A CA 320 C C . ALA A 45 ? 0.4375 0.4171 0.4911 -0.0501 0.0249 -0.0344 73 ALA A C 321 O O . ALA A 45 ? 0.4795 0.4581 0.5323 -0.0488 0.0225 -0.0320 73 ALA A O 322 C CB . ALA A 45 ? 0.5212 0.4851 0.5627 -0.0514 0.0284 -0.0375 73 ALA A CB 323 N N . ASN A 46 ? 0.4877 0.4740 0.5445 -0.0519 0.0265 -0.0358 74 ASN A N 324 C CA . ASN A 46 ? 0.5240 0.5168 0.5836 -0.0522 0.0253 -0.0346 74 ASN A CA 325 C C . ASN A 46 ? 0.6341 0.6365 0.7025 -0.0510 0.0235 -0.0334 74 ASN A C 326 O O . ASN A 46 ? 0.5405 0.5494 0.6118 -0.0517 0.0230 -0.0330 74 ASN A O 327 C CB . ASN A 46 ? 0.4709 0.4634 0.5261 -0.0553 0.0282 -0.0369 74 ASN A CB 328 C CG . ASN A 46 ? 0.4272 0.4100 0.4732 -0.0560 0.0291 -0.0373 74 ASN A CG 329 O OD1 . ASN A 46 ? 0.4407 0.4226 0.4842 -0.0554 0.0277 -0.0360 74 ASN A OD1 330 N ND2 . ASN A 46 ? 0.3496 0.3250 0.3904 -0.0569 0.0311 -0.0391 74 ASN A ND2 331 N N . GLY A 47 ? 0.6593 0.6619 0.7316 -0.0491 0.0222 -0.0328 75 GLY A N 332 C CA . GLY A 47 ? 0.5520 0.5622 0.6321 -0.0474 0.0199 -0.0315 75 GLY A CA 333 C C . GLY A 47 ? 0.4620 0.4806 0.5469 -0.0485 0.0213 -0.0335 75 GLY A C 334 O O . GLY A 47 ? 0.5316 0.5572 0.6217 -0.0477 0.0193 -0.0320 75 GLY A O 335 N N . LEU A 48 ? 0.3285 0.3464 0.4114 -0.0506 0.0247 -0.0368 76 LEU A N 336 C CA . LEU A 48 ? 0.4696 0.4959 0.5574 -0.0519 0.0263 -0.0392 76 LEU A CA 337 C C . LEU A 48 ? 0.7516 0.7797 0.8431 -0.0505 0.0271 -0.0411 76 LEU A C 338 O O . LEU A 48 ? 0.6327 0.6542 0.7208 -0.0501 0.0282 -0.0420 76 LEU A O 339 C CB . LEU A 48 ? 0.5751 0.6006 0.6581 -0.0558 0.0298 -0.0418 76 LEU A CB 340 C CG . LEU A 48 ? 0.5536 0.5781 0.6327 -0.0573 0.0295 -0.0406 76 LEU A CG 341 C CD1 . LEU A 48 ? 0.4131 0.4331 0.4853 -0.0611 0.0331 -0.0433 76 LEU A CD1 342 C CD2 . LEU A 48 ? 0.5176 0.5516 0.6027 -0.0571 0.0277 -0.0397 76 LEU A CD2 343 N N . PRO A 49 ? 0.8022 0.8395 0.9009 -0.0497 0.0265 -0.0420 77 PRO A N 344 C CA . PRO A 49 ? 0.8233 0.8643 0.9268 -0.0478 0.0268 -0.0440 77 PRO A CA 345 C C . PRO A 49 ? 0.8707 0.9106 0.9716 -0.0501 0.0311 -0.0479 77 PRO A C 346 O O . PRO A 49 ? 0.8869 0.9248 0.9830 -0.0537 0.0340 -0.0492 77 PRO A O 347 C CB . PRO A 49 ? 0.7798 0.8316 0.8906 -0.0472 0.0255 -0.0443 77 PRO A CB 348 C CG . PRO A 49 ? 0.7858 0.8392 0.8957 -0.0484 0.0241 -0.0421 77 PRO A CG 349 C CD . PRO A 49 ? 0.7780 0.8229 0.8803 -0.0503 0.0252 -0.0411 77 PRO A CD 350 N N . ASP A 50 ? 0.8661 0.9069 0.9698 -0.0479 0.0315 -0.0495 78 ASP A N 351 C CA . ASP A 50 ? 0.8611 0.9019 0.9630 -0.0498 0.0356 -0.0533 78 ASP A CA 352 C C . ASP A 50 ? 0.9304 0.9794 1.0343 -0.0534 0.0388 -0.0562 78 ASP A C 353 O O . ASP A 50 ? 1.0604 1.1068 1.1594 -0.0570 0.0426 -0.0584 78 ASP A O 354 C CB . ASP A 50 ? 0.9048 0.9478 1.0111 -0.0462 0.0350 -0.0546 78 ASP A CB 355 C CG . ASP A 50 ? 1.1059 1.1402 1.2098 -0.0429 0.0322 -0.0523 78 ASP A CG 356 O OD1 . ASP A 50 ? 1.1955 1.2257 1.2977 -0.0423 0.0293 -0.0488 78 ASP A OD1 357 O OD2 . ASP A 50 ? 1.1061 1.1381 1.2100 -0.0408 0.0328 -0.0539 78 ASP A OD2 358 N N . GLY A 51 ? 0.8408 0.8994 0.9513 -0.0527 0.0371 -0.0560 79 GLY A N 359 C CA . GLY A 51 ? 0.8023 0.8698 0.9158 -0.0559 0.0398 -0.0590 79 GLY A CA 360 C C . GLY A 51 ? 0.8595 0.9256 0.9683 -0.0604 0.0413 -0.0588 79 GLY A C 361 O O . GLY A 51 ? 0.8797 0.9532 0.9908 -0.0634 0.0432 -0.0610 79 GLY A O 362 N N . THR A 52 ? 0.8094 0.8661 0.9117 -0.0607 0.0403 -0.0562 80 THR A N 363 C CA . THR A 52 ? 0.7346 0.7883 0.8315 -0.0644 0.0413 -0.0558 80 THR A CA 364 C C . THR A 52 ? 0.6556 0.7061 0.7466 -0.0691 0.0459 -0.0589 80 THR A C 365 O O . THR A 52 ? 0.5976 0.6412 0.6841 -0.0694 0.0479 -0.0597 80 THR A O 366 C CB . THR A 52 ? 0.7462 0.7905 0.8375 -0.0630 0.0390 -0.0524 80 THR A CB 367 O OG1 . THR A 52 ? 0.6811 0.7283 0.7776 -0.0590 0.0349 -0.0495 80 THR A OG1 368 C CG2 . THR A 52 ? 0.7678 0.8097 0.8538 -0.0662 0.0397 -0.0521 80 THR A CG2 369 N N . LEU A 53 ? 0.6338 0.6892 0.7249 -0.0729 0.0476 -0.0605 81 LEU A N 370 C CA . LEU A 53 ? 0.6204 0.6732 0.7059 -0.0781 0.0519 -0.0633 81 LEU A CA 371 C C . LEU A 53 ? 0.5744 0.6146 0.6494 -0.0800 0.0526 -0.0622 81 LEU A C 372 O O . LEU A 53 ? 0.6198 0.6556 0.6924 -0.0782 0.0499 -0.0594 81 LEU A O 373 C CB . LEU A 53 ? 0.6541 0.7162 0.7430 -0.0818 0.0533 -0.0655 81 LEU A CB 374 C CG . LEU A 53 ? 0.6400 0.7154 0.7393 -0.0803 0.0529 -0.0672 81 LEU A CG 375 C CD1 . LEU A 53 ? 0.6315 0.7155 0.7335 -0.0843 0.0539 -0.0692 81 LEU A CD1 376 C CD2 . LEU A 53 ? 0.5193 0.5963 0.6201 -0.0802 0.0557 -0.0698 81 LEU A CD2 377 N N . SER A 54 ? 0.5048 0.5393 0.5732 -0.0837 0.0564 -0.0643 82 SER A N 378 C CA . SER A 54 ? 0.4990 0.5207 0.5566 -0.0856 0.0573 -0.0635 82 SER A CA 379 C C . SER A 54 ? 0.5766 0.5972 0.6305 -0.0883 0.0567 -0.0631 82 SER A C 380 O O . SER A 54 ? 0.5637 0.5740 0.6091 -0.0889 0.0564 -0.0619 82 SER A O 381 C CB . SER A 54 ? 0.5241 0.5404 0.5753 -0.0894 0.0615 -0.0660 82 SER A CB 382 O OG . SER A 54 ? 0.6657 0.6840 0.7143 -0.0949 0.0642 -0.0682 82 SER A OG 383 N N . SER A 55 ? 0.5716 0.6028 0.6320 -0.0898 0.0565 -0.0641 83 SER A N 384 C CA . SER A 55 ? 0.5810 0.6121 0.6384 -0.0925 0.0561 -0.0640 83 SER A CA 385 C C . SER A 55 ? 0.5073 0.5397 0.5674 -0.0884 0.0519 -0.0610 83 SER A C 386 O O . SER A 55 ? 0.4559 0.4892 0.5145 -0.0898 0.0509 -0.0606 83 SER A O 387 C CB . SER A 55 ? 0.5088 0.5509 0.5715 -0.0964 0.0578 -0.0667 83 SER A CB 388 O OG . SER A 55 ? 0.5939 0.6481 0.6675 -0.0932 0.0557 -0.0664 83 SER A OG 389 N N . ALA A 56 ? 0.4913 0.5238 0.5553 -0.0836 0.0495 -0.0588 84 ALA A N 390 C CA . ALA A 56 ? 0.5486 0.5823 0.6151 -0.0798 0.0455 -0.0557 84 ALA A CA 391 C C . ALA A 56 ? 0.5369 0.5616 0.5947 -0.0806 0.0449 -0.0545 84 ALA A C 392 O O . ALA A 56 ? 0.5390 0.5533 0.5889 -0.0811 0.0461 -0.0545 84 ALA A O 393 C CB . ALA A 56 ? 0.3887 0.4212 0.4586 -0.0751 0.0433 -0.0536 84 ALA A CB 394 N N . PRO A 57 ? 0.4210 0.4498 0.4802 -0.0804 0.0430 -0.0535 85 PRO A N 395 C CA . PRO A 57 ? 0.5845 0.6059 0.6354 -0.0818 0.0430 -0.0532 85 PRO A CA 396 C C . PRO A 57 ? 0.6090 0.6232 0.6560 -0.0781 0.0406 -0.0504 85 PRO A C 397 O O . PRO A 57 ? 0.5293 0.5472 0.5817 -0.0743 0.0380 -0.0480 85 PRO A O 398 C CB . PRO A 57 ? 0.4554 0.4853 0.5104 -0.0827 0.0416 -0.0533 85 PRO A CB 399 C CG . PRO A 57 ? 0.4888 0.5284 0.5538 -0.0792 0.0392 -0.0517 85 PRO A CG 400 C CD . PRO A 57 ? 0.4301 0.4704 0.4984 -0.0788 0.0408 -0.0527 85 PRO A CD 401 N N . VAL A 58 ? 0.6319 0.6355 0.6692 -0.0792 0.0415 -0.0508 86 VAL A N 402 C CA . VAL A 58 ? 0.5261 0.5236 0.5591 -0.0759 0.0392 -0.0485 86 VAL A CA 403 C C . VAL A 58 ? 0.4692 0.4642 0.4966 -0.0773 0.0389 -0.0490 86 VAL A C 404 O O . VAL A 58 ? 0.5011 0.4896 0.5210 -0.0808 0.0411 -0.0512 86 VAL A O 405 C CB . VAL A 58 ? 0.5482 0.5345 0.5741 -0.0753 0.0400 -0.0485 86 VAL A CB 406 C CG1 . VAL A 58 ? 0.5114 0.4924 0.5336 -0.0716 0.0374 -0.0462 86 VAL A CG1 407 C CG2 . VAL A 58 ? 0.5865 0.5748 0.6174 -0.0743 0.0406 -0.0485 86 VAL A CG2 408 N N . ALA A 59 ? 0.4570 0.4567 0.4874 -0.0747 0.0362 -0.0471 87 ALA A N 409 C CA . ALA A 59 ? 0.4426 0.4408 0.4681 -0.0756 0.0357 -0.0476 87 ALA A CA 410 C C . ALA A 59 ? 0.5354 0.5218 0.5507 -0.0746 0.0357 -0.0476 87 ALA A C 411 O O . ALA A 59 ? 0.5339 0.5152 0.5475 -0.0721 0.0350 -0.0463 87 ALA A O 412 C CB . ALA A 59 ? 0.3410 0.3480 0.3726 -0.0728 0.0329 -0.0454 87 ALA A CB 413 N N . ALA A 60 ? 0.5115 0.4933 0.5197 -0.0766 0.0362 -0.0491 88 ALA A N 414 C CA . ALA A 60 ? 0.5336 0.5047 0.5320 -0.0751 0.0356 -0.0491 88 ALA A CA 415 C C . ALA A 60 ? 0.4368 0.4100 0.4376 -0.0699 0.0327 -0.0464 88 ALA A C 416 O O . ALA A 60 ? 0.3083 0.2911 0.3162 -0.0683 0.0310 -0.0449 88 ALA A O 417 C CB . ALA A 60 ? 0.4742 0.4423 0.4662 -0.0774 0.0360 -0.0509 88 ALA A CB 418 N N . ASN A 61 ? 0.3660 0.3305 0.3610 -0.0676 0.0321 -0.0459 89 ASN A N 419 C CA . ASN A 61 ? 0.4069 0.3717 0.4026 -0.0629 0.0295 -0.0436 89 ASN A CA 420 C C . ASN A 61 ? 0.5477 0.5199 0.5527 -0.0606 0.0282 -0.0411 89 ASN A C 421 O O . ASN A 61 ? 0.5588 0.5310 0.5645 -0.0571 0.0261 -0.0391 89 ASN A O 422 C CB . ASN A 61 ? 0.4152 0.3845 0.4108 -0.0612 0.0278 -0.0431 89 ASN A CB 423 C CG . ASN A 61 ? 0.4247 0.3867 0.4110 -0.0632 0.0288 -0.0455 89 ASN A CG 424 O OD1 . ASN A 61 ? 0.5115 0.4631 0.4887 -0.0620 0.0287 -0.0464 89 ASN A OD1 425 N ND2 . ASN A 61 ? 0.4160 0.3831 0.4043 -0.0662 0.0296 -0.0468 89 ASN A ND2 426 N N . SER A 62 ? 0.5321 0.5100 0.5438 -0.0627 0.0293 -0.0412 90 SER A N 427 C CA . SER A 62 ? 0.4630 0.4472 0.4832 -0.0606 0.0279 -0.0390 90 SER A CA 428 C C . SER A 62 ? 0.4038 0.3806 0.4213 -0.0599 0.0284 -0.0389 90 SER A C 429 O O . SER A 62 ? 0.4464 0.4143 0.4564 -0.0618 0.0304 -0.0409 90 SER A O 430 C CB . SER A 62 ? 0.4637 0.4571 0.4920 -0.0626 0.0286 -0.0393 90 SER A CB 431 O OG . SER A 62 ? 0.5689 0.5590 0.5962 -0.0653 0.0312 -0.0413 90 SER A OG 432 N N . THR A 63 ? 0.4557 0.4357 0.4789 -0.0574 0.0267 -0.0367 91 THR A N 433 C CA . THR A 63 ? 0.4862 0.4590 0.5066 -0.0563 0.0267 -0.0365 91 THR A CA 434 C C . THR A 63 ? 0.4515 0.4264 0.4769 -0.0575 0.0279 -0.0370 91 THR A C 435 O O . THR A 63 ? 0.3814 0.3649 0.4145 -0.0578 0.0276 -0.0364 91 THR A O 436 C CB . THR A 63 ? 0.4110 0.3844 0.4332 -0.0526 0.0238 -0.0337 91 THR A CB 437 O OG1 . THR A 63 ? 0.4922 0.4753 0.5237 -0.0516 0.0221 -0.0315 91 THR A OG1 438 C CG2 . THR A 63 ? 0.3230 0.2944 0.3401 -0.0509 0.0226 -0.0334 91 THR A CG2 439 N N . VAL A 64 ? 0.4206 0.3872 0.4410 -0.0580 0.0293 -0.0381 92 VAL A N 440 C CA . VAL A 64 ? 0.3858 0.3532 0.4099 -0.0587 0.0305 -0.0387 92 VAL A CA 441 C C . VAL A 64 ? 0.3696 0.3292 0.3900 -0.0568 0.0297 -0.0380 92 VAL A C 442 O O . VAL A 64 ? 0.3964 0.3468 0.4083 -0.0569 0.0303 -0.0388 92 VAL A O 443 C CB . VAL A 64 ? 0.5243 0.4893 0.5450 -0.0626 0.0341 -0.0418 92 VAL A CB 444 C CG1 . VAL A 64 ? 0.4747 0.4417 0.4998 -0.0630 0.0354 -0.0426 92 VAL A CG1 445 C CG2 . VAL A 64 ? 0.4433 0.4151 0.4664 -0.0650 0.0350 -0.0428 92 VAL A CG2 446 N N . LYS A 65 ? 0.3158 0.2786 0.3423 -0.0551 0.0284 -0.0367 93 LYS A N 447 C CA . LYS A 65 ? 0.3477 0.3036 0.3714 -0.0534 0.0276 -0.0362 93 LYS A CA 448 C C . LYS A 65 ? 0.3769 0.3267 0.3960 -0.0555 0.0307 -0.0388 93 LYS A C 449 O O . LYS A 65 ? 0.4726 0.4269 0.4961 -0.0569 0.0324 -0.0400 93 LYS A O 450 C CB . LYS A 65 ? 0.4074 0.3688 0.4391 -0.0511 0.0252 -0.0340 93 LYS A CB 451 C CG . LYS A 65 ? 0.5558 0.5114 0.5855 -0.0486 0.0230 -0.0324 93 LYS A CG 452 C CD . LYS A 65 ? 0.5398 0.5020 0.5779 -0.0467 0.0201 -0.0299 93 LYS A CD 453 C CE . LYS A 65 ? 0.5959 0.5538 0.6329 -0.0444 0.0174 -0.0279 93 LYS A CE 454 N NZ . LYS A 65 ? 0.5773 0.5266 0.6094 -0.0442 0.0183 -0.0293 93 LYS A NZ 455 N N . ILE A 66 ? 0.3928 0.3323 0.4030 -0.0557 0.0314 -0.0396 94 ILE A N 456 C CA . ILE A 66 ? 0.3641 0.2971 0.3690 -0.0580 0.0345 -0.0420 94 ILE A CA 457 C C . ILE A 66 ? 0.3969 0.3226 0.3986 -0.0559 0.0335 -0.0414 94 ILE A C 458 O O . ILE A 66 ? 0.5157 0.4344 0.5116 -0.0543 0.0319 -0.0406 94 ILE A O 459 C CB . ILE A 66 ? 0.4948 0.4210 0.4905 -0.0609 0.0369 -0.0439 94 ILE A CB 460 C CG1 . ILE A 66 ? 0.4553 0.3894 0.4547 -0.0631 0.0377 -0.0445 94 ILE A CG1 461 C CG2 . ILE A 66 ? 0.4688 0.3881 0.4585 -0.0636 0.0402 -0.0463 94 ILE A CG2 462 C CD1 . ILE A 66 ? 0.5472 0.4754 0.5382 -0.0664 0.0400 -0.0465 94 ILE A CD1 463 N N . PRO A 67 ? 0.3846 0.3124 0.3906 -0.0557 0.0341 -0.0419 95 PRO A N 464 C CA . PRO A 67 ? 0.5241 0.4454 0.5276 -0.0539 0.0333 -0.0416 95 PRO A CA 465 C C . PRO A 67 ? 0.5477 0.4591 0.5417 -0.0559 0.0362 -0.0439 95 PRO A C 466 O O . PRO A 67 ? 0.5149 0.4264 0.5064 -0.0592 0.0395 -0.0460 95 PRO A O 467 C CB . PRO A 67 ? 0.4907 0.4190 0.5028 -0.0531 0.0331 -0.0416 95 PRO A CB 468 C CG . PRO A 67 ? 0.6137 0.5515 0.6317 -0.0550 0.0347 -0.0425 95 PRO A CG 469 C CD . PRO A 67 ? 0.5256 0.4627 0.5393 -0.0571 0.0356 -0.0429 95 PRO A CD 470 N N . PHE A 68 ? 0.4547 0.3575 0.4431 -0.0542 0.0350 -0.0435 96 PHE A N 471 C CA . PHE A 68 ? 0.4852 0.3780 0.4641 -0.0560 0.0377 -0.0455 96 PHE A CA 472 C C . PHE A 68 ? 0.4655 0.3512 0.4413 -0.0536 0.0359 -0.0449 96 PHE A C 473 O O . PHE A 68 ? 0.4413 0.3290 0.4213 -0.0505 0.0325 -0.0428 96 PHE A O 474 C CB . PHE A 68 ? 0.4739 0.3595 0.4435 -0.0577 0.0386 -0.0461 96 PHE A CB 475 C CG . PHE A 68 ? 0.5236 0.4061 0.4908 -0.0548 0.0351 -0.0442 96 PHE A CG 476 C CD1 . PHE A 68 ? 0.5298 0.4027 0.4900 -0.0528 0.0335 -0.0438 96 PHE A CD1 477 C CD2 . PHE A 68 ? 0.3002 0.1898 0.2724 -0.0539 0.0333 -0.0429 96 PHE A CD2 478 C CE1 . PHE A 68 ? 0.5777 0.4486 0.5361 -0.0499 0.0302 -0.0422 96 PHE A CE1 479 C CE2 . PHE A 68 ? 0.4270 0.3146 0.3973 -0.0511 0.0303 -0.0413 96 PHE A CE2 480 C CZ . PHE A 68 ? 0.4419 0.3204 0.4055 -0.0491 0.0287 -0.0409 96 PHE A CZ 481 N N . ARG A 69 ? 0.4855 0.3627 0.4533 -0.0551 0.0384 -0.0467 97 ARG A N 482 C CA . ARG A 69 ? 0.5264 0.3956 0.4898 -0.0529 0.0369 -0.0464 97 ARG A CA 483 C C . ARG A 69 ? 0.5417 0.4020 0.4968 -0.0515 0.0348 -0.0455 97 ARG A C 484 O O . ARG A 69 ? 0.5762 0.4303 0.5232 -0.0534 0.0364 -0.0465 97 ARG A O 485 C CB . ARG A 69 ? 0.5030 0.3671 0.4613 -0.0550 0.0404 -0.0487 97 ARG A CB 486 C CG . ARG A 69 ? 0.7214 0.5826 0.6805 -0.0524 0.0389 -0.0485 97 ARG A CG 487 C CD . ARG A 69 ? 0.9131 0.7629 0.8613 -0.0535 0.0408 -0.0501 97 ARG A CD 488 N NE . ARG A 69 ? 0.9753 0.8250 0.9201 -0.0576 0.0456 -0.0525 97 ARG A NE 489 C CZ . ARG A 69 ? 1.0448 0.8851 0.9795 -0.0596 0.0483 -0.0542 97 ARG A CZ 490 N NH1 . ARG A 69 ? 1.1378 0.9677 1.0647 -0.0578 0.0465 -0.0537 97 ARG A NH1 491 N NH2 . ARG A 69 ? 1.0106 0.8521 0.9429 -0.0637 0.0528 -0.0563 97 ARG A NH2 492 N N . CYS A 70 ? 0.5619 0.4219 0.5193 -0.0481 0.0309 -0.0435 98 CYS A N 493 C CA . CYS A 70 ? 0.4232 0.2752 0.3733 -0.0462 0.0285 -0.0428 98 CYS A CA 494 C C . CYS A 70 ? 0.5242 0.3659 0.4668 -0.0453 0.0283 -0.0435 98 CYS A C 495 O O . CYS A 70 ? 0.5168 0.3594 0.4628 -0.0445 0.0279 -0.0435 98 CYS A O 496 C CB . CYS A 70 ? 0.3916 0.2499 0.3487 -0.0431 0.0244 -0.0402 98 CYS A CB 497 S SG . CYS A 70 ? 0.4989 0.3493 0.4484 -0.0402 0.0210 -0.0393 98 CYS A SG 498 N N . ARG A 71 ? 0.5649 0.3963 0.4968 -0.0454 0.0284 -0.0442 99 ARG A N 499 C CA . ARG A 71 ? 0.6207 0.4415 0.5445 -0.0441 0.0275 -0.0446 99 ARG A CA 500 C C . ARG A 71 ? 0.5728 0.3889 0.4925 -0.0409 0.0236 -0.0433 99 ARG A C 501 O O . ARG A 71 ? 0.6293 0.4442 0.5456 -0.0408 0.0233 -0.0433 99 ARG A O 502 C CB . ARG A 71 ? 0.6826 0.4938 0.5959 -0.0471 0.0312 -0.0468 99 ARG A CB 503 C CG . ARG A 71 ? 0.7190 0.5182 0.6224 -0.0456 0.0300 -0.0471 99 ARG A CG 504 C CD . ARG A 71 ? 0.7865 0.5764 0.6796 -0.0488 0.0340 -0.0492 99 ARG A CD 505 N NE . ARG A 71 ? 0.8746 0.6524 0.7577 -0.0471 0.0324 -0.0495 99 ARG A NE 506 C CZ . ARG A 71 ? 0.9867 0.7597 0.8664 -0.0474 0.0336 -0.0504 99 ARG A CZ 507 N NH1 . ARG A 71 ? 0.9833 0.7626 0.8689 -0.0492 0.0364 -0.0514 99 ARG A NH1 508 N NH2 . ARG A 71 ? 0.9792 0.7410 0.8494 -0.0457 0.0318 -0.0505 99 ARG A NH2 509 N N . CYS A 72 ? 0.5561 0.3696 0.4761 -0.0382 0.0207 -0.0425 100 CYS A N 510 C CA . CYS A 72 ? 0.6530 0.4624 0.5694 -0.0350 0.0168 -0.0414 100 CYS A CA 511 C C . CYS A 72 ? 0.6806 0.4761 0.5840 -0.0348 0.0172 -0.0428 100 CYS A C 512 O O . CYS A 72 ? 0.6343 0.4247 0.5341 -0.0361 0.0190 -0.0439 100 CYS A O 513 C CB . CYS A 72 ? 0.6256 0.4407 0.5501 -0.0324 0.0130 -0.0396 100 CYS A CB 514 S SG . CYS A 72 ? 0.7159 0.5465 0.6545 -0.0322 0.0117 -0.0375 100 CYS A SG 515 N N . ASN A 73 ? 0.7095 0.4988 0.6054 -0.0333 0.0157 -0.0429 101 ASN A N 516 C CA . ASN A 73 ? 0.7141 0.4897 0.5972 -0.0327 0.0154 -0.0440 101 ASN A CA 517 C C . ASN A 73 ? 0.7264 0.4979 0.6070 -0.0286 0.0109 -0.0432 101 ASN A C 518 O O . ASN A 73 ? 0.7858 0.5458 0.6553 -0.0276 0.0102 -0.0441 101 ASN A O 519 C CB . ASN A 73 ? 0.6705 0.4381 0.5433 -0.0342 0.0174 -0.0452 101 ASN A CB 520 C CG . ASN A 73 ? 0.6934 0.4634 0.5666 -0.0317 0.0148 -0.0445 101 ASN A CG 521 O OD1 . ASN A 73 ? 0.6212 0.3979 0.5012 -0.0285 0.0113 -0.0431 101 ASN A OD1 522 N ND2 . ASN A 73 ? 0.8777 0.6413 0.7426 -0.0332 0.0165 -0.0456 101 ASN A ND2 523 N N . GLY A 74 ? 0.7547 0.5354 0.6452 -0.0264 0.0077 -0.0415 102 GLY A N 524 C CA . GLY A 74 ? 0.7196 0.4979 0.6089 -0.0227 0.0032 -0.0408 102 GLY A CA 525 C C . GLY A 74 ? 0.7494 0.5334 0.6417 -0.0200 0.0004 -0.0397 102 GLY A C 526 O O . GLY A 74 ? 0.6864 0.4740 0.5827 -0.0172 -0.0035 -0.0386 102 GLY A O 527 N N . ASP A 75 ? 0.6129 0.3979 0.5036 -0.0211 0.0023 -0.0402 103 ASP A N 528 C CA . ASP A 75 ? 0.7198 0.5098 0.6124 -0.0185 0.0001 -0.0396 103 ASP A CA 529 C C . ASP A 75 ? 0.6422 0.4437 0.5441 -0.0205 0.0020 -0.0388 103 ASP A C 530 O O . ASP A 75 ? 0.5283 0.3396 0.4380 -0.0188 -0.0001 -0.0375 103 ASP A O 531 C CB . ASP A 75 ? 0.7926 0.5718 0.6728 -0.0175 0.0003 -0.0411 103 ASP A CB 532 C CG . ASP A 75 ? 0.9440 0.7123 0.8148 -0.0146 -0.0025 -0.0417 103 ASP A CG 533 O OD1 . ASP A 75 ? 1.0799 0.8522 0.9553 -0.0117 -0.0061 -0.0407 103 ASP A OD1 534 O OD2 . ASP A 75 ? 0.9530 0.7087 0.8117 -0.0152 -0.0012 -0.0431 103 ASP A OD2 535 N N . VAL A 76 ? 0.5318 0.3322 0.4329 -0.0242 0.0060 -0.0397 104 VAL A N 536 C CA . VAL A 76 ? 0.4841 0.2930 0.3913 -0.0262 0.0080 -0.0395 104 VAL A CA 537 C C . VAL A 76 ? 0.6199 0.4327 0.5322 -0.0299 0.0115 -0.0398 104 VAL A C 538 O O . VAL A 76 ? 0.5818 0.3884 0.4903 -0.0312 0.0129 -0.0406 104 VAL A O 539 C CB . VAL A 76 ? 0.6866 0.4887 0.5844 -0.0265 0.0094 -0.0409 104 VAL A CB 540 C CG1 . VAL A 76 ? 0.6368 0.4282 0.5249 -0.0299 0.0130 -0.0427 104 VAL A CG1 541 C CG2 . VAL A 76 ? 0.7617 0.5730 0.6657 -0.0274 0.0102 -0.0405 104 VAL A CG2 542 N N . GLY A 77 ? 0.6021 0.4256 0.5234 -0.0313 0.0125 -0.0391 105 GLY A N 543 C CA . GLY A 77 ? 0.6135 0.4415 0.5397 -0.0346 0.0158 -0.0396 105 GLY A CA 544 C C . GLY A 77 ? 0.5968 0.4244 0.5197 -0.0375 0.0190 -0.0409 105 GLY A C 545 O O . GLY A 77 ? 0.5516 0.3831 0.4758 -0.0367 0.0182 -0.0404 105 GLY A O 546 N N . GLN A 78 ? 0.4368 0.2600 0.3556 -0.0408 0.0227 -0.0425 106 GLN A N 547 C CA . GLN A 78 ? 0.5380 0.3608 0.4537 -0.0441 0.0259 -0.0439 106 GLN A CA 548 C C . GLN A 78 ? 0.5131 0.3417 0.4343 -0.0476 0.0293 -0.0447 106 GLN A C 549 O O . GLN A 78 ? 0.5176 0.3455 0.4404 -0.0478 0.0300 -0.0449 106 GLN A O 550 C CB . GLN A 78 ? 0.5470 0.3557 0.4484 -0.0452 0.0272 -0.0454 106 GLN A CB 551 C CG . GLN A 78 ? 0.5982 0.4005 0.4934 -0.0414 0.0236 -0.0448 106 GLN A CG 552 C CD . GLN A 78 ? 0.7293 0.5167 0.6105 -0.0417 0.0241 -0.0462 106 GLN A CD 553 O OE1 . GLN A 78 ? 0.7967 0.5779 0.6734 -0.0434 0.0258 -0.0469 106 GLN A OE1 554 N NE2 . GLN A 78 ? 0.6566 0.4374 0.5299 -0.0401 0.0226 -0.0465 106 GLN A NE2 555 N N . SER A 79 ? 0.5129 0.3475 0.4373 -0.0502 0.0314 -0.0452 107 SER A N 556 C CA . SER A 79 ? 0.4593 0.2995 0.3885 -0.0537 0.0349 -0.0464 107 SER A CA 557 C C . SER A 79 ? 0.5585 0.3883 0.4779 -0.0563 0.0379 -0.0483 107 SER A C 558 O O . SER A 79 ? 0.5156 0.3348 0.4240 -0.0572 0.0385 -0.0491 107 SER A O 559 C CB . SER A 79 ? 0.5535 0.4002 0.4857 -0.0562 0.0366 -0.0469 107 SER A CB 560 O OG . SER A 79 ? 0.5109 0.3489 0.4327 -0.0579 0.0376 -0.0480 107 SER A OG 561 N N . ASP A 80 ? 0.6587 0.4912 0.5818 -0.0573 0.0397 -0.0490 108 ASP A N 562 C CA . ASP A 80 ? 0.6238 0.4464 0.5382 -0.0586 0.0418 -0.0504 108 ASP A CA 563 C C . ASP A 80 ? 0.6401 0.4582 0.5472 -0.0636 0.0463 -0.0525 108 ASP A C 564 O O . ASP A 80 ? 0.6577 0.4815 0.5689 -0.0664 0.0495 -0.0538 108 ASP A O 565 C CB . ASP A 80 ? 0.6054 0.4329 0.5267 -0.0575 0.0418 -0.0504 108 ASP A CB 566 C CG . ASP A 80 ? 0.6873 0.5047 0.6000 -0.0579 0.0432 -0.0516 108 ASP A CG 567 O OD1 . ASP A 80 ? 0.8110 0.6171 0.7122 -0.0588 0.0437 -0.0521 108 ASP A OD1 568 O OD2 . ASP A 80 ? 0.7022 0.5228 0.6196 -0.0571 0.0436 -0.0519 108 ASP A OD2 569 N N . ARG A 81 ? 0.7318 0.5394 0.6277 -0.0646 0.0463 -0.0528 109 ARG A N 570 C CA . ARG A 81 ? 0.7401 0.5417 0.6273 -0.0696 0.0502 -0.0546 109 ARG A CA 571 C C . ARG A 81 ? 0.6756 0.4874 0.5698 -0.0731 0.0527 -0.0554 109 ARG A C 572 O O . ARG A 81 ? 0.8521 0.6614 0.7411 -0.0779 0.0563 -0.0570 109 ARG A O 573 C CB . ARG A 81 ? 0.7009 0.4954 0.5813 -0.0720 0.0533 -0.0560 109 ARG A CB 574 C CG . ARG A 81 ? 0.8428 0.6260 0.7150 -0.0688 0.0509 -0.0554 109 ARG A CG 575 C CD . ARG A 81 ? 1.0740 0.8444 0.9334 -0.0687 0.0496 -0.0552 109 ARG A CD 576 N NE . ARG A 81 ? 1.2255 0.9876 1.0797 -0.0641 0.0457 -0.0542 109 ARG A NE 577 C CZ . ARG A 81 ? 1.2660 1.0144 1.1071 -0.0636 0.0446 -0.0543 109 ARG A CZ 578 N NH1 . ARG A 81 ? 1.2723 1.0130 1.1037 -0.0675 0.0470 -0.0553 109 ARG A NH1 579 N NH2 . ARG A 81 ? 1.1921 0.9344 1.0297 -0.0591 0.0408 -0.0534 109 ARG A NH2 580 N N . LEU A 82 ? 0.6382 0.4615 0.5437 -0.0708 0.0505 -0.0542 110 LEU A N 581 C CA . LEU A 82 ? 0.5318 0.3654 0.4445 -0.0733 0.0520 -0.0546 110 LEU A CA 582 C C . LEU A 82 ? 0.5668 0.4047 0.4840 -0.0699 0.0482 -0.0528 110 LEU A C 583 O O . LEU A 82 ? 0.5571 0.3937 0.4754 -0.0656 0.0448 -0.0512 110 LEU A O 584 C CB . LEU A 82 ? 0.5426 0.3885 0.4670 -0.0737 0.0534 -0.0550 110 LEU A CB 585 C CG . LEU A 82 ? 0.6146 0.4586 0.5358 -0.0773 0.0576 -0.0571 110 LEU A CG 586 C CD1 . LEU A 82 ? 0.4727 0.3277 0.4052 -0.0762 0.0582 -0.0575 110 LEU A CD1 587 C CD2 . LEU A 82 ? 0.6669 0.5106 0.5839 -0.0829 0.0612 -0.0589 110 LEU A CD2 588 N N . PRO A 83 ? 0.5372 0.3804 0.4567 -0.0720 0.0489 -0.0532 111 PRO A N 589 C CA . PRO A 83 ? 0.6620 0.5068 0.5799 -0.0774 0.0527 -0.0551 111 PRO A CA 590 C C . PRO A 83 ? 0.5909 0.4218 0.4943 -0.0805 0.0544 -0.0563 111 PRO A C 591 O O . PRO A 83 ? 0.5960 0.4166 0.4911 -0.0780 0.0521 -0.0555 111 PRO A O 592 C CB . PRO A 83 ? 0.6413 0.4959 0.5666 -0.0772 0.0515 -0.0545 111 PRO A CB 593 C CG . PRO A 83 ? 0.5742 0.4261 0.4984 -0.0725 0.0474 -0.0527 111 PRO A CG 594 C CD . PRO A 83 ? 0.5220 0.3705 0.4464 -0.0689 0.0456 -0.0516 111 PRO A CD 595 N N . ILE A 84 ? 0.6541 0.4850 0.5548 -0.0860 0.0582 -0.0581 112 ILE A N 596 C CA . ILE A 84 ? 0.7703 0.5882 0.6571 -0.0899 0.0602 -0.0593 112 ILE A CA 597 C C . ILE A 84 ? 0.7767 0.5960 0.6623 -0.0926 0.0604 -0.0598 112 ILE A C 598 O O . ILE A 84 ? 0.7687 0.5994 0.6630 -0.0949 0.0618 -0.0604 112 ILE A O 599 C CB . ILE A 84 ? 0.8313 0.6473 0.7147 -0.0949 0.0647 -0.0611 112 ILE A CB 600 C CG1 . ILE A 84 ? 0.7362 0.5447 0.6149 -0.0925 0.0643 -0.0607 112 ILE A CG1 601 C CG2 . ILE A 84 ? 0.8527 0.6591 0.7243 -0.1007 0.0674 -0.0625 112 ILE A CG2 602 C CD1 . ILE A 84 ? 0.7668 0.5612 0.6342 -0.0897 0.0615 -0.0597 112 ILE A CD1 603 N N . TYR A 85 ? 0.7659 0.5733 0.6404 -0.0921 0.0588 -0.0597 113 TYR A N 604 C CA . TYR A 85 ? 0.8534 0.6607 0.7254 -0.0946 0.0588 -0.0603 113 TYR A CA 605 C C . TYR A 85 ? 0.9561 0.7499 0.8137 -0.1000 0.0613 -0.0618 113 TYR A C 606 O O . TYR A 85 ? 0.9765 0.7561 0.8222 -0.0990 0.0605 -0.0616 113 TYR A O 607 C CB . TYR A 85 ? 0.7043 0.5109 0.5765 -0.0894 0.0545 -0.0590 113 TYR A CB 608 C CG . TYR A 85 ? 0.7715 0.5791 0.6422 -0.0916 0.0544 -0.0597 113 TYR A CG 609 C CD1 . TYR A 85 ? 0.6517 0.4735 0.5340 -0.0921 0.0544 -0.0596 113 TYR A CD1 610 C CD2 . TYR A 85 ? 0.7624 0.5561 0.6192 -0.0935 0.0543 -0.0605 113 TYR A CD2 611 C CE1 . TYR A 85 ? 0.6705 0.4931 0.5511 -0.0942 0.0543 -0.0604 113 TYR A CE1 612 C CE2 . TYR A 85 ? 0.7740 0.5680 0.6289 -0.0956 0.0541 -0.0613 113 TYR A CE2 613 C CZ . TYR A 85 ? 0.7748 0.5833 0.6415 -0.0960 0.0542 -0.0613 113 TYR A CZ 614 O OH . TYR A 85 ? 0.6780 0.4863 0.5422 -0.0981 0.0539 -0.0622 113 TYR A OH 615 N N . VAL A 86 ? 0.9467 0.7449 0.8055 -0.1057 0.0641 -0.0632 114 VAL A N 616 C CA . VAL A 86 ? 0.8916 0.6777 0.7371 -0.1116 0.0665 -0.0646 114 VAL A CA 617 C C . VAL A 86 ? 0.7935 0.5729 0.6321 -0.1113 0.0642 -0.0646 114 VAL A C 618 O O . VAL A 86 ? 0.8139 0.6026 0.6596 -0.1118 0.0637 -0.0649 114 VAL A O 619 C CB . VAL A 86 ? 0.9508 0.7446 0.8003 -0.1186 0.0712 -0.0663 114 VAL A CB 620 C CG1 . VAL A 86 ? 0.8378 0.6343 0.6901 -0.1191 0.0737 -0.0665 114 VAL A CG1 621 C CG2 . VAL A 86 ? 1.0495 0.8601 0.9130 -0.1188 0.0710 -0.0665 114 VAL A CG2 622 N N . VAL A 87 ? 0.7971 0.5600 0.6214 -0.1104 0.0628 -0.0645 115 VAL A N 623 C CA . VAL A 87 ? 0.8872 0.6414 0.7031 -0.1094 0.0603 -0.0647 115 VAL A CA 624 C C . VAL A 87 ? 1.0375 0.7926 0.8512 -0.1161 0.0626 -0.0662 115 VAL A C 625 O O . VAL A 87 ? 1.0287 0.7817 0.8386 -0.1227 0.0664 -0.0673 115 VAL A O 626 C CB . VAL A 87 ? 0.8689 0.6037 0.6681 -0.1082 0.0589 -0.0645 115 VAL A CB 627 C CG1 . VAL A 87 ? 0.8738 0.5995 0.6642 -0.1067 0.0561 -0.0649 115 VAL A CG1 628 C CG2 . VAL A 87 ? 0.8088 0.5423 0.6096 -0.1017 0.0565 -0.0632 115 VAL A CG2 629 N N . GLN A 88 ? 1.0656 0.8250 0.8824 -0.1143 0.0604 -0.0662 116 GLN A N 630 C CA . GLN A 88 ? 1.1273 0.8880 0.9425 -0.1202 0.0620 -0.0677 116 GLN A CA 631 C C . GLN A 88 ? 1.1974 0.9412 0.9967 -0.1215 0.0606 -0.0684 116 GLN A C 632 O O . GLN A 88 ? 1.1690 0.9017 0.9599 -0.1164 0.0576 -0.0677 116 GLN A O 633 C CB . GLN A 88 ? 1.1132 0.8911 0.9431 -0.1182 0.0609 -0.0675 116 GLN A CB 634 C CG . GLN A 88 ? 1.1608 0.9541 1.0054 -0.1170 0.0622 -0.0668 116 GLN A CG 635 C CD . GLN A 88 ? 1.2065 1.0044 1.0534 -0.1240 0.0668 -0.0681 116 GLN A CD 636 O OE1 . GLN A 88 ? 1.1152 0.9024 0.9522 -0.1277 0.0691 -0.0687 116 GLN A OE1 637 N NE2 . GLN A 88 ? 1.2502 1.0641 1.1100 -0.1258 0.0681 -0.0686 116 GLN A NE2 638 N N . PRO A 89 ? 1.1932 0.9350 0.9881 -0.1283 0.0627 -0.0699 117 PRO A N 639 C CA . PRO A 89 ? 1.1819 0.9075 0.9613 -0.1305 0.0615 -0.0708 117 PRO A CA 640 C C . PRO A 89 ? 1.1307 0.8486 0.9047 -0.1230 0.0568 -0.0701 117 PRO A C 641 O O . PRO A 89 ? 1.2413 0.9421 1.0009 -0.1217 0.0553 -0.0701 117 PRO A O 642 C CB . PRO A 89 ? 1.1503 0.8838 0.9341 -0.1363 0.0630 -0.0722 117 PRO A CB 643 C CG . PRO A 89 ? 1.0961 0.8451 0.8926 -0.1403 0.0668 -0.0724 117 PRO A CG 644 C CD . PRO A 89 ? 1.1277 0.8823 0.9317 -0.1349 0.0664 -0.0709 117 PRO A CD 645 N N . GLN A 90 ? 0.9422 0.6725 0.7274 -0.1180 0.0544 -0.0697 118 GLN A N 646 C CA . GLN A 90 ? 0.9600 0.6849 0.7412 -0.1107 0.0500 -0.0692 118 GLN A CA 647 C C . GLN A 90 ? 1.0477 0.7833 0.8403 -0.1030 0.0477 -0.0675 118 GLN A C 648 O O . GLN A 90 ? 1.0018 0.7451 0.8008 -0.0981 0.0451 -0.0671 118 GLN A O 649 C CB . GLN A 90 ? 1.0285 0.7553 0.8093 -0.1113 0.0486 -0.0703 118 GLN A CB 650 C CG . GLN A 90 ? 1.1394 0.8780 0.9285 -0.1181 0.0516 -0.0713 118 GLN A CG 651 C CD . GLN A 90 ? 1.2160 0.9542 1.0026 -0.1190 0.0500 -0.0725 118 GLN A CD 652 O OE1 . GLN A 90 ? 1.2425 0.9768 1.0257 -0.1131 0.0465 -0.0724 118 GLN A OE1 653 N NE2 . GLN A 90 ? 1.2494 0.9918 1.0376 -0.1264 0.0525 -0.0738 118 GLN A NE2 654 N N . ASP A 91 ? 1.0450 0.7813 0.8400 -0.1022 0.0488 -0.0666 119 ASP A N 655 C CA . ASP A 91 ? 0.8720 0.6172 0.6770 -0.0954 0.0467 -0.0649 119 ASP A CA 656 C C . ASP A 91 ? 0.9865 0.7186 0.7812 -0.0896 0.0435 -0.0644 119 ASP A C 657 O O . ASP A 91 ? 1.0927 0.8085 0.8730 -0.0916 0.0438 -0.0651 119 ASP A O 658 C CB . ASP A 91 ? 0.8022 0.5555 0.6157 -0.0973 0.0494 -0.0642 119 ASP A CB 659 C CG . ASP A 91 ? 0.7207 0.4927 0.5503 -0.0988 0.0508 -0.0640 119 ASP A CG 660 O OD1 . ASP A 91 ? 0.6911 0.4708 0.5262 -0.0976 0.0494 -0.0641 119 ASP A OD1 661 O OD2 . ASP A 91 ? 0.6783 0.4575 0.5151 -0.1008 0.0533 -0.0637 119 ASP A OD2 662 N N . GLY A 92 ? 1.0149 0.7541 0.8169 -0.0826 0.0404 -0.0632 120 GLY A N 663 C CA . GLY A 92 ? 0.9492 0.6795 0.7447 -0.0763 0.0372 -0.0626 120 GLY A CA 664 C C . GLY A 92 ? 0.9913 0.7337 0.7995 -0.0722 0.0364 -0.0609 120 GLY A C 665 O O . GLY A 92 ? 0.9497 0.7078 0.7716 -0.0721 0.0368 -0.0602 120 GLY A O 666 N N . LEU A 93 ? 0.9252 0.6600 0.7285 -0.0689 0.0350 -0.0602 121 LEU A N 667 C CA . LEU A 93 ? 0.8010 0.5453 0.6147 -0.0654 0.0341 -0.0587 121 LEU A CA 668 C C . LEU A 93 ? 0.8702 0.6288 0.6962 -0.0606 0.0317 -0.0576 121 LEU A C 669 O O . LEU A 93 ? 0.8634 0.6357 0.7025 -0.0604 0.0322 -0.0565 121 LEU A O 670 C CB . LEU A 93 ? 0.7120 0.4445 0.5168 -0.0614 0.0319 -0.0583 121 LEU A CB 671 C CG . LEU A 93 ? 0.7797 0.5010 0.5754 -0.0658 0.0346 -0.0588 121 LEU A CG 672 C CD1 . LEU A 93 ? 0.8902 0.6014 0.6786 -0.0611 0.0320 -0.0583 121 LEU A CD1 673 C CD2 . LEU A 93 ? 0.7786 0.5104 0.5845 -0.0705 0.0383 -0.0585 121 LEU A CD2 674 N N . ASP A 94 ? 0.8356 0.5907 0.6568 -0.0567 0.0289 -0.0581 122 ASP A N 675 C CA . ASP A 94 ? 0.7936 0.5612 0.6248 -0.0519 0.0264 -0.0572 122 ASP A CA 676 C C . ASP A 94 ? 0.7968 0.5780 0.6387 -0.0552 0.0282 -0.0571 122 ASP A C 677 O O . ASP A 94 ? 0.8178 0.6130 0.6720 -0.0529 0.0273 -0.0558 122 ASP A O 678 C CB . ASP A 94 ? 0.7111 0.4707 0.5331 -0.0472 0.0232 -0.0582 122 ASP A CB 679 C CG . ASP A 94 ? 0.7519 0.5239 0.5835 -0.0415 0.0204 -0.0572 122 ASP A CG 680 O OD1 . ASP A 94 ? 0.7079 0.4832 0.5436 -0.0370 0.0184 -0.0560 122 ASP A OD1 681 O OD2 . ASP A 94 ? 0.7417 0.5197 0.5761 -0.0414 0.0202 -0.0577 122 ASP A OD2 682 N N . ALA A 95 ? 0.7452 0.5221 0.5820 -0.0607 0.0306 -0.0586 123 ALA A N 683 C CA . ALA A 95 ? 0.7375 0.5269 0.5840 -0.0643 0.0325 -0.0586 123 ALA A CA 684 C C . ALA A 95 ? 0.7685 0.5685 0.6262 -0.0673 0.0350 -0.0577 123 ALA A C 685 O O . ALA A 95 ? 0.7750 0.5892 0.6449 -0.0675 0.0353 -0.0569 123 ALA A O 686 C CB . ALA A 95 ? 0.6931 0.4749 0.5309 -0.0696 0.0343 -0.0605 123 ALA A CB 687 N N . ILE A 96 ? 0.6890 0.4817 0.5421 -0.0696 0.0367 -0.0578 124 ILE A N 688 C CA . ILE A 96 ? 0.6496 0.4513 0.5124 -0.0719 0.0389 -0.0571 124 ILE A CA 689 C C . ILE A 96 ? 0.6590 0.4710 0.5328 -0.0665 0.0365 -0.0551 124 ILE A C 690 O O . ILE A 96 ? 0.6556 0.4810 0.5417 -0.0669 0.0370 -0.0542 124 ILE A O 691 C CB . ILE A 96 ? 0.6866 0.4772 0.5410 -0.0747 0.0410 -0.0576 124 ILE A CB 692 C CG1 . ILE A 96 ? 0.7111 0.4926 0.5555 -0.0811 0.0439 -0.0595 124 ILE A CG1 693 C CG2 . ILE A 96 ? 0.6688 0.4689 0.5336 -0.0756 0.0427 -0.0568 124 ILE A CG2 694 C CD1 . ILE A 96 ? 0.5604 0.3267 0.3920 -0.0835 0.0453 -0.0601 124 ILE A CD1 695 N N . ALA A 97 ? 0.5687 0.3740 0.4375 -0.0616 0.0337 -0.0544 125 ALA A N 696 C CA . ALA A 97 ? 0.4950 0.3085 0.3725 -0.0564 0.0311 -0.0526 125 ALA A CA 697 C C . ALA A 97 ? 0.7295 0.5570 0.6178 -0.0545 0.0297 -0.0516 125 ALA A C 698 O O . ALA A 97 ? 0.7489 0.5885 0.6491 -0.0538 0.0295 -0.0502 125 ALA A O 699 C CB . ALA A 97 ? 0.5082 0.3115 0.3770 -0.0514 0.0280 -0.0525 125 ALA A CB 700 N N . ARG A 98 ? 0.7129 0.5385 0.5967 -0.0539 0.0288 -0.0525 126 ARG A N 701 C CA . ARG A 98 ? 0.6066 0.4444 0.4992 -0.0515 0.0273 -0.0517 126 ARG A CA 702 C C . ARG A 98 ? 0.6093 0.4573 0.5097 -0.0557 0.0294 -0.0519 126 ARG A C 703 O O . ARG A 98 ? 0.6695 0.5304 0.5809 -0.0544 0.0286 -0.0505 126 ARG A O 704 C CB . ARG A 98 ? 0.5953 0.4271 0.4798 -0.0481 0.0250 -0.0526 126 ARG A CB 705 C CG . ARG A 98 ? 0.6899 0.5139 0.5682 -0.0429 0.0223 -0.0523 126 ARG A CG 706 C CD . ARG A 98 ? 0.5901 0.4107 0.4623 -0.0387 0.0198 -0.0532 126 ARG A CD 707 N NE . ARG A 98 ? 0.6573 0.4819 0.5329 -0.0327 0.0167 -0.0520 126 ARG A NE 708 C CZ . ARG A 98 ? 0.6884 0.5034 0.5566 -0.0295 0.0150 -0.0523 126 ARG A CZ 709 N NH1 . ARG A 98 ? 0.8209 0.6213 0.6776 -0.0318 0.0161 -0.0536 126 ARG A NH1 710 N NH2 . ARG A 98 ? 0.5878 0.4078 0.4599 -0.0241 0.0121 -0.0512 126 ARG A NH2 711 N N . ASN A 99 ? 0.6447 0.4866 0.5390 -0.0608 0.0320 -0.0537 127 ASN A N 712 C CA . ASN A 99 ? 0.5424 0.3930 0.4427 -0.0650 0.0339 -0.0543 127 ASN A CA 713 C C . ASN A 99 ? 0.5069 0.3639 0.4146 -0.0690 0.0366 -0.0541 127 ASN A C 714 O O . ASN A 99 ? 0.6465 0.5137 0.5621 -0.0717 0.0379 -0.0543 127 ASN A O 715 C CB . ASN A 99 ? 0.6326 0.4739 0.5223 -0.0685 0.0350 -0.0564 127 ASN A CB 716 C CG . ASN A 99 ? 0.7264 0.5607 0.6080 -0.0642 0.0321 -0.0568 127 ASN A CG 717 O OD1 . ASN A 99 ? 0.6368 0.4784 0.5240 -0.0593 0.0297 -0.0557 127 ASN A OD1 718 N ND2 . ASN A 99 ? 0.8519 0.6715 0.7199 -0.0658 0.0324 -0.0585 127 ASN A ND2 719 N N . VAL A 100 ? 0.4556 0.3064 0.3603 -0.0695 0.0377 -0.0540 128 VAL A N 720 C CA . VAL A 100 ? 0.6266 0.4840 0.5388 -0.0726 0.0401 -0.0539 128 VAL A CA 721 C C . VAL A 100 ? 0.6076 0.4724 0.5291 -0.0687 0.0385 -0.0519 128 VAL A C 722 O O . VAL A 100 ? 0.5654 0.4415 0.4977 -0.0694 0.0392 -0.0512 128 VAL A O 723 C CB . VAL A 100 ? 0.6391 0.4858 0.5423 -0.0770 0.0431 -0.0555 128 VAL A CB 724 C CG1 . VAL A 100 ? 0.4999 0.3549 0.4113 -0.0805 0.0459 -0.0558 128 VAL A CG1 725 C CG2 . VAL A 100 ? 0.5823 0.4207 0.4755 -0.0809 0.0443 -0.0573 128 VAL A CG2 726 N N . PHE A 101 ? 0.5541 0.4123 0.4712 -0.0645 0.0363 -0.0510 129 PHE A N 727 C CA . PHE A 101 ? 0.4176 0.2809 0.3421 -0.0613 0.0347 -0.0492 129 PHE A CA 728 C C . PHE A 101 ? 0.5567 0.4256 0.4858 -0.0560 0.0311 -0.0473 129 PHE A C 729 O O . PHE A 101 ? 0.4940 0.3621 0.4245 -0.0526 0.0292 -0.0460 129 PHE A O 730 C CB . PHE A 101 ? 0.4772 0.3294 0.3940 -0.0613 0.0354 -0.0496 129 PHE A CB 731 C CG . PHE A 101 ? 0.5608 0.4096 0.4746 -0.0665 0.0391 -0.0512 129 PHE A CG 732 C CD1 . PHE A 101 ? 0.4921 0.3499 0.4152 -0.0684 0.0409 -0.0510 129 PHE A CD1 733 C CD2 . PHE A 101 ? 0.5988 0.4354 0.5004 -0.0697 0.0409 -0.0529 129 PHE A CD2 734 C CE1 . PHE A 101 ? 0.4851 0.3409 0.4059 -0.0732 0.0445 -0.0527 129 PHE A CE1 735 C CE2 . PHE A 101 ? 0.4981 0.3321 0.3969 -0.0750 0.0446 -0.0544 129 PHE A CE2 736 C CZ . PHE A 101 ? 0.5785 0.4225 0.4872 -0.0767 0.0465 -0.0544 129 PHE A CZ 737 N N . ASN A 102 ? 0.4894 0.3639 0.4208 -0.0555 0.0303 -0.0473 130 ASN A N 738 C CA . ASN A 102 ? 0.4977 0.3807 0.4357 -0.0512 0.0274 -0.0455 130 ASN A CA 739 C C . ASN A 102 ? 0.4387 0.3150 0.3709 -0.0466 0.0247 -0.0450 130 ASN A C 740 O O . ASN A 102 ? 0.4418 0.3250 0.3800 -0.0429 0.0223 -0.0432 130 ASN A O 741 C CB . ASN A 102 ? 0.4846 0.3791 0.4351 -0.0507 0.0270 -0.0435 130 ASN A CB 742 C CG . ASN A 102 ? 0.5031 0.4070 0.4613 -0.0543 0.0289 -0.0437 130 ASN A CG 743 O OD1 . ASN A 102 ? 0.6232 0.5358 0.5909 -0.0540 0.0286 -0.0423 130 ASN A OD1 744 N ND2 . ASN A 102 ? 0.4188 0.3210 0.3731 -0.0574 0.0307 -0.0455 130 ASN A ND2 745 N N . ALA A 103 ? 0.5475 0.4103 0.4679 -0.0468 0.0251 -0.0465 131 ALA A N 746 C CA . ALA A 103 ? 0.5931 0.4485 0.5075 -0.0425 0.0226 -0.0462 131 ALA A CA 747 C C . ALA A 103 ? 0.6190 0.4782 0.5399 -0.0404 0.0213 -0.0444 131 ALA A C 748 O O . ALA A 103 ? 0.5972 0.4559 0.5175 -0.0361 0.0185 -0.0436 131 ALA A O 749 C CB . ALA A 103 ? 0.3385 0.1962 0.2518 -0.0382 0.0199 -0.0461 131 ALA A CB 750 N N . PHE A 104 ? 0.4828 0.3457 0.4094 -0.0434 0.0232 -0.0440 132 PHE A N 751 C CA . PHE A 104 ? 0.4314 0.2957 0.3624 -0.0418 0.0221 -0.0426 132 PHE A CA 752 C C . PHE A 104 ? 0.5102 0.3611 0.4307 -0.0406 0.0216 -0.0435 132 PHE A C 753 O O . PHE A 104 ? 0.5334 0.3837 0.4554 -0.0381 0.0198 -0.0424 132 PHE A O 754 C CB . PHE A 104 ? 0.3779 0.2482 0.3166 -0.0451 0.0243 -0.0423 132 PHE A CB 755 C CG . PHE A 104 ? 0.3449 0.2292 0.2958 -0.0449 0.0236 -0.0407 132 PHE A CG 756 C CD1 . PHE A 104 ? 0.3837 0.2749 0.3410 -0.0413 0.0206 -0.0385 132 PHE A CD1 757 C CD2 . PHE A 104 ? 0.3490 0.2399 0.3049 -0.0483 0.0259 -0.0412 132 PHE A CD2 758 C CE1 . PHE A 104 ? 0.3408 0.2446 0.3090 -0.0412 0.0199 -0.0368 132 PHE A CE1 759 C CE2 . PHE A 104 ? 0.3626 0.2660 0.3294 -0.0479 0.0251 -0.0397 132 PHE A CE2 760 C CZ . PHE A 104 ? 0.3820 0.2915 0.3546 -0.0444 0.0221 -0.0374 132 PHE A CZ 761 N N . VAL A 105 ? 0.5421 0.3820 0.4516 -0.0427 0.0232 -0.0454 133 VAL A N 762 C CA . VAL A 105 ? 0.5327 0.3588 0.4305 -0.0412 0.0224 -0.0463 133 VAL A CA 763 C C . VAL A 105 ? 0.7139 0.5320 0.6018 -0.0397 0.0214 -0.0475 133 VAL A C 764 O O . VAL A 105 ? 0.7844 0.6055 0.6726 -0.0414 0.0224 -0.0482 133 VAL A O 765 C CB . VAL A 105 ? 0.5537 0.3712 0.4453 -0.0455 0.0256 -0.0475 133 VAL A CB 766 C CG1 . VAL A 105 ? 0.5399 0.3651 0.4410 -0.0468 0.0267 -0.0465 133 VAL A CG1 767 C CG2 . VAL A 105 ? 0.4204 0.2354 0.3077 -0.0502 0.0286 -0.0491 133 VAL A CG2 768 N N . THR A 106 ? 0.7543 0.5618 0.6329 -0.0364 0.0193 -0.0480 134 THR A N 769 C CA . THR A 106 ? 0.7291 0.5262 0.5960 -0.0351 0.0184 -0.0495 134 THR A CA 770 C C . THR A 106 ? 0.6605 0.4432 0.5151 -0.0390 0.0208 -0.0510 134 THR A C 771 O O . THR A 106 ? 0.6658 0.4457 0.5201 -0.0418 0.0227 -0.0509 134 THR A O 772 C CB . THR A 106 ? 0.6356 0.4283 0.4980 -0.0291 0.0145 -0.0493 134 THR A CB 773 O OG1 . THR A 106 ? 0.7729 0.5568 0.6300 -0.0287 0.0141 -0.0493 134 THR A OG1 774 C CG2 . THR A 106 ? 0.4707 0.2776 0.3451 -0.0253 0.0121 -0.0477 134 THR A CG2 775 N N . TYR A 107 ? 0.6759 0.4490 0.5199 -0.0393 0.0207 -0.0525 135 TYR A N 776 C CA . TYR A 107 ? 0.6289 0.3873 0.4601 -0.0435 0.0229 -0.0540 135 TYR A CA 777 C C . TYR A 107 ? 0.5736 0.3204 0.3962 -0.0414 0.0216 -0.0539 135 TYR A C 778 O O . TYR A 107 ? 0.7613 0.4989 0.5767 -0.0453 0.0239 -0.0545 135 TYR A O 779 C CB . TYR A 107 ? 0.8419 0.5919 0.6630 -0.0443 0.0228 -0.0555 135 TYR A CB 780 C CG . TYR A 107 ? 0.8815 0.6233 0.6942 -0.0383 0.0189 -0.0560 135 TYR A CG 781 C CD1 . TYR A 107 ? 0.9650 0.6910 0.7644 -0.0368 0.0177 -0.0567 135 TYR A CD1 782 C CD2 . TYR A 107 ? 0.7999 0.5500 0.6179 -0.0339 0.0165 -0.0559 135 TYR A CD2 783 C CE1 . TYR A 107 ? 1.0590 0.7778 0.8508 -0.0308 0.0139 -0.0573 135 TYR A CE1 784 C CE2 . TYR A 107 ? 0.8595 0.6031 0.6702 -0.0279 0.0129 -0.0566 135 TYR A CE2 785 C CZ . TYR A 107 ? 1.0390 0.7669 0.8368 -0.0263 0.0115 -0.0573 135 TYR A CZ 786 O OH . TYR A 107 ? 1.1377 0.8589 0.9280 -0.0201 0.0078 -0.0581 135 TYR A OH 787 N N . GLN A 108 ? 0.6105 0.3584 0.4342 -0.0352 0.0178 -0.0532 136 GLN A N 788 C CA . GLN A 108 ? 0.7102 0.4491 0.5275 -0.0325 0.0160 -0.0530 136 GLN A CA 789 C C . GLN A 108 ? 0.9232 0.6665 0.7471 -0.0351 0.0180 -0.0521 136 GLN A C 790 O O . GLN A 108 ? 1.1223 0.8549 0.9379 -0.0368 0.0190 -0.0525 136 GLN A O 791 C CB . GLN A 108 ? 0.8169 0.5603 0.6377 -0.0255 0.0116 -0.0523 136 GLN A CB 792 C CG . GLN A 108 ? 0.9000 0.6389 0.7140 -0.0213 0.0090 -0.0534 136 GLN A CG 793 C CD . GLN A 108 ? 0.9356 0.6877 0.7591 -0.0208 0.0090 -0.0532 136 GLN A CD 794 O OE1 . GLN A 108 ? 1.0479 0.8079 0.8787 -0.0253 0.0119 -0.0528 136 GLN A OE1 795 N NE2 . GLN A 108 ? 0.8668 0.6221 0.6909 -0.0151 0.0057 -0.0534 136 GLN A NE2 796 N N . GLU A 109 ? 0.8303 0.5890 0.6687 -0.0355 0.0185 -0.0508 137 GLU A N 797 C CA . GLU A 109 ? 0.7820 0.5456 0.6273 -0.0378 0.0202 -0.0500 137 GLU A CA 798 C C . GLU A 109 ? 0.6210 0.3802 0.4624 -0.0440 0.0246 -0.0510 137 GLU A C 799 O O . GLU A 109 ? 0.7684 0.5233 0.6076 -0.0459 0.0261 -0.0511 137 GLU A O 800 C CB . GLU A 109 ? 0.7919 0.5727 0.6534 -0.0369 0.0197 -0.0484 137 GLU A CB 801 C CG . GLU A 109 ? 0.7650 0.5508 0.6312 -0.0312 0.0156 -0.0471 137 GLU A CG 802 C CD . GLU A 109 ? 0.7506 0.5528 0.6312 -0.0303 0.0148 -0.0456 137 GLU A CD 803 O OE1 . GLU A 109 ? 0.7490 0.5581 0.6348 -0.0333 0.0170 -0.0457 137 GLU A OE1 804 O OE2 . GLU A 109 ? 0.6646 0.4726 0.5510 -0.0265 0.0119 -0.0442 137 GLU A OE2 805 N N . ILE A 110 ? 0.5601 0.3207 0.4008 -0.0474 0.0266 -0.0519 138 ILE A N 806 C CA . ILE A 110 ? 0.7201 0.4759 0.5561 -0.0536 0.0308 -0.0530 138 ILE A CA 807 C C . ILE A 110 ? 0.8431 0.5811 0.6630 -0.0546 0.0311 -0.0541 138 ILE A C 808 O O . ILE A 110 ? 0.8326 0.5650 0.6478 -0.0589 0.0341 -0.0547 138 ILE A O 809 C CB . ILE A 110 ? 0.7389 0.4993 0.5767 -0.0573 0.0327 -0.0539 138 ILE A CB 810 C CG1 . ILE A 110 ? 0.6107 0.3884 0.4639 -0.0558 0.0320 -0.0528 138 ILE A CG1 811 C CG2 . ILE A 110 ? 0.6897 0.4466 0.5237 -0.0641 0.0372 -0.0551 138 ILE A CG2 812 C CD1 . ILE A 110 ? 0.6462 0.4296 0.5022 -0.0593 0.0338 -0.0535 138 ILE A CD1 813 N N . ALA A 111 ? 0.9034 0.6323 0.7146 -0.0504 0.0278 -0.0542 139 ALA A N 814 C CA . ALA A 111 ? 0.9380 0.6491 0.7330 -0.0506 0.0275 -0.0551 139 ALA A CA 815 C C . ALA A 111 ? 0.8623 0.5691 0.6556 -0.0493 0.0271 -0.0545 139 ALA A C 816 O O . ALA A 111 ? 0.7417 0.4396 0.5271 -0.0533 0.0297 -0.0551 139 ALA A O 817 C CB . ALA A 111 ? 0.9130 0.6160 0.6996 -0.0457 0.0237 -0.0555 139 ALA A CB 818 N N . ALA A 112 ? 0.7749 0.4886 0.5758 -0.0440 0.0238 -0.0534 140 ALA A N 819 C CA . ALA A 112 ? 0.8640 0.5740 0.6636 -0.0424 0.0229 -0.0529 140 ALA A CA 820 C C . ALA A 112 ? 0.9280 0.6425 0.7328 -0.0471 0.0267 -0.0528 140 ALA A C 821 O O . ALA A 112 ? 0.9992 0.7043 0.7962 -0.0485 0.0279 -0.0532 140 ALA A O 822 C CB . ALA A 112 ? 0.8279 0.5467 0.6365 -0.0364 0.0188 -0.0516 140 ALA A CB 823 N N . ALA A 113 ? 0.8595 0.5879 0.6767 -0.0495 0.0288 -0.0525 141 ALA A N 824 C CA . ALA A 113 ? 0.8075 0.5422 0.6314 -0.0534 0.0322 -0.0525 141 ALA A CA 825 C C . ALA A 113 ? 0.8786 0.6044 0.6930 -0.0594 0.0366 -0.0540 141 ALA A C 826 O O . ALA A 113 ? 0.8514 0.5778 0.6670 -0.0620 0.0391 -0.0543 141 ALA A O 827 C CB . ALA A 113 ? 0.7160 0.4675 0.5550 -0.0542 0.0330 -0.0519 141 ALA A CB 828 N N . ASN A 114 ? 1.0004 0.7183 0.8056 -0.0619 0.0375 -0.0549 142 ASN A N 829 C CA . ASN A 114 ? 0.9101 0.6201 0.7065 -0.0683 0.0417 -0.0562 142 ASN A CA 830 C C . ASN A 114 ? 0.9765 0.6678 0.7556 -0.0684 0.0412 -0.0567 142 ASN A C 831 O O . ASN A 114 ? 0.9606 0.6429 0.7298 -0.0737 0.0443 -0.0576 142 ASN A O 832 C CB . ASN A 114 ? 0.8678 0.5823 0.6660 -0.0725 0.0440 -0.0569 142 ASN A CB 833 C CG . ASN A 114 ? 0.8560 0.5888 0.6708 -0.0734 0.0453 -0.0566 142 ASN A CG 834 O OD1 . ASN A 114 ? 0.8056 0.5443 0.6252 -0.0776 0.0489 -0.0572 142 ASN A OD1 835 N ND2 . ASN A 114 ? 0.8379 0.5798 0.6614 -0.0693 0.0423 -0.0557 142 ASN A ND2 836 N N . ASN A 115 ? 1.1179 0.8035 0.8934 -0.0626 0.0370 -0.0559 143 ASN A N 837 C CA . ASN A 115 ? 1.2572 0.9254 1.0170 -0.0613 0.0356 -0.0562 143 ASN A CA 838 C C . ASN A 115 ? 1.3076 0.9655 1.0548 -0.0631 0.0357 -0.0560 143 ASN A C 839 O O . ASN A 115 ? 1.3253 0.9753 1.0642 -0.0588 0.0323 -0.0550 143 ASN A O 840 C CB . ASN A 115 ? 1.3019 0.9672 1.0592 -0.0639 0.0382 -0.0562 143 ASN A CB 841 C CG . ASN A 115 ? 1.2918 0.9620 1.0563 -0.0593 0.0357 -0.0554 143 ASN A CG 842 O OD1 . ASN A 115 ? 1.2655 0.9375 1.0328 -0.0535 0.0313 -0.0547 143 ASN A OD1 843 N ND2 . ASN A 115 ? 1.2892 0.9626 1.0571 -0.0617 0.0384 -0.0556 143 ASN A ND2 844 N N . ILE A 116 ? 1.4021 1.0615 1.1487 -0.0692 0.0396 -0.0568 144 ILE A N 845 C CA . ILE A 116 ? 1.5467 1.1978 1.2822 -0.0715 0.0400 -0.0563 144 ILE A CA 846 C C . ILE A 116 ? 1.5707 1.2193 1.3039 -0.0673 0.0362 -0.0564 144 ILE A C 847 O O . ILE A 116 ? 1.5441 1.1832 1.2664 -0.0658 0.0343 -0.0555 144 ILE A O 848 C CB . ILE A 116 ? 1.4720 1.1261 1.2082 -0.0796 0.0451 -0.0573 144 ILE A CB 849 C CG1 . ILE A 116 ? 1.4486 1.1053 1.1870 -0.0836 0.0490 -0.0575 144 ILE A CG1 850 C CG2 . ILE A 116 ? 1.4762 1.1208 1.2001 -0.0823 0.0455 -0.0566 144 ILE A CG2 851 C CD1 . ILE A 116 ? 1.4129 1.0733 1.1523 -0.0917 0.0543 -0.0587 144 ILE A CD1 852 N N . PRO A 117 ? 1.5042 1.1612 1.2474 -0.0654 0.0351 -0.0575 145 PRO A N 853 C CA . PRO A 117 ? 1.4756 1.1291 1.2149 -0.0610 0.0314 -0.0577 145 PRO A CA 854 C C . PRO A 117 ? 1.5106 1.1602 1.2474 -0.0532 0.0265 -0.0570 145 PRO A C 855 O O . PRO A 117 ? 1.5617 1.2167 1.3060 -0.0500 0.0251 -0.0571 145 PRO A O 856 C CB . PRO A 117 ? 1.4193 1.0862 1.1713 -0.0615 0.0320 -0.0585 145 PRO A CB 857 C CG . PRO A 117 ? 1.3926 1.0726 1.1570 -0.0650 0.0353 -0.0580 145 PRO A CG 858 C CD . PRO A 117 ? 1.4206 1.0930 1.1791 -0.0671 0.0371 -0.0579 145 PRO A CD 859 N N . ASP A 118 ? 1.5046 1.1447 1.2306 -0.0503 0.0238 -0.0563 146 ASP A N 860 C CA . ASP A 118 ? 1.4520 1.0884 1.1749 -0.0426 0.0188 -0.0560 146 ASP A CA 861 C C . ASP A 118 ? 1.4888 1.1240 1.2094 -0.0402 0.0167 -0.0570 146 ASP A C 862 O O . ASP A 118 ? 1.5143 1.1515 1.2374 -0.0341 0.0131 -0.0577 146 ASP A O 863 C CB . ASP A 118 ? 1.4441 1.0701 1.1559 -0.0409 0.0172 -0.0544 146 ASP A CB 864 C CG . ASP A 118 ? 1.4557 1.0781 1.1627 -0.0475 0.0215 -0.0535 146 ASP A CG 865 O OD1 . ASP A 118 ? 1.5217 1.1395 1.2242 -0.0469 0.0212 -0.0524 146 ASP A OD1 866 O OD2 . ASP A 118 ? 1.3828 1.0068 1.0903 -0.0534 0.0250 -0.0541 146 ASP A OD2 867 N N . PRO A 119 ? 1.5433 1.1749 1.2585 -0.0448 0.0189 -0.0571 147 PRO A N 868 C CA . PRO A 119 ? 1.5216 1.1554 1.2382 -0.0439 0.0180 -0.0585 147 PRO A CA 869 C C . PRO A 119 ? 1.4676 1.1088 1.1911 -0.0510 0.0224 -0.0594 147 PRO A C 870 O O . PRO A 119 ? 1.3976 1.0414 1.1240 -0.0562 0.0260 -0.0590 147 PRO A O 871 C CB . PRO A 119 ? 1.4958 1.1181 1.1992 -0.0431 0.0164 -0.0579 147 PRO A CB 872 C CG . PRO A 119 ? 1.5428 1.1573 1.2381 -0.0458 0.0177 -0.0560 147 PRO A CG 873 C CD . PRO A 119 ? 1.5830 1.2047 1.2867 -0.0486 0.0205 -0.0558 147 PRO A CD 874 N N . ASN A 120 ? 1.4643 1.1090 1.1904 -0.0513 0.0223 -0.0608 148 ASN A N 875 C CA . ASN A 120 ? 1.4064 1.0586 1.1393 -0.0581 0.0263 -0.0617 148 ASN A CA 876 C C . ASN A 120 ? 1.3545 1.0007 1.0793 -0.0642 0.0288 -0.0616 148 ASN A C 877 O O . ASN A 120 ? 1.0937 0.7375 0.8147 -0.0646 0.0280 -0.0623 148 ASN A O 878 C CB . ASN A 120 ? 1.4070 1.0754 1.1534 -0.0548 0.0249 -0.0615 148 ASN A CB 879 C CG . ASN A 120 ? 1.4534 1.1309 1.2088 -0.0475 0.0216 -0.0604 148 ASN A CG 880 O OD1 . ASN A 120 ? 1.2923 0.9674 1.0473 -0.0459 0.0211 -0.0596 148 ASN A OD1 881 N ND2 . ASN A 120 ? 1.5589 1.2470 1.3225 -0.0433 0.0194 -0.0603 148 ASN A ND2 882 N N . LYS A 121 ? 1.3954 1.0388 1.1171 -0.0687 0.0316 -0.0604 149 LYS A N 883 C CA . LYS A 121 ? 1.4513 1.0894 1.1656 -0.0753 0.0345 -0.0600 149 LYS A CA 884 C C . LYS A 121 ? 1.2717 0.9176 0.9936 -0.0817 0.0393 -0.0604 149 LYS A C 885 O O . LYS A 121 ? 1.2832 0.9293 1.0062 -0.0812 0.0401 -0.0596 149 LYS A O 886 C CB . LYS A 121 ? 1.6852 1.3102 1.3859 -0.0736 0.0329 -0.0583 149 LYS A CB 887 C CG . LYS A 121 ? 1.8365 1.4563 1.5332 -0.0648 0.0276 -0.0579 149 LYS A CG 888 C CD . LYS A 121 ? 1.9316 1.5490 1.6250 -0.0625 0.0251 -0.0589 149 LYS A CD 889 C CE . LYS A 121 ? 1.9495 1.5654 1.6424 -0.0535 0.0201 -0.0592 149 LYS A CE 890 N NZ . LYS A 121 ? 1.9494 1.5545 1.6316 -0.0492 0.0171 -0.0577 149 LYS A NZ 891 N N . ILE A 122 ? 1.0876 0.7399 0.8143 -0.0877 0.0424 -0.0616 150 ILE A N 892 C CA . ILE A 122 ? 1.0455 0.7069 0.7810 -0.0935 0.0468 -0.0623 150 ILE A CA 893 C C . ILE A 122 ? 1.2195 0.8822 0.9534 -0.1017 0.0508 -0.0631 150 ILE A C 894 O O . ILE A 122 ? 1.2614 0.9203 0.9899 -0.1031 0.0500 -0.0633 150 ILE A O 895 C CB . ILE A 122 ? 1.3061 0.9827 1.0576 -0.0914 0.0466 -0.0631 150 ILE A CB 896 C CG1 . ILE A 122 ? 1.2623 0.9465 1.0190 -0.0920 0.0460 -0.0637 150 ILE A CG1 897 C CG2 . ILE A 122 ? 1.2672 0.9464 1.0232 -0.0831 0.0427 -0.0619 150 ILE A CG2 898 C CD1 . ILE A 122 ? 1.2144 0.9182 0.9892 -0.0885 0.0451 -0.0629 150 ILE A CD1 899 N N . ASN A 123 ? 1.2338 0.9019 0.9720 -0.1072 0.0550 -0.0635 151 ASN A N 900 C CA . ASN A 123 ? 1.2244 0.8943 0.9611 -0.1155 0.0591 -0.0643 151 ASN A CA 901 C C . ASN A 123 ? 1.1141 0.7984 0.8645 -0.1201 0.0623 -0.0662 151 ASN A C 902 O O . ASN A 123 ? 1.2423 0.9373 1.0040 -0.1178 0.0628 -0.0659 151 ASN A O 903 C CB . ASN A 123 ? 1.3149 0.9774 1.0424 -0.1191 0.0617 -0.0632 151 ASN A CB 904 C CG . ASN A 123 ? 1.4014 1.0492 1.1136 -0.1170 0.0592 -0.0614 151 ASN A CG 905 O OD1 . ASN A 123 ? 1.4896 1.1319 1.1938 -0.1216 0.0603 -0.0613 151 ASN A OD1 906 N ND2 . ASN A 123 ? 1.3653 1.0068 1.0737 -0.1098 0.0554 -0.0601 151 ASN A ND2 907 N N . VAL A 124 ? 1.0595 0.7471 0.8106 -0.1255 0.0641 -0.0673 152 VAL A N 908 C CA . VAL A 124 ? 1.0680 0.7727 0.8335 -0.1293 0.0668 -0.0683 152 VAL A CA 909 C C . VAL A 124 ? 1.1371 0.8494 0.9086 -0.1331 0.0710 -0.0685 152 VAL A C 910 O O . VAL A 124 ? 1.1297 0.8311 0.8905 -0.1372 0.0734 -0.0689 152 VAL A O 911 C CB . VAL A 124 ? 0.9919 0.6955 0.7536 -0.1358 0.0683 -0.0697 152 VAL A CB 912 C CG1 . VAL A 124 ? 1.0295 0.7527 0.8070 -0.1393 0.0709 -0.0704 152 VAL A CG1 913 C CG2 . VAL A 124 ? 1.0019 0.6985 0.7580 -0.1317 0.0641 -0.0696 152 VAL A CG2 914 N N . SER A 125 ? 1.0907 0.8214 0.8790 -0.1313 0.0716 -0.0684 153 SER A N 915 C CA . SER A 125 ? 1.0332 0.7740 0.8297 -0.1342 0.0754 -0.0688 153 SER A CA 916 C C . SER A 125 ? 0.9482 0.6845 0.7428 -0.1301 0.0749 -0.0678 153 SER A C 917 O O . SER A 125 ? 1.0029 0.7469 0.8040 -0.1315 0.0777 -0.0682 153 SER A O 918 C CB . SER A 125 ? 1.1240 0.8628 0.9149 -0.1435 0.0801 -0.0704 153 SER A CB 919 O OG . SER A 125 ? 1.1291 0.8844 0.9332 -0.1461 0.0834 -0.0713 153 SER A OG 920 N N . GLN A 126 ? 0.8257 0.5498 0.6117 -0.1248 0.0712 -0.0667 154 GLN A N 921 C CA . GLN A 126 ? 0.8902 0.6108 0.6757 -0.1195 0.0696 -0.0656 154 GLN A CA 922 C C . GLN A 126 ? 0.9723 0.7099 0.7751 -0.1142 0.0680 -0.0647 154 GLN A C 923 O O . GLN A 126 ? 0.8817 0.6297 0.6940 -0.1122 0.0663 -0.0645 154 GLN A O 924 C CB . GLN A 126 ? 0.8946 0.6001 0.6683 -0.1145 0.0653 -0.0647 154 GLN A CB 925 C CG . GLN A 126 ? 0.9260 0.6284 0.6998 -0.1080 0.0626 -0.0635 154 GLN A CG 926 C CD . GLN A 126 ? 0.9623 0.6513 0.7255 -0.1027 0.0582 -0.0628 154 GLN A CD 927 O OE1 . GLN A 126 ? 1.1087 0.7917 0.8655 -0.1034 0.0569 -0.0633 154 GLN A OE1 928 N NE2 . GLN A 126 ? 1.0233 0.7077 0.7845 -0.0974 0.0557 -0.0619 154 GLN A NE2 929 N N . THR A 127 ? 0.9530 0.6934 0.7597 -0.1122 0.0687 -0.0643 155 THR A N 930 C CA . THR A 127 ? 0.9881 0.7430 0.8100 -0.1072 0.0670 -0.0634 155 THR A CA 931 C C . THR A 127 ? 0.9645 0.7144 0.7851 -0.0997 0.0624 -0.0618 155 THR A C 932 O O . THR A 127 ? 0.9254 0.6626 0.7355 -0.0982 0.0615 -0.0615 155 THR A O 933 C CB . THR A 127 ? 0.9616 0.7238 0.7899 -0.1088 0.0701 -0.0639 155 THR A CB 934 O OG1 . THR A 127 ? 1.0745 0.8233 0.8910 -0.1093 0.0710 -0.0640 155 THR A OG1 935 C CG2 . THR A 127 ? 0.8794 0.6508 0.7126 -0.1155 0.0746 -0.0656 155 THR A CG2 936 N N . LEU A 128 ? 0.8679 0.6282 0.6993 -0.0951 0.0593 -0.0608 156 LEU A N 937 C CA . LEU A 128 ? 0.8636 0.6218 0.6957 -0.0881 0.0549 -0.0592 156 LEU A CA 938 C C . LEU A 128 ? 0.8117 0.5837 0.6584 -0.0846 0.0539 -0.0582 156 LEU A C 939 O O . LEU A 128 ? 0.7522 0.5379 0.6107 -0.0858 0.0551 -0.0583 156 LEU A O 940 C CB . LEU A 128 ? 0.8972 0.6553 0.7288 -0.0853 0.0517 -0.0588 156 LEU A CB 941 C CG . LEU A 128 ? 0.9410 0.6859 0.7588 -0.0876 0.0516 -0.0597 156 LEU A CG 942 C CD1 . LEU A 128 ? 0.8865 0.6359 0.7078 -0.0847 0.0488 -0.0594 156 LEU A CD1 943 C CD2 . LEU A 128 ? 0.9096 0.6376 0.7132 -0.0854 0.0500 -0.0596 156 LEU A CD2 944 N N . TRP A 129 ? 0.8545 0.6224 0.7000 -0.0803 0.0517 -0.0572 157 TRP A N 945 C CA . TRP A 129 ? 0.7823 0.5618 0.6406 -0.0763 0.0499 -0.0560 157 TRP A CA 946 C C . TRP A 129 ? 0.7405 0.5250 0.6042 -0.0714 0.0458 -0.0545 157 TRP A C 947 O O . TRP A 129 ? 0.7331 0.5089 0.5893 -0.0680 0.0429 -0.0541 157 TRP A O 948 C CB . TRP A 129 ? 0.7725 0.5453 0.6270 -0.0738 0.0491 -0.0555 157 TRP A CB 949 C CG . TRP A 129 ? 0.8026 0.5850 0.6686 -0.0691 0.0463 -0.0541 157 TRP A CG 950 C CD1 . TRP A 129 ? 0.7518 0.5490 0.6318 -0.0686 0.0463 -0.0535 157 TRP A CD1 951 C CD2 . TRP A 129 ? 0.8285 0.6063 0.6928 -0.0642 0.0429 -0.0529 157 TRP A CD2 952 N NE1 . TRP A 129 ? 0.8125 0.6140 0.6992 -0.0640 0.0433 -0.0520 157 TRP A NE1 953 C CE2 . TRP A 129 ? 0.7931 0.5833 0.6708 -0.0614 0.0411 -0.0517 157 TRP A CE2 954 C CE3 . TRP A 129 ? 0.7354 0.4996 0.5881 -0.0621 0.0411 -0.0529 157 TRP A CE3 955 C CZ2 . TRP A 129 ? 0.5582 0.3478 0.4380 -0.0568 0.0377 -0.0503 157 TRP A CZ2 956 C CZ3 . TRP A 129 ? 0.7820 0.5461 0.6371 -0.0573 0.0376 -0.0517 157 TRP A CZ3 957 C CH2 . TRP A 129 ? 0.6218 0.3987 0.4906 -0.0548 0.0359 -0.0504 157 TRP A CH2 958 N N . ILE A 130 ? 0.6838 0.4826 0.5604 -0.0708 0.0455 -0.0539 158 ILE A N 959 C CA . ILE A 130 ? 0.6502 0.4553 0.5330 -0.0662 0.0418 -0.0524 158 ILE A CA 960 C C . ILE A 130 ? 0.6780 0.4892 0.5692 -0.0618 0.0392 -0.0508 158 ILE A C 961 O O . ILE A 130 ? 0.5832 0.4045 0.4846 -0.0624 0.0401 -0.0504 158 ILE A O 962 C CB . ILE A 130 ? 0.5965 0.4137 0.4883 -0.0681 0.0426 -0.0525 158 ILE A CB 963 C CG1 . ILE A 130 ? 0.5968 0.4086 0.4809 -0.0732 0.0454 -0.0543 158 ILE A CG1 964 C CG2 . ILE A 130 ? 0.5534 0.3768 0.4507 -0.0636 0.0389 -0.0511 158 ILE A CG2 965 C CD1 . ILE A 130 ? 0.5930 0.3913 0.4638 -0.0723 0.0439 -0.0548 158 ILE A CD1 966 N N . PRO A 131 ? 0.6090 0.4141 0.4959 -0.0574 0.0358 -0.0499 159 PRO A N 967 C CA . PRO A 131 ? 0.5779 0.3880 0.4719 -0.0536 0.0332 -0.0483 159 PRO A CA 968 C C . PRO A 131 ? 0.5062 0.3291 0.4119 -0.0506 0.0306 -0.0466 159 PRO A C 969 O O . PRO A 131 ? 0.5061 0.3284 0.4112 -0.0467 0.0273 -0.0456 159 PRO A O 970 C CB . PRO A 131 ? 0.6584 0.4566 0.5423 -0.0502 0.0305 -0.0482 159 PRO A CB 971 C CG . PRO A 131 ? 0.6299 0.4221 0.5057 -0.0503 0.0301 -0.0489 159 PRO A CG 972 C CD . PRO A 131 ? 0.5899 0.3833 0.4650 -0.0558 0.0341 -0.0503 159 PRO A CD 973 N N . LEU A 132 ? 0.5285 0.3629 0.4445 -0.0525 0.0320 -0.0463 160 LEU A N 974 C CA . LEU A 132 ? 0.5153 0.3619 0.4425 -0.0500 0.0296 -0.0445 160 LEU A CA 975 C C . LEU A 132 ? 0.5336 0.3813 0.4644 -0.0459 0.0262 -0.0428 160 LEU A C 976 O O . LEU A 132 ? 0.5651 0.4092 0.4951 -0.0458 0.0264 -0.0428 160 LEU A O 977 C CB . LEU A 132 ? 0.4505 0.3084 0.3880 -0.0525 0.0316 -0.0445 160 LEU A CB 978 C CG . LEU A 132 ? 0.4310 0.2888 0.3658 -0.0570 0.0350 -0.0463 160 LEU A CG 979 C CD1 . LEU A 132 ? 0.4585 0.3271 0.4033 -0.0593 0.0370 -0.0465 160 LEU A CD1 980 C CD2 . LEU A 132 ? 0.5165 0.3756 0.4496 -0.0564 0.0339 -0.0462 160 LEU A CD2 981 N N . PRO A 133 ? 0.4823 0.3352 0.4170 -0.0427 0.0231 -0.0413 161 PRO A N 982 C CA . PRO A 133 ? 0.4329 0.2868 0.3704 -0.0389 0.0198 -0.0397 161 PRO A CA 983 C C . PRO A 133 ? 0.5425 0.4056 0.4910 -0.0390 0.0192 -0.0381 161 PRO A C 984 O O . PRO A 133 ? 0.4415 0.3143 0.3984 -0.0403 0.0199 -0.0375 161 PRO A O 985 C CB . PRO A 133 ? 0.3875 0.2456 0.3263 -0.0360 0.0171 -0.0387 161 PRO A CB 986 C CG . PRO A 133 ? 0.3632 0.2283 0.3058 -0.0383 0.0190 -0.0390 161 PRO A CG 987 C CD . PRO A 133 ? 0.4924 0.3520 0.4301 -0.0424 0.0227 -0.0410 161 PRO A CD 988 N N . CYS A 134 ? 0.4852 0.3445 0.4331 -0.0374 0.0176 -0.0376 162 CYS A N 989 C CA . CYS A 134 ? 0.4249 0.2909 0.3818 -0.0373 0.0169 -0.0363 162 CYS A CA 990 C C . CYS A 134 ? 0.4798 0.3414 0.4351 -0.0346 0.0140 -0.0354 162 CYS A C 991 O O . CYS A 134 ? 0.4396 0.2933 0.3871 -0.0329 0.0126 -0.0359 162 CYS A O 992 C CB . CYS A 134 ? 0.3548 0.2203 0.3125 -0.0404 0.0203 -0.0377 162 CYS A CB 993 S SG . CYS A 134 ? 0.4741 0.3255 0.4197 -0.0419 0.0227 -0.0401 162 CYS A SG 994 N N . SER A 135 ? 0.4336 0.3002 0.3965 -0.0343 0.0128 -0.0342 163 SER A N 995 C CA . SER A 135 ? 0.5299 0.3926 0.4920 -0.0323 0.0101 -0.0334 163 SER A CA 996 C C . SER A 135 ? 0.5307 0.3971 0.4995 -0.0331 0.0102 -0.0328 163 SER A C 997 O O . SER A 135 ? 0.4742 0.3485 0.4501 -0.0345 0.0115 -0.0325 163 SER A O 998 C CB . SER A 135 ? 0.5236 0.3911 0.4892 -0.0295 0.0062 -0.0314 163 SER A CB 999 O OG . SER A 135 ? 0.4898 0.3537 0.4547 -0.0277 0.0034 -0.0307 163 SER A OG 1000 N N . CYS A 136 ? 0.4925 0.3534 0.4591 -0.0319 0.0086 -0.0328 164 CYS A N 1001 C CA . CYS A 136 ? 0.5864 0.4506 0.5595 -0.0320 0.0079 -0.0320 164 CYS A CA 1002 C C . CYS A 136 ? 0.5637 0.4298 0.5406 -0.0299 0.0035 -0.0299 164 CYS A C 1003 O O . CYS A 136 ? 0.5239 0.3903 0.5044 -0.0296 0.0022 -0.0293 164 CYS A O 1004 C CB . CYS A 136 ? 0.5163 0.3724 0.4838 -0.0330 0.0102 -0.0341 164 CYS A CB 1005 S SG . CYS A 136 ? 0.5821 0.4351 0.5440 -0.0361 0.0156 -0.0369 164 CYS A SG 1006 N N . ASP A 137 ? 0.4617 0.3292 0.4377 -0.0283 0.0012 -0.0288 165 ASP A N 1007 C CA . ASP A 137 ? 0.4244 0.2946 0.4042 -0.0265 -0.0030 -0.0268 165 ASP A CA 1008 C C . ASP A 137 ? 0.5066 0.3865 0.4968 -0.0273 -0.0040 -0.0247 165 ASP A C 1009 O O . ASP A 137 ? 0.5093 0.3958 0.5039 -0.0285 -0.0023 -0.0244 165 ASP A O 1010 C CB . ASP A 137 ? 0.4382 0.3108 0.4168 -0.0247 -0.0049 -0.0260 165 ASP A CB 1011 C CG . ASP A 137 ? 0.5646 0.4273 0.5328 -0.0232 -0.0050 -0.0278 165 ASP A CG 1012 O OD1 . ASP A 137 ? 0.6367 0.4905 0.5991 -0.0231 -0.0049 -0.0289 165 ASP A OD1 1013 O OD2 . ASP A 137 ? 0.6142 0.4777 0.5796 -0.0219 -0.0053 -0.0280 165 ASP A OD2 1014 N N . LYS A 138 ? 0.5582 0.4385 0.5518 -0.0267 -0.0071 -0.0232 166 LYS A N 1015 C CA . LYS A 138 ? 0.6153 0.5043 0.6182 -0.0273 -0.0090 -0.0207 166 LYS A CA 1016 C C . LYS A 138 ? 0.5897 0.4867 0.5965 -0.0267 -0.0111 -0.0187 166 LYS A C 1017 O O . LYS A 138 ? 0.4728 0.3678 0.4751 -0.0253 -0.0118 -0.0192 166 LYS A O 1018 C CB . LYS A 138 ? 0.6740 0.5598 0.6784 -0.0270 -0.0117 -0.0199 166 LYS A CB 1019 C CG . LYS A 138 ? 0.6411 0.5212 0.6437 -0.0276 -0.0097 -0.0217 166 LYS A CG 1020 C CD . LYS A 138 ? 0.5834 0.4583 0.5855 -0.0270 -0.0124 -0.0213 166 LYS A CD 1021 C CE . LYS A 138 ? 0.7238 0.5925 0.7229 -0.0272 -0.0100 -0.0235 166 LYS A CE 1022 N NZ . LYS A 138 ? 0.8797 0.7516 0.8851 -0.0276 -0.0108 -0.0227 166 LYS A NZ 1023 N N . GLU A 139 ? 0.5471 0.4530 0.5620 -0.0276 -0.0121 -0.0164 167 GLU A N 1024 C CA . GLU A 139 ? 0.6069 0.5210 0.6260 -0.0273 -0.0141 -0.0143 167 GLU A CA 1025 C C . GLU A 139 ? 0.7051 0.6222 0.7294 -0.0276 -0.0179 -0.0118 167 GLU A C 1026 O O . GLU A 139 ? 0.6263 0.5472 0.6564 -0.0290 -0.0185 -0.0101 167 GLU A O 1027 C CB . GLU A 139 ? 0.5301 0.4527 0.5540 -0.0283 -0.0124 -0.0136 167 GLU A CB 1028 C CG . GLU A 139 ? 0.5160 0.4472 0.5433 -0.0278 -0.0140 -0.0117 167 GLU A CG 1029 C CD . GLU A 139 ? 0.6323 0.5602 0.6536 -0.0257 -0.0144 -0.0130 167 GLU A CD 1030 O OE1 . GLU A 139 ? 0.7058 0.6393 0.7295 -0.0248 -0.0168 -0.0115 167 GLU A OE1 1031 O OE2 . GLU A 139 ? 0.5459 0.4658 0.5599 -0.0250 -0.0125 -0.0155 167 GLU A OE2 1032 N N . GLU A 140 ? 0.7024 0.6176 0.7244 -0.0264 -0.0204 -0.0115 168 GLU A N 1033 C CA . GLU A 140 ? 0.7299 0.6469 0.7558 -0.0269 -0.0241 -0.0094 168 GLU A CA 1034 C C . GLU A 140 ? 0.7732 0.6849 0.8000 -0.0279 -0.0246 -0.0093 168 GLU A C 1035 O O . GLU A 140 ? 0.7619 0.6776 0.7945 -0.0293 -0.0264 -0.0070 168 GLU A O 1036 C CB . GLU A 140 ? 0.8629 0.7912 0.8963 -0.0280 -0.0256 -0.0064 168 GLU A CB 1037 C CG . GLU A 140 ? 1.0415 0.9742 1.0757 -0.0272 -0.0284 -0.0053 168 GLU A CG 1038 C CD . GLU A 140 ? 1.1363 1.0754 1.1702 -0.0259 -0.0272 -0.0057 168 GLU A CD 1039 O OE1 . GLU A 140 ? 1.0942 1.0425 1.1337 -0.0270 -0.0270 -0.0038 168 GLU A OE1 1040 O OE2 . GLU A 140 ? 1.1772 1.1118 1.2050 -0.0237 -0.0266 -0.0079 168 GLU A OE2 1041 N N . GLY A 141 ? 0.6566 0.5589 0.6771 -0.0272 -0.0228 -0.0118 169 GLY A N 1042 C CA . GLY A 141 ? 0.4988 0.3953 0.5190 -0.0277 -0.0232 -0.0123 169 GLY A CA 1043 C C . GLY A 141 ? 0.7225 0.6207 0.7459 -0.0286 -0.0207 -0.0127 169 GLY A C 1044 O O . GLY A 141 ? 0.6531 0.5461 0.6757 -0.0286 -0.0206 -0.0135 169 GLY A O 1045 N N . SER A 142 ? 0.7115 0.6169 0.7382 -0.0292 -0.0188 -0.0122 170 SER A N 1046 C CA . SER A 142 ? 0.6601 0.5681 0.6902 -0.0300 -0.0166 -0.0125 170 SER A CA 1047 C C . SER A 142 ? 0.7029 0.6081 0.7284 -0.0299 -0.0125 -0.0154 170 SER A C 1048 O O . SER A 142 ? 0.5194 0.4231 0.5403 -0.0295 -0.0112 -0.0165 170 SER A O 1049 C CB . SER A 142 ? 0.7190 0.6371 0.7562 -0.0310 -0.0173 -0.0100 170 SER A CB 1050 O OG . SER A 142 ? 0.7662 0.6866 0.8082 -0.0317 -0.0208 -0.0073 170 SER A OG 1051 N N . ASN A 143 ? 0.7012 0.6057 0.7279 -0.0303 -0.0104 -0.0167 171 ASN A N 1052 C CA . ASN A 143 ? 0.6397 0.5427 0.6629 -0.0308 -0.0063 -0.0193 171 ASN A CA 1053 C C . ASN A 143 ? 0.5967 0.5078 0.6235 -0.0317 -0.0047 -0.0188 171 ASN A C 1054 O O . ASN A 143 ? 0.5588 0.4772 0.5923 -0.0321 -0.0058 -0.0169 171 ASN A O 1055 C CB . ASN A 143 ? 0.5705 0.4700 0.5934 -0.0308 -0.0045 -0.0212 171 ASN A CB 1056 C CG . ASN A 143 ? 0.8158 0.7054 0.8322 -0.0300 -0.0047 -0.0229 171 ASN A CG 1057 O OD1 . ASN A 143 ? 0.9100 0.7966 0.9274 -0.0292 -0.0073 -0.0221 171 ASN A OD1 1058 N ND2 . ASN A 143 ? 0.8411 0.7252 0.8502 -0.0302 -0.0020 -0.0252 171 ASN A ND2 1059 N N . VAL A 144 ? 0.4728 0.3822 0.4945 -0.0319 -0.0022 -0.0205 172 VAL A N 1060 C CA . VAL A 144 ? 0.4750 0.3913 0.4990 -0.0328 -0.0006 -0.0203 172 VAL A CA 1061 C C . VAL A 144 ? 0.4674 0.3807 0.4867 -0.0339 0.0035 -0.0232 172 VAL A C 1062 O O . VAL A 144 ? 0.4843 0.3895 0.4970 -0.0339 0.0050 -0.0253 172 VAL A O 1063 C CB . VAL A 144 ? 0.4031 0.3218 0.4259 -0.0320 -0.0021 -0.0190 172 VAL A CB 1064 C CG1 . VAL A 144 ? 0.3680 0.2935 0.3974 -0.0317 -0.0056 -0.0158 172 VAL A CG1 1065 C CG2 . VAL A 144 ? 0.3356 0.2456 0.3504 -0.0309 -0.0025 -0.0204 172 VAL A CG2 1066 N N . MET A 145 ? 0.4589 0.3788 0.4814 -0.0350 0.0052 -0.0233 173 MET A N 1067 C CA . MET A 145 ? 0.3546 0.2724 0.3724 -0.0364 0.0088 -0.0258 173 MET A CA 1068 C C . MET A 145 ? 0.4222 0.3407 0.4367 -0.0361 0.0086 -0.0255 173 MET A C 1069 O O . MET A 145 ? 0.3780 0.3042 0.3975 -0.0359 0.0073 -0.0238 173 MET A O 1070 C CB . MET A 145 ? 0.4067 0.3314 0.4301 -0.0378 0.0108 -0.0264 173 MET A CB 1071 C CG . MET A 145 ? 0.4841 0.4058 0.5023 -0.0398 0.0148 -0.0294 173 MET A CG 1072 S SD . MET A 145 ? 0.7244 0.6556 0.7483 -0.0417 0.0169 -0.0299 173 MET A SD 1073 C CE . MET A 145 ? 0.5272 0.4652 0.5605 -0.0407 0.0152 -0.0286 173 MET A CE 1074 N N . HIS A 146 ? 0.3727 0.2831 0.3787 -0.0360 0.0098 -0.0272 174 HIS A N 1075 C CA . HIS A 146 ? 0.4221 0.3321 0.4240 -0.0355 0.0097 -0.0273 174 HIS A CA 1076 C C . HIS A 146 ? 0.4459 0.3590 0.4473 -0.0374 0.0125 -0.0286 174 HIS A C 1077 O O . HIS A 146 ? 0.5228 0.4321 0.5207 -0.0393 0.0155 -0.0308 174 HIS A O 1078 C CB . HIS A 146 ? 0.4004 0.3001 0.3930 -0.0344 0.0095 -0.0286 174 HIS A CB 1079 C CG . HIS A 146 ? 0.4673 0.3649 0.4603 -0.0322 0.0061 -0.0271 174 HIS A CG 1080 N ND1 . HIS A 146 ? 0.3687 0.2691 0.3625 -0.0302 0.0033 -0.0256 174 HIS A ND1 1081 C CD2 . HIS A 146 ? 0.4927 0.3861 0.4856 -0.0319 0.0051 -0.0270 174 HIS A CD2 1082 C CE1 . HIS A 146 ? 0.4005 0.2985 0.3947 -0.0289 0.0006 -0.0246 174 HIS A CE1 1083 N NE2 . HIS A 146 ? 0.4860 0.3795 0.4796 -0.0298 0.0016 -0.0254 174 HIS A NE2 1084 N N . LEU A 147 ? 0.4858 0.4060 0.4907 -0.0369 0.0114 -0.0274 175 LEU A N 1085 C CA . LEU A 147 ? 0.3915 0.3155 0.3965 -0.0385 0.0136 -0.0283 175 LEU A CA 1086 C C . LEU A 147 ? 0.4240 0.3452 0.4229 -0.0374 0.0131 -0.0288 175 LEU A C 1087 O O . LEU A 147 ? 0.3699 0.2939 0.3702 -0.0352 0.0105 -0.0272 175 LEU A O 1088 C CB . LEU A 147 ? 0.3095 0.2448 0.3239 -0.0388 0.0126 -0.0264 175 LEU A CB 1089 C CG . LEU A 147 ? 0.3989 0.3398 0.4146 -0.0402 0.0142 -0.0271 175 LEU A CG 1090 C CD1 . LEU A 147 ? 0.3694 0.3083 0.3834 -0.0429 0.0176 -0.0295 175 LEU A CD1 1091 C CD2 . LEU A 147 ? 0.3353 0.2872 0.3600 -0.0399 0.0125 -0.0247 175 LEU A CD2 1092 N N . ALA A 148 ? 0.3783 0.2937 0.3702 -0.0389 0.0157 -0.0311 176 ALA A N 1093 C CA . ALA A 148 ? 0.3017 0.2138 0.2871 -0.0380 0.0155 -0.0319 176 ALA A CA 1094 C C . ALA A 148 ? 0.3165 0.2376 0.3067 -0.0386 0.0157 -0.0314 176 ALA A C 1095 O O . ALA A 148 ? 0.4108 0.3355 0.4038 -0.0412 0.0179 -0.0322 176 ALA A O 1096 C CB . ALA A 148 ? 0.2931 0.1944 0.2684 -0.0398 0.0181 -0.0346 176 ALA A CB 1097 N N . TYR A 149 ? 0.3112 0.2363 0.3025 -0.0362 0.0135 -0.0301 177 TYR A N 1098 C CA . TYR A 149 ? 0.3020 0.2367 0.2986 -0.0363 0.0132 -0.0292 177 TYR A CA 1099 C C . TYR A 149 ? 0.4391 0.3716 0.4295 -0.0346 0.0128 -0.0302 177 TYR A C 1100 O O . TYR A 149 ? 0.3874 0.3168 0.3743 -0.0317 0.0109 -0.0299 177 TYR A O 1101 C CB . TYR A 149 ? 0.3409 0.2849 0.3463 -0.0349 0.0107 -0.0263 177 TYR A CB 1102 C CG . TYR A 149 ? 0.3272 0.2813 0.3382 -0.0350 0.0103 -0.0251 177 TYR A CG 1103 C CD1 . TYR A 149 ? 0.3449 0.3052 0.3617 -0.0373 0.0116 -0.0249 177 TYR A CD1 1104 C CD2 . TYR A 149 ? 0.4057 0.3638 0.4164 -0.0327 0.0086 -0.0243 177 TYR A CD2 1105 C CE1 . TYR A 149 ? 0.3660 0.3354 0.3876 -0.0374 0.0111 -0.0237 177 TYR A CE1 1106 C CE2 . TYR A 149 ? 0.3097 0.2773 0.3254 -0.0329 0.0083 -0.0231 177 TYR A CE2 1107 C CZ . TYR A 149 ? 0.3627 0.3355 0.3835 -0.0353 0.0096 -0.0228 177 TYR A CZ 1108 O OH . TYR A 149 ? 0.4056 0.3874 0.4310 -0.0355 0.0092 -0.0217 177 TYR A OH 1109 N N . SER A 150 ? 0.3038 0.2377 0.2927 -0.0363 0.0145 -0.0315 178 SER A N 1110 C CA . SER A 150 ? 0.3259 0.2581 0.3092 -0.0348 0.0141 -0.0325 178 SER A CA 1111 C C . SER A 150 ? 0.4098 0.3534 0.3998 -0.0333 0.0126 -0.0307 178 SER A C 1112 O O . SER A 150 ? 0.3729 0.3239 0.3686 -0.0352 0.0134 -0.0302 178 SER A O 1113 C CB . SER A 150 ? 0.4351 0.3616 0.4120 -0.0376 0.0167 -0.0350 178 SER A CB 1114 O OG . SER A 150 ? 0.4924 0.4166 0.4634 -0.0359 0.0161 -0.0361 178 SER A OG 1115 N N . VAL A 151 ? 0.3739 0.3191 0.3632 -0.0298 0.0103 -0.0299 179 VAL A N 1116 C CA . VAL A 151 ? 0.3482 0.3045 0.3438 -0.0283 0.0088 -0.0281 179 VAL A CA 1117 C C . VAL A 151 ? 0.4078 0.3673 0.4021 -0.0292 0.0100 -0.0292 179 VAL A C 1118 O O . VAL A 151 ? 0.4316 0.3840 0.4178 -0.0289 0.0108 -0.0315 179 VAL A O 1119 C CB . VAL A 151 ? 0.3301 0.2869 0.3238 -0.0243 0.0064 -0.0276 179 VAL A CB 1120 C CG1 . VAL A 151 ? 0.3146 0.2827 0.3136 -0.0229 0.0053 -0.0261 179 VAL A CG1 1121 C CG2 . VAL A 151 ? 0.3599 0.3155 0.3561 -0.0234 0.0047 -0.0261 179 VAL A CG2 1122 N N . GLY A 152 ? 0.3530 0.3228 0.3553 -0.0305 0.0100 -0.0275 180 GLY A N 1123 C CA . GLY A 152 ? 0.3784 0.3529 0.3809 -0.0313 0.0108 -0.0282 180 GLY A CA 1124 C C . GLY A 152 ? 0.4928 0.4724 0.4947 -0.0282 0.0093 -0.0278 180 GLY A C 1125 O O . GLY A 152 ? 0.5479 0.5306 0.5519 -0.0256 0.0074 -0.0263 180 GLY A O 1126 N N . LYS A 153 ? 0.5724 0.5531 0.5713 -0.0283 0.0100 -0.0292 181 LYS A N 1127 C CA . LYS A 153 ? 0.5571 0.5431 0.5551 -0.0252 0.0087 -0.0291 181 LYS A CA 1128 C C . LYS A 153 ? 0.5175 0.5164 0.5249 -0.0248 0.0075 -0.0260 181 LYS A C 1129 O O . LYS A 153 ? 0.4653 0.4703 0.4786 -0.0273 0.0081 -0.0247 181 LYS A O 1130 C CB . LYS A 153 ? 0.6321 0.6159 0.6246 -0.0257 0.0098 -0.0314 181 LYS A CB 1131 C CG . LYS A 153 ? 0.7262 0.7199 0.7216 -0.0242 0.0091 -0.0307 181 LYS A CG 1132 C CD . LYS A 153 ? 0.7703 0.7589 0.7573 -0.0232 0.0096 -0.0336 181 LYS A CD 1133 C CE . LYS A 153 ? 0.8639 0.8450 0.8430 -0.0190 0.0084 -0.0352 181 LYS A CE 1134 N NZ . LYS A 153 ? 0.7581 0.7473 0.7385 -0.0149 0.0069 -0.0347 181 LYS A NZ 1135 N N . GLY A 154 ? 0.4411 0.4442 0.4494 -0.0216 0.0058 -0.0250 182 GLY A N 1136 C CA . GLY A 154 ? 0.4013 0.4165 0.4177 -0.0212 0.0046 -0.0220 182 GLY A CA 1137 C C . GLY A 154 ? 0.4778 0.4950 0.5005 -0.0224 0.0036 -0.0194 182 GLY A C 1138 O O . GLY A 154 ? 0.4993 0.5257 0.5285 -0.0225 0.0025 -0.0167 182 GLY A O 1139 N N . GLU A 155 ? 0.4262 0.4346 0.4466 -0.0235 0.0041 -0.0202 183 GLU A N 1140 C CA . GLU A 155 ? 0.4389 0.4483 0.4647 -0.0246 0.0031 -0.0180 183 GLU A CA 1141 C C . GLU A 155 ? 0.5140 0.5243 0.5402 -0.0220 0.0010 -0.0169 183 GLU A C 1142 O O . GLU A 155 ? 0.6033 0.6103 0.6240 -0.0191 0.0005 -0.0186 183 GLU A O 1143 C CB . GLU A 155 ? 0.3904 0.3906 0.4139 -0.0267 0.0044 -0.0193 183 GLU A CB 1144 C CG . GLU A 155 ? 0.4802 0.4824 0.5065 -0.0298 0.0061 -0.0196 183 GLU A CG 1145 C CD . GLU A 155 ? 0.6397 0.6336 0.6636 -0.0321 0.0077 -0.0211 183 GLU A CD 1146 O OE1 . GLU A 155 ? 0.5595 0.5448 0.5788 -0.0314 0.0078 -0.0222 183 GLU A OE1 1147 O OE2 . GLU A 155 ? 0.8133 0.8096 0.8402 -0.0346 0.0090 -0.0214 183 GLU A OE2 1148 N N . ASN A 156 ? 0.4300 0.4451 0.4629 -0.0230 -0.0003 -0.0142 184 ASN A N 1149 C CA . ASN A 156 ? 0.4235 0.4398 0.4576 -0.0212 -0.0023 -0.0130 184 ASN A CA 1150 C C . ASN A 156 ? 0.4084 0.4196 0.4444 -0.0227 -0.0030 -0.0120 184 ASN A C 1151 O O . ASN A 156 ? 0.4483 0.4577 0.4866 -0.0253 -0.0021 -0.0116 184 ASN A O 1152 C CB . ASN A 156 ? 0.5039 0.5325 0.5441 -0.0208 -0.0037 -0.0103 184 ASN A CB 1153 C CG . ASN A 156 ? 0.5268 0.5622 0.5742 -0.0238 -0.0037 -0.0075 184 ASN A CG 1154 O OD1 . ASN A 156 ? 0.6606 0.6952 0.7119 -0.0256 -0.0047 -0.0056 184 ASN A OD1 1155 N ND2 . ASN A 156 ? 0.5288 0.5707 0.5776 -0.0243 -0.0029 -0.0072 184 ASN A ND2 1156 N N . THR A 157 ? 0.3730 0.3819 0.4081 -0.0211 -0.0047 -0.0118 185 THR A N 1157 C CA . THR A 157 ? 0.4709 0.4738 0.5067 -0.0222 -0.0054 -0.0112 185 THR A CA 1158 C C . THR A 157 ? 0.5151 0.5244 0.5589 -0.0247 -0.0065 -0.0080 185 THR A C 1159 O O . THR A 157 ? 0.5814 0.5860 0.6265 -0.0263 -0.0065 -0.0076 185 THR A O 1160 C CB . THR A 157 ? 0.5735 0.5728 0.6062 -0.0197 -0.0073 -0.0118 185 THR A CB 1161 O OG1 . THR A 157 ? 0.5865 0.5955 0.6229 -0.0182 -0.0090 -0.0102 185 THR A OG1 1162 C CG2 . THR A 157 ? 0.5950 0.5851 0.6185 -0.0173 -0.0063 -0.0151 185 THR A CG2 1163 N N . SER A 158 ? 0.5272 0.5469 0.5762 -0.0249 -0.0073 -0.0058 186 SER A N 1164 C CA . SER A 158 ? 0.3983 0.4242 0.4545 -0.0273 -0.0085 -0.0025 186 SER A CA 1165 C C . SER A 158 ? 0.4201 0.4445 0.4779 -0.0295 -0.0071 -0.0025 186 SER A C 1166 O O . SER A 158 ? 0.5737 0.5951 0.6340 -0.0311 -0.0076 -0.0015 186 SER A O 1167 C CB . SER A 158 ? 0.4811 0.5186 0.5417 -0.0273 -0.0095 -0.0002 186 SER A CB 1168 O OG . SER A 158 ? 0.6279 0.6704 0.6948 -0.0298 -0.0109 0.0032 186 SER A OG 1169 N N . ALA A 159 ? 0.4777 0.5042 0.5340 -0.0295 -0.0053 -0.0038 187 ALA A N 1170 C CA . ALA A 159 ? 0.4152 0.4414 0.4734 -0.0315 -0.0040 -0.0039 187 ALA A CA 1171 C C . ALA A 159 ? 0.4742 0.4904 0.5288 -0.0321 -0.0026 -0.0063 187 ALA A C 1172 O O . ALA A 159 ? 0.5769 0.5923 0.6344 -0.0338 -0.0022 -0.0059 187 ALA A O 1173 C CB . ALA A 159 ? 0.3626 0.3933 0.4198 -0.0314 -0.0025 -0.0049 187 ALA A CB 1174 N N . ILE A 160 ? 0.4062 0.4150 0.4544 -0.0305 -0.0019 -0.0088 188 ILE A N 1175 C CA . ILE A 160 ? 0.4086 0.4077 0.4527 -0.0312 -0.0005 -0.0110 188 ILE A CA 1176 C C . ILE A 160 ? 0.3887 0.3850 0.4356 -0.0318 -0.0019 -0.0096 188 ILE A C 1177 O O . ILE A 160 ? 0.4418 0.4351 0.4900 -0.0332 -0.0010 -0.0100 188 ILE A O 1178 C CB . ILE A 160 ? 0.3813 0.3723 0.4170 -0.0294 0.0004 -0.0138 188 ILE A CB 1179 C CG1 . ILE A 160 ? 0.3176 0.3094 0.3494 -0.0292 0.0021 -0.0157 188 ILE A CG1 1180 C CG2 . ILE A 160 ? 0.3031 0.2839 0.3345 -0.0301 0.0015 -0.0157 188 ILE A CG2 1181 C CD1 . ILE A 160 ? 0.2554 0.2402 0.2789 -0.0269 0.0023 -0.0181 188 ILE A CD1 1182 N N . ALA A 161 ? 0.4433 0.4408 0.4913 -0.0306 -0.0041 -0.0080 189 ALA A N 1183 C CA . ALA A 161 ? 0.4944 0.4893 0.5450 -0.0312 -0.0058 -0.0065 189 ALA A CA 1184 C C . ALA A 161 ? 0.5766 0.5762 0.6337 -0.0332 -0.0064 -0.0043 189 ALA A C 1185 O O . ALA A 161 ? 0.6258 0.6208 0.6837 -0.0340 -0.0063 -0.0046 189 ALA A O 1186 C CB . ALA A 161 ? 0.5324 0.5297 0.5839 -0.0299 -0.0083 -0.0049 189 ALA A CB 1187 N N . ALA A 162 ? 0.5428 0.5515 0.6043 -0.0337 -0.0069 -0.0023 190 ALA A N 1188 C CA . ALA A 162 ? 0.5301 0.5435 0.5976 -0.0355 -0.0079 0.0001 190 ALA A CA 1189 C C . ALA A 162 ? 0.5258 0.5365 0.5933 -0.0364 -0.0060 -0.0016 190 ALA A C 1190 O O . ALA A 162 ? 0.6387 0.6478 0.7092 -0.0372 -0.0067 -0.0008 190 ALA A O 1191 C CB . ALA A 162 ? 0.4073 0.4309 0.4788 -0.0360 -0.0087 0.0026 190 ALA A CB 1192 N N . LYS A 163 ? 0.4226 0.4329 0.4869 -0.0362 -0.0036 -0.0040 191 LYS A N 1193 C CA . LYS A 163 ? 0.3876 0.3960 0.4520 -0.0372 -0.0016 -0.0059 191 LYS A CA 1194 C C . LYS A 163 ? 0.4218 0.4218 0.4842 -0.0373 -0.0011 -0.0074 191 LYS A C 1195 O O . LYS A 163 ? 0.4827 0.4822 0.5473 -0.0382 -0.0003 -0.0081 191 LYS A O 1196 C CB . LYS A 163 ? 0.4596 0.4678 0.5198 -0.0373 0.0008 -0.0085 191 LYS A CB 1197 C CG . LYS A 163 ? 0.6972 0.7024 0.7570 -0.0386 0.0030 -0.0108 191 LYS A CG 1198 C CD . LYS A 163 ? 0.7910 0.7982 0.8489 -0.0395 0.0052 -0.0128 191 LYS A CD 1199 C CE . LYS A 163 ? 0.8603 0.8672 0.9206 -0.0411 0.0066 -0.0142 191 LYS A CE 1200 N NZ . LYS A 163 ? 0.9262 0.9361 0.9860 -0.0425 0.0086 -0.0161 191 LYS A NZ 1201 N N . TYR A 164 ? 0.4742 0.4678 0.5325 -0.0363 -0.0016 -0.0081 192 TYR A N 1202 C CA . TYR A 164 ? 0.5678 0.5534 0.6237 -0.0364 -0.0010 -0.0096 192 TYR A CA 1203 C C . TYR A 164 ? 0.5233 0.5075 0.5821 -0.0361 -0.0036 -0.0075 192 TYR A C 1204 O O . TYR A 164 ? 0.4774 0.4543 0.5335 -0.0358 -0.0036 -0.0087 192 TYR A O 1205 C CB . TYR A 164 ? 0.4968 0.4742 0.5449 -0.0357 0.0008 -0.0124 192 TYR A CB 1206 C CG . TYR A 164 ? 0.5217 0.4990 0.5669 -0.0366 0.0036 -0.0149 192 TYR A CG 1207 C CD1 . TYR A 164 ? 0.4244 0.4014 0.4711 -0.0382 0.0056 -0.0163 192 TYR A CD1 1208 C CD2 . TYR A 164 ? 0.3699 0.3477 0.4110 -0.0360 0.0043 -0.0158 192 TYR A CD2 1209 C CE1 . TYR A 164 ? 0.4351 0.4125 0.4794 -0.0394 0.0081 -0.0185 192 TYR A CE1 1210 C CE2 . TYR A 164 ? 0.3600 0.3373 0.3982 -0.0371 0.0068 -0.0180 192 TYR A CE2 1211 C CZ . TYR A 164 ? 0.4458 0.4230 0.4856 -0.0390 0.0087 -0.0192 192 TYR A CZ 1212 O OH . TYR A 164 ? 0.5138 0.4909 0.5510 -0.0405 0.0111 -0.0214 192 TYR A OH 1213 N N . GLY A 165 ? 0.5173 0.5083 0.5813 -0.0364 -0.0059 -0.0044 193 GLY A N 1214 C CA . GLY A 165 ? 0.5394 0.5297 0.6068 -0.0366 -0.0086 -0.0020 193 GLY A CA 1215 C C . GLY A 165 ? 0.5973 0.5818 0.6609 -0.0357 -0.0098 -0.0024 193 GLY A C 1216 O O . GLY A 165 ? 0.7036 0.6825 0.7667 -0.0356 -0.0110 -0.0024 193 GLY A O 1217 N N . VAL A 166 ? 0.4897 0.4757 0.5504 -0.0348 -0.0096 -0.0028 194 VAL A N 1218 C CA . VAL A 166 ? 0.5439 0.5250 0.6007 -0.0335 -0.0107 -0.0034 194 VAL A CA 1219 C C . VAL A 166 ? 0.5600 0.5484 0.6190 -0.0331 -0.0126 -0.0012 194 VAL A C 1220 O O . VAL A 166 ? 0.6531 0.6491 0.7146 -0.0334 -0.0121 -0.0002 194 VAL A O 1221 C CB . VAL A 166 ? 0.6393 0.6132 0.6888 -0.0324 -0.0082 -0.0068 194 VAL A CB 1222 C CG1 . VAL A 166 ? 0.5332 0.5062 0.5786 -0.0306 -0.0089 -0.0074 194 VAL A CG1 1223 C CG2 . VAL A 166 ? 0.5852 0.5500 0.6318 -0.0326 -0.0076 -0.0085 194 VAL A CG2 1224 N N . THR A 167 ? 0.5995 0.5859 0.6578 -0.0325 -0.0148 -0.0005 195 THR A N 1225 C CA . THR A 167 ? 0.6570 0.6503 0.7171 -0.0320 -0.0165 0.0012 195 THR A CA 1226 C C . THR A 167 ? 0.5808 0.5739 0.6359 -0.0298 -0.0151 -0.0011 195 THR A C 1227 O O . THR A 167 ? 0.5643 0.5493 0.6135 -0.0285 -0.0138 -0.0039 195 THR A O 1228 C CB . THR A 167 ? 0.6985 0.6896 0.7594 -0.0321 -0.0194 0.0025 195 THR A CB 1229 O OG1 . THR A 167 ? 0.7430 0.7411 0.8102 -0.0342 -0.0215 0.0060 195 THR A OG1 1230 C CG2 . THR A 167 ? 0.5703 0.5626 0.6285 -0.0302 -0.0204 0.0017 195 THR A CG2 1231 N N . GLU A 168 ? 0.4756 0.4776 0.5330 -0.0293 -0.0154 0.0000 196 GLU A N 1232 C CA . GLU A 168 ? 0.4842 0.4864 0.5370 -0.0269 -0.0143 -0.0022 196 GLU A CA 1233 C C . GLU A 168 ? 0.5488 0.5451 0.5968 -0.0247 -0.0156 -0.0038 196 GLU A C 1234 O O . GLU A 168 ? 0.5521 0.5417 0.5935 -0.0228 -0.0142 -0.0066 196 GLU A O 1235 C CB . GLU A 168 ? 0.4119 0.4255 0.4683 -0.0266 -0.0146 -0.0007 196 GLU A CB 1236 C CG . GLU A 168 ? 0.5180 0.5316 0.5693 -0.0238 -0.0136 -0.0031 196 GLU A CG 1237 C CD . GLU A 168 ? 0.6473 0.6719 0.7016 -0.0232 -0.0136 -0.0020 196 GLU A CD 1238 O OE1 . GLU A 168 ? 0.6874 0.7200 0.7478 -0.0254 -0.0141 0.0008 196 GLU A OE1 1239 O OE2 . GLU A 168 ? 0.6607 0.6858 0.7109 -0.0205 -0.0130 -0.0040 196 GLU A OE2 1240 N N . SER A 169 ? 0.5151 0.5130 0.5659 -0.0250 -0.0182 -0.0021 197 SER A N 1241 C CA . SER A 169 ? 0.5772 0.5697 0.6236 -0.0228 -0.0197 -0.0036 197 SER A CA 1242 C C . SER A 169 ? 0.5233 0.5033 0.5638 -0.0225 -0.0188 -0.0058 197 SER A C 1243 O O . SER A 169 ? 0.5123 0.4856 0.5464 -0.0201 -0.0188 -0.0081 197 SER A O 1244 C CB . SER A 169 ? 0.6402 0.6379 0.6913 -0.0234 -0.0228 -0.0012 197 SER A CB 1245 O OG . SER A 169 ? 0.7731 0.7703 0.8284 -0.0263 -0.0238 0.0010 197 SER A OG 1246 N N . THR A 170 ? 0.4385 0.4153 0.4810 -0.0248 -0.0181 -0.0051 198 THR A N 1247 C CA . THR A 170 ? 0.5652 0.5308 0.6022 -0.0248 -0.0166 -0.0073 198 THR A CA 1248 C C . THR A 170 ? 0.5782 0.5397 0.6090 -0.0236 -0.0138 -0.0101 198 THR A C 1249 O O . THR A 170 ? 0.5166 0.4691 0.5403 -0.0222 -0.0132 -0.0124 198 THR A O 1250 C CB . THR A 170 ? 0.6052 0.5697 0.6459 -0.0272 -0.0160 -0.0063 198 THR A CB 1251 O OG1 . THR A 170 ? 0.7684 0.7336 0.8131 -0.0282 -0.0187 -0.0041 198 THR A OG1 1252 C CG2 . THR A 170 ? 0.4442 0.3986 0.4792 -0.0272 -0.0138 -0.0089 198 THR A CG2 1253 N N . LEU A 171 ? 0.5778 0.5455 0.6109 -0.0242 -0.0122 -0.0098 199 LEU A N 1254 C CA . LEU A 171 ? 0.5201 0.4841 0.5475 -0.0234 -0.0097 -0.0123 199 LEU A CA 1255 C C . LEU A 171 ? 0.4765 0.4380 0.4982 -0.0204 -0.0106 -0.0138 199 LEU A C 1256 O O . LEU A 171 ? 0.4508 0.4033 0.4648 -0.0193 -0.0094 -0.0163 199 LEU A O 1257 C CB . LEU A 171 ? 0.4427 0.4148 0.4740 -0.0246 -0.0082 -0.0116 199 LEU A CB 1258 C CG . LEU A 171 ? 0.5132 0.4814 0.5391 -0.0245 -0.0054 -0.0142 199 LEU A CG 1259 C CD1 . LEU A 171 ? 0.4031 0.3628 0.4260 -0.0262 -0.0034 -0.0158 199 LEU A CD1 1260 C CD2 . LEU A 171 ? 0.3665 0.3436 0.3966 -0.0255 -0.0044 -0.0133 199 LEU A CD2 1261 N N . LEU A 172 ? 0.5568 0.5263 0.5822 -0.0190 -0.0128 -0.0123 200 LEU A N 1262 C CA . LEU A 172 ? 0.4828 0.4518 0.5037 -0.0157 -0.0140 -0.0136 200 LEU A CA 1263 C C . LEU A 172 ? 0.5565 0.5164 0.5719 -0.0140 -0.0155 -0.0150 200 LEU A C 1264 O O . LEU A 172 ? 0.5928 0.5463 0.6008 -0.0114 -0.0154 -0.0173 200 LEU A O 1265 C CB . LEU A 172 ? 0.5462 0.5275 0.5735 -0.0149 -0.0159 -0.0116 200 LEU A CB 1266 C CG . LEU A 172 ? 0.5673 0.5573 0.5983 -0.0159 -0.0144 -0.0107 200 LEU A CG 1267 C CD1 . LEU A 172 ? 0.5035 0.5065 0.5416 -0.0160 -0.0160 -0.0082 200 LEU A CD1 1268 C CD2 . LEU A 172 ? 0.5735 0.5595 0.5978 -0.0140 -0.0125 -0.0135 200 LEU A CD2 1269 N N . THR A 173 ? 0.5579 0.5165 0.5763 -0.0153 -0.0171 -0.0136 201 THR A N 1270 C CA . THR A 173 ? 0.5418 0.4916 0.5549 -0.0137 -0.0187 -0.0148 201 THR A CA 1271 C C . THR A 173 ? 0.4625 0.3998 0.4678 -0.0141 -0.0165 -0.0171 201 THR A C 1272 O O . THR A 173 ? 0.5052 0.4339 0.5028 -0.0120 -0.0169 -0.0192 201 THR A O 1273 C CB . THR A 173 ? 0.5873 0.5389 0.6055 -0.0151 -0.0213 -0.0127 201 THR A CB 1274 O OG1 . THR A 173 ? 0.8016 0.7510 0.8226 -0.0181 -0.0200 -0.0118 201 THR A OG1 1275 C CG2 . THR A 173 ? 0.4667 0.4309 0.4925 -0.0152 -0.0234 -0.0103 201 THR A CG2 1276 N N . ARG A 174 ? 0.4384 0.3749 0.4459 -0.0169 -0.0143 -0.0168 202 ARG A N 1277 C CA . ARG A 174 ? 0.5002 0.4260 0.5009 -0.0178 -0.0118 -0.0190 202 ARG A CA 1278 C C . ARG A 174 ? 0.5289 0.4501 0.5220 -0.0162 -0.0102 -0.0213 202 ARG A C 1279 O O . ARG A 174 ? 0.5350 0.4455 0.5197 -0.0157 -0.0092 -0.0234 202 ARG A O 1280 C CB . ARG A 174 ? 0.5385 0.4666 0.5440 -0.0209 -0.0097 -0.0183 202 ARG A CB 1281 C CG . ARG A 174 ? 0.5020 0.4204 0.5015 -0.0222 -0.0069 -0.0205 202 ARG A CG 1282 C CD . ARG A 174 ? 0.4752 0.3850 0.4709 -0.0219 -0.0079 -0.0210 202 ARG A CD 1283 N NE . ARG A 174 ? 0.4464 0.3457 0.4340 -0.0225 -0.0053 -0.0235 202 ARG A NE 1284 C CZ . ARG A 174 ? 0.4977 0.3880 0.4801 -0.0223 -0.0056 -0.0245 202 ARG A CZ 1285 N NH1 . ARG A 174 ? 0.5723 0.4626 0.5570 -0.0213 -0.0086 -0.0233 202 ARG A NH1 1286 N NH2 . ARG A 174 ? 0.5206 0.4017 0.4954 -0.0232 -0.0030 -0.0268 202 ARG A NH2 1287 N N . ASN A 175 ? 0.5136 0.4423 0.5091 -0.0155 -0.0099 -0.0210 203 ASN A N 1288 C CA . ASN A 175 ? 0.4670 0.3906 0.4548 -0.0141 -0.0084 -0.0233 203 ASN A CA 1289 C C . ASN A 175 ? 0.4958 0.4194 0.4796 -0.0102 -0.0106 -0.0242 203 ASN A C 1290 O O . ASN A 175 ? 0.5515 0.4719 0.5294 -0.0086 -0.0097 -0.0259 203 ASN A O 1291 C CB . ASN A 175 ? 0.5086 0.4381 0.4994 -0.0159 -0.0061 -0.0232 203 ASN A CB 1292 C CG . ASN A 175 ? 0.5005 0.4273 0.4926 -0.0194 -0.0036 -0.0234 203 ASN A CG 1293 O OD1 . ASN A 175 ? 0.4447 0.3624 0.4298 -0.0203 -0.0015 -0.0254 203 ASN A OD1 1294 N ND2 . ASN A 175 ? 0.4485 0.3832 0.4493 -0.0214 -0.0037 -0.0212 203 ASN A ND2 1295 N N . LYS A 176 ? 0.6830 0.6098 0.6698 -0.0085 -0.0135 -0.0230 204 LYS A N 1296 C CA . LYS A 176 ? 0.6034 0.5317 0.5876 -0.0045 -0.0160 -0.0237 204 LYS A CA 1297 C C . LYS A 176 ? 0.5308 0.4666 0.5160 -0.0028 -0.0155 -0.0241 204 LYS A C 1298 O O . LYS A 176 ? 0.5309 0.4618 0.5089 0.0001 -0.0156 -0.0262 204 LYS A O 1299 C CB . LYS A 176 ? 0.6675 0.5826 0.6410 -0.0022 -0.0165 -0.0261 204 LYS A CB 1300 C CG . LYS A 176 ? 0.7870 0.6933 0.7581 -0.0040 -0.0165 -0.0261 204 LYS A CG 1301 C CD . LYS A 176 ? 0.9536 0.8463 0.9130 -0.0018 -0.0166 -0.0286 204 LYS A CD 1302 C CE . LYS A 176 ? 1.1032 0.9866 1.0593 -0.0035 -0.0164 -0.0288 204 LYS A CE 1303 N NZ . LYS A 176 ? 1.1295 1.0045 1.0802 -0.0064 -0.0128 -0.0301 204 LYS A NZ 1304 N N . ILE A 177 ? 0.4718 0.4191 0.4656 -0.0047 -0.0151 -0.0220 205 ILE A N 1305 C CA . ILE A 177 ? 0.6246 0.5801 0.6201 -0.0033 -0.0146 -0.0221 205 ILE A CA 1306 C C . ILE A 177 ? 0.6813 0.6484 0.6832 -0.0014 -0.0171 -0.0206 205 ILE A C 1307 O O . ILE A 177 ? 0.6203 0.5960 0.6306 -0.0037 -0.0178 -0.0179 205 ILE A O 1308 C CB . ILE A 177 ? 0.5780 0.5388 0.5785 -0.0068 -0.0121 -0.0209 205 ILE A CB 1309 C CG1 . ILE A 177 ? 0.4191 0.3694 0.4129 -0.0085 -0.0094 -0.0229 205 ILE A CG1 1310 C CG2 . ILE A 177 ? 0.4939 0.4653 0.4979 -0.0057 -0.0120 -0.0205 205 ILE A CG2 1311 C CD1 . ILE A 177 ? 0.4026 0.3575 0.4019 -0.0123 -0.0072 -0.0217 205 ILE A CD1 1312 N N . ASP A 178 ? 0.7035 0.6706 0.7010 0.0028 -0.0185 -0.0223 206 ASP A N 1313 C CA . ASP A 178 ? 0.6771 0.6554 0.6801 0.0051 -0.0210 -0.0213 206 ASP A CA 1314 C C . ASP A 178 ? 0.7332 0.7243 0.7427 0.0042 -0.0200 -0.0199 206 ASP A C 1315 O O . ASP A 178 ? 0.8163 0.8188 0.8339 0.0031 -0.0211 -0.0175 206 ASP A O 1316 C CB . ASP A 178 ? 0.6625 0.6369 0.6584 0.0103 -0.0227 -0.0240 206 ASP A CB 1317 C CG . ASP A 178 ? 0.7958 0.7580 0.7851 0.0115 -0.0241 -0.0252 206 ASP A CG 1318 O OD1 . ASP A 178 ? 0.7813 0.7427 0.7742 0.0090 -0.0250 -0.0236 206 ASP A OD1 1319 O OD2 . ASP A 178 ? 0.8559 0.8089 0.8360 0.0149 -0.0244 -0.0279 206 ASP A OD2 1320 N N . ASP A 179 ? 0.6474 0.6365 0.6530 0.0047 -0.0179 -0.0213 207 ASP A N 1321 C CA . ASP A 179 ? 0.5282 0.5289 0.5390 0.0042 -0.0169 -0.0203 207 ASP A CA 1322 C C . ASP A 179 ? 0.5179 0.5164 0.5288 0.0008 -0.0141 -0.0199 207 ASP A C 1323 O O . ASP A 179 ? 0.5117 0.5022 0.5154 0.0015 -0.0126 -0.0222 207 ASP A O 1324 C CB . ASP A 179 ? 0.4857 0.4891 0.4923 0.0090 -0.0175 -0.0225 207 ASP A CB 1325 C CG . ASP A 179 ? 0.5472 0.5638 0.5593 0.0090 -0.0167 -0.0215 207 ASP A CG 1326 O OD1 . ASP A 179 ? 0.6287 0.6535 0.6485 0.0053 -0.0160 -0.0186 207 ASP A OD1 1327 O OD2 . ASP A 179 ? 0.7260 0.7448 0.7345 0.0128 -0.0168 -0.0235 207 ASP A OD2 1328 N N . PRO A 180 ? 0.5982 0.6038 0.6170 -0.0030 -0.0136 -0.0171 208 PRO A N 1329 C CA . PRO A 180 ? 0.5598 0.5655 0.5804 -0.0064 -0.0113 -0.0164 208 PRO A CA 1330 C C . PRO A 180 ? 0.5604 0.5687 0.5782 -0.0051 -0.0098 -0.0179 208 PRO A C 1331 O O . PRO A 180 ? 0.6219 0.6247 0.6365 -0.0068 -0.0078 -0.0190 208 PRO A O 1332 C CB . PRO A 180 ? 0.5287 0.5452 0.5591 -0.0093 -0.0120 -0.0128 208 PRO A CB 1333 C CG . PRO A 180 ? 0.5229 0.5397 0.5554 -0.0087 -0.0144 -0.0118 208 PRO A CG 1334 C CD . PRO A 180 ? 0.6257 0.6396 0.6522 -0.0043 -0.0156 -0.0143 208 PRO A CD 1335 N N . THR A 181 ? 0.5772 0.5941 0.5963 -0.0022 -0.0108 -0.0180 209 THR A N 1336 C CA . THR A 181 ? 0.5736 0.5941 0.5904 -0.0008 -0.0095 -0.0193 209 THR A CA 1337 C C . THR A 181 ? 0.4655 0.4740 0.4721 0.0013 -0.0086 -0.0228 209 THR A C 1338 O O . THR A 181 ? 0.6950 0.7033 0.6985 0.0017 -0.0072 -0.0242 209 THR A O 1339 C CB . THR A 181 ? 0.5920 0.6246 0.6121 0.0022 -0.0107 -0.0189 209 THR A CB 1340 O OG1 . THR A 181 ? 0.6579 0.6872 0.6735 0.0065 -0.0125 -0.0209 209 THR A OG1 1341 C CG2 . THR A 181 ? 0.5298 0.5744 0.5598 -0.0005 -0.0115 -0.0152 209 THR A CG2 1342 N N . LYS A 182 ? 0.5168 0.5150 0.5179 0.0027 -0.0095 -0.0242 210 LYS A N 1343 C CA . LYS A 182 ? 0.4694 0.4548 0.4598 0.0047 -0.0089 -0.0274 210 LYS A CA 1344 C C . LYS A 182 ? 0.5042 0.4799 0.4914 0.0008 -0.0067 -0.0279 210 LYS A C 1345 O O . LYS A 182 ? 0.5433 0.5071 0.5214 0.0016 -0.0061 -0.0304 210 LYS A O 1346 C CB . LYS A 182 ? 0.5984 0.5769 0.5837 0.0082 -0.0110 -0.0288 210 LYS A CB 1347 C CG . LYS A 182 ? 0.6682 0.6561 0.6563 0.0124 -0.0134 -0.0287 210 LYS A CG 1348 C CD . LYS A 182 ? 0.8474 0.8379 0.8313 0.0163 -0.0133 -0.0309 210 LYS A CD 1349 C CE . LYS A 182 ? 0.9846 0.9831 0.9703 0.0210 -0.0158 -0.0313 210 LYS A CE 1350 N NZ . LYS A 182 ? 1.0074 1.0077 0.9976 0.0206 -0.0177 -0.0297 210 LYS A NZ 1351 N N . LEU A 183 ? 0.5557 0.5363 0.5501 -0.0033 -0.0057 -0.0256 211 LEU A N 1352 C CA . LEU A 183 ? 0.4505 0.4234 0.4431 -0.0071 -0.0036 -0.0260 211 LEU A CA 1353 C C . LEU A 183 ? 0.3803 0.3479 0.3662 -0.0073 -0.0017 -0.0284 211 LEU A C 1354 O O . LEU A 183 ? 0.4368 0.4116 0.4246 -0.0070 -0.0013 -0.0284 211 LEU A O 1355 C CB . LEU A 183 ? 0.4278 0.4091 0.4299 -0.0109 -0.0029 -0.0232 211 LEU A CB 1356 C CG . LEU A 183 ? 0.5678 0.5427 0.5701 -0.0146 -0.0013 -0.0231 211 LEU A CG 1357 C CD1 . LEU A 183 ? 0.5069 0.4754 0.5080 -0.0142 -0.0025 -0.0229 211 LEU A CD1 1358 C CD2 . LEU A 183 ? 0.6166 0.6001 0.6276 -0.0178 -0.0006 -0.0208 211 LEU A CD2 1359 N N . GLN A 184 ? 0.4479 0.4028 0.4255 -0.0081 -0.0007 -0.0306 212 GLN A N 1360 C CA . GLN A 184 ? 0.4624 0.4115 0.4333 -0.0090 0.0011 -0.0328 212 GLN A CA 1361 C C . GLN A 184 ? 0.4803 0.4280 0.4531 -0.0138 0.0036 -0.0326 212 GLN A C 1362 O O . GLN A 184 ? 0.6391 0.5845 0.6145 -0.0164 0.0042 -0.0318 212 GLN A O 1363 C CB . GLN A 184 ? 0.5644 0.5000 0.5236 -0.0066 0.0007 -0.0355 212 GLN A CB 1364 C CG . GLN A 184 ? 0.7226 0.6600 0.6786 -0.0014 -0.0014 -0.0365 212 GLN A CG 1365 C CD . GLN A 184 ? 0.8433 0.7668 0.7875 0.0013 -0.0022 -0.0391 212 GLN A CD 1366 O OE1 . GLN A 184 ? 0.8956 0.8080 0.8340 -0.0011 -0.0011 -0.0399 212 GLN A OE1 1367 N NE2 . GLN A 184 ? 0.9210 0.8450 0.8612 0.0062 -0.0041 -0.0404 212 GLN A NE2 1368 N N . MET A 185 ? 0.4177 0.3670 0.3891 -0.0150 0.0049 -0.0337 213 MET A N 1369 C CA . MET A 185 ? 0.4750 0.4220 0.4466 -0.0194 0.0073 -0.0342 213 MET A CA 1370 C C . MET A 185 ? 0.5418 0.4749 0.5049 -0.0209 0.0084 -0.0361 213 MET A C 1371 O O . MET A 185 ? 0.4476 0.3713 0.4015 -0.0186 0.0078 -0.0379 213 MET A O 1372 C CB . MET A 185 ? 0.5385 0.4879 0.5081 -0.0199 0.0082 -0.0355 213 MET A CB 1373 C CG . MET A 185 ? 0.7658 0.7141 0.7361 -0.0246 0.0106 -0.0361 213 MET A CG 1374 S SD . MET A 185 ? 1.1046 1.0525 1.0697 -0.0250 0.0114 -0.0383 213 MET A SD 1375 C CE . MET A 185 ? 1.0175 0.9690 0.9877 -0.0307 0.0138 -0.0382 213 MET A CE 1376 N N . GLY A 186 ? 0.4313 0.3631 0.3975 -0.0245 0.0100 -0.0356 214 GLY A N 1377 C CA . GLY A 186 ? 0.2942 0.2136 0.2527 -0.0265 0.0115 -0.0373 214 GLY A CA 1378 C C . GLY A 186 ? 0.4580 0.3714 0.4141 -0.0245 0.0101 -0.0368 214 GLY A C 1379 O O . GLY A 186 ? 0.5595 0.4630 0.5097 -0.0262 0.0113 -0.0380 214 GLY A O 1380 N N . GLN A 187 ? 0.3174 0.2373 0.2783 -0.0212 0.0077 -0.0352 215 GLN A N 1381 C CA . GLN A 187 ? 0.4902 0.4064 0.4510 -0.0197 0.0062 -0.0344 215 GLN A CA 1382 C C . GLN A 187 ? 0.4464 0.3633 0.4124 -0.0232 0.0076 -0.0333 215 GLN A C 1383 O O . GLN A 187 ? 0.4492 0.3753 0.4238 -0.0252 0.0082 -0.0318 215 GLN A O 1384 C CB . GLN A 187 ? 0.4275 0.3530 0.3945 -0.0163 0.0035 -0.0325 215 GLN A CB 1385 C CG . GLN A 187 ? 0.4734 0.3949 0.4396 -0.0144 0.0015 -0.0319 215 GLN A CG 1386 C CD . GLN A 187 ? 0.5134 0.4433 0.4840 -0.0107 -0.0013 -0.0306 215 GLN A CD 1387 O OE1 . GLN A 187 ? 0.5312 0.4696 0.5050 -0.0094 -0.0017 -0.0302 215 GLN A OE1 1388 N NE2 . GLN A 187 ? 0.4567 0.3843 0.4273 -0.0090 -0.0033 -0.0300 215 GLN A NE2 1389 N N . ILE A 188 ? 0.5021 0.4092 0.4627 -0.0236 0.0079 -0.0341 216 ILE A N 1390 C CA . ILE A 188 ? 0.5295 0.4358 0.4936 -0.0265 0.0092 -0.0335 216 ILE A CA 1391 C C . ILE A 188 ? 0.5237 0.4342 0.4940 -0.0249 0.0069 -0.0314 216 ILE A C 1392 O O . ILE A 188 ? 0.5215 0.4266 0.4876 -0.0224 0.0051 -0.0316 216 ILE A O 1393 C CB . ILE A 188 ? 0.5053 0.3983 0.4598 -0.0281 0.0110 -0.0356 216 ILE A CB 1394 C CG1 . ILE A 188 ? 0.4937 0.3812 0.4408 -0.0298 0.0130 -0.0377 216 ILE A CG1 1395 C CG2 . ILE A 188 ? 0.3805 0.2733 0.3388 -0.0310 0.0126 -0.0352 216 ILE A CG2 1396 C CD1 . ILE A 188 ? 0.3382 0.2334 0.2912 -0.0332 0.0151 -0.0377 216 ILE A CD1 1397 N N . LEU A 189 ? 0.4577 0.3773 0.4376 -0.0265 0.0070 -0.0295 217 LEU A N 1398 C CA . LEU A 189 ? 0.4051 0.3288 0.3912 -0.0255 0.0048 -0.0274 217 LEU A CA 1399 C C . LEU A 189 ? 0.4001 0.3199 0.3875 -0.0278 0.0059 -0.0274 217 LEU A C 1400 O O . LEU A 189 ? 0.4335 0.3537 0.4223 -0.0306 0.0083 -0.0281 217 LEU A O 1401 C CB . LEU A 189 ? 0.4504 0.3873 0.4464 -0.0255 0.0036 -0.0250 217 LEU A CB 1402 C CG . LEU A 189 ? 0.5298 0.4731 0.5264 -0.0231 0.0022 -0.0245 217 LEU A CG 1403 C CD1 . LEU A 189 ? 0.5477 0.5038 0.5542 -0.0236 0.0011 -0.0218 217 LEU A CD1 1404 C CD2 . LEU A 189 ? 0.4772 0.4171 0.4696 -0.0197 0.0000 -0.0248 217 LEU A CD2 1405 N N . ASP A 190 ? 0.4322 0.3487 0.4194 -0.0264 0.0040 -0.0267 218 ASP A N 1406 C CA . ASP A 190 ? 0.4189 0.3326 0.4081 -0.0280 0.0044 -0.0264 218 ASP A CA 1407 C C . ASP A 190 ? 0.4534 0.3772 0.4530 -0.0282 0.0027 -0.0237 218 ASP A C 1408 O O . ASP A 190 ? 0.4124 0.3395 0.4148 -0.0265 -0.0001 -0.0220 218 ASP A O 1409 C CB . ASP A 190 ? 0.3180 0.2225 0.3010 -0.0262 0.0030 -0.0270 218 ASP A CB 1410 C CG . ASP A 190 ? 0.5540 0.4556 0.5391 -0.0274 0.0030 -0.0266 218 ASP A CG 1411 O OD1 . ASP A 190 ? 0.4499 0.3567 0.4415 -0.0293 0.0039 -0.0259 218 ASP A OD1 1412 O OD2 . ASP A 190 ? 0.5455 0.4396 0.5257 -0.0261 0.0018 -0.0271 218 ASP A OD2 1413 N N . VAL A 191 ? 0.4392 0.3679 0.4442 -0.0305 0.0042 -0.0233 219 VAL A N 1414 C CA . VAL A 191 ? 0.4260 0.3638 0.4404 -0.0310 0.0026 -0.0207 219 VAL A CA 1415 C C . VAL A 191 ? 0.4460 0.3810 0.4629 -0.0318 0.0023 -0.0204 219 VAL A C 1416 O O . VAL A 191 ? 0.4263 0.3586 0.4425 -0.0335 0.0046 -0.0218 219 VAL A O 1417 C CB . VAL A 191 ? 0.4107 0.3563 0.4299 -0.0326 0.0041 -0.0204 219 VAL A CB 1418 C CG1 . VAL A 191 ? 0.4348 0.3897 0.4630 -0.0328 0.0021 -0.0175 219 VAL A CG1 1419 C CG2 . VAL A 191 ? 0.3977 0.3451 0.4136 -0.0317 0.0046 -0.0211 219 VAL A CG2 1420 N N . PRO A 192 ? 0.4598 0.3950 0.4791 -0.0307 -0.0005 -0.0186 220 PRO A N 1421 C CA . PRO A 192 ? 0.5061 0.4378 0.5271 -0.0314 -0.0009 -0.0184 220 PRO A CA 1422 C C . PRO A 192 ? 0.5113 0.4505 0.5407 -0.0326 -0.0014 -0.0166 220 PRO A C 1423 O O . PRO A 192 ? 0.4455 0.3897 0.4802 -0.0323 -0.0041 -0.0141 220 PRO A O 1424 C CB . PRO A 192 ? 0.4652 0.3942 0.4852 -0.0297 -0.0040 -0.0173 220 PRO A CB 1425 C CG . PRO A 192 ? 0.4381 0.3725 0.4588 -0.0284 -0.0055 -0.0161 220 PRO A CG 1426 C CD . PRO A 192 ? 0.4180 0.3571 0.4389 -0.0290 -0.0034 -0.0168 220 PRO A CD 1427 N N . LEU A 193 ? 0.5211 0.4609 0.5515 -0.0340 0.0012 -0.0179 221 LEU A N 1428 C CA . LEU A 193 ? 0.4342 0.3805 0.4721 -0.0349 0.0007 -0.0165 221 LEU A CA 1429 C C . LEU A 193 ? 0.5341 0.4777 0.5744 -0.0345 -0.0013 -0.0155 221 LEU A C 1430 O O . LEU A 193 ? 0.4871 0.4233 0.5234 -0.0343 -0.0002 -0.0174 221 LEU A O 1431 C CB . LEU A 193 ? 0.3997 0.3473 0.4380 -0.0363 0.0039 -0.0186 221 LEU A CB 1432 C CG . LEU A 193 ? 0.5526 0.5056 0.5913 -0.0372 0.0057 -0.0191 221 LEU A CG 1433 C CD1 . LEU A 193 ? 0.5455 0.4969 0.5792 -0.0365 0.0055 -0.0194 221 LEU A CD1 1434 C CD2 . LEU A 193 ? 0.5072 0.4586 0.5441 -0.0389 0.0091 -0.0219 221 LEU A CD2 1435 N N . PRO A 194 ? 0.5431 0.4922 0.5893 -0.0344 -0.0041 -0.0126 222 PRO A N 1436 C CA . PRO A 194 ? 0.6229 0.5701 0.6719 -0.0341 -0.0068 -0.0111 222 PRO A CA 1437 C C . PRO A 194 ? 0.7402 0.6838 0.7895 -0.0342 -0.0053 -0.0128 222 PRO A C 1438 O O . PRO A 194 ? 0.8998 0.8377 0.9479 -0.0336 -0.0065 -0.0131 222 PRO A O 1439 C CB . PRO A 194 ? 0.6485 0.6041 0.7044 -0.0347 -0.0091 -0.0078 222 PRO A CB 1440 C CG . PRO A 194 ? 0.6448 0.6070 0.7014 -0.0351 -0.0078 -0.0077 222 PRO A CG 1441 C CD . PRO A 194 ? 0.5981 0.5562 0.6486 -0.0348 -0.0049 -0.0106 222 PRO A CD 1442 N N . VAL A 195 ? 0.6952 0.6428 0.7463 -0.0349 -0.0029 -0.0141 223 VAL A N 1443 C CA . VAL A 195 ? 0.9024 0.8480 0.9540 -0.0350 -0.0009 -0.0162 223 VAL A CA 1444 C C . VAL A 195 ? 0.9285 0.8648 0.9743 -0.0345 0.0001 -0.0185 223 VAL A C 1445 O O . VAL A 195 ? 0.8723 0.8044 0.9182 -0.0336 -0.0019 -0.0179 223 VAL A O 1446 C CB . VAL A 195 ? 1.1223 1.0723 1.1743 -0.0361 0.0024 -0.0181 223 VAL A CB 1447 N N . ALA B 1 ? 0.7758 0.7416 0.6858 -0.0524 0.0116 -0.0704 29 ALA B N 1448 C CA . ALA B 1 ? 0.8738 0.8392 0.7804 -0.0454 0.0104 -0.0701 29 ALA B CA 1449 C C . ALA B 1 ? 0.9430 0.9232 0.8608 -0.0419 0.0102 -0.0667 29 ALA B C 1450 O O . ALA B 1 ? 0.7329 0.7245 0.6575 -0.0428 0.0099 -0.0655 29 ALA B O 1451 C CB . ALA B 1 ? 1.0068 0.9678 0.9041 -0.0433 0.0089 -0.0730 29 ALA B CB 1452 N N . ASN B 2 ? 1.1070 1.0869 1.0264 -0.0381 0.0103 -0.0650 30 ASN B N 1453 C CA . ASN B 2 ? 1.2253 1.2180 1.1537 -0.0343 0.0099 -0.0619 30 ASN B CA 1454 C C . ASN B 2 ? 0.5475 0.5532 0.4881 -0.0376 0.0105 -0.0590 30 ASN B C 1455 O O . ASN B 2 ? 0.6198 0.6246 0.5646 -0.0418 0.0115 -0.0583 30 ASN B O 1456 C CB . ASN B 2 ? 1.5021 1.4975 1.4257 -0.0292 0.0086 -0.0631 30 ASN B CB 1457 C CG . ASN B 2 ? 1.5658 1.5743 1.4971 -0.0251 0.0081 -0.0603 30 ASN B CG 1458 O OD1 . ASN B 2 ? 1.6298 1.6499 1.5706 -0.0268 0.0084 -0.0576 30 ASN B OD1 1459 N ND2 . ASN B 2 ? 1.6083 1.6149 1.5354 -0.0195 0.0074 -0.0608 30 ASN B ND2 1460 N N . PHE B 3 ? 0.5589 0.5766 0.5051 -0.0355 0.0097 -0.0572 31 PHE B N 1461 C CA . PHE B 3 ? 0.4764 0.5053 0.4319 -0.0387 0.0098 -0.0552 31 PHE B CA 1462 C C . PHE B 3 ? 0.5605 0.5911 0.5121 -0.0394 0.0090 -0.0572 31 PHE B C 1463 O O . PHE B 3 ? 0.5878 0.6184 0.5341 -0.0355 0.0082 -0.0583 31 PHE B O 1464 C CB . PHE B 3 ? 0.3861 0.4275 0.3507 -0.0360 0.0094 -0.0515 31 PHE B CB 1465 C CG . PHE B 3 ? 0.4171 0.4584 0.3868 -0.0354 0.0100 -0.0491 31 PHE B CG 1466 C CD1 . PHE B 3 ? 0.3437 0.3753 0.3112 -0.0377 0.0109 -0.0501 31 PHE B CD1 1467 C CD2 . PHE B 3 ? 0.2903 0.3414 0.2670 -0.0327 0.0095 -0.0458 31 PHE B CD2 1468 C CE1 . PHE B 3 ? 0.4374 0.4690 0.4095 -0.0371 0.0113 -0.0480 31 PHE B CE1 1469 C CE2 . PHE B 3 ? 0.4296 0.4804 0.4109 -0.0322 0.0099 -0.0437 31 PHE B CE2 1470 C CZ . PHE B 3 ? 0.4576 0.4987 0.4366 -0.0343 0.0107 -0.0448 31 PHE B CZ 1471 N N . THR B 4 ? 0.5702 0.6030 0.5245 -0.0442 0.0092 -0.0578 32 THR B N 1472 C CA . THR B 4 ? 0.5769 0.6117 0.5277 -0.0451 0.0083 -0.0597 32 THR B CA 1473 C C . THR B 4 ? 0.6060 0.6540 0.5629 -0.0425 0.0074 -0.0572 32 THR B C 1474 O O . THR B 4 ? 0.5548 0.6111 0.5203 -0.0417 0.0075 -0.0538 32 THR B O 1475 C CB . THR B 4 ? 0.5471 0.5809 0.4992 -0.0511 0.0086 -0.0611 32 THR B CB 1476 O OG1 . THR B 4 ? 0.5694 0.6129 0.5327 -0.0533 0.0089 -0.0583 32 THR B OG1 1477 C CG2 . THR B 4 ? 0.4336 0.4542 0.3791 -0.0541 0.0096 -0.0635 32 THR B CG2 1478 N N . CYS B 5 ? 0.5230 0.5725 0.4750 -0.0412 0.0064 -0.0589 33 CYS B N 1479 C CA . CYS B 5 ? 0.4816 0.5434 0.4385 -0.0390 0.0055 -0.0567 33 CYS B CA 1480 C C . CYS B 5 ? 0.5023 0.5646 0.4552 -0.0410 0.0046 -0.0590 33 CYS B C 1481 O O . CYS B 5 ? 0.6339 0.6872 0.5774 -0.0407 0.0043 -0.0624 33 CYS B O 1482 C CB . CYS B 5 ? 0.5631 0.6267 0.5170 -0.0331 0.0054 -0.0561 33 CYS B CB 1483 S SG . CYS B 5 ? 0.6181 0.6974 0.5783 -0.0306 0.0046 -0.0530 33 CYS B SG 1484 N N . ALA B 6 ? 0.4648 0.5373 0.4248 -0.0430 0.0040 -0.0572 34 ALA B N 1485 C CA . ALA B 6 ? 0.4784 0.5518 0.4357 -0.0457 0.0030 -0.0594 34 ALA B CA 1486 C C . ALA B 6 ? 0.5186 0.6015 0.4763 -0.0430 0.0018 -0.0583 34 ALA B C 1487 O O . ALA B 6 ? 0.5815 0.6678 0.5388 -0.0451 0.0008 -0.0594 34 ALA B O 1488 C CB . ALA B 6 ? 0.4480 0.5242 0.4121 -0.0511 0.0030 -0.0589 34 ALA B CB 1489 N N . VAL B 7 ? 0.4392 0.5270 0.3980 -0.0384 0.0020 -0.0562 35 VAL B N 1490 C CA . VAL B 7 ? 0.3885 0.4849 0.3468 -0.0357 0.0012 -0.0554 35 VAL B CA 1491 C C . VAL B 7 ? 0.4487 0.5386 0.3959 -0.0329 0.0007 -0.0591 35 VAL B C 1492 O O . VAL B 7 ? 0.4303 0.5085 0.3702 -0.0331 0.0010 -0.0623 35 VAL B O 1493 C CB . VAL B 7 ? 0.5717 0.6768 0.5355 -0.0322 0.0016 -0.0515 35 VAL B CB 1494 C CG1 . VAL B 7 ? 0.5521 0.6635 0.5264 -0.0348 0.0018 -0.0478 35 VAL B CG1 1495 C CG2 . VAL B 7 ? 0.4816 0.5806 0.4410 -0.0282 0.0025 -0.0524 35 VAL B CG2 1496 N N . ALA B 8 ? 0.4870 0.5842 0.4326 -0.0303 0.0000 -0.0588 36 ALA B N 1497 C CA . ALA B 8 ? 0.6058 0.6976 0.5409 -0.0272 -0.0005 -0.0625 36 ALA B CA 1498 C C . ALA B 8 ? 0.6613 0.7467 0.5914 -0.0226 0.0003 -0.0636 36 ALA B C 1499 O O . ALA B 8 ? 0.5684 0.6594 0.5036 -0.0201 0.0011 -0.0607 36 ALA B O 1500 C CB . ALA B 8 ? 0.5592 0.6612 0.4942 -0.0249 -0.0012 -0.0616 36 ALA B CB 1501 N N . SER B 9 ? 0.6298 0.7033 0.5496 -0.0216 -0.0001 -0.0677 37 SER B N 1502 C CA . SER B 9 ? 0.6511 0.7175 0.5644 -0.0168 0.0003 -0.0694 37 SER B CA 1503 C C . SER B 9 ? 0.6102 0.6866 0.5245 -0.0111 0.0005 -0.0680 37 SER B C 1504 O O . SER B 9 ? 0.6960 0.7798 0.6096 -0.0101 0.0000 -0.0680 37 SER B O 1505 C CB . SER B 9 ? 0.6908 0.7438 0.5917 -0.0164 -0.0006 -0.0742 37 SER B CB 1506 O OG . SER B 9 ? 0.7254 0.7713 0.6191 -0.0110 -0.0006 -0.0761 37 SER B OG 1507 N N . GLY B 10 ? 0.5533 0.6303 0.4694 -0.0075 0.0013 -0.0668 38 GLY B N 1508 C CA . GLY B 10 ? 0.5450 0.6321 0.4627 -0.0023 0.0017 -0.0654 38 GLY B CA 1509 C C . GLY B 10 ? 0.5850 0.6853 0.5141 -0.0035 0.0025 -0.0605 38 GLY B C 1510 O O . GLY B 10 ? 0.4917 0.6013 0.4234 0.0003 0.0030 -0.0587 38 GLY B O 1511 N N . THR B 11 ? 0.4937 0.5952 0.4298 -0.0088 0.0025 -0.0581 39 THR B N 1512 C CA . THR B 11 ? 0.4157 0.5283 0.3623 -0.0102 0.0030 -0.0534 39 THR B CA 1513 C C . THR B 11 ? 0.4415 0.5536 0.3915 -0.0081 0.0039 -0.0517 39 THR B C 1514 O O . THR B 11 ? 0.4563 0.5580 0.4038 -0.0086 0.0041 -0.0533 39 THR B O 1515 C CB . THR B 11 ? 0.5215 0.6344 0.4746 -0.0161 0.0027 -0.0515 39 THR B CB 1516 O OG1 . THR B 11 ? 0.4872 0.6016 0.4378 -0.0183 0.0018 -0.0529 39 THR B OG1 1517 C CG2 . THR B 11 ? 0.3877 0.5110 0.3513 -0.0173 0.0031 -0.0466 39 THR B CG2 1518 N N . THR B 12 ? 0.3538 0.4770 0.3095 -0.0061 0.0044 -0.0485 40 THR B N 1519 C CA . THR B 12 ? 0.4815 0.6053 0.4420 -0.0050 0.0051 -0.0463 40 THR B CA 1520 C C . THR B 12 ? 0.4039 0.5370 0.3751 -0.0083 0.0052 -0.0414 40 THR B C 1521 O O . THR B 12 ? 0.4758 0.6182 0.4506 -0.0095 0.0050 -0.0391 40 THR B O 1522 C CB . THR B 12 ? 0.4430 0.5704 0.4006 0.0007 0.0055 -0.0472 40 THR B CB 1523 O OG1 . THR B 12 ? 0.4119 0.5533 0.3750 0.0016 0.0059 -0.0439 40 THR B OG1 1524 C CG2 . THR B 12 ? 0.4201 0.5409 0.3671 0.0044 0.0051 -0.0519 40 THR B CG2 1525 N N . CYS B 13 ? 0.3323 0.4621 0.3082 -0.0097 0.0055 -0.0397 41 CYS B N 1526 C CA . CYS B 13 ? 0.4814 0.6194 0.4669 -0.0121 0.0056 -0.0350 41 CYS B CA 1527 C C . CYS B 13 ? 0.5330 0.6689 0.5216 -0.0110 0.0061 -0.0338 41 CYS B C 1528 O O . CYS B 13 ? 0.5458 0.6738 0.5292 -0.0084 0.0063 -0.0365 41 CYS B O 1529 C CB . CYS B 13 ? 0.2830 0.4193 0.2728 -0.0172 0.0051 -0.0339 41 CYS B CB 1530 S SG . CYS B 13 ? 0.4504 0.5729 0.4384 -0.0196 0.0053 -0.0364 41 CYS B SG 1531 N N . LYS B 14 ? 0.5069 0.6494 0.5037 -0.0129 0.0060 -0.0296 42 LYS B N 1532 C CA . LYS B 14 ? 0.4896 0.6304 0.4900 -0.0123 0.0063 -0.0281 42 LYS B CA 1533 C C . LYS B 14 ? 0.4489 0.5801 0.4507 -0.0154 0.0063 -0.0286 42 LYS B C 1534 O O . LYS B 14 ? 0.4447 0.5763 0.4503 -0.0191 0.0059 -0.0273 42 LYS B O 1535 C CB . LYS B 14 ? 0.5865 0.7381 0.5947 -0.0131 0.0062 -0.0234 42 LYS B CB 1536 C CG . LYS B 14 ? 0.7684 0.9185 0.7799 -0.0123 0.0064 -0.0221 42 LYS B CG 1537 C CD . LYS B 14 ? 0.8493 1.0101 0.8680 -0.0131 0.0063 -0.0175 42 LYS B CD 1538 C CE . LYS B 14 ? 0.8909 1.0482 0.9148 -0.0147 0.0060 -0.0155 42 LYS B CE 1539 N NZ . LYS B 14 ? 0.9693 1.1327 1.0007 -0.0182 0.0054 -0.0109 42 LYS B NZ 1540 N N . SER B 15 ? 0.3555 0.4782 0.3541 -0.0137 0.0065 -0.0305 43 SER B N 1541 C CA . SER B 15 ? 0.3184 0.4322 0.3183 -0.0164 0.0067 -0.0308 43 SER B CA 1542 C C . SER B 15 ? 0.3828 0.4953 0.3851 -0.0147 0.0068 -0.0295 43 SER B C 1543 O O . SER B 15 ? 0.3871 0.5060 0.3902 -0.0116 0.0067 -0.0285 43 SER B O 1544 C CB . SER B 15 ? 0.4235 0.5253 0.4151 -0.0165 0.0069 -0.0351 43 SER B CB 1545 O OG . SER B 15 ? 0.5250 0.6270 0.5145 -0.0186 0.0067 -0.0365 43 SER B OG 1546 N N . ALA B 16 ? 0.3932 0.4975 0.3963 -0.0167 0.0070 -0.0298 44 ALA B N 1547 C CA . ALA B 16 ? 0.3550 0.4566 0.3596 -0.0151 0.0070 -0.0289 44 ALA B CA 1548 C C . ALA B 16 ? 0.3475 0.4365 0.3485 -0.0164 0.0073 -0.0311 44 ALA B C 1549 O O . ALA B 16 ? 0.3497 0.4337 0.3498 -0.0196 0.0077 -0.0322 44 ALA B O 1550 C CB . ALA B 16 ? 0.3251 0.4352 0.3389 -0.0168 0.0066 -0.0245 44 ALA B CB 1551 N N . ILE B 17 ? 0.3065 0.3909 0.3057 -0.0139 0.0072 -0.0316 45 ILE B N 1552 C CA . ILE B 17 ? 0.3398 0.4132 0.3368 -0.0153 0.0075 -0.0328 45 ILE B CA 1553 C C . ILE B 17 ? 0.4121 0.4889 0.4161 -0.0158 0.0072 -0.0296 45 ILE B C 1554 O O . ILE B 17 ? 0.3552 0.4403 0.3627 -0.0136 0.0067 -0.0276 45 ILE B O 1555 C CB . ILE B 17 ? 0.3685 0.4312 0.3558 -0.0118 0.0074 -0.0364 45 ILE B CB 1556 C CG1 . ILE B 17 ? 0.3191 0.3862 0.3063 -0.0070 0.0067 -0.0359 45 ILE B CG1 1557 C CG2 . ILE B 17 ? 0.3955 0.4537 0.3750 -0.0113 0.0075 -0.0397 45 ILE B CG2 1558 C CD1 . ILE B 17 ? 0.2709 0.3275 0.2488 -0.0032 0.0063 -0.0394 45 ILE B CD1 1559 N N . LEU B 18 ? 0.3833 0.4541 0.3893 -0.0187 0.0076 -0.0292 46 LEU B N 1560 C CA . LEU B 18 ? 0.3980 0.4699 0.4093 -0.0189 0.0072 -0.0267 46 LEU B CA 1561 C C . LEU B 18 ? 0.3651 0.4276 0.3702 -0.0162 0.0071 -0.0289 46 LEU B C 1562 O O . LEU B 18 ? 0.3866 0.4386 0.3872 -0.0175 0.0077 -0.0309 46 LEU B O 1563 C CB . LEU B 18 ? 0.2369 0.3074 0.2536 -0.0230 0.0075 -0.0251 46 LEU B CB 1564 C CG . LEU B 18 ? 0.3376 0.4086 0.3594 -0.0231 0.0070 -0.0226 46 LEU B CG 1565 C CD1 . LEU B 18 ? 0.2616 0.3441 0.2897 -0.0221 0.0060 -0.0191 46 LEU B CD1 1566 C CD2 . LEU B 18 ? 0.2651 0.3322 0.2905 -0.0267 0.0074 -0.0219 46 LEU B CD2 1567 N N . TYR B 19 ? 0.3960 0.4624 0.4008 -0.0124 0.0063 -0.0285 47 TYR B N 1568 C CA . TYR B 19 ? 0.4457 0.5038 0.4439 -0.0090 0.0059 -0.0309 47 TYR B CA 1569 C C . TYR B 19 ? 0.3887 0.4433 0.3895 -0.0092 0.0055 -0.0295 47 TYR B C 1570 O O . TYR B 19 ? 0.4262 0.4888 0.4341 -0.0095 0.0049 -0.0265 47 TYR B O 1571 C CB . TYR B 19 ? 0.3579 0.4223 0.3541 -0.0043 0.0052 -0.0316 47 TYR B CB 1572 C CG . TYR B 19 ? 0.4077 0.4638 0.3965 -0.0001 0.0046 -0.0344 47 TYR B CG 1573 C CD1 . TYR B 19 ? 0.2975 0.3413 0.2768 0.0005 0.0048 -0.0379 47 TYR B CD1 1574 C CD2 . TYR B 19 ? 0.3882 0.4486 0.3790 0.0033 0.0036 -0.0335 47 TYR B CD2 1575 C CE1 . TYR B 19 ? 0.2777 0.3130 0.2494 0.0046 0.0040 -0.0405 47 TYR B CE1 1576 C CE2 . TYR B 19 ? 0.3699 0.4228 0.3537 0.0076 0.0027 -0.0362 47 TYR B CE2 1577 C CZ . TYR B 19 ? 0.4041 0.4441 0.3781 0.0083 0.0029 -0.0397 47 TYR B CZ 1578 O OH . TYR B 19 ? 0.3530 0.3846 0.3194 0.0127 0.0018 -0.0423 47 TYR B OH 1579 N N . THR B 20 ? 0.3527 0.3950 0.3472 -0.0089 0.0057 -0.0318 48 THR B N 1580 C CA . THR B 20 ? 0.3222 0.3600 0.3178 -0.0086 0.0051 -0.0310 48 THR B CA 1581 C C . THR B 20 ? 0.3896 0.4245 0.3800 -0.0036 0.0040 -0.0326 48 THR B C 1582 O O . THR B 20 ? 0.5184 0.5439 0.4999 -0.0014 0.0039 -0.0358 48 THR B O 1583 C CB . THR B 20 ? 0.3607 0.3866 0.3527 -0.0117 0.0061 -0.0323 48 THR B CB 1584 O OG1 . THR B 20 ? 0.5074 0.5361 0.5035 -0.0160 0.0072 -0.0314 48 THR B OG1 1585 C CG2 . THR B 20 ? 0.2718 0.2944 0.2662 -0.0119 0.0056 -0.0309 48 THR B CG2 1586 N N . SER B 21 ? 0.4042 0.4469 0.4001 -0.0018 0.0029 -0.0305 49 SER B N 1587 C CA . SER B 21 ? 0.3778 0.4197 0.3698 0.0032 0.0016 -0.0320 49 SER B CA 1588 C C . SER B 21 ? 0.3322 0.3609 0.3178 0.0044 0.0011 -0.0339 49 SER B C 1589 O O . SER B 21 ? 0.3642 0.3906 0.3531 0.0025 0.0009 -0.0323 49 SER B O 1590 C CB . SER B 21 ? 0.3531 0.4075 0.3531 0.0043 0.0007 -0.0292 49 SER B CB 1591 O OG . SER B 21 ? 0.5407 0.5956 0.5373 0.0094 -0.0006 -0.0308 49 SER B OG 1592 N N . PRO B 22 ? 0.4286 0.4484 0.4046 0.0077 0.0007 -0.0373 50 PRO B N 1593 C CA . PRO B 22 ? 0.3606 0.3669 0.3294 0.0089 0.0001 -0.0391 50 PRO B CA 1594 C C . PRO B 22 ? 0.4602 0.4695 0.4323 0.0116 -0.0015 -0.0379 50 PRO B C 1595 O O . PRO B 22 ? 0.5741 0.5748 0.5441 0.0108 -0.0018 -0.0379 50 PRO B O 1596 C CB . PRO B 22 ? 0.3301 0.3286 0.2883 0.0129 -0.0004 -0.0427 50 PRO B CB 1597 C CG . PRO B 22 ? 0.3935 0.3991 0.3528 0.0122 0.0005 -0.0430 50 PRO B CG 1598 C CD . PRO B 22 ? 0.3231 0.3445 0.2939 0.0109 0.0007 -0.0396 50 PRO B CD 1599 N N . ASN B 23 ? 0.5082 0.5298 0.4854 0.0146 -0.0024 -0.0369 51 ASN B N 1600 C CA . ASN B 23 ? 0.5320 0.5577 0.5123 0.0174 -0.0041 -0.0360 51 ASN B CA 1601 C C . ASN B 23 ? 0.5468 0.5882 0.5383 0.0159 -0.0043 -0.0325 51 ASN B C 1602 O O . ASN B 23 ? 0.5517 0.6009 0.5477 0.0134 -0.0031 -0.0310 51 ASN B O 1603 C CB . ASN B 23 ? 0.6273 0.6522 0.6013 0.0239 -0.0056 -0.0389 51 ASN B CB 1604 C CG . ASN B 23 ? 0.8657 0.8742 0.8277 0.0259 -0.0060 -0.0424 51 ASN B CG 1605 O OD1 . ASN B 23 ? 0.9496 0.9469 0.9082 0.0226 -0.0052 -0.0424 51 ASN B OD1 1606 N ND2 . ASN B 23 ? 0.8742 0.8808 0.8294 0.0316 -0.0072 -0.0453 51 ASN B ND2 1607 N N . ALA B 24 ? 0.5939 0.6396 0.5892 0.0175 -0.0058 -0.0313 52 ALA B N 1608 C CA . ALA B 24 ? 0.5427 0.6038 0.5479 0.0166 -0.0061 -0.0283 52 ALA B CA 1609 C C . ALA B 24 ? 0.5725 0.6428 0.5768 0.0206 -0.0062 -0.0297 52 ALA B C 1610 O O . ALA B 24 ? 0.5354 0.6020 0.5335 0.0256 -0.0072 -0.0327 52 ALA B O 1611 C CB . ALA B 24 ? 0.3350 0.3979 0.3439 0.0173 -0.0078 -0.0270 52 ALA B CB 1612 N N . THR B 25 ? 0.4531 0.5356 0.4637 0.0186 -0.0053 -0.0275 53 THR B N 1613 C CA . THR B 25 ? 0.4961 0.5876 0.5057 0.0222 -0.0051 -0.0289 53 THR B CA 1614 C C . THR B 25 ? 0.5161 0.6234 0.5352 0.0195 -0.0046 -0.0253 53 THR B C 1615 O O . THR B 25 ? 0.5926 0.7033 0.6184 0.0161 -0.0050 -0.0222 53 THR B O 1616 C CB . THR B 25 ? 0.4440 0.5288 0.4465 0.0226 -0.0038 -0.0313 53 THR B CB 1617 O OG1 . THR B 25 ? 0.5065 0.6000 0.5077 0.0265 -0.0037 -0.0329 53 THR B OG1 1618 C CG2 . THR B 25 ? 0.4468 0.5319 0.4529 0.0168 -0.0023 -0.0290 53 THR B CG2 1619 N N . THR B 26 ? 0.4140 0.5306 0.4334 0.0211 -0.0038 -0.0257 54 THR B N 1620 C CA . THR B 26 ? 0.3724 0.5036 0.4000 0.0182 -0.0031 -0.0223 54 THR B CA 1621 C C . THR B 26 ? 0.4181 0.5516 0.4440 0.0170 -0.0016 -0.0225 54 THR B C 1622 O O . THR B 26 ? 0.4779 0.6034 0.4963 0.0193 -0.0012 -0.0257 54 THR B O 1623 C CB . THR B 26 ? 0.3998 0.5443 0.4308 0.0218 -0.0038 -0.0223 54 THR B CB 1624 O OG1 . THR B 26 ? 0.4521 0.5982 0.4772 0.0269 -0.0035 -0.0258 54 THR B OG1 1625 C CG2 . THR B 26 ? 0.2377 0.3798 0.2696 0.0238 -0.0056 -0.0228 54 THR B CG2 1626 N N . TYR B 27 ? 0.3570 0.5013 0.3896 0.0134 -0.0009 -0.0191 55 TYR B N 1627 C CA . TYR B 27 ? 0.4292 0.5775 0.4608 0.0123 0.0004 -0.0189 55 TYR B CA 1628 C C . TYR B 27 ? 0.4920 0.6444 0.5183 0.0176 0.0008 -0.0223 55 TYR B C 1629 O O . TYR B 27 ? 0.4594 0.6076 0.4803 0.0185 0.0015 -0.0244 55 TYR B O 1630 C CB . TYR B 27 ? 0.4635 0.6237 0.5031 0.0079 0.0009 -0.0145 55 TYR B CB 1631 C CG . TYR B 27 ? 0.3868 0.5417 0.4306 0.0028 0.0005 -0.0115 55 TYR B CG 1632 C CD1 . TYR B 27 ? 0.4397 0.5872 0.4818 -0.0001 0.0012 -0.0114 55 TYR B CD1 1633 C CD2 . TYR B 27 ? 0.5055 0.6621 0.5546 0.0010 -0.0005 -0.0090 55 TYR B CD2 1634 C CE1 . TYR B 27 ? 0.5054 0.6480 0.5512 -0.0044 0.0008 -0.0090 55 TYR B CE1 1635 C CE2 . TYR B 27 ? 0.3837 0.5347 0.4362 -0.0034 -0.0010 -0.0065 55 TYR B CE2 1636 C CZ . TYR B 27 ? 0.4742 0.6184 0.5251 -0.0059 -0.0003 -0.0065 55 TYR B CZ 1637 O OH . TYR B 27 ? 0.6556 0.7946 0.7098 -0.0099 -0.0007 -0.0043 55 TYR B OH 1638 N N . GLY B 28 ? 0.4546 0.6155 0.4827 0.0212 0.0001 -0.0228 56 GLY B N 1639 C CA . GLY B 28 ? 0.3067 0.4724 0.3303 0.0269 0.0003 -0.0261 56 GLY B CA 1640 C C . GLY B 28 ? 0.3801 0.5318 0.3938 0.0309 -0.0002 -0.0306 56 GLY B C 1641 O O . GLY B 28 ? 0.5095 0.6604 0.5175 0.0337 0.0004 -0.0332 56 GLY B O 1642 N N . ASN B 29 ? 0.3952 0.5352 0.4062 0.0313 -0.0013 -0.0315 57 ASN B N 1643 C CA . ASN B 29 ? 0.4949 0.6200 0.4959 0.0346 -0.0019 -0.0356 57 ASN B CA 1644 C C . ASN B 29 ? 0.5181 0.6347 0.5148 0.0314 -0.0008 -0.0362 57 ASN B C 1645 O O . ASN B 29 ? 0.5117 0.6210 0.5001 0.0343 -0.0007 -0.0396 57 ASN B O 1646 C CB . ASN B 29 ? 0.5311 0.6450 0.5301 0.0349 -0.0032 -0.0361 57 ASN B CB 1647 C CG . ASN B 29 ? 0.5671 0.6875 0.5686 0.0390 -0.0047 -0.0365 57 ASN B CG 1648 O OD1 . ASN B 29 ? 0.5123 0.6440 0.5151 0.0429 -0.0048 -0.0375 57 ASN B OD1 1649 N ND2 . ASN B 29 ? 0.7121 0.8257 0.7144 0.0381 -0.0059 -0.0359 57 ASN B ND2 1650 N N . LEU B 30 ? 0.4829 0.6006 0.4852 0.0255 0.0001 -0.0328 58 LEU B N 1651 C CA . LEU B 30 ? 0.4210 0.5323 0.4205 0.0220 0.0011 -0.0330 58 LEU B CA 1652 C C . LEU B 30 ? 0.4399 0.5587 0.4377 0.0234 0.0019 -0.0340 58 LEU B C 1653 O O . LEU B 30 ? 0.5234 0.6345 0.5142 0.0240 0.0022 -0.0367 58 LEU B O 1654 C CB . LEU B 30 ? 0.3428 0.4565 0.3500 0.0158 0.0016 -0.0290 58 LEU B CB 1655 C CG . LEU B 30 ? 0.4139 0.5180 0.4218 0.0138 0.0010 -0.0283 58 LEU B CG 1656 C CD1 . LEU B 30 ? 0.4191 0.5258 0.4345 0.0079 0.0014 -0.0244 58 LEU B CD1 1657 C CD2 . LEU B 30 ? 0.4929 0.5812 0.4917 0.0148 0.0009 -0.0318 58 LEU B CD2 1658 N N . VAL B 31 ? 0.4391 0.5728 0.4432 0.0237 0.0022 -0.0318 59 VAL B N 1659 C CA . VAL B 31 ? 0.5432 0.6856 0.5459 0.0255 0.0030 -0.0327 59 VAL B CA 1660 C C . VAL B 31 ? 0.5785 0.7160 0.5722 0.0317 0.0026 -0.0374 59 VAL B C 1661 O O . VAL B 31 ? 0.6658 0.8001 0.6539 0.0325 0.0030 -0.0396 59 VAL B O 1662 C CB . VAL B 31 ? 0.5151 0.6749 0.5257 0.0254 0.0034 -0.0297 59 VAL B CB 1663 C CG1 . VAL B 31 ? 0.3116 0.4804 0.3194 0.0288 0.0042 -0.0315 59 VAL B CG1 1664 C CG2 . VAL B 31 ? 0.3593 0.5244 0.3781 0.0190 0.0039 -0.0248 59 VAL B CG2 1665 N N . ALA B 32 ? 0.4828 0.6186 0.4746 0.0362 0.0014 -0.0392 60 ALA B N 1666 C CA . ALA B 32 ? 0.4396 0.5705 0.4226 0.0427 0.0007 -0.0438 60 ALA B CA 1667 C C . ALA B 32 ? 0.4521 0.5654 0.4255 0.0427 0.0003 -0.0468 60 ALA B C 1668 O O . ALA B 32 ? 0.5546 0.6640 0.5206 0.0456 0.0003 -0.0500 60 ALA B O 1669 C CB . ALA B 32 ? 0.4268 0.5600 0.4104 0.0475 -0.0007 -0.0450 60 ALA B CB 1670 N N . ARG B 33 ? 0.3077 0.4102 0.2810 0.0393 0.0000 -0.0458 61 ARG B N 1671 C CA . ARG B 33 ? 0.4306 0.5161 0.3949 0.0385 -0.0003 -0.0485 61 ARG B CA 1672 C C . ARG B 33 ? 0.4923 0.5762 0.4546 0.0350 0.0009 -0.0486 61 ARG B C 1673 O O . ARG B 33 ? 0.5213 0.5948 0.4746 0.0363 0.0006 -0.0518 61 ARG B O 1674 C CB . ARG B 33 ? 0.4327 0.5085 0.3983 0.0347 -0.0005 -0.0469 61 ARG B CB 1675 C CG . ARG B 33 ? 0.5385 0.5994 0.4973 0.0314 -0.0001 -0.0484 61 ARG B CG 1676 C CD . ARG B 33 ? 0.6104 0.6613 0.5697 0.0279 -0.0002 -0.0473 61 ARG B CD 1677 N NE . ARG B 33 ? 0.6658 0.7150 0.6247 0.0316 -0.0015 -0.0477 61 ARG B NE 1678 C CZ . ARG B 33 ? 0.7127 0.7563 0.6736 0.0295 -0.0018 -0.0463 61 ARG B CZ 1679 N NH1 . ARG B 33 ? 0.5640 0.6032 0.5276 0.0237 -0.0008 -0.0444 61 ARG B NH1 1680 N NH2 . ARG B 33 ? 0.7624 0.8051 0.7226 0.0333 -0.0033 -0.0468 61 ARG B NH2 1681 N N . PHE B 34 ? 0.5006 0.5947 0.4713 0.0304 0.0020 -0.0451 62 PHE B N 1682 C CA . PHE B 34 ? 0.4736 0.5663 0.4429 0.0268 0.0029 -0.0450 62 PHE B CA 1683 C C . PHE B 34 ? 0.5173 0.6202 0.4857 0.0297 0.0033 -0.0460 62 PHE B C 1684 O O . PHE B 34 ? 0.4073 0.5050 0.3689 0.0303 0.0034 -0.0486 62 PHE B O 1685 C CB . PHE B 34 ? 0.3320 0.4274 0.3094 0.0203 0.0037 -0.0411 62 PHE B CB 1686 C CG . PHE B 34 ? 0.4393 0.5211 0.4145 0.0171 0.0036 -0.0414 62 PHE B CG 1687 C CD1 . PHE B 34 ? 0.3100 0.3816 0.2795 0.0145 0.0040 -0.0433 62 PHE B CD1 1688 C CD2 . PHE B 34 ? 0.4135 0.4930 0.3920 0.0167 0.0031 -0.0399 62 PHE B CD2 1689 C CE1 . PHE B 34 ? 0.3661 0.4257 0.3334 0.0114 0.0041 -0.0437 62 PHE B CE1 1690 C CE2 . PHE B 34 ? 0.3998 0.4669 0.3759 0.0139 0.0031 -0.0403 62 PHE B CE2 1691 C CZ . PHE B 34 ? 0.3846 0.4419 0.3552 0.0112 0.0037 -0.0422 62 PHE B CZ 1692 N N . ASN B 35 ? 0.3900 0.5074 0.3649 0.0313 0.0035 -0.0440 63 ASN B N 1693 C CA . ASN B 35 ? 0.4720 0.6003 0.4463 0.0344 0.0040 -0.0448 63 ASN B CA 1694 C C . ASN B 35 ? 0.3916 0.5215 0.3655 0.0308 0.0048 -0.0442 63 ASN B C 1695 O O . ASN B 35 ? 0.4210 0.5530 0.3899 0.0336 0.0050 -0.0465 63 ASN B O 1696 C CB . ASN B 35 ? 0.4880 0.6115 0.4533 0.0413 0.0031 -0.0496 63 ASN B CB 1697 C CG . ASN B 35 ? 0.6356 0.7731 0.6019 0.0456 0.0035 -0.0502 63 ASN B CG 1698 O OD1 . ASN B 35 ? 0.7134 0.8652 0.6882 0.0442 0.0043 -0.0470 63 ASN B OD1 1699 N ND2 . ASN B 35 ? 0.7287 0.8623 0.6863 0.0508 0.0031 -0.0544 63 ASN B ND2 1700 N N . THR B 36 ? 0.3387 0.4673 0.3177 0.0248 0.0053 -0.0411 64 THR B N 1701 C CA . THR B 36 ? 0.4434 0.5730 0.4228 0.0208 0.0059 -0.0403 64 THR B CA 1702 C C . THR B 36 ? 0.4704 0.6139 0.4592 0.0173 0.0065 -0.0357 64 THR B C 1703 O O . THR B 36 ? 0.4620 0.6084 0.4521 0.0142 0.0069 -0.0345 64 THR B O 1704 C CB . THR B 36 ? 0.4205 0.5379 0.3988 0.0161 0.0058 -0.0402 64 THR B CB 1705 O OG1 . THR B 36 ? 0.4684 0.5860 0.4535 0.0133 0.0057 -0.0372 64 THR B OG1 1706 C CG2 . THR B 36 ? 0.3210 0.4230 0.2893 0.0182 0.0052 -0.0446 64 THR B CG2 1707 N N . THR B 37 ? 0.4877 0.6393 0.4828 0.0178 0.0065 -0.0331 65 THR B N 1708 C CA . THR B 37 ? 0.4594 0.6225 0.4636 0.0139 0.0069 -0.0284 65 THR B CA 1709 C C . THR B 37 ? 0.4736 0.6478 0.4825 0.0162 0.0070 -0.0268 65 THR B C 1710 O O . THR B 37 ? 0.6024 0.7740 0.6089 0.0202 0.0065 -0.0290 65 THR B O 1711 C CB . THR B 37 ? 0.5591 0.7161 0.5680 0.0088 0.0066 -0.0257 65 THR B CB 1712 O OG1 . THR B 37 ? 0.5523 0.7199 0.5695 0.0053 0.0067 -0.0210 65 THR B OG1 1713 C CG2 . THR B 37 ? 0.5240 0.6733 0.5325 0.0103 0.0059 -0.0266 65 THR B CG2 1714 N N . THR B 38 ? 0.4052 0.5919 0.4208 0.0136 0.0075 -0.0229 66 THR B N 1715 C CA . THR B 38 ? 0.3030 0.5010 0.3237 0.0150 0.0076 -0.0211 66 THR B CA 1716 C C . THR B 38 ? 0.3984 0.5942 0.4253 0.0116 0.0069 -0.0180 66 THR B C 1717 O O . THR B 38 ? 0.3774 0.5656 0.4057 0.0077 0.0065 -0.0165 66 THR B O 1718 C CB . THR B 38 ? 0.5265 0.7396 0.5511 0.0136 0.0086 -0.0183 66 THR B CB 1719 O OG1 . THR B 38 ? 0.4589 0.6732 0.4885 0.0077 0.0086 -0.0141 66 THR B OG1 1720 C CG2 . THR B 38 ? 0.4192 0.6340 0.4374 0.0167 0.0093 -0.0213 66 THR B CG2 1721 N N . LEU B 39 ? 0.3796 0.5821 0.4102 0.0132 0.0066 -0.0171 67 LEU B N 1722 C CA . LEU B 39 ? 0.4501 0.6511 0.4868 0.0098 0.0058 -0.0140 67 LEU B CA 1723 C C . LEU B 39 ? 0.5441 0.7494 0.5869 0.0037 0.0059 -0.0092 67 LEU B C 1724 O O . LEU B 39 ? 0.6371 0.8344 0.6819 0.0004 0.0053 -0.0077 67 LEU B O 1725 C CB . LEU B 39 ? 0.3781 0.5870 0.4183 0.0122 0.0054 -0.0137 67 LEU B CB 1726 C CG . LEU B 39 ? 0.4360 0.6432 0.4825 0.0081 0.0044 -0.0102 67 LEU B CG 1727 C CD1 . LEU B 39 ? 0.4470 0.6383 0.4900 0.0081 0.0036 -0.0121 67 LEU B CD1 1728 C CD2 . LEU B 39 ? 0.5381 0.7552 0.5892 0.0094 0.0040 -0.0092 67 LEU B CD2 1729 N N . PRO B 40 ? 0.5684 0.7862 0.6139 0.0024 0.0067 -0.0068 68 PRO B N 1730 C CA . PRO B 40 ? 0.5272 0.7475 0.5779 -0.0033 0.0066 -0.0022 68 PRO B CA 1731 C C . PRO B 40 ? 0.5169 0.7275 0.5651 -0.0056 0.0064 -0.0025 68 PRO B C 1732 O O . PRO B 40 ? 0.5395 0.7470 0.5917 -0.0098 0.0057 0.0005 68 PRO B O 1733 C CB . PRO B 40 ? 0.4823 0.7171 0.5348 -0.0039 0.0076 -0.0001 68 PRO B CB 1734 C CG . PRO B 40 ? 0.5008 0.7413 0.5497 0.0015 0.0084 -0.0036 68 PRO B CG 1735 C CD . PRO B 40 ? 0.4921 0.7224 0.5371 0.0056 0.0077 -0.0077 68 PRO B CD 1736 N N . ASP B 41 ? 0.4658 0.6715 0.5076 -0.0029 0.0068 -0.0063 69 ASP B N 1737 C CA . ASP B 41 ? 0.3579 0.5546 0.3974 -0.0052 0.0066 -0.0069 69 ASP B CA 1738 C C . ASP B 41 ? 0.4859 0.6697 0.5249 -0.0060 0.0059 -0.0081 69 ASP B C 1739 O O . ASP B 41 ? 0.4300 0.6083 0.4707 -0.0095 0.0055 -0.0067 69 ASP B O 1740 C CB . ASP B 41 ? 0.4538 0.6489 0.4864 -0.0024 0.0073 -0.0105 69 ASP B CB 1741 C CG . ASP B 41 ? 0.6320 0.8391 0.6653 -0.0027 0.0080 -0.0089 69 ASP B CG 1742 O OD1 . ASP B 41 ? 0.6662 0.8813 0.7052 -0.0061 0.0079 -0.0046 69 ASP B OD1 1743 O OD2 . ASP B 41 ? 0.6397 0.8477 0.6673 0.0003 0.0086 -0.0119 69 ASP B OD2 1744 N N . LEU B 42 ? 0.4982 0.6772 0.5347 -0.0027 0.0057 -0.0106 70 LEU B N 1745 C CA . LEU B 42 ? 0.4580 0.6252 0.4939 -0.0034 0.0051 -0.0116 70 LEU B CA 1746 C C . LEU B 42 ? 0.4851 0.6543 0.5284 -0.0075 0.0044 -0.0073 70 LEU B C 1747 O O . LEU B 42 ? 0.5085 0.6703 0.5530 -0.0104 0.0040 -0.0066 70 LEU B O 1748 C CB . LEU B 42 ? 0.3567 0.5193 0.3884 0.0011 0.0048 -0.0148 70 LEU B CB 1749 C CG . LEU B 42 ? 0.4046 0.5546 0.4345 0.0011 0.0042 -0.0162 70 LEU B CG 1750 C CD1 . LEU B 42 ? 0.2926 0.4311 0.3185 -0.0010 0.0044 -0.0179 70 LEU B CD1 1751 C CD2 . LEU B 42 ? 0.4917 0.6381 0.5165 0.0063 0.0037 -0.0196 70 LEU B CD2 1752 N N . LEU B 43 ? 0.5185 0.6981 0.5667 -0.0077 0.0042 -0.0046 71 LEU B N 1753 C CA . LEU B 43 ? 0.5147 0.6967 0.5696 -0.0117 0.0034 -0.0003 71 LEU B CA 1754 C C . LEU B 43 ? 0.4221 0.6039 0.4797 -0.0159 0.0032 0.0025 71 LEU B C 1755 O O . LEU B 43 ? 0.4807 0.6570 0.5413 -0.0189 0.0024 0.0043 71 LEU B O 1756 C CB . LEU B 43 ? 0.4818 0.6763 0.5411 -0.0117 0.0033 0.0023 71 LEU B CB 1757 C CG . LEU B 43 ? 0.5911 0.7878 0.6492 -0.0075 0.0032 0.0000 71 LEU B CG 1758 C CD1 . LEU B 43 ? 0.5556 0.7666 0.6182 -0.0078 0.0034 0.0025 71 LEU B CD1 1759 C CD2 . LEU B 43 ? 0.6175 0.8049 0.6765 -0.0077 0.0021 -0.0004 71 LEU B CD2 1760 N N . GLY B 44 ? 0.3755 0.5632 0.4317 -0.0161 0.0038 0.0027 72 GLY B N 1761 C CA . GLY B 44 ? 0.4752 0.6631 0.5334 -0.0198 0.0035 0.0052 72 GLY B CA 1762 C C . GLY B 44 ? 0.4945 0.6711 0.5507 -0.0208 0.0033 0.0032 72 GLY B C 1763 O O . GLY B 44 ? 0.5312 0.7049 0.5909 -0.0240 0.0025 0.0055 72 GLY B O 1764 N N . ALA B 45 ? 0.5250 0.6951 0.5754 -0.0180 0.0040 -0.0011 73 ALA B N 1765 C CA . ALA B 45 ? 0.4626 0.6220 0.5105 -0.0191 0.0039 -0.0032 73 ALA B CA 1766 C C . ALA B 45 ? 0.4448 0.5967 0.4955 -0.0207 0.0033 -0.0025 73 ALA B C 1767 O O . ALA B 45 ? 0.5235 0.6688 0.5745 -0.0228 0.0032 -0.0029 73 ALA B O 1768 C CB . ALA B 45 ? 0.3068 0.4600 0.3473 -0.0159 0.0047 -0.0080 73 ALA B CB 1769 N N . ASN B 46 ? 0.4798 0.6332 0.5326 -0.0197 0.0030 -0.0014 74 ASN B N 1770 C CA . ASN B 46 ? 0.5875 0.7339 0.6428 -0.0211 0.0023 -0.0007 74 ASN B CA 1771 C C . ASN B 46 ? 0.6726 0.8243 0.7346 -0.0240 0.0012 0.0038 74 ASN B C 1772 O O . ASN B 46 ? 0.6782 0.8257 0.7425 -0.0246 0.0005 0.0046 74 ASN B O 1773 C CB . ASN B 46 ? 0.5458 0.6875 0.5977 -0.0178 0.0024 -0.0033 74 ASN B CB 1774 C CG . ASN B 46 ? 0.5305 0.6637 0.5752 -0.0154 0.0032 -0.0078 74 ASN B CG 1775 O OD1 . ASN B 46 ? 0.5801 0.7031 0.6225 -0.0162 0.0033 -0.0095 74 ASN B OD1 1776 N ND2 . ASN B 46 ? 0.3935 0.5307 0.4341 -0.0126 0.0037 -0.0097 74 ASN B ND2 1777 N N . GLY B 47 ? 0.6269 0.7875 0.6918 -0.0257 0.0010 0.0067 75 GLY B N 1778 C CA . GLY B 47 ? 0.5918 0.7568 0.6625 -0.0289 -0.0001 0.0113 75 GLY B CA 1779 C C . GLY B 47 ? 0.6494 0.8176 0.7229 -0.0286 -0.0007 0.0129 75 GLY B C 1780 O O . GLY B 47 ? 0.5818 0.7486 0.6593 -0.0311 -0.0019 0.0157 75 GLY B O 1781 N N . LEU B 48 ? 0.6426 0.8152 0.7138 -0.0256 0.0000 0.0111 76 LEU B N 1782 C CA . LEU B 48 ? 0.5212 0.6972 0.5948 -0.0249 -0.0006 0.0120 76 LEU B CA 1783 C C . LEU B 48 ? 0.5261 0.7150 0.6029 -0.0260 -0.0006 0.0151 76 LEU B C 1784 O O . LEU B 48 ? 0.5660 0.7615 0.6415 -0.0256 0.0003 0.0152 76 LEU B O 1785 C CB . LEU B 48 ? 0.5873 0.7596 0.6563 -0.0204 0.0000 0.0077 76 LEU B CB 1786 C CG . LEU B 48 ? 0.6462 0.8051 0.7114 -0.0194 0.0000 0.0046 76 LEU B CG 1787 C CD1 . LEU B 48 ? 0.6200 0.7756 0.6792 -0.0148 0.0007 0.0003 76 LEU B CD1 1788 C CD2 . LEU B 48 ? 0.5867 0.7400 0.6551 -0.0211 -0.0012 0.0061 76 LEU B CD2 1789 N N . PRO B 49 ? 0.5427 0.7352 0.6237 -0.0275 -0.0015 0.0177 77 PRO B N 1790 C CA . PRO B 49 ? 0.5655 0.7707 0.6497 -0.0292 -0.0014 0.0209 77 PRO B CA 1791 C C . PRO B 49 ? 0.7293 0.9427 0.8109 -0.0254 0.0000 0.0183 77 PRO B C 1792 O O . PRO B 49 ? 0.8181 1.0285 0.8968 -0.0214 0.0003 0.0146 77 PRO B O 1793 C CB . PRO B 49 ? 0.5508 0.7571 0.6394 -0.0312 -0.0027 0.0233 77 PRO B CB 1794 C CG . PRO B 49 ? 0.4949 0.6887 0.5828 -0.0309 -0.0037 0.0218 77 PRO B CG 1795 C CD . PRO B 49 ? 0.6022 0.7876 0.6851 -0.0282 -0.0027 0.0179 77 PRO B CD 1796 N N . ASP B 50 ? 0.6239 0.8477 0.7063 -0.0267 0.0007 0.0204 78 ASP B N 1797 C CA . ASP B 50 ? 0.5695 0.8027 0.6497 -0.0233 0.0022 0.0183 78 ASP B CA 1798 C C . ASP B 50 ? 0.6091 0.8482 0.6909 -0.0209 0.0021 0.0172 78 ASP B C 1799 O O . ASP B 50 ? 0.6352 0.8781 0.7140 -0.0164 0.0031 0.0137 78 ASP B O 1800 C CB . ASP B 50 ? 0.6056 0.8491 0.6871 -0.0262 0.0028 0.0216 78 ASP B CB 1801 C CG . ASP B 50 ? 0.7584 0.9959 0.8379 -0.0280 0.0027 0.0223 78 ASP B CG 1802 O OD1 . ASP B 50 ? 0.7735 1.0009 0.8537 -0.0297 0.0015 0.0228 78 ASP B OD1 1803 O OD2 . ASP B 50 ? 0.8945 1.1378 0.9719 -0.0277 0.0037 0.0223 78 ASP B OD2 1804 N N . GLY B 51 ? 0.6483 0.8882 0.7348 -0.0237 0.0009 0.0199 79 GLY B N 1805 C CA . GLY B 51 ? 0.5438 0.7899 0.6326 -0.0218 0.0006 0.0191 79 GLY B CA 1806 C C . GLY B 51 ? 0.5048 0.7409 0.5907 -0.0177 0.0000 0.0151 79 GLY B C 1807 O O . GLY B 51 ? 0.5135 0.7527 0.6011 -0.0160 -0.0007 0.0142 79 GLY B O 1808 N N . THR B 52 ? 0.5999 0.8239 0.6813 -0.0164 0.0000 0.0127 80 THR B N 1809 C CA . THR B 52 ? 0.5574 0.7710 0.6351 -0.0127 -0.0005 0.0088 80 THR B CA 1810 C C . THR B 52 ? 0.5141 0.7329 0.5884 -0.0071 0.0002 0.0050 80 THR B C 1811 O O . THR B 52 ? 0.5955 0.8187 0.6668 -0.0053 0.0015 0.0037 80 THR B O 1812 C CB . THR B 52 ? 0.5846 0.7848 0.6580 -0.0128 -0.0004 0.0071 80 THR B CB 1813 O OG1 . THR B 52 ? 0.5919 0.7884 0.6688 -0.0177 -0.0011 0.0106 80 THR B OG1 1814 C CG2 . THR B 52 ? 0.5750 0.7639 0.6443 -0.0094 -0.0010 0.0034 80 THR B CG2 1815 N N . LEU B 53 ? 0.4402 0.6587 0.5147 -0.0043 -0.0007 0.0033 81 LEU B N 1816 C CA . LEU B 53 ? 0.5243 0.7476 0.5956 0.0015 -0.0003 -0.0005 81 LEU B CA 1817 C C . LEU B 53 ? 0.5470 0.7576 0.6105 0.0057 -0.0002 -0.0049 81 LEU B C 1818 O O . LEU B 53 ? 0.4429 0.6407 0.5043 0.0044 -0.0008 -0.0053 81 LEU B O 1819 C CB . LEU B 53 ? 0.5286 0.7572 0.6034 0.0031 -0.0015 -0.0006 81 LEU B CB 1820 C CG . LEU B 53 ? 0.5987 0.8408 0.6812 -0.0011 -0.0017 0.0036 81 LEU B CG 1821 C CD1 . LEU B 53 ? 0.6361 0.8821 0.7217 0.0005 -0.0031 0.0031 81 LEU B CD1 1822 C CD2 . LEU B 53 ? 0.5731 0.8295 0.6567 -0.0009 0.0000 0.0044 81 LEU B CD2 1823 N N . SER B 54 ? 0.5592 0.7733 0.6183 0.0108 0.0005 -0.0084 82 SER B N 1824 C CA . SER B 54 ? 0.5630 0.7648 0.6139 0.0149 0.0004 -0.0128 82 SER B CA 1825 C C . SER B 54 ? 0.5381 0.7300 0.5868 0.0174 -0.0012 -0.0148 82 SER B C 1826 O O . SER B 54 ? 0.4863 0.6650 0.5282 0.0195 -0.0014 -0.0178 82 SER B O 1827 C CB . SER B 54 ? 0.4078 0.6160 0.4543 0.0201 0.0013 -0.0161 82 SER B CB 1828 O OG . SER B 54 ? 0.5521 0.7644 0.5982 0.0252 0.0004 -0.0185 82 SER B OG 1829 N N . SER B 55 ? 0.4638 0.6618 0.5178 0.0169 -0.0022 -0.0132 83 SER B N 1830 C CA . SER B 55 ? 0.5099 0.6995 0.5622 0.0192 -0.0039 -0.0149 83 SER B CA 1831 C C . SER B 55 ? 0.5286 0.7083 0.5829 0.0144 -0.0046 -0.0125 83 SER B C 1832 O O . SER B 55 ? 0.4588 0.6297 0.5112 0.0157 -0.0059 -0.0137 83 SER B O 1833 C CB . SER B 55 ? 0.4895 0.6908 0.5464 0.0214 -0.0049 -0.0148 83 SER B CB 1834 O OG . SER B 55 ? 0.6102 0.8213 0.6753 0.0161 -0.0048 -0.0102 83 SER B OG 1835 N N . ALA B 56 ? 0.5230 0.7038 0.5808 0.0091 -0.0037 -0.0092 84 ALA B N 1836 C CA . ALA B 56 ? 0.5224 0.6942 0.5821 0.0046 -0.0043 -0.0069 84 ALA B CA 1837 C C . ALA B 56 ? 0.6243 0.7800 0.6771 0.0060 -0.0043 -0.0099 84 ALA B C 1838 O O . ALA B 56 ? 0.5928 0.7442 0.6400 0.0079 -0.0033 -0.0123 84 ALA B O 1839 C CB . ALA B 56 ? 0.4693 0.6454 0.5332 -0.0006 -0.0034 -0.0032 84 ALA B CB 1840 N N . PRO B 57 ? 0.6614 0.8081 0.7143 0.0049 -0.0054 -0.0096 85 PRO B N 1841 C CA . PRO B 57 ? 0.5956 0.7269 0.6414 0.0064 -0.0055 -0.0126 85 PRO B CA 1842 C C . PRO B 57 ? 0.6095 0.7330 0.6540 0.0028 -0.0043 -0.0120 85 PRO B C 1843 O O . PRO B 57 ? 0.6629 0.7896 0.7128 -0.0016 -0.0041 -0.0087 85 PRO B O 1844 C CB . PRO B 57 ? 0.5167 0.6431 0.5643 0.0058 -0.0071 -0.0118 85 PRO B CB 1845 C CG . PRO B 57 ? 0.5504 0.6862 0.6065 0.0014 -0.0075 -0.0075 85 PRO B CG 1846 C CD . PRO B 57 ? 0.5840 0.7342 0.6433 0.0019 -0.0067 -0.0065 85 PRO B CD 1847 N N . VAL B 58 ? 0.5678 0.6810 0.6048 0.0047 -0.0036 -0.0153 86 VAL B N 1848 C CA . VAL B 58 ? 0.5057 0.6094 0.5407 0.0015 -0.0027 -0.0154 86 VAL B CA 1849 C C . VAL B 58 ? 0.5303 0.6202 0.5594 0.0029 -0.0032 -0.0178 86 VAL B C 1850 O O . VAL B 58 ? 0.6349 0.7203 0.6579 0.0072 -0.0037 -0.0209 86 VAL B O 1851 C CB . VAL B 58 ? 0.5315 0.6353 0.5629 0.0015 -0.0013 -0.0168 86 VAL B CB 1852 C CG1 . VAL B 58 ? 0.5399 0.6551 0.5717 0.0046 -0.0012 -0.0173 86 VAL B CG1 1853 C CG2 . VAL B 58 ? 0.5200 0.6099 0.5427 0.0029 -0.0008 -0.0205 86 VAL B CG2 1854 N N . ALA B 59 ? 0.3988 0.4825 0.4300 -0.0006 -0.0033 -0.0163 87 ALA B N 1855 C CA . ALA B 59 ? 0.4444 0.5154 0.4706 0.0003 -0.0038 -0.0182 87 ALA B CA 1856 C C . ALA B 59 ? 0.4980 0.5576 0.5158 0.0009 -0.0026 -0.0215 87 ALA B C 1857 O O . ALA B 59 ? 0.3968 0.4571 0.4140 -0.0008 -0.0013 -0.0218 87 ALA B O 1858 C CB . ALA B 59 ? 0.4533 0.5216 0.4844 -0.0037 -0.0041 -0.0157 87 ALA B CB 1859 N N . ALA B 60 ? 0.5335 0.5822 0.5446 0.0032 -0.0031 -0.0240 88 ALA B N 1860 C CA . ALA B 60 ? 0.4841 0.5199 0.4869 0.0029 -0.0021 -0.0268 88 ALA B CA 1861 C C . ALA B 60 ? 0.4984 0.5312 0.5042 -0.0023 -0.0007 -0.0254 88 ALA B C 1862 O O . ALA B 60 ? 0.4348 0.4695 0.4465 -0.0049 -0.0010 -0.0229 88 ALA B O 1863 C CB . ALA B 60 ? 0.5087 0.5332 0.5048 0.0054 -0.0031 -0.0289 88 ALA B CB 1864 N N . ASN B 61 ? 0.4674 0.4956 0.4689 -0.0036 0.0007 -0.0271 89 ASN B N 1865 C CA . ASN B 61 ? 0.4500 0.4753 0.4535 -0.0083 0.0022 -0.0264 89 ASN B CA 1866 C C . ASN B 61 ? 0.4506 0.4871 0.4627 -0.0111 0.0025 -0.0235 89 ASN B C 1867 O O . ASN B 61 ? 0.5194 0.5546 0.5335 -0.0146 0.0036 -0.0230 89 ASN B O 1868 C CB . ASN B 61 ? 0.4642 0.4808 0.4673 -0.0102 0.0023 -0.0261 89 ASN B CB 1869 C CG . ASN B 61 ? 0.4430 0.4471 0.4367 -0.0079 0.0021 -0.0290 89 ASN B CG 1870 O OD1 . ASN B 61 ? 0.3866 0.3822 0.3733 -0.0086 0.0032 -0.0314 89 ASN B OD1 1871 N ND2 . ASN B 61 ? 0.4151 0.4179 0.4083 -0.0052 0.0005 -0.0288 89 ASN B ND2 1872 N N . SER B 62 ? 0.4581 0.5058 0.4752 -0.0096 0.0015 -0.0215 90 SER B N 1873 C CA . SER B 62 ? 0.4378 0.4961 0.4625 -0.0122 0.0017 -0.0186 90 SER B CA 1874 C C . SER B 62 ? 0.4865 0.5475 0.5083 -0.0119 0.0027 -0.0201 90 SER B C 1875 O O . SER B 62 ? 0.4176 0.4751 0.4328 -0.0089 0.0028 -0.0229 90 SER B O 1876 C CB . SER B 62 ? 0.4522 0.5214 0.4831 -0.0112 0.0004 -0.0158 90 SER B CB 1877 O OG . SER B 62 ? 0.5156 0.5912 0.5444 -0.0079 0.0002 -0.0168 90 SER B OG 1878 N N . THR B 63 ? 0.4757 0.5429 0.5024 -0.0148 0.0032 -0.0182 91 THR B N 1879 C CA . THR B 63 ? 0.3856 0.4552 0.4098 -0.0149 0.0040 -0.0196 91 THR B CA 1880 C C . THR B 63 ? 0.5151 0.5976 0.5435 -0.0140 0.0036 -0.0175 91 THR B C 1881 O O . THR B 63 ? 0.4207 0.5107 0.4557 -0.0151 0.0028 -0.0142 91 THR B O 1882 C CB . THR B 63 ? 0.4233 0.4905 0.4492 -0.0189 0.0049 -0.0194 91 THR B CB 1883 O OG1 . THR B 63 ? 0.4825 0.5566 0.5166 -0.0214 0.0044 -0.0158 91 THR B OG1 1884 C CG2 . THR B 63 ? 0.4095 0.4643 0.4310 -0.0202 0.0057 -0.0216 91 THR B CG2 1885 N N . VAL B 64 ? 0.4578 0.5425 0.4821 -0.0122 0.0040 -0.0193 92 VAL B N 1886 C CA . VAL B 64 ? 0.2905 0.3874 0.3182 -0.0114 0.0038 -0.0176 92 VAL B CA 1887 C C . VAL B 64 ? 0.4046 0.5018 0.4289 -0.0119 0.0046 -0.0193 92 VAL B C 1888 O O . VAL B 64 ? 0.4982 0.5871 0.5153 -0.0107 0.0051 -0.0227 92 VAL B O 1889 C CB . VAL B 64 ? 0.3370 0.4387 0.3628 -0.0070 0.0033 -0.0184 92 VAL B CB 1890 C CG1 . VAL B 64 ? 0.2753 0.3904 0.3051 -0.0066 0.0033 -0.0164 92 VAL B CG1 1891 C CG2 . VAL B 64 ? 0.3809 0.4817 0.4095 -0.0063 0.0023 -0.0172 92 VAL B CG2 1892 N N . LYS B 65 ? 0.3810 0.4872 0.4102 -0.0140 0.0047 -0.0168 93 LYS B N 1893 C CA . LYS B 65 ? 0.3518 0.4600 0.3784 -0.0146 0.0052 -0.0180 93 LYS B CA 1894 C C . LYS B 65 ? 0.3734 0.4863 0.3958 -0.0106 0.0053 -0.0197 93 LYS B C 1895 O O . LYS B 65 ? 0.2985 0.4204 0.3241 -0.0090 0.0049 -0.0179 93 LYS B O 1896 C CB . LYS B 65 ? 0.3788 0.4956 0.4121 -0.0178 0.0050 -0.0145 93 LYS B CB 1897 C CG . LYS B 65 ? 0.5865 0.6994 0.6199 -0.0210 0.0053 -0.0151 93 LYS B CG 1898 C CD . LYS B 65 ? 0.7056 0.8263 0.7460 -0.0239 0.0047 -0.0113 93 LYS B CD 1899 C CE . LYS B 65 ? 0.7400 0.8652 0.7792 -0.0247 0.0048 -0.0118 93 LYS B CE 1900 N NZ . LYS B 65 ? 0.7116 0.8451 0.7571 -0.0271 0.0040 -0.0080 93 LYS B NZ 1901 N N . ILE B 66 ? 0.3724 0.4792 0.3874 -0.0089 0.0057 -0.0234 94 ILE B N 1902 C CA . ILE B 66 ? 0.2686 0.3793 0.2789 -0.0047 0.0057 -0.0254 94 ILE B CA 1903 C C . ILE B 66 ? 0.3244 0.4373 0.3319 -0.0054 0.0061 -0.0265 94 ILE B C 1904 O O . ILE B 66 ? 0.3566 0.4607 0.3588 -0.0064 0.0064 -0.0292 94 ILE B O 1905 C CB . ILE B 66 ? 0.4127 0.5137 0.4153 -0.0008 0.0055 -0.0290 94 ILE B CB 1906 C CG1 . ILE B 66 ? 0.4093 0.5091 0.4151 -0.0001 0.0049 -0.0277 94 ILE B CG1 1907 C CG2 . ILE B 66 ? 0.2537 0.3589 0.2512 0.0040 0.0054 -0.0314 94 ILE B CG2 1908 C CD1 . ILE B 66 ? 0.5369 0.6280 0.5358 0.0039 0.0044 -0.0308 94 ILE B CD1 1909 N N . PRO B 67 ? 0.3997 0.5246 0.4110 -0.0053 0.0062 -0.0244 95 PRO B N 1910 C CA . PRO B 67 ? 0.3879 0.5165 0.3969 -0.0058 0.0065 -0.0252 95 PRO B CA 1911 C C . PRO B 67 ? 0.4627 0.5896 0.4638 -0.0013 0.0066 -0.0289 95 PRO B C 1912 O O . PRO B 67 ? 0.4808 0.6099 0.4806 0.0026 0.0065 -0.0297 95 PRO B O 1913 C CB . PRO B 67 ? 0.3304 0.4726 0.3463 -0.0071 0.0064 -0.0211 95 PRO B CB 1914 C CG . PRO B 67 ? 0.3612 0.5074 0.3822 -0.0065 0.0061 -0.0187 95 PRO B CG 1915 C CD . PRO B 67 ? 0.3861 0.5216 0.4039 -0.0049 0.0059 -0.0210 95 PRO B CD 1916 N N . PHE B 68 ? 0.4123 0.5357 0.4082 -0.0018 0.0067 -0.0313 96 PHE B N 1917 C CA . PHE B 68 ? 0.4435 0.5647 0.4313 0.0023 0.0067 -0.0350 96 PHE B CA 1918 C C . PHE B 68 ? 0.4032 0.5262 0.3888 0.0006 0.0068 -0.0358 96 PHE B C 1919 O O . PHE B 68 ? 0.3503 0.4734 0.3397 -0.0038 0.0068 -0.0341 96 PHE B O 1920 C CB . PHE B 68 ? 0.3166 0.4235 0.2965 0.0042 0.0064 -0.0388 96 PHE B CB 1921 C CG . PHE B 68 ? 0.3222 0.4186 0.3004 -0.0001 0.0065 -0.0397 96 PHE B CG 1922 C CD1 . PHE B 68 ? 0.2757 0.3671 0.2481 -0.0013 0.0065 -0.0423 96 PHE B CD1 1923 C CD2 . PHE B 68 ? 0.4398 0.5319 0.4223 -0.0031 0.0067 -0.0380 96 PHE B CD2 1924 C CE1 . PHE B 68 ? 0.4064 0.4890 0.3776 -0.0055 0.0067 -0.0432 96 PHE B CE1 1925 C CE2 . PHE B 68 ? 0.3889 0.4721 0.3701 -0.0071 0.0069 -0.0389 96 PHE B CE2 1926 C CZ . PHE B 68 ? 0.3878 0.4666 0.3636 -0.0084 0.0070 -0.0414 96 PHE B CZ 1927 N N . ARG B 69 ? 0.4725 0.5963 0.4515 0.0042 0.0068 -0.0387 97 ARG B N 1928 C CA . ARG B 69 ? 0.4304 0.5545 0.4057 0.0030 0.0067 -0.0401 97 ARG B CA 1929 C C . ARG B 69 ? 0.4872 0.5973 0.4556 0.0015 0.0064 -0.0436 97 ARG B C 1930 O O . ARG B 69 ? 0.3871 0.4879 0.3486 0.0044 0.0061 -0.0467 97 ARG B O 1931 C CB . ARG B 69 ? 0.3389 0.4691 0.3094 0.0077 0.0068 -0.0420 97 ARG B CB 1932 C CG . ARG B 69 ? 0.4750 0.6201 0.4516 0.0093 0.0073 -0.0389 97 ARG B CG 1933 C CD . ARG B 69 ? 0.5947 0.7494 0.5786 0.0049 0.0075 -0.0347 97 ARG B CD 1934 N NE . ARG B 69 ? 0.5997 0.7536 0.5803 0.0030 0.0072 -0.0359 97 ARG B NE 1935 C CZ . ARG B 69 ? 0.6060 0.7660 0.5915 -0.0009 0.0071 -0.0329 97 ARG B CZ 1936 N NH1 . ARG B 69 ? 0.4685 0.6272 0.4504 -0.0022 0.0067 -0.0344 97 ARG B NH1 1937 N NH2 . ARG B 69 ? 0.5572 0.7240 0.5510 -0.0034 0.0071 -0.0285 97 ARG B NH2 1938 N N . CYS B 70 ? 0.4639 0.5725 0.4342 -0.0032 0.0063 -0.0429 98 CYS B N 1939 C CA . CYS B 70 ? 0.3889 0.4854 0.3527 -0.0053 0.0061 -0.0462 98 CYS B CA 1940 C C . CYS B 70 ? 0.4651 0.5613 0.4224 -0.0045 0.0057 -0.0489 98 CYS B C 1941 O O . CYS B 70 ? 0.4623 0.5681 0.4229 -0.0054 0.0056 -0.0473 98 CYS B O 1942 C CB . CYS B 70 ? 0.3166 0.4121 0.2864 -0.0109 0.0063 -0.0442 98 CYS B CB 1943 S SG . CYS B 70 ? 0.5197 0.6021 0.4830 -0.0145 0.0062 -0.0478 98 CYS B SG 1944 N N . ARG B 71 ? 0.4784 0.5632 0.4263 -0.0032 0.0053 -0.0530 99 ARG B N 1945 C CA . ARG B 71 ? 0.4622 0.5449 0.4032 -0.0030 0.0048 -0.0558 99 ARG B CA 1946 C C . ARG B 71 ? 0.4205 0.4922 0.3576 -0.0076 0.0045 -0.0580 99 ARG B C 1947 O O . ARG B 71 ? 0.4677 0.5284 0.4012 -0.0083 0.0046 -0.0595 99 ARG B O 1948 C CB . ARG B 71 ? 0.4848 0.5637 0.4166 0.0028 0.0043 -0.0593 99 ARG B CB 1949 C CG . ARG B 71 ? 0.5134 0.5887 0.4374 0.0028 0.0036 -0.0625 99 ARG B CG 1950 C CD . ARG B 71 ? 0.5300 0.6029 0.4451 0.0090 0.0030 -0.0659 99 ARG B CD 1951 N NE . ARG B 71 ? 0.7214 0.7916 0.6294 0.0088 0.0022 -0.0688 99 ARG B NE 1952 C CZ . ARG B 71 ? 0.7722 0.8292 0.6719 0.0068 0.0015 -0.0721 99 ARG B CZ 1953 N NH1 . ARG B 71 ? 0.7502 0.8056 0.6438 0.0066 0.0006 -0.0746 99 ARG B NH1 1954 N NH2 . ARG B 71 ? 0.7845 0.8297 0.6820 0.0047 0.0015 -0.0728 99 ARG B NH2 1955 N N . CYS B 72 ? 0.3790 0.4541 0.3170 -0.0108 0.0042 -0.0581 100 CYS B N 1956 C CA . CYS B 72 ? 0.4777 0.5439 0.4126 -0.0156 0.0040 -0.0600 100 CYS B CA 1957 C C . CYS B 72 ? 0.5132 0.5715 0.4372 -0.0143 0.0031 -0.0643 100 CYS B C 1958 O O . CYS B 72 ? 0.5719 0.6359 0.4935 -0.0116 0.0026 -0.0650 100 CYS B O 1959 C CB . CYS B 72 ? 0.5940 0.6686 0.5370 -0.0203 0.0039 -0.0576 100 CYS B CB 1960 S SG . CYS B 72 ? 0.6033 0.6851 0.5589 -0.0229 0.0047 -0.0529 100 CYS B SG 1961 N N . ASN B 73 ? 0.5832 0.6280 0.5002 -0.0162 0.0030 -0.0672 101 ASN B N 1962 C CA . ASN B 73 ? 0.7096 0.7462 0.6163 -0.0161 0.0020 -0.0711 101 ASN B CA 1963 C C . ASN B 73 ? 0.8029 0.8403 0.7128 -0.0226 0.0019 -0.0710 101 ASN B C 1964 O O . ASN B 73 ? 0.9869 1.0329 0.9070 -0.0256 0.0025 -0.0678 101 ASN B O 1965 C CB . ASN B 73 ? 0.6565 0.6776 0.5524 -0.0139 0.0017 -0.0745 101 ASN B CB 1966 C CG . ASN B 73 ? 0.6349 0.6464 0.5312 -0.0183 0.0024 -0.0743 101 ASN B CG 1967 O OD1 . ASN B 73 ? 0.5836 0.5980 0.4866 -0.0237 0.0031 -0.0727 101 ASN B OD1 1968 N ND2 . ASN B 73 ? 0.5107 0.5108 0.3997 -0.0155 0.0023 -0.0760 101 ASN B ND2 1969 N N . GLY B 74 ? 0.7294 0.7589 0.6314 -0.0248 0.0011 -0.0744 102 GLY B N 1970 C CA . GLY B 74 ? 0.7064 0.7382 0.6123 -0.0310 0.0009 -0.0742 102 GLY B CA 1971 C C . GLY B 74 ? 0.6628 0.6931 0.5754 -0.0360 0.0020 -0.0726 102 GLY B C 1972 O O . GLY B 74 ? 0.6536 0.6898 0.5727 -0.0405 0.0021 -0.0714 102 GLY B O 1973 N N . ASP B 75 ? 0.5826 0.6054 0.4936 -0.0348 0.0029 -0.0724 103 ASP B N 1974 C CA . ASP B 75 ? 0.6961 0.7134 0.6099 -0.0396 0.0040 -0.0719 103 ASP B CA 1975 C C . ASP B 75 ? 0.7239 0.7457 0.6461 -0.0385 0.0051 -0.0686 103 ASP B C 1976 O O . ASP B 75 ? 0.7650 0.7891 0.6942 -0.0426 0.0059 -0.0669 103 ASP B O 1977 C CB . ASP B 75 ? 0.7565 0.7573 0.6587 -0.0402 0.0039 -0.0753 103 ASP B CB 1978 C CG . ASP B 75 ? 0.9004 0.8947 0.7935 -0.0420 0.0027 -0.0789 103 ASP B CG 1979 O OD1 . ASP B 75 ? 0.8884 0.8888 0.7853 -0.0460 0.0024 -0.0790 103 ASP B OD1 1980 O OD2 . ASP B 75 ? 0.8924 0.8753 0.7743 -0.0392 0.0020 -0.0818 103 ASP B OD2 1981 N N . VAL B 76 ? 0.6515 0.6741 0.5724 -0.0330 0.0050 -0.0677 104 VAL B N 1982 C CA . VAL B 76 ? 0.5973 0.6205 0.5233 -0.0316 0.0059 -0.0653 104 VAL B CA 1983 C C . VAL B 76 ? 0.5581 0.5915 0.4883 -0.0261 0.0056 -0.0629 104 VAL B C 1984 O O . VAL B 76 ? 0.5131 0.5494 0.4392 -0.0224 0.0048 -0.0641 104 VAL B O 1985 C CB . VAL B 76 ? 0.6293 0.6373 0.5461 -0.0309 0.0061 -0.0677 104 VAL B CB 1986 C CG1 . VAL B 76 ? 0.4870 0.4909 0.3955 -0.0245 0.0052 -0.0695 104 VAL B CG1 1987 C CG2 . VAL B 76 ? 0.7931 0.8001 0.7150 -0.0315 0.0071 -0.0655 104 VAL B CG2 1988 N N . GLY B 77 ? 0.4291 0.4681 0.3674 -0.0256 0.0062 -0.0597 105 GLY B N 1989 C CA . GLY B 77 ? 0.3124 0.3609 0.2548 -0.0208 0.0061 -0.0574 105 GLY B CA 1990 C C . GLY B 77 ? 0.4676 0.5103 0.4070 -0.0169 0.0062 -0.0576 105 GLY B C 1991 O O . GLY B 77 ? 0.4709 0.5074 0.4115 -0.0189 0.0068 -0.0572 105 GLY B O 1992 N N . GLN B 78 ? 0.4082 0.4533 0.3438 -0.0114 0.0057 -0.0584 106 GLN B N 1993 C CA . GLN B 78 ? 0.4537 0.4937 0.3860 -0.0070 0.0056 -0.0590 106 GLN B CA 1994 C C . GLN B 78 ? 0.4154 0.4677 0.3529 -0.0026 0.0055 -0.0568 106 GLN B C 1995 O O . GLN B 78 ? 0.3807 0.4422 0.3196 -0.0014 0.0053 -0.0564 106 GLN B O 1996 C CB . GLN B 78 ? 0.4342 0.4614 0.3538 -0.0041 0.0048 -0.0634 106 GLN B CB 1997 C CG . GLN B 78 ? 0.4115 0.4253 0.3247 -0.0088 0.0048 -0.0658 106 GLN B CG 1998 C CD . GLN B 78 ? 0.5549 0.5571 0.4549 -0.0064 0.0038 -0.0701 106 GLN B CD 1999 O OE1 . GLN B 78 ? 0.5571 0.5639 0.4542 -0.0031 0.0031 -0.0714 106 GLN B OE1 2000 N NE2 . GLN B 78 ? 0.4650 0.4522 0.3569 -0.0081 0.0036 -0.0724 106 GLN B NE2 2001 N N . SER B 79 ? 0.4409 0.4936 0.3813 -0.0003 0.0056 -0.0554 107 SER B N 2002 C CA . SER B 79 ? 0.4580 0.5226 0.4029 0.0040 0.0055 -0.0536 107 SER B CA 2003 C C . SER B 79 ? 0.4993 0.5634 0.4359 0.0092 0.0048 -0.0568 107 SER B C 2004 O O . SER B 79 ? 0.4260 0.4782 0.3531 0.0116 0.0042 -0.0604 107 SER B O 2005 C CB . SER B 79 ? 0.4240 0.4875 0.3718 0.0059 0.0055 -0.0522 107 SER B CB 2006 O OG . SER B 79 ? 0.4179 0.4679 0.3567 0.0084 0.0049 -0.0554 107 SER B OG 2007 N N . ASP B 80 ? 0.4405 0.5172 0.3806 0.0110 0.0050 -0.0556 108 ASP B N 2008 C CA . ASP B 80 ? 0.4109 0.4884 0.3437 0.0150 0.0045 -0.0586 108 ASP B CA 2009 C C . ASP B 80 ? 0.4762 0.5516 0.4032 0.0218 0.0039 -0.0611 108 ASP B C 2010 O O . ASP B 80 ? 0.4508 0.5375 0.3820 0.0252 0.0042 -0.0598 108 ASP B O 2011 C CB . ASP B 80 ? 0.4008 0.4932 0.3393 0.0146 0.0050 -0.0564 108 ASP B CB 2012 C CG . ASP B 80 ? 0.4064 0.4993 0.3371 0.0179 0.0045 -0.0596 108 ASP B CG 2013 O OD1 . ASP B 80 ? 0.6165 0.6973 0.5374 0.0196 0.0038 -0.0636 108 ASP B OD1 2014 O OD2 . ASP B 80 ? 0.5424 0.6475 0.4765 0.0187 0.0049 -0.0581 108 ASP B OD2 2015 N N . ARG B 81 ? 0.4703 0.5311 0.3876 0.0236 0.0031 -0.0647 109 ARG B N 2016 C CA . ARG B 81 ? 0.5190 0.5754 0.4294 0.0304 0.0022 -0.0677 109 ARG B CA 2017 C C . ARG B 81 ? 0.5895 0.6519 0.5061 0.0331 0.0023 -0.0656 109 ARG B C 2018 O O . ARG B 81 ? 0.6651 0.7281 0.5781 0.0392 0.0016 -0.0675 109 ARG B O 2019 C CB . ARG B 81 ? 0.5261 0.5875 0.4311 0.0354 0.0018 -0.0703 109 ARG B CB 2020 C CG . ARG B 81 ? 0.8195 0.8739 0.7175 0.0328 0.0014 -0.0727 109 ARG B CG 2021 C CD . ARG B 81 ? 1.1797 1.2149 1.0663 0.0327 0.0003 -0.0764 109 ARG B CD 2022 N NE . ARG B 81 ? 1.1964 1.2257 1.0793 0.0277 0.0002 -0.0775 109 ARG B NE 2023 C CZ . ARG B 81 ? 1.2121 1.2262 1.0839 0.0273 -0.0009 -0.0811 109 ARG B CZ 2024 N NH1 . ARG B 81 ? 1.2195 1.2219 1.0821 0.0319 -0.0020 -0.0841 109 ARG B NH1 2025 N NH2 . ARG B 81 ? 1.2359 1.2464 1.1055 0.0223 -0.0009 -0.0818 109 ARG B NH2 2026 N N . LEU B 82 ? 0.5604 0.6272 0.4862 0.0284 0.0031 -0.0617 110 LEU B N 2027 C CA . LEU B 82 ? 0.4594 0.5300 0.3911 0.0298 0.0031 -0.0596 110 LEU B CA 2028 C C . LEU B 82 ? 0.3884 0.4515 0.3233 0.0242 0.0034 -0.0577 110 LEU B C 2029 O O . LEU B 82 ? 0.3732 0.4328 0.3085 0.0191 0.0039 -0.0572 110 LEU B O 2030 C CB . LEU B 82 ? 0.5224 0.6109 0.4642 0.0300 0.0039 -0.0561 110 LEU B CB 2031 C CG . LEU B 82 ? 0.5110 0.6102 0.4515 0.0356 0.0039 -0.0574 110 LEU B CG 2032 C CD1 . LEU B 82 ? 0.4281 0.5446 0.3790 0.0335 0.0049 -0.0532 110 LEU B CD1 2033 C CD2 . LEU B 82 ? 0.3450 0.4424 0.2822 0.0419 0.0030 -0.0595 110 LEU B CD2 2034 N N . PRO B 83 ? 0.3568 0.4167 0.2936 0.0251 0.0031 -0.0568 111 PRO B N 2035 C CA . PRO B 83 ? 0.4098 0.4719 0.3454 0.0311 0.0023 -0.0578 111 PRO B CA 2036 C C . PRO B 83 ? 0.5450 0.5932 0.4682 0.0358 0.0010 -0.0624 111 PRO B C 2037 O O . PRO B 83 ? 0.4184 0.4538 0.3340 0.0336 0.0008 -0.0645 111 PRO B O 2038 C CB . PRO B 83 ? 0.3736 0.4345 0.3153 0.0289 0.0023 -0.0551 111 PRO B CB 2039 C CG . PRO B 83 ? 0.3949 0.4454 0.3354 0.0231 0.0028 -0.0547 111 PRO B CG 2040 C CD . PRO B 83 ? 0.3075 0.3614 0.2481 0.0199 0.0036 -0.0548 111 PRO B CD 2041 N N . ILE B 84 ? 0.5558 0.6073 0.4771 0.0422 0.0001 -0.0639 112 ILE B N 2042 C CA . ILE B 84 ? 0.4621 0.5009 0.3720 0.0475 -0.0014 -0.0681 112 ILE B CA 2043 C C . ILE B 84 ? 0.4229 0.4559 0.3329 0.0490 -0.0023 -0.0677 112 ILE B C 2044 O O . ILE B 84 ? 0.4933 0.5371 0.4111 0.0507 -0.0023 -0.0657 112 ILE B O 2045 C CB . ILE B 84 ? 0.5614 0.6073 0.4677 0.0547 -0.0021 -0.0708 112 ILE B CB 2046 C CG1 . ILE B 84 ? 0.5398 0.5944 0.4473 0.0534 -0.0012 -0.0707 112 ILE B CG1 2047 C CG2 . ILE B 84 ? 0.6207 0.6511 0.5135 0.0598 -0.0039 -0.0755 112 ILE B CG2 2048 C CD1 . ILE B 84 ? 0.5905 0.6325 0.4902 0.0499 -0.0012 -0.0726 112 ILE B CD1 2049 N N . TYR B 85 ? 0.3979 0.4136 0.2987 0.0487 -0.0032 -0.0699 113 TYR B N 2050 C CA . TYR B 85 ? 0.4634 0.4716 0.3627 0.0505 -0.0042 -0.0700 113 TYR B CA 2051 C C . TYR B 85 ? 0.5137 0.5110 0.4010 0.0577 -0.0063 -0.0743 113 TYR B C 2052 O O . TYR B 85 ? 0.5213 0.5072 0.3982 0.0585 -0.0070 -0.0774 113 TYR B O 2053 C CB . TYR B 85 ? 0.3521 0.3492 0.2511 0.0439 -0.0035 -0.0685 113 TYR B CB 2054 C CG . TYR B 85 ? 0.3545 0.3432 0.2515 0.0454 -0.0046 -0.0684 113 TYR B CG 2055 C CD1 . TYR B 85 ? 0.3447 0.3425 0.2517 0.0445 -0.0043 -0.0652 113 TYR B CD1 2056 C CD2 . TYR B 85 ? 0.3998 0.3711 0.2844 0.0479 -0.0060 -0.0716 113 TYR B CD2 2057 C CE1 . TYR B 85 ? 0.4119 0.4023 0.3170 0.0460 -0.0054 -0.0653 113 TYR B CE1 2058 C CE2 . TYR B 85 ? 0.3700 0.3333 0.2523 0.0494 -0.0071 -0.0716 113 TYR B CE2 2059 C CZ . TYR B 85 ? 0.5130 0.4861 0.4056 0.0485 -0.0068 -0.0685 113 TYR B CZ 2060 O OH . TYR B 85 ? 0.4817 0.4468 0.3716 0.0502 -0.0080 -0.0685 113 TYR B OH 2061 N N . VAL B 86 ? 0.4918 0.4934 0.3807 0.0632 -0.0076 -0.0746 114 VAL B N 2062 C CA . VAL B 86 ? 0.5380 0.5294 0.4160 0.0704 -0.0098 -0.0786 114 VAL B CA 2063 C C . VAL B 86 ? 0.5686 0.5432 0.4400 0.0697 -0.0110 -0.0791 114 VAL B C 2064 O O . VAL B 86 ? 0.4443 0.4219 0.3221 0.0685 -0.0110 -0.0767 114 VAL B O 2065 C CB . VAL B 86 ? 0.4789 0.4841 0.3613 0.0776 -0.0108 -0.0792 114 VAL B CB 2066 C CG1 . VAL B 86 ? 0.5263 0.5201 0.3971 0.0855 -0.0134 -0.0835 114 VAL B CG1 2067 C CG2 . VAL B 86 ? 0.4466 0.4668 0.3334 0.0787 -0.0096 -0.0793 114 VAL B CG2 2068 N N . VAL B 87 ? 0.5354 0.4922 0.3937 0.0704 -0.0121 -0.0822 115 VAL B N 2069 C CA . VAL B 87 ? 0.5132 0.4529 0.3642 0.0689 -0.0130 -0.0826 115 VAL B CA 2070 C C . VAL B 87 ? 0.5264 0.4664 0.3771 0.0752 -0.0151 -0.0832 115 VAL B C 2071 O O . VAL B 87 ? 0.6377 0.5802 0.4845 0.0827 -0.0168 -0.0859 115 VAL B O 2072 C CB . VAL B 87 ? 0.5339 0.4541 0.3696 0.0692 -0.0141 -0.0862 115 VAL B CB 2073 C CG1 . VAL B 87 ? 0.5382 0.4407 0.3663 0.0672 -0.0149 -0.0864 115 VAL B CG1 2074 C CG2 . VAL B 87 ? 0.4192 0.3394 0.2552 0.0630 -0.0123 -0.0858 115 VAL B CG2 2075 N N . GLN B 88 ? 0.4157 0.3539 0.2709 0.0721 -0.0148 -0.0808 116 GLN B N 2076 C CA . GLN B 88 ? 0.6321 0.5705 0.4877 0.0771 -0.0168 -0.0810 116 GLN B CA 2077 C C . GLN B 88 ? 0.6344 0.5517 0.4770 0.0788 -0.0187 -0.0831 116 GLN B C 2078 O O . GLN B 88 ? 0.6505 0.5535 0.4857 0.0740 -0.0180 -0.0835 116 GLN B O 2079 C CB . GLN B 88 ? 0.6652 0.6148 0.5339 0.0729 -0.0155 -0.0768 116 GLN B CB 2080 C CG . GLN B 88 ? 0.7160 0.6854 0.5978 0.0702 -0.0135 -0.0740 116 GLN B CG 2081 C CD . GLN B 88 ? 0.7344 0.7178 0.6197 0.0771 -0.0145 -0.0753 116 GLN B CD 2082 O OE1 . GLN B 88 ? 0.8090 0.7991 0.6987 0.0807 -0.0158 -0.0748 116 GLN B OE1 2083 N NE2 . GLN B 88 ? 0.6810 0.6691 0.5640 0.0792 -0.0141 -0.0771 116 GLN B NE2 2084 N N . PRO B 89 ? 0.5652 0.4806 0.4047 0.0855 -0.0212 -0.0846 117 PRO B N 2085 C CA . PRO B 89 ? 0.5861 0.4821 0.4143 0.0866 -0.0231 -0.0860 117 PRO B CA 2086 C C . PRO B 89 ? 0.5792 0.4694 0.4105 0.0783 -0.0212 -0.0829 117 PRO B C 2087 O O . PRO B 89 ? 0.6263 0.5298 0.4704 0.0740 -0.0194 -0.0795 117 PRO B O 2088 C CB . PRO B 89 ? 0.5609 0.4626 0.3912 0.0939 -0.0256 -0.0867 117 PRO B CB 2089 C CG . PRO B 89 ? 0.6099 0.5301 0.4478 0.0987 -0.0256 -0.0873 117 PRO B CG 2090 C CD . PRO B 89 ? 0.6020 0.5324 0.4472 0.0928 -0.0226 -0.0854 117 PRO B CD 2091 N N . GLN B 90 ? 0.5741 0.4444 0.3935 0.0761 -0.0218 -0.0840 118 GLN B N 2092 C CA . GLN B 90 ? 0.5105 0.3734 0.3310 0.0684 -0.0200 -0.0815 118 GLN B CA 2093 C C . GLN B 90 ? 0.5153 0.3828 0.3415 0.0604 -0.0168 -0.0797 118 GLN B C 2094 O O . GLN B 90 ? 0.6592 0.5234 0.4883 0.0538 -0.0150 -0.0775 118 GLN B O 2095 C CB . GLN B 90 ? 0.4699 0.3410 0.3003 0.0678 -0.0200 -0.0787 118 GLN B CB 2096 C CG . GLN B 90 ? 0.5929 0.4655 0.4217 0.0759 -0.0230 -0.0801 118 GLN B CG 2097 C CD . GLN B 90 ? 0.7039 0.5560 0.5188 0.0782 -0.0253 -0.0820 118 GLN B CD 2098 O OE1 . GLN B 90 ? 0.6123 0.4507 0.4211 0.0726 -0.0241 -0.0814 118 GLN B OE1 2099 N NE2 . GLN B 90 ? 0.7420 0.5925 0.5523 0.0865 -0.0285 -0.0842 118 GLN B NE2 2100 N N . ASP B 91 ? 0.5428 0.4177 0.3704 0.0610 -0.0162 -0.0807 119 ASP B N 2101 C CA . ASP B 91 ? 0.6584 0.5391 0.4924 0.0535 -0.0134 -0.0788 119 ASP B CA 2102 C C . ASP B 91 ? 0.6631 0.5275 0.4858 0.0493 -0.0128 -0.0806 119 ASP B C 2103 O O . ASP B 91 ? 0.6372 0.4884 0.4469 0.0531 -0.0147 -0.0838 119 ASP B O 2104 C CB . ASP B 91 ? 0.6673 0.5654 0.5097 0.0552 -0.0127 -0.0785 119 ASP B CB 2105 C CG . ASP B 91 ? 0.6631 0.5805 0.5212 0.0541 -0.0115 -0.0750 119 ASP B CG 2106 O OD1 . ASP B 91 ? 0.6545 0.5719 0.5176 0.0513 -0.0111 -0.0726 119 ASP B OD1 2107 O OD2 . ASP B 91 ? 0.4110 0.3433 0.2762 0.0556 -0.0110 -0.0745 119 ASP B OD2 2108 N N . GLY B 92 ? 0.5300 0.3957 0.3577 0.0413 -0.0103 -0.0786 120 GLY B N 2109 C CA . GLY B 92 ? 0.4321 0.2866 0.2520 0.0361 -0.0092 -0.0799 120 GLY B CA 2110 C C . GLY B 92 ? 0.5852 0.4536 0.4157 0.0309 -0.0069 -0.0780 120 GLY B C 2111 O O . GLY B 92 ? 0.6657 0.5488 0.5092 0.0294 -0.0057 -0.0751 120 GLY B O 2112 N N . LEU B 93 ? 0.5114 0.3748 0.3361 0.0284 -0.0065 -0.0798 121 LEU B N 2113 C CA . LEU B 93 ? 0.6691 0.5450 0.5029 0.0239 -0.0046 -0.0784 121 LEU B CA 2114 C C . LEU B 93 ? 0.6846 0.5668 0.5289 0.0168 -0.0022 -0.0751 121 LEU B C 2115 O O . LEU B 93 ? 0.7012 0.5991 0.5577 0.0152 -0.0010 -0.0726 121 LEU B O 2116 C CB . LEU B 93 ? 0.6225 0.4885 0.4465 0.0214 -0.0046 -0.0811 121 LEU B CB 2117 C CG . LEU B 93 ? 0.6530 0.5308 0.4818 0.0212 -0.0041 -0.0813 121 LEU B CG 2118 C CD1 . LEU B 93 ? 0.6387 0.5312 0.4741 0.0281 -0.0051 -0.0809 121 LEU B CD1 2119 C CD2 . LEU B 93 ? 0.5709 0.4353 0.3864 0.0211 -0.0051 -0.0848 121 LEU B CD2 2120 N N . ASP B 94 ? 0.6390 0.5084 0.4780 0.0126 -0.0015 -0.0751 122 ASP B N 2121 C CA . ASP B 94 ? 0.5784 0.4520 0.4260 0.0059 0.0007 -0.0723 122 ASP B CA 2122 C C . ASP B 94 ? 0.5466 0.4320 0.4056 0.0077 0.0008 -0.0694 122 ASP B C 2123 O O . ASP B 94 ? 0.6720 0.5696 0.5426 0.0041 0.0024 -0.0668 122 ASP B O 2124 C CB . ASP B 94 ? 0.6588 0.5154 0.4971 0.0018 0.0013 -0.0732 122 ASP B CB 2125 C CG . ASP B 94 ? 0.6770 0.5376 0.5236 -0.0053 0.0038 -0.0708 122 ASP B CG 2126 O OD1 . ASP B 94 ? 0.6915 0.5572 0.5424 -0.0105 0.0054 -0.0704 122 ASP B OD1 2127 O OD2 . ASP B 94 ? 0.7340 0.5929 0.5829 -0.0054 0.0041 -0.0693 122 ASP B OD2 2128 N N . ALA B 95 ? 0.4993 0.3813 0.3548 0.0135 -0.0010 -0.0699 123 ALA B N 2129 C CA . ALA B 95 ? 0.4623 0.3545 0.3276 0.0155 -0.0012 -0.0673 123 ALA B CA 2130 C C . ALA B 95 ? 0.4750 0.3863 0.3516 0.0179 -0.0013 -0.0658 123 ALA B C 2131 O O . ALA B 95 ? 0.5336 0.4565 0.4213 0.0167 -0.0006 -0.0629 123 ALA B O 2132 C CB . ALA B 95 ? 0.3912 0.2743 0.2490 0.0213 -0.0035 -0.0686 123 ALA B CB 2133 N N . ILE B 96 ? 0.4862 0.4002 0.3594 0.0212 -0.0020 -0.0677 124 ILE B N 2134 C CA . ILE B 96 ? 0.4989 0.4303 0.3815 0.0230 -0.0018 -0.0664 124 ILE B CA 2135 C C . ILE B 96 ? 0.4792 0.4197 0.3711 0.0165 0.0003 -0.0640 124 ILE B C 2136 O O . ILE B 96 ? 0.4714 0.4262 0.3746 0.0159 0.0008 -0.0611 124 ILE B O 2137 C CB . ILE B 96 ? 0.5917 0.5224 0.4670 0.0278 -0.0030 -0.0695 124 ILE B CB 2138 C CG1 . ILE B 96 ? 0.5010 0.4268 0.3693 0.0355 -0.0054 -0.0717 124 ILE B CG1 2139 C CG2 . ILE B 96 ? 0.5090 0.4573 0.3935 0.0284 -0.0024 -0.0681 124 ILE B CG2 2140 C CD1 . ILE B 96 ? 0.4855 0.4061 0.3439 0.0400 -0.0067 -0.0753 124 ILE B CD1 2141 N N . ALA B 97 ? 0.4264 0.3586 0.3132 0.0118 0.0013 -0.0652 125 ALA B N 2142 C CA . ALA B 97 ? 0.4653 0.4046 0.3599 0.0054 0.0032 -0.0633 125 ALA B CA 2143 C C . ALA B 97 ? 0.4734 0.4179 0.3777 0.0019 0.0043 -0.0600 125 ALA B C 2144 O O . ALA B 97 ? 0.5707 0.5285 0.4859 0.0000 0.0051 -0.0574 125 ALA B O 2145 C CB . ALA B 97 ? 0.5005 0.4276 0.3868 0.0008 0.0040 -0.0654 125 ALA B CB 2146 N N . ARG B 98 ? 0.3841 0.3175 0.2840 0.0012 0.0043 -0.0603 126 ARG B N 2147 C CA . ARG B 98 ? 0.3990 0.3347 0.3064 -0.0026 0.0054 -0.0577 126 ARG B CA 2148 C C . ARG B 98 ? 0.5264 0.4705 0.4410 0.0011 0.0044 -0.0555 126 ARG B C 2149 O O . ARG B 98 ? 0.4905 0.4439 0.4152 -0.0014 0.0052 -0.0526 126 ARG B O 2150 C CB . ARG B 98 ? 0.4346 0.3542 0.3335 -0.0054 0.0060 -0.0590 126 ARG B CB 2151 C CG . ARG B 98 ? 0.4334 0.3440 0.3251 -0.0099 0.0071 -0.0611 126 ARG B CG 2152 C CD . ARG B 98 ? 0.4293 0.3239 0.3124 -0.0132 0.0079 -0.0622 126 ARG B CD 2153 N NE . ARG B 98 ? 0.5355 0.4287 0.4196 -0.0202 0.0100 -0.0624 126 ARG B NE 2154 C CZ . ARG B 98 ? 0.7262 0.6135 0.6033 -0.0226 0.0102 -0.0646 126 ARG B CZ 2155 N NH1 . ARG B 98 ? 0.9551 0.8371 0.8237 -0.0183 0.0085 -0.0668 126 ARG B NH1 2156 N NH2 . ARG B 98 ? 0.6953 0.5825 0.5741 -0.0290 0.0121 -0.0647 126 ARG B NH2 2157 N N . ASN B 99 ? 0.5228 0.4634 0.4320 0.0069 0.0026 -0.0568 127 ASN B N 2158 C CA . ASN B 99 ? 0.4442 0.3918 0.3597 0.0101 0.0016 -0.0549 127 ASN B CA 2159 C C . ASN B 99 ? 0.4995 0.4631 0.4229 0.0135 0.0009 -0.0535 127 ASN B C 2160 O O . ASN B 99 ? 0.4608 0.4333 0.3922 0.0145 0.0004 -0.0512 127 ASN B O 2161 C CB . ASN B 99 ? 0.4763 0.4124 0.3829 0.0144 -0.0001 -0.0567 127 ASN B CB 2162 C CG . ASN B 99 ? 0.5802 0.5001 0.4784 0.0110 0.0005 -0.0579 127 ASN B CG 2163 O OD1 . ASN B 99 ? 0.6675 0.5870 0.5697 0.0054 0.0023 -0.0564 127 ASN B OD1 2164 N ND2 . ASN B 99 ? 0.6371 0.5436 0.5236 0.0146 -0.0009 -0.0605 127 ASN B ND2 2165 N N . VAL B 100 ? 0.4825 0.4497 0.4034 0.0153 0.0008 -0.0551 128 VAL B N 2166 C CA . VAL B 100 ? 0.5400 0.5230 0.4684 0.0181 0.0004 -0.0538 128 VAL B CA 2167 C C . VAL B 100 ? 0.4138 0.4068 0.3500 0.0134 0.0020 -0.0517 128 VAL B C 2168 O O . VAL B 100 ? 0.5666 0.5730 0.5127 0.0128 0.0022 -0.0489 128 VAL B O 2169 C CB . VAL B 100 ? 0.6316 0.6144 0.5528 0.0242 -0.0009 -0.0568 128 VAL B CB 2170 C CG1 . VAL B 100 ? 0.4468 0.4474 0.3767 0.0270 -0.0010 -0.0552 128 VAL B CG1 2171 C CG2 . VAL B 100 ? 0.4983 0.4701 0.4108 0.0292 -0.0027 -0.0592 128 VAL B CG2 2172 N N . PHE B 101 ? 0.3647 0.3510 0.2965 0.0098 0.0029 -0.0531 129 PHE B N 2173 C CA . PHE B 101 ? 0.3809 0.3763 0.3191 0.0058 0.0041 -0.0515 129 PHE B CA 2174 C C . PHE B 101 ? 0.3479 0.3404 0.2899 -0.0007 0.0056 -0.0501 129 PHE B C 2175 O O . PHE B 101 ? 0.4197 0.4141 0.3627 -0.0042 0.0065 -0.0502 129 PHE B O 2176 C CB . PHE B 101 ? 0.4742 0.4680 0.4055 0.0073 0.0039 -0.0543 129 PHE B CB 2177 C CG . PHE B 101 ? 0.5517 0.5520 0.4814 0.0137 0.0027 -0.0553 129 PHE B CG 2178 C CD1 . PHE B 101 ? 0.5163 0.5325 0.4547 0.0147 0.0029 -0.0531 129 PHE B CD1 2179 C CD2 . PHE B 101 ? 0.5123 0.5029 0.4318 0.0188 0.0014 -0.0586 129 PHE B CD2 2180 C CE1 . PHE B 101 ? 0.4252 0.4484 0.3625 0.0205 0.0019 -0.0541 129 PHE B CE1 2181 C CE2 . PHE B 101 ? 0.4248 0.4221 0.3431 0.0250 0.0002 -0.0598 129 PHE B CE2 2182 C CZ . PHE B 101 ? 0.5619 0.5759 0.4893 0.0258 0.0006 -0.0576 129 PHE B CZ 2183 N N . ASN B 102 ? 0.3788 0.3666 0.3226 -0.0022 0.0058 -0.0489 130 ASN B N 2184 C CA . ASN B 102 ? 0.4270 0.4147 0.3764 -0.0079 0.0072 -0.0471 130 ASN B CA 2185 C C . ASN B 102 ? 0.4037 0.3832 0.3478 -0.0122 0.0084 -0.0491 130 ASN B C 2186 O O . ASN B 102 ? 0.4972 0.4802 0.4471 -0.0168 0.0095 -0.0478 130 ASN B O 2187 C CB . ASN B 102 ? 0.4055 0.4083 0.3668 -0.0098 0.0075 -0.0438 130 ASN B CB 2188 C CG . ASN B 102 ? 0.3116 0.3229 0.2799 -0.0073 0.0066 -0.0411 130 ASN B CG 2189 O OD1 . ASN B 102 ? 0.5251 0.5478 0.5023 -0.0086 0.0066 -0.0383 130 ASN B OD1 2190 N ND2 . ASN B 102 ? 0.4711 0.4768 0.4356 -0.0040 0.0056 -0.0418 130 ASN B ND2 2191 N N . ALA B 103 ? 0.4937 0.4628 0.4270 -0.0107 0.0080 -0.0523 131 ALA B N 2192 C CA . ALA B 103 ? 0.3853 0.3469 0.3128 -0.0148 0.0090 -0.0544 131 ALA B CA 2193 C C . ALA B 103 ? 0.4813 0.4535 0.4150 -0.0175 0.0096 -0.0536 131 ALA B C 2194 O O . ALA B 103 ? 0.5312 0.5010 0.4648 -0.0224 0.0107 -0.0542 131 ALA B O 2195 C CB . ALA B 103 ? 0.3913 0.3434 0.3171 -0.0196 0.0103 -0.0545 131 ALA B CB 2196 N N . PHE B 104 ? 0.4938 0.4779 0.4328 -0.0144 0.0088 -0.0522 132 PHE B N 2197 C CA . PHE B 104 ? 0.4638 0.4572 0.4070 -0.0162 0.0090 -0.0518 132 PHE B CA 2198 C C . PHE B 104 ? 0.4982 0.4842 0.4317 -0.0162 0.0088 -0.0552 132 PHE B C 2199 O O . PHE B 104 ? 0.4359 0.4253 0.3707 -0.0193 0.0092 -0.0556 132 PHE B O 2200 C CB . PHE B 104 ? 0.3402 0.3480 0.2909 -0.0130 0.0083 -0.0494 132 PHE B CB 2201 C CG . PHE B 104 ? 0.4211 0.4383 0.3831 -0.0149 0.0087 -0.0457 132 PHE B CG 2202 C CD1 . PHE B 104 ? 0.4198 0.4407 0.3879 -0.0199 0.0096 -0.0442 132 PHE B CD1 2203 C CD2 . PHE B 104 ? 0.3681 0.3902 0.3343 -0.0119 0.0080 -0.0437 132 PHE B CD2 2204 C CE1 . PHE B 104 ? 0.2987 0.3275 0.2766 -0.0215 0.0097 -0.0409 132 PHE B CE1 2205 C CE2 . PHE B 104 ? 0.4015 0.4314 0.3775 -0.0138 0.0082 -0.0402 132 PHE B CE2 2206 C CZ . PHE B 104 ? 0.3153 0.3482 0.2969 -0.0185 0.0090 -0.0388 132 PHE B CZ 2207 N N . VAL B 105 ? 0.4397 0.4151 0.3632 -0.0126 0.0079 -0.0577 133 VAL B N 2208 C CA . VAL B 105 ? 0.5174 0.4824 0.4300 -0.0128 0.0076 -0.0612 133 VAL B CA 2209 C C . VAL B 105 ? 0.5940 0.5426 0.4970 -0.0136 0.0076 -0.0631 133 VAL B C 2210 O O . VAL B 105 ? 0.6720 0.6177 0.5759 -0.0122 0.0075 -0.0621 133 VAL B O 2211 C CB . VAL B 105 ? 0.4608 0.4281 0.3684 -0.0069 0.0061 -0.0629 133 VAL B CB 2212 C CG1 . VAL B 105 ? 0.4378 0.4204 0.3535 -0.0066 0.0062 -0.0612 133 VAL B CG1 2213 C CG2 . VAL B 105 ? 0.4496 0.4149 0.3548 -0.0008 0.0050 -0.0630 133 VAL B CG2 2214 N N . THR B 106 ? 0.5933 0.5312 0.4872 -0.0163 0.0077 -0.0658 134 THR B N 2215 C CA . THR B 106 ? 0.6280 0.5488 0.5104 -0.0167 0.0075 -0.0681 134 THR B CA 2216 C C . THR B 106 ? 0.6228 0.5361 0.4945 -0.0106 0.0056 -0.0708 134 THR B C 2217 O O . THR B 106 ? 0.5240 0.4452 0.3969 -0.0068 0.0046 -0.0713 134 THR B O 2218 C CB . THR B 106 ? 0.5911 0.5037 0.4685 -0.0231 0.0086 -0.0697 134 THR B CB 2219 O OG1 . THR B 106 ? 0.6111 0.5223 0.4826 -0.0224 0.0077 -0.0721 134 THR B OG1 2220 C CG2 . THR B 106 ? 0.5765 0.4992 0.4655 -0.0288 0.0104 -0.0673 134 THR B CG2 2221 N N . TYR B 107 ? 0.6373 0.5351 0.4983 -0.0095 0.0049 -0.0726 135 TYR B N 2222 C CA . TYR B 107 ? 0.5570 0.4459 0.4066 -0.0036 0.0028 -0.0755 135 TYR B CA 2223 C C . TYR B 107 ? 0.6327 0.5162 0.4744 -0.0051 0.0023 -0.0783 135 TYR B C 2224 O O . TYR B 107 ? 0.6579 0.5411 0.4942 0.0003 0.0007 -0.0803 135 TYR B O 2225 C CB . TYR B 107 ? 0.6571 0.5302 0.4968 -0.0018 0.0019 -0.0767 135 TYR B CB 2226 C CG . TYR B 107 ? 0.6479 0.5045 0.4776 -0.0075 0.0026 -0.0782 135 TYR B CG 2227 C CD1 . TYR B 107 ? 0.6093 0.4548 0.4275 -0.0084 0.0018 -0.0813 135 TYR B CD1 2228 C CD2 . TYR B 107 ? 0.6909 0.5423 0.5218 -0.0118 0.0040 -0.0768 135 TYR B CD2 2229 C CE1 . TYR B 107 ? 0.6459 0.4759 0.4543 -0.0138 0.0024 -0.0827 135 TYR B CE1 2230 C CE2 . TYR B 107 ? 0.7171 0.5532 0.5383 -0.0172 0.0048 -0.0782 135 TYR B CE2 2231 C CZ . TYR B 107 ? 0.7531 0.5786 0.5631 -0.0182 0.0040 -0.0811 135 TYR B CZ 2232 O OH . TYR B 107 ? 0.8711 0.6815 0.6710 -0.0238 0.0047 -0.0825 135 TYR B OH 2233 N N . GLN B 108 ? 0.6040 0.4840 0.4454 -0.0123 0.0038 -0.0784 136 GLN B N 2234 C CA . GLN B 108 ? 0.5525 0.4289 0.3876 -0.0144 0.0034 -0.0809 136 GLN B CA 2235 C C . GLN B 108 ? 0.5045 0.3969 0.3478 -0.0120 0.0031 -0.0801 136 GLN B C 2236 O O . GLN B 108 ? 0.7381 0.6287 0.5750 -0.0092 0.0019 -0.0825 136 GLN B O 2237 C CB . GLN B 108 ? 0.6081 0.4799 0.4430 -0.0230 0.0051 -0.0810 136 GLN B CB 2238 C CG . GLN B 108 ? 0.5508 0.4055 0.3760 -0.0262 0.0055 -0.0820 136 GLN B CG 2239 C CD . GLN B 108 ? 0.7376 0.5952 0.5703 -0.0284 0.0071 -0.0793 136 GLN B CD 2240 O OE1 . GLN B 108 ? 0.8620 0.7318 0.7050 -0.0253 0.0072 -0.0769 136 GLN B OE1 2241 N NE2 . GLN B 108 ? 0.7919 0.6382 0.6192 -0.0339 0.0083 -0.0798 136 GLN B NE2 2242 N N . GLU B 109 ? 0.6158 0.5236 0.4727 -0.0129 0.0043 -0.0769 137 GLU B N 2243 C CA . GLU B 109 ? 0.6128 0.5360 0.4773 -0.0106 0.0041 -0.0759 137 GLU B CA 2244 C C . GLU B 109 ? 0.4730 0.3997 0.3351 -0.0025 0.0025 -0.0767 137 GLU B C 2245 O O . GLU B 109 ? 0.5114 0.4424 0.3714 0.0001 0.0017 -0.0781 137 GLU B O 2246 C CB . GLU B 109 ? 0.5468 0.4850 0.4259 -0.0136 0.0055 -0.0722 137 GLU B CB 2247 C CG . GLU B 109 ? 0.6032 0.5421 0.4857 -0.0210 0.0069 -0.0718 137 GLU B CG 2248 C CD . GLU B 109 ? 0.6927 0.6430 0.5884 -0.0242 0.0083 -0.0683 137 GLU B CD 2249 O OE1 . GLU B 109 ? 0.6846 0.6376 0.5849 -0.0219 0.0084 -0.0663 137 GLU B OE1 2250 O OE2 . GLU B 109 ? 0.7093 0.6659 0.6106 -0.0290 0.0091 -0.0676 137 GLU B OE2 2251 N N . ILE B 110 ? 0.4033 0.3275 0.2650 0.0016 0.0019 -0.0761 138 ILE B N 2252 C CA . ILE B 110 ? 0.4630 0.3897 0.3217 0.0095 0.0003 -0.0773 138 ILE B CA 2253 C C . ILE B 110 ? 0.5668 0.4808 0.4114 0.0126 -0.0013 -0.0814 138 ILE B C 2254 O O . ILE B 110 ? 0.5585 0.4783 0.4016 0.0170 -0.0022 -0.0828 138 ILE B O 2255 C CB . ILE B 110 ? 0.5396 0.4639 0.3990 0.0132 -0.0002 -0.0763 138 ILE B CB 2256 C CG1 . ILE B 110 ? 0.4996 0.4361 0.3728 0.0103 0.0012 -0.0722 138 ILE B CG1 2257 C CG2 . ILE B 110 ? 0.5130 0.4415 0.3701 0.0215 -0.0019 -0.0776 138 ILE B CG2 2258 C CD1 . ILE B 110 ? 0.4314 0.3666 0.3063 0.0136 0.0006 -0.0710 138 ILE B CD1 2259 N N . ALA B 111 ? 0.6313 0.5279 0.4653 0.0100 -0.0016 -0.0833 139 ALA B N 2260 C CA . ALA B 111 ? 0.6299 0.5118 0.4492 0.0123 -0.0033 -0.0872 139 ALA B CA 2261 C C . ALA B 111 ? 0.6798 0.5655 0.4976 0.0109 -0.0035 -0.0888 139 ALA B C 2262 O O . ALA B 111 ? 0.7330 0.6175 0.5443 0.0165 -0.0051 -0.0913 139 ALA B O 2263 C CB . ALA B 111 ? 0.6447 0.5079 0.4540 0.0077 -0.0033 -0.0884 139 ALA B CB 2264 N N . ALA B 112 ? 0.6584 0.5484 0.4820 0.0036 -0.0019 -0.0875 140 ALA B N 2265 C CA . ALA B 112 ? 0.6412 0.5351 0.4639 0.0016 -0.0020 -0.0888 140 ALA B CA 2266 C C . ALA B 112 ? 0.7321 0.6420 0.5616 0.0068 -0.0023 -0.0881 140 ALA B C 2267 O O . ALA B 112 ? 0.8947 0.8045 0.7186 0.0093 -0.0034 -0.0905 140 ALA B O 2268 C CB . ALA B 112 ? 0.5560 0.4539 0.3856 -0.0071 -0.0002 -0.0871 140 ALA B CB 2269 N N . ALA B 113 ? 0.6975 0.6212 0.5388 0.0082 -0.0014 -0.0849 141 ALA B N 2270 C CA . ALA B 113 ? 0.7965 0.7362 0.6449 0.0126 -0.0014 -0.0838 141 ALA B CA 2271 C C . ALA B 113 ? 0.7351 0.6717 0.5756 0.0210 -0.0032 -0.0865 141 ALA B C 2272 O O . ALA B 113 ? 0.7742 0.7200 0.6155 0.0250 -0.0036 -0.0872 141 ALA B O 2273 C CB . ALA B 113 ? 0.7926 0.7468 0.6551 0.0118 -0.0001 -0.0796 141 ALA B CB 2274 N N . ASN B 114 ? 0.7337 0.6576 0.5664 0.0239 -0.0042 -0.0879 142 ASN B N 2275 C CA . ASN B 114 ? 0.7575 0.6783 0.5828 0.0324 -0.0061 -0.0905 142 ASN B CA 2276 C C . ASN B 114 ? 0.7732 0.6754 0.5823 0.0343 -0.0079 -0.0949 142 ASN B C 2277 O O . ASN B 114 ? 0.7256 0.6216 0.5268 0.0413 -0.0097 -0.0973 142 ASN B O 2278 C CB . ASN B 114 ? 0.6842 0.6065 0.5130 0.0363 -0.0063 -0.0891 142 ASN B CB 2279 C CG . ASN B 114 ? 0.7063 0.6480 0.5503 0.0361 -0.0049 -0.0852 142 ASN B CG 2280 O OD1 . ASN B 114 ? 0.5864 0.5403 0.4342 0.0414 -0.0052 -0.0852 142 ASN B OD1 2281 N ND2 . ASN B 114 ? 0.7548 0.6995 0.6073 0.0300 -0.0034 -0.0820 142 ASN B ND2 2282 N N . ASN B 115 ? 0.7149 0.6085 0.5192 0.0280 -0.0076 -0.0958 143 ASN B N 2283 C CA . ASN B 115 ? 0.7559 0.6314 0.5444 0.0289 -0.0094 -0.0998 143 ASN B CA 2284 C C . ASN B 115 ? 0.7472 0.6060 0.5255 0.0318 -0.0109 -0.1013 143 ASN B C 2285 O O . ASN B 115 ? 0.7771 0.6236 0.5428 0.0367 -0.0130 -0.1048 143 ASN B O 2286 C CB . ASN B 115 ? 0.8172 0.6965 0.6008 0.0354 -0.0109 -0.1027 143 ASN B CB 2287 C CG . ASN B 115 ? 1.0312 0.9193 0.8187 0.0314 -0.0101 -0.1026 143 ASN B CG 2288 O OD1 . ASN B 115 ? 1.0050 0.9095 0.8009 0.0339 -0.0094 -0.1014 143 ASN B OD1 2289 N ND2 . ASN B 115 ? 1.1271 1.0042 0.9084 0.0249 -0.0101 -0.1038 143 ASN B ND2 2290 N N . ILE B 116 ? 0.7483 0.6078 0.5327 0.0295 -0.0098 -0.0986 144 ILE B N 2291 C CA . ILE B 116 ? 0.7597 0.6031 0.5348 0.0311 -0.0110 -0.0996 144 ILE B CA 2292 C C . ILE B 116 ? 0.8737 0.6998 0.6387 0.0242 -0.0109 -0.1009 144 ILE B C 2293 O O . ILE B 116 ? 0.9260 0.7551 0.6973 0.0163 -0.0089 -0.0989 144 ILE B O 2294 C CB . ILE B 116 ? 0.8105 0.6601 0.5953 0.0303 -0.0098 -0.0962 144 ILE B CB 2295 C CG1 . ILE B 116 ? 0.8999 0.7691 0.6969 0.0356 -0.0095 -0.0943 144 ILE B CG1 2296 C CG2 . ILE B 116 ? 0.7431 0.5758 0.5176 0.0326 -0.0113 -0.0974 144 ILE B CG2 2297 C CD1 . ILE B 116 ? 0.9450 0.8146 0.7360 0.0448 -0.0117 -0.0971 144 ILE B CD1 2298 N N . PRO B 117 ? 0.9096 0.7174 0.6587 0.0271 -0.0132 -0.1044 145 PRO B N 2299 C CA . PRO B 117 ? 0.8719 0.6622 0.6104 0.0201 -0.0131 -0.1057 145 PRO B CA 2300 C C . PRO B 117 ? 0.8402 0.6206 0.5773 0.0157 -0.0122 -0.1040 145 PRO B C 2301 O O . PRO B 117 ? 0.9184 0.6937 0.6551 0.0073 -0.0106 -0.1032 145 PRO B O 2302 C CB . PRO B 117 ? 0.9237 0.6976 0.6453 0.0255 -0.0162 -0.1100 145 PRO B CB 2303 C CG . PRO B 117 ? 0.9615 0.7436 0.6847 0.0358 -0.0178 -0.1109 145 PRO B CG 2304 C CD . PRO B 117 ? 0.9569 0.7595 0.6971 0.0367 -0.0159 -0.1073 145 PRO B CD 2305 N N . ASP B 118 ? 0.7408 0.5187 0.4769 0.0213 -0.0132 -0.1035 146 ASP B N 2306 C CA . ASP B 118 ? 0.8017 0.5722 0.5377 0.0177 -0.0123 -0.1016 146 ASP B CA 2307 C C . ASP B 118 ? 0.8473 0.6342 0.5982 0.0198 -0.0110 -0.0982 146 ASP B C 2308 O O . ASP B 118 ? 0.8734 0.6631 0.6246 0.0274 -0.0126 -0.0985 146 ASP B O 2309 C CB . ASP B 118 ? 0.8547 0.6042 0.5741 0.0221 -0.0150 -0.1041 146 ASP B CB 2310 C CG . ASP B 118 ? 0.9787 0.7176 0.6955 0.0181 -0.0141 -0.1025 146 ASP B CG 2311 O OD1 . ASP B 118 ? 1.0235 0.7717 0.7516 0.0123 -0.0115 -0.0994 146 ASP B OD1 2312 O OD2 . ASP B 118 ? 1.1260 0.8471 0.8290 0.0211 -0.0163 -0.1043 146 ASP B OD2 2313 N N . PRO B 119 ? 0.9170 0.7140 0.6798 0.0129 -0.0083 -0.0951 147 PRO B N 2314 C CA . PRO B 119 ? 0.8874 0.6993 0.6641 0.0143 -0.0071 -0.0919 147 PRO B CA 2315 C C . PRO B 119 ? 0.8235 0.6279 0.5965 0.0185 -0.0083 -0.0915 147 PRO B C 2316 O O . PRO B 119 ? 0.7755 0.5924 0.5590 0.0214 -0.0080 -0.0893 147 PRO B O 2317 C CB . PRO B 119 ? 0.8300 0.6480 0.6162 0.0053 -0.0042 -0.0892 147 PRO B CB 2318 C CG . PRO B 119 ? 0.9916 0.7969 0.7683 -0.0010 -0.0038 -0.0911 147 PRO B CG 2319 C CD . PRO B 119 ? 0.9644 0.7535 0.7249 0.0035 -0.0065 -0.0947 147 PRO B CD 2320 N N . ASN B 120 ? 0.7578 0.5423 0.5159 0.0192 -0.0098 -0.0937 148 ASN B N 2321 C CA . ASN B 120 ? 0.7899 0.5655 0.5432 0.0229 -0.0112 -0.0935 148 ASN B CA 2322 C C . ASN B 120 ? 0.7994 0.5758 0.5486 0.0332 -0.0141 -0.0955 148 ASN B C 2323 O O . ASN B 120 ? 0.8845 0.6572 0.6318 0.0378 -0.0155 -0.0953 148 ASN B O 2324 C CB . ASN B 120 ? 0.8067 0.5600 0.5453 0.0187 -0.0115 -0.0949 148 ASN B CB 2325 C CG . ASN B 120 ? 0.8376 0.5907 0.5815 0.0098 -0.0086 -0.0923 148 ASN B CG 2326 O OD1 . ASN B 120 ? 0.8838 0.6510 0.6413 0.0084 -0.0069 -0.0894 148 ASN B OD1 2327 N ND2 . ASN B 120 ? 0.9212 0.6589 0.6547 0.0036 -0.0080 -0.0934 148 ASN B ND2 2328 N N . LYS B 121 ? 0.6870 0.4687 0.4352 0.0370 -0.0151 -0.0975 149 LYS B N 2329 C CA . LYS B 121 ? 0.7875 0.5705 0.5316 0.0470 -0.0178 -0.0998 149 LYS B CA 2330 C C . LYS B 121 ? 0.7159 0.5206 0.4726 0.0507 -0.0172 -0.0990 149 LYS B C 2331 O O . LYS B 121 ? 0.7424 0.5534 0.5013 0.0487 -0.0163 -0.0995 149 LYS B O 2332 C CB . LYS B 121 ? 0.8628 0.6289 0.5902 0.0501 -0.0202 -0.1038 149 LYS B CB 2333 C CG . LYS B 121 ? 0.9937 0.7370 0.7067 0.0448 -0.0206 -0.1049 149 LYS B CG 2334 C CD . LYS B 121 ? 1.0655 0.7936 0.7674 0.0504 -0.0233 -0.1062 149 LYS B CD 2335 C CE . LYS B 121 ? 1.0370 0.7427 0.7254 0.0447 -0.0235 -0.1066 149 LYS B CE 2336 N NZ . LYS B 121 ? 1.1105 0.7974 0.7817 0.0518 -0.0273 -0.1100 149 LYS B NZ 2337 N N . ILE B 122 ? 0.6581 0.4736 0.4224 0.0563 -0.0178 -0.0978 150 ILE B N 2338 C CA . ILE B 122 ? 0.6499 0.4859 0.4255 0.0609 -0.0175 -0.0971 150 ILE B CA 2339 C C . ILE B 122 ? 0.6992 0.5364 0.4730 0.0701 -0.0200 -0.0984 150 ILE B C 2340 O O . ILE B 122 ? 0.7314 0.5575 0.4996 0.0713 -0.0212 -0.0985 150 ILE B O 2341 C CB . ILE B 122 ? 0.6414 0.4955 0.4341 0.0555 -0.0147 -0.0929 150 ILE B CB 2342 C CG1 . ILE B 122 ? 0.4591 0.3114 0.2557 0.0544 -0.0146 -0.0905 150 ILE B CG1 2343 C CG2 . ILE B 122 ? 0.6422 0.4965 0.4377 0.0467 -0.0124 -0.0916 150 ILE B CG2 2344 C CD1 . ILE B 122 ? 0.8016 0.6697 0.6141 0.0491 -0.0121 -0.0864 150 ILE B CD1 2345 N N . ASN B 123 ? 0.6530 0.5044 0.4318 0.0764 -0.0205 -0.0994 151 ASN B N 2346 C CA . ASN B 123 ? 0.6293 0.4838 0.4065 0.0858 -0.0229 -0.1011 151 ASN B CA 2347 C C . ASN B 123 ? 0.6289 0.5049 0.4218 0.0876 -0.0219 -0.0983 151 ASN B C 2348 O O . ASN B 123 ? 0.6651 0.5571 0.4695 0.0841 -0.0197 -0.0960 151 ASN B O 2349 C CB . ASN B 123 ? 0.6842 0.5370 0.4528 0.0929 -0.0248 -0.1052 151 ASN B CB 2350 C CG . ASN B 123 ? 0.9292 0.7582 0.6797 0.0943 -0.0271 -0.1087 151 ASN B CG 2351 O OD1 . ASN B 123 ? 1.0183 0.8346 0.7631 0.0871 -0.0262 -0.1083 151 ASN B OD1 2352 N ND2 . ASN B 123 ? 0.9969 0.8194 0.7379 0.1035 -0.0302 -0.1123 151 ASN B ND2 2353 N N . VAL B 124 ? 0.5710 0.4472 0.3641 0.0931 -0.0237 -0.0986 152 VAL B N 2354 C CA . VAL B 124 ? 0.6213 0.5179 0.4284 0.0956 -0.0232 -0.0964 152 VAL B CA 2355 C C . VAL B 124 ? 0.6583 0.5705 0.4699 0.0997 -0.0227 -0.0976 152 VAL B C 2356 O O . VAL B 124 ? 0.6397 0.5455 0.4412 0.1053 -0.0244 -0.1014 152 VAL B O 2357 C CB . VAL B 124 ? 0.6045 0.4983 0.4089 0.1027 -0.0258 -0.0976 152 VAL B CB 2358 C CG1 . VAL B 124 ? 0.6073 0.5228 0.4252 0.1061 -0.0255 -0.0960 152 VAL B CG1 2359 C CG2 . VAL B 124 ? 0.5812 0.4600 0.3813 0.0988 -0.0262 -0.0962 152 VAL B CG2 2360 N N . SER B 125 ? 0.6272 0.5592 0.4534 0.0967 -0.0205 -0.0944 153 SER B N 2361 C CA . SER B 125 ? 0.5900 0.5391 0.4222 0.0995 -0.0196 -0.0949 153 SER B CA 2362 C C . SER B 125 ? 0.6135 0.5605 0.4424 0.0956 -0.0182 -0.0956 153 SER B C 2363 O O . SER B 125 ? 0.6434 0.6033 0.4761 0.0977 -0.0175 -0.0961 153 SER B O 2364 C CB . SER B 125 ? 0.5868 0.5396 0.4144 0.1099 -0.0219 -0.0986 153 SER B CB 2365 O OG . SER B 125 ? 0.7324 0.6905 0.5651 0.1134 -0.0231 -0.0977 153 SER B OG 2366 N N . GLN B 126 ? 0.5610 0.4918 0.3824 0.0899 -0.0180 -0.0957 154 GLN B N 2367 C CA . GLN B 126 ? 0.4397 0.3697 0.2599 0.0848 -0.0165 -0.0957 154 GLN B CA 2368 C C . GLN B 126 ? 0.5667 0.5142 0.4020 0.0785 -0.0137 -0.0914 154 GLN B C 2369 O O . GLN B 126 ? 0.6172 0.5688 0.4610 0.0748 -0.0128 -0.0881 154 GLN B O 2370 C CB . GLN B 126 ? 0.5202 0.4293 0.3298 0.0796 -0.0167 -0.0966 154 GLN B CB 2371 C CG . GLN B 126 ? 0.5765 0.4835 0.3849 0.0732 -0.0152 -0.0965 154 GLN B CG 2372 C CD . GLN B 126 ? 0.6088 0.4955 0.4071 0.0677 -0.0155 -0.0972 154 GLN B CD 2373 O OE1 . GLN B 126 ? 0.6122 0.4872 0.4054 0.0682 -0.0165 -0.0973 154 GLN B OE1 2374 N NE2 . GLN B 126 ? 0.6290 0.5113 0.4241 0.0624 -0.0146 -0.0977 154 GLN B NE2 2375 N N . THR B 127 ? 0.5332 0.4908 0.3719 0.0773 -0.0125 -0.0913 155 THR B N 2376 C CA . THR B 127 ? 0.6349 0.6087 0.4873 0.0715 -0.0100 -0.0872 155 THR B CA 2377 C C . THR B 127 ? 0.5775 0.5450 0.4293 0.0633 -0.0086 -0.0860 155 THR B C 2378 O O . THR B 127 ? 0.6546 0.6131 0.4975 0.0629 -0.0091 -0.0887 155 THR B O 2379 C CB . THR B 127 ? 0.6106 0.6025 0.4690 0.0750 -0.0093 -0.0872 155 THR B CB 2380 O OG1 . THR B 127 ? 0.6179 0.6039 0.4666 0.0773 -0.0100 -0.0907 155 THR B OG1 2381 C CG2 . THR B 127 ? 0.5770 0.5791 0.4389 0.0823 -0.0103 -0.0877 155 THR B CG2 2382 N N . LEU B 128 ? 0.5454 0.5181 0.4070 0.0568 -0.0070 -0.0821 156 LEU B N 2383 C CA . LEU B 128 ? 0.5417 0.5096 0.4041 0.0488 -0.0056 -0.0808 156 LEU B CA 2384 C C . LEU B 128 ? 0.5023 0.4872 0.3773 0.0446 -0.0037 -0.0773 156 LEU B C 2385 O O . LEU B 128 ? 0.5670 0.5644 0.4523 0.0448 -0.0031 -0.0743 156 LEU B O 2386 C CB . LEU B 128 ? 0.5040 0.4612 0.3662 0.0444 -0.0053 -0.0794 156 LEU B CB 2387 C CG . LEU B 128 ? 0.5209 0.4601 0.3707 0.0479 -0.0072 -0.0823 156 LEU B CG 2388 C CD1 . LEU B 128 ? 0.4004 0.3317 0.2517 0.0436 -0.0067 -0.0803 156 LEU B CD1 2389 C CD2 . LEU B 128 ? 0.4750 0.3996 0.3115 0.0477 -0.0081 -0.0860 156 LEU B CD2 2390 N N . TRP B 129 ? 0.5297 0.5146 0.4033 0.0409 -0.0030 -0.0778 157 TRP B N 2391 C CA . TRP B 129 ? 0.4899 0.4879 0.3744 0.0356 -0.0014 -0.0745 157 TRP B CA 2392 C C . TRP B 129 ? 0.4562 0.4485 0.3445 0.0286 -0.0004 -0.0722 157 TRP B C 2393 O O . TRP B 129 ? 0.6365 0.6149 0.5172 0.0255 -0.0005 -0.0740 157 TRP B O 2394 C CB . TRP B 129 ? 0.4361 0.4350 0.3167 0.0344 -0.0012 -0.0762 157 TRP B CB 2395 C CG . TRP B 129 ? 0.5944 0.6038 0.4844 0.0282 0.0002 -0.0731 157 TRP B CG 2396 C CD1 . TRP B 129 ? 0.6353 0.6587 0.5377 0.0261 0.0013 -0.0690 157 TRP B CD1 2397 C CD2 . TRP B 129 ? 0.4886 0.4947 0.3762 0.0233 0.0006 -0.0738 157 TRP B CD2 2398 N NE1 . TRP B 129 ? 0.5973 0.6261 0.5048 0.0206 0.0023 -0.0672 157 TRP B NE1 2399 C CE2 . TRP B 129 ? 0.4562 0.4751 0.3552 0.0188 0.0019 -0.0701 157 TRP B CE2 2400 C CE3 . TRP B 129 ? 0.4475 0.4409 0.3243 0.0223 -0.0002 -0.0773 157 TRP B CE3 2401 C CZ2 . TRP B 129 ? 0.4621 0.4820 0.3623 0.0135 0.0023 -0.0699 157 TRP B CZ2 2402 C CZ3 . TRP B 129 ? 0.5579 0.5526 0.4361 0.0167 0.0004 -0.0771 157 TRP B CZ3 2403 C CH2 . TRP B 129 ? 0.4881 0.4962 0.3780 0.0125 0.0016 -0.0734 157 TRP B CH2 2404 N N . ILE B 130 ? 0.3985 0.4012 0.2981 0.0262 0.0006 -0.0684 158 ILE B N 2405 C CA . ILE B 130 ? 0.3640 0.3629 0.2682 0.0197 0.0017 -0.0661 158 ILE B CA 2406 C C . ILE B 130 ? 0.4077 0.4154 0.3188 0.0144 0.0028 -0.0641 158 ILE B C 2407 O O . ILE B 130 ? 0.4628 0.4850 0.3830 0.0145 0.0033 -0.0615 158 ILE B O 2408 C CB . ILE B 130 ? 0.4504 0.4549 0.3629 0.0199 0.0019 -0.0631 158 ILE B CB 2409 C CG1 . ILE B 130 ? 0.5113 0.5082 0.4175 0.0255 0.0005 -0.0649 158 ILE B CG1 2410 C CG2 . ILE B 130 ? 0.3576 0.3586 0.2749 0.0134 0.0030 -0.0608 158 ILE B CG2 2411 C CD1 . ILE B 130 ? 0.4969 0.4746 0.3915 0.0250 -0.0002 -0.0678 158 ILE B CD1 2412 N N . PRO B 131 ? 0.3793 0.3786 0.2859 0.0098 0.0032 -0.0655 159 PRO B N 2413 C CA . PRO B 131 ? 0.3606 0.3685 0.2736 0.0050 0.0041 -0.0639 159 PRO B CA 2414 C C . PRO B 131 ? 0.4242 0.4361 0.3469 -0.0005 0.0052 -0.0605 159 PRO B C 2415 O O . PRO B 131 ? 0.4132 0.4179 0.3345 -0.0055 0.0058 -0.0610 159 PRO B O 2416 C CB . PRO B 131 ? 0.4716 0.4677 0.3748 0.0026 0.0038 -0.0672 159 PRO B CB 2417 C CG . PRO B 131 ? 0.3745 0.3547 0.2692 0.0027 0.0034 -0.0692 159 PRO B CG 2418 C CD . PRO B 131 ? 0.4008 0.3826 0.2957 0.0089 0.0027 -0.0688 159 PRO B CD 2419 N N . LEU B 132 ? 0.4992 0.5221 0.4314 0.0004 0.0055 -0.0572 160 LEU B N 2420 C CA . LEU B 132 ? 0.4617 0.4897 0.4036 -0.0043 0.0064 -0.0538 160 LEU B CA 2421 C C . LEU B 132 ? 0.4380 0.4699 0.3830 -0.0092 0.0070 -0.0533 160 LEU B C 2422 O O . LEU B 132 ? 0.4680 0.5064 0.4127 -0.0082 0.0067 -0.0537 160 LEU B O 2423 C CB . LEU B 132 ? 0.4509 0.4921 0.4023 -0.0024 0.0064 -0.0503 160 LEU B CB 2424 C CG . LEU B 132 ? 0.5014 0.5414 0.4506 0.0029 0.0056 -0.0507 160 LEU B CG 2425 C CD1 . LEU B 132 ? 0.4934 0.5480 0.4519 0.0045 0.0056 -0.0473 160 LEU B CD1 2426 C CD2 . LEU B 132 ? 0.4778 0.5066 0.4247 0.0019 0.0057 -0.0511 160 LEU B CD2 2427 N N . PRO B 133 ? 0.3820 0.4100 0.3300 -0.0143 0.0077 -0.0525 161 PRO B N 2428 C CA . PRO B 133 ? 0.3481 0.3791 0.2989 -0.0190 0.0082 -0.0524 161 PRO B CA 2429 C C . PRO B 133 ? 0.4593 0.5053 0.4205 -0.0199 0.0081 -0.0489 161 PRO B C 2430 O O . PRO B 133 ? 0.3853 0.4375 0.3538 -0.0194 0.0082 -0.0459 161 PRO B O 2431 C CB . PRO B 133 ? 0.3128 0.3358 0.2642 -0.0237 0.0091 -0.0525 161 PRO B CB 2432 C CG . PRO B 133 ? 0.3078 0.3306 0.2630 -0.0218 0.0092 -0.0505 161 PRO B CG 2433 C CD . PRO B 133 ? 0.3378 0.3606 0.2882 -0.0158 0.0083 -0.0513 161 PRO B CD 2434 N N . CYS B 134 ? 0.3532 0.4044 0.3148 -0.0214 0.0079 -0.0493 162 CYS B N 2435 C CA . CYS B 134 ? 0.2801 0.3447 0.2503 -0.0221 0.0077 -0.0461 162 CYS B CA 2436 C C . CYS B 134 ? 0.4096 0.4763 0.3794 -0.0252 0.0074 -0.0471 162 CYS B C 2437 O O . CYS B 134 ? 0.4265 0.4844 0.3895 -0.0269 0.0075 -0.0503 162 CYS B O 2438 C CB . CYS B 134 ? 0.3206 0.3932 0.2910 -0.0172 0.0072 -0.0451 162 CYS B CB 2439 S SG . CYS B 134 ? 0.4862 0.5547 0.4455 -0.0133 0.0066 -0.0492 162 CYS B SG 2440 N N . SER B 135 ? 0.4465 0.5246 0.4234 -0.0262 0.0071 -0.0444 163 SER B N 2441 C CA . SER B 135 ? 0.5616 0.6429 0.5383 -0.0289 0.0066 -0.0453 163 SER B CA 2442 C C . SER B 135 ? 0.6079 0.7024 0.5906 -0.0279 0.0060 -0.0422 163 SER B C 2443 O O . SER B 135 ? 0.5484 0.6495 0.5369 -0.0264 0.0060 -0.0390 163 SER B O 2444 C CB . SER B 135 ? 0.4945 0.5730 0.4750 -0.0341 0.0069 -0.0454 163 SER B CB 2445 O OG . SER B 135 ? 0.5470 0.6287 0.5275 -0.0367 0.0063 -0.0464 163 SER B OG 2446 N N . CYS B 136 ? 0.5054 0.6035 0.4863 -0.0289 0.0053 -0.0432 164 CYS B N 2447 C CA . CYS B 136 ? 0.4935 0.6036 0.4799 -0.0287 0.0047 -0.0403 164 CYS B CA 2448 C C . CYS B 136 ? 0.5187 0.6318 0.5093 -0.0330 0.0040 -0.0399 164 CYS B C 2449 O O . CYS B 136 ? 0.4768 0.5989 0.4708 -0.0333 0.0032 -0.0379 164 CYS B O 2450 C CB . CYS B 136 ? 0.4684 0.5822 0.4490 -0.0252 0.0043 -0.0416 164 CYS B CB 2451 S SG . CYS B 136 ? 0.5283 0.6401 0.5045 -0.0196 0.0050 -0.0423 164 CYS B SG 2452 N N . ASP B 137 ? 0.4914 0.5972 0.4817 -0.0364 0.0043 -0.0417 165 ASP B N 2453 C CA . ASP B 137 ? 0.4924 0.6011 0.4872 -0.0405 0.0037 -0.0415 165 ASP B CA 2454 C C . ASP B 137 ? 0.4780 0.5957 0.4825 -0.0412 0.0032 -0.0373 165 ASP B C 2455 O O . ASP B 137 ? 0.4279 0.5457 0.4363 -0.0402 0.0037 -0.0350 165 ASP B O 2456 C CB . ASP B 137 ? 0.4721 0.5720 0.4660 -0.0440 0.0045 -0.0438 165 ASP B CB 2457 C CG . ASP B 137 ? 0.4184 0.5089 0.4028 -0.0446 0.0047 -0.0481 165 ASP B CG 2458 O OD1 . ASP B 137 ? 0.5117 0.6037 0.4912 -0.0433 0.0039 -0.0495 165 ASP B OD1 2459 O OD2 . ASP B 137 ? 0.4535 0.5349 0.4352 -0.0467 0.0056 -0.0500 165 ASP B OD2 2460 N N . LYS B 138 ? 0.6022 0.7268 0.6105 -0.0431 0.0020 -0.0363 166 LYS B N 2461 C CA . LYS B 138 ? 0.5733 0.7047 0.5906 -0.0444 0.0013 -0.0327 166 LYS B CA 2462 C C . LYS B 138 ? 0.5195 0.6458 0.5400 -0.0475 0.0019 -0.0338 166 LYS B C 2463 O O . LYS B 138 ? 0.5594 0.6782 0.5753 -0.0492 0.0027 -0.0373 166 LYS B O 2464 C CB . LYS B 138 ? 0.4246 0.5643 0.4442 -0.0454 -0.0003 -0.0316 166 LYS B CB 2465 C CG . LYS B 138 ? 0.4448 0.5916 0.4629 -0.0426 -0.0009 -0.0295 166 LYS B CG 2466 C CD . LYS B 138 ? 0.4254 0.5781 0.4436 -0.0439 -0.0025 -0.0296 166 LYS B CD 2467 C CE . LYS B 138 ? 0.5270 0.6867 0.5428 -0.0414 -0.0031 -0.0279 166 LYS B CE 2468 N NZ . LYS B 138 ? 0.6819 0.8503 0.7039 -0.0419 -0.0045 -0.0237 166 LYS B NZ 2469 N N . GLU B 139 ? 0.5379 0.6681 0.5662 -0.0483 0.0015 -0.0308 167 GLU B N 2470 C CA . GLU B 139 ? 0.5020 0.6291 0.5344 -0.0511 0.0020 -0.0316 167 GLU B CA 2471 C C . GLU B 139 ? 0.6160 0.7503 0.6542 -0.0532 0.0005 -0.0308 167 GLU B C 2472 O O . GLU B 139 ? 0.6128 0.7535 0.6568 -0.0524 -0.0007 -0.0273 167 GLU B O 2473 C CB . GLU B 139 ? 0.4326 0.5578 0.4691 -0.0502 0.0027 -0.0293 167 GLU B CB 2474 C CG . GLU B 139 ? 0.4842 0.6060 0.5248 -0.0529 0.0033 -0.0302 167 GLU B CG 2475 C CD . GLU B 139 ? 0.5961 0.7105 0.6318 -0.0554 0.0046 -0.0344 167 GLU B CD 2476 O OE1 . GLU B 139 ? 0.5463 0.6610 0.5855 -0.0584 0.0048 -0.0357 167 GLU B OE1 2477 O OE2 . GLU B 139 ? 0.6570 0.7653 0.6850 -0.0545 0.0054 -0.0365 167 GLU B OE2 2478 N N . GLU B 140 ? 0.6598 0.7928 0.6960 -0.0558 0.0004 -0.0340 168 GLU B N 2479 C CA . GLU B 140 ? 0.6578 0.7976 0.6991 -0.0578 -0.0012 -0.0338 168 GLU B CA 2480 C C . GLU B 140 ? 0.6812 0.8297 0.7248 -0.0559 -0.0031 -0.0306 168 GLU B C 2481 O O . GLU B 140 ? 0.6061 0.7605 0.6564 -0.0560 -0.0045 -0.0281 168 GLU B O 2482 C CB . GLU B 140 ? 0.6476 0.7881 0.6963 -0.0596 -0.0010 -0.0332 168 GLU B CB 2483 C CG . GLU B 140 ? 0.7898 0.9227 0.8365 -0.0623 0.0009 -0.0367 168 GLU B CG 2484 C CD . GLU B 140 ? 1.0416 1.1747 1.0864 -0.0656 0.0007 -0.0403 168 GLU B CD 2485 O OE1 . GLU B 140 ? 1.1142 1.2534 1.1594 -0.0657 -0.0010 -0.0403 168 GLU B OE1 2486 O OE2 . GLU B 140 ? 1.1686 1.2954 1.2110 -0.0683 0.0023 -0.0432 168 GLU B OE2 2487 N N . GLY B 141 ? 0.6032 0.7522 0.6410 -0.0539 -0.0033 -0.0307 169 GLY B N 2488 C CA . GLY B 141 ? 0.5109 0.6678 0.5497 -0.0523 -0.0049 -0.0280 169 GLY B CA 2489 C C . GLY B 141 ? 0.5504 0.7105 0.5913 -0.0497 -0.0049 -0.0238 169 GLY B C 2490 O O . GLY B 141 ? 0.6337 0.8002 0.6747 -0.0485 -0.0061 -0.0213 169 GLY B O 2491 N N . SER B 142 ? 0.4902 0.6460 0.5327 -0.0491 -0.0037 -0.0229 170 SER B N 2492 C CA . SER B 142 ? 0.5277 0.6864 0.5724 -0.0470 -0.0037 -0.0190 170 SER B CA 2493 C C . SER B 142 ? 0.5227 0.6776 0.5618 -0.0447 -0.0021 -0.0198 170 SER B C 2494 O O . SER B 142 ? 0.6036 0.7514 0.6381 -0.0447 -0.0008 -0.0232 170 SER B O 2495 C CB . SER B 142 ? 0.5697 0.7273 0.6210 -0.0478 -0.0038 -0.0169 170 SER B CB 2496 O OG . SER B 142 ? 0.7656 0.9298 0.8221 -0.0477 -0.0056 -0.0130 170 SER B OG 2497 N N . ASN B 143 ? 0.3886 0.5483 0.4280 -0.0426 -0.0023 -0.0168 171 ASN B N 2498 C CA . ASN B 143 ? 0.3536 0.5111 0.3887 -0.0400 -0.0009 -0.0173 171 ASN B CA 2499 C C . ASN B 143 ? 0.4833 0.6360 0.5210 -0.0398 0.0000 -0.0164 171 ASN B C 2500 O O . ASN B 143 ? 0.6256 0.7807 0.6694 -0.0406 -0.0007 -0.0132 171 ASN B O 2501 C CB . ASN B 143 ? 0.3778 0.5433 0.4126 -0.0382 -0.0013 -0.0143 171 ASN B CB 2502 C CG . ASN B 143 ? 0.5081 0.6775 0.5385 -0.0378 -0.0020 -0.0156 171 ASN B CG 2503 O OD1 . ASN B 143 ? 0.5353 0.7003 0.5608 -0.0380 -0.0017 -0.0195 171 ASN B OD1 2504 N ND2 . ASN B 143 ? 0.4919 0.6695 0.5239 -0.0375 -0.0029 -0.0124 171 ASN B ND2 2505 N N . VAL B 144 ? 0.5368 0.6825 0.5697 -0.0385 0.0014 -0.0193 172 VAL B N 2506 C CA . VAL B 144 ? 0.4750 0.6152 0.5093 -0.0381 0.0023 -0.0190 172 VAL B CA 2507 C C . VAL B 144 ? 0.5454 0.6828 0.5743 -0.0350 0.0033 -0.0203 172 VAL B C 2508 O O . VAL B 144 ? 0.5064 0.6439 0.5295 -0.0333 0.0035 -0.0224 172 VAL B O 2509 C CB . VAL B 144 ? 0.5242 0.6560 0.5578 -0.0403 0.0029 -0.0219 172 VAL B CB 2510 C CG1 . VAL B 144 ? 0.4491 0.5832 0.4899 -0.0430 0.0021 -0.0202 172 VAL B CG1 2511 C CG2 . VAL B 144 ? 0.4530 0.5807 0.4800 -0.0408 0.0033 -0.0260 172 VAL B CG2 2512 N N . MET B 145 ? 0.5588 0.6939 0.5897 -0.0340 0.0037 -0.0190 173 MET B N 2513 C CA . MET B 145 ? 0.5057 0.6362 0.5312 -0.0311 0.0046 -0.0209 173 MET B CA 2514 C C . MET B 145 ? 0.5220 0.6418 0.5452 -0.0319 0.0054 -0.0235 173 MET B C 2515 O O . MET B 145 ? 0.4834 0.6010 0.5111 -0.0334 0.0055 -0.0220 173 MET B O 2516 C CB . MET B 145 ? 0.5026 0.6384 0.5309 -0.0289 0.0046 -0.0179 173 MET B CB 2517 C CG . MET B 145 ? 0.4314 0.5647 0.4537 -0.0252 0.0053 -0.0202 173 MET B CG 2518 S SD . MET B 145 ? 0.6810 0.8163 0.7065 -0.0232 0.0054 -0.0178 173 MET B SD 2519 C CE . MET B 145 ? 0.5662 0.6929 0.5951 -0.0259 0.0055 -0.0176 173 MET B CE 2520 N N . HIS B 146 ? 0.4506 0.5635 0.4663 -0.0309 0.0060 -0.0273 174 HIS B N 2521 C CA . HIS B 146 ? 0.3950 0.4970 0.4071 -0.0318 0.0068 -0.0300 174 HIS B CA 2522 C C . HIS B 146 ? 0.4120 0.5103 0.4234 -0.0293 0.0072 -0.0294 174 HIS B C 2523 O O . HIS B 146 ? 0.4533 0.5536 0.4618 -0.0259 0.0071 -0.0296 174 HIS B O 2524 C CB . HIS B 146 ? 0.3880 0.4834 0.3917 -0.0318 0.0071 -0.0341 174 HIS B CB 2525 C CG . HIS B 146 ? 0.5334 0.6309 0.5378 -0.0349 0.0067 -0.0350 174 HIS B CG 2526 N ND1 . HIS B 146 ? 0.4394 0.5312 0.4438 -0.0386 0.0072 -0.0368 174 HIS B ND1 2527 C CD2 . HIS B 146 ? 0.5249 0.6300 0.5301 -0.0350 0.0059 -0.0344 174 HIS B CD2 2528 C CE1 . HIS B 146 ? 0.4376 0.5336 0.4430 -0.0407 0.0066 -0.0374 174 HIS B CE1 2529 N NE2 . HIS B 146 ? 0.4630 0.5668 0.4687 -0.0385 0.0057 -0.0359 174 HIS B NE2 2530 N N . LEU B 147 ? 0.3655 0.4589 0.3799 -0.0311 0.0076 -0.0289 175 LEU B N 2531 C CA . LEU B 147 ? 0.3826 0.4714 0.3963 -0.0291 0.0078 -0.0285 175 LEU B CA 2532 C C . LEU B 147 ? 0.4154 0.4920 0.4233 -0.0302 0.0087 -0.0317 175 LEU B C 2533 O O . LEU B 147 ? 0.4036 0.4769 0.4130 -0.0336 0.0092 -0.0324 175 LEU B O 2534 C CB . LEU B 147 ? 0.3500 0.4433 0.3719 -0.0303 0.0074 -0.0248 175 LEU B CB 2535 C CG . LEU B 147 ? 0.4750 0.5633 0.4966 -0.0287 0.0076 -0.0245 175 LEU B CG 2536 C CD1 . LEU B 147 ? 0.5161 0.6077 0.5350 -0.0247 0.0072 -0.0244 175 LEU B CD1 2537 C CD2 . LEU B 147 ? 0.4441 0.5358 0.4737 -0.0303 0.0071 -0.0210 175 LEU B CD2 2538 N N . ALA B 148 ? 0.4686 0.5384 0.4697 -0.0272 0.0088 -0.0337 176 ALA B N 2539 C CA . ALA B 148 ? 0.3720 0.4294 0.3669 -0.0281 0.0096 -0.0366 176 ALA B CA 2540 C C . ALA B 148 ? 0.4131 0.4673 0.4114 -0.0284 0.0098 -0.0350 176 ALA B C 2541 O O . ALA B 148 ? 0.4065 0.4632 0.4063 -0.0254 0.0092 -0.0335 176 ALA B O 2542 C CB . ALA B 148 ? 0.3380 0.3887 0.3234 -0.0246 0.0094 -0.0396 176 ALA B CB 2543 N N . TYR B 149 ? 0.4549 0.5037 0.4543 -0.0319 0.0106 -0.0355 177 TYR B N 2544 C CA . TYR B 149 ? 0.3041 0.3505 0.3074 -0.0326 0.0109 -0.0339 177 TYR B CA 2545 C C . TYR B 149 ? 0.3188 0.3526 0.3156 -0.0339 0.0119 -0.0365 177 TYR B C 2546 O O . TYR B 149 ? 0.3460 0.3753 0.3404 -0.0372 0.0129 -0.0385 177 TYR B O 2547 C CB . TYR B 149 ? 0.3478 0.4010 0.3599 -0.0358 0.0109 -0.0315 177 TYR B CB 2548 C CG . TYR B 149 ? 0.3645 0.4158 0.3812 -0.0365 0.0110 -0.0298 177 TYR B CG 2549 C CD1 . TYR B 149 ? 0.4605 0.5040 0.4758 -0.0391 0.0122 -0.0313 177 TYR B CD1 2550 C CD2 . TYR B 149 ? 0.4262 0.4836 0.4484 -0.0347 0.0100 -0.0266 177 TYR B CD2 2551 C CE1 . TYR B 149 ? 0.4408 0.4825 0.4599 -0.0396 0.0123 -0.0298 177 TYR B CE1 2552 C CE2 . TYR B 149 ? 0.4915 0.5467 0.5174 -0.0353 0.0099 -0.0251 177 TYR B CE2 2553 C CZ . TYR B 149 ? 0.4644 0.5117 0.4887 -0.0376 0.0111 -0.0268 177 TYR B CZ 2554 O OH . TYR B 149 ? 0.3809 0.4260 0.4086 -0.0380 0.0110 -0.0254 177 TYR B OH 2555 N N . SER B 150 ? 0.3887 0.4171 0.3830 -0.0316 0.0117 -0.0364 178 SER B N 2556 C CA . SER B 150 ? 0.4431 0.4592 0.4312 -0.0327 0.0126 -0.0385 178 SER B CA 2557 C C . SER B 150 ? 0.5153 0.5310 0.5092 -0.0355 0.0133 -0.0370 178 SER B C 2558 O O . SER B 150 ? 0.4421 0.4621 0.4417 -0.0342 0.0126 -0.0345 178 SER B O 2559 C CB . SER B 150 ? 0.2941 0.3038 0.2759 -0.0285 0.0118 -0.0394 178 SER B CB 2560 O OG . SER B 150 ? 0.3979 0.3953 0.3734 -0.0298 0.0127 -0.0412 178 SER B OG 2561 N N . VAL B 151 ? 0.4735 0.4842 0.4659 -0.0394 0.0147 -0.0387 179 VAL B N 2562 C CA . VAL B 151 ? 0.4524 0.4628 0.4500 -0.0422 0.0156 -0.0377 179 VAL B CA 2563 C C . VAL B 151 ? 0.3381 0.3411 0.3334 -0.0409 0.0157 -0.0374 179 VAL B C 2564 O O . VAL B 151 ? 0.3870 0.3794 0.3738 -0.0405 0.0162 -0.0396 179 VAL B O 2565 C CB . VAL B 151 ? 0.4454 0.4513 0.4407 -0.0467 0.0173 -0.0401 179 VAL B CB 2566 C CG1 . VAL B 151 ? 0.3497 0.3537 0.3490 -0.0492 0.0185 -0.0395 179 VAL B CG1 2567 C CG2 . VAL B 151 ? 0.4544 0.4686 0.4535 -0.0485 0.0172 -0.0401 179 VAL B CG2 2568 N N . GLY B 152 ? 0.4056 0.4135 0.4082 -0.0404 0.0152 -0.0348 180 GLY B N 2569 C CA . GLY B 152 ? 0.2743 0.2755 0.2751 -0.0393 0.0151 -0.0345 180 GLY B CA 2570 C C . GLY B 152 ? 0.4470 0.4409 0.4459 -0.0429 0.0170 -0.0360 180 GLY B C 2571 O O . GLY B 152 ? 0.5572 0.5541 0.5592 -0.0462 0.0181 -0.0366 180 GLY B O 2572 N N . LYS B 153 ? 0.4446 0.4291 0.4382 -0.0422 0.0173 -0.0368 181 LYS B N 2573 C CA . LYS B 153 ? 0.6256 0.6029 0.6169 -0.0455 0.0192 -0.0383 181 LYS B CA 2574 C C . LYS B 153 ? 0.5148 0.4995 0.5159 -0.0471 0.0194 -0.0364 181 LYS B C 2575 O O . LYS B 153 ? 0.5024 0.4930 0.5095 -0.0451 0.0179 -0.0338 181 LYS B O 2576 C CB . LYS B 153 ? 0.7352 0.7013 0.7192 -0.0440 0.0192 -0.0390 181 LYS B CB 2577 C CG . LYS B 153 ? 0.8514 0.8086 0.8310 -0.0476 0.0214 -0.0409 181 LYS B CG 2578 C CD . LYS B 153 ? 0.8905 0.8464 0.8736 -0.0475 0.0215 -0.0396 181 LYS B CD 2579 C CE . LYS B 153 ? 0.8728 0.8199 0.8508 -0.0512 0.0239 -0.0416 181 LYS B CE 2580 N NZ . LYS B 153 ? 0.7665 0.7010 0.7325 -0.0511 0.0244 -0.0438 181 LYS B NZ 2581 N N . GLY B 154 ? 0.5424 0.5275 0.5450 -0.0509 0.0212 -0.0376 182 GLY B N 2582 C CA . GLY B 154 ? 0.4631 0.4544 0.4743 -0.0523 0.0215 -0.0363 182 GLY B CA 2583 C C . GLY B 154 ? 0.5288 0.5321 0.5485 -0.0523 0.0203 -0.0345 182 GLY B C 2584 O O . GLY B 154 ? 0.5597 0.5685 0.5866 -0.0532 0.0203 -0.0334 182 GLY B O 2585 N N . GLU B 155 ? 0.5104 0.5174 0.5289 -0.0510 0.0194 -0.0343 183 GLU B N 2586 C CA . GLU B 155 ? 0.4078 0.4258 0.4335 -0.0511 0.0183 -0.0328 183 GLU B CA 2587 C C . GLU B 155 ? 0.4373 0.4582 0.4643 -0.0546 0.0196 -0.0347 183 GLU B C 2588 O O . GLU B 155 ? 0.6416 0.6559 0.6625 -0.0569 0.0212 -0.0374 183 GLU B O 2589 C CB . GLU B 155 ? 0.3458 0.3677 0.3702 -0.0482 0.0166 -0.0316 183 GLU B CB 2590 C CG . GLU B 155 ? 0.4149 0.4384 0.4416 -0.0449 0.0150 -0.0289 183 GLU B CG 2591 C CD . GLU B 155 ? 0.5534 0.5813 0.5788 -0.0421 0.0136 -0.0279 183 GLU B CD 2592 O OE1 . GLU B 155 ? 0.4865 0.5153 0.5083 -0.0422 0.0138 -0.0295 183 GLU B OE1 2593 O OE2 . GLU B 155 ? 0.7715 0.8025 0.7996 -0.0397 0.0122 -0.0256 183 GLU B OE2 2594 N N . ASN B 156 ? 0.4109 0.4414 0.4457 -0.0550 0.0187 -0.0332 184 ASN B N 2595 C CA . ASN B 156 ? 0.4853 0.5205 0.5226 -0.0581 0.0195 -0.0348 184 ASN B CA 2596 C C . ASN B 156 ? 0.4873 0.5314 0.5280 -0.0571 0.0178 -0.0334 184 ASN B C 2597 O O . ASN B 156 ? 0.5822 0.6300 0.6248 -0.0543 0.0161 -0.0309 184 ASN B O 2598 C CB . ASN B 156 ? 0.4960 0.5340 0.5398 -0.0598 0.0202 -0.0347 184 ASN B CB 2599 C CG . ASN B 156 ? 0.5658 0.6096 0.6170 -0.0575 0.0184 -0.0315 184 ASN B CG 2600 O OD1 . ASN B 156 ? 0.6526 0.7047 0.7090 -0.0566 0.0167 -0.0297 184 ASN B OD1 2601 N ND2 . ASN B 156 ? 0.5922 0.6314 0.6437 -0.0566 0.0186 -0.0308 184 ASN B ND2 2602 N N . THR B 157 ? 0.5189 0.5667 0.5604 -0.0596 0.0183 -0.0351 185 THR B N 2603 C CA . THR B 157 ? 0.4203 0.4756 0.4635 -0.0588 0.0168 -0.0343 185 THR B CA 2604 C C . THR B 157 ? 0.5693 0.6341 0.6214 -0.0577 0.0151 -0.0313 185 THR B C 2605 O O . THR B 157 ? 0.6847 0.7555 0.7386 -0.0560 0.0134 -0.0294 185 THR B O 2606 C CB . THR B 157 ? 0.5989 0.6550 0.6399 -0.0620 0.0177 -0.0371 185 THR B CB 2607 O OG1 . THR B 157 ? 0.7517 0.8103 0.7975 -0.0648 0.0187 -0.0382 185 THR B OG1 2608 C CG2 . THR B 157 ? 0.6722 0.7182 0.7033 -0.0631 0.0192 -0.0399 185 THR B CG2 2609 N N . SER B 158 ? 0.5810 0.6468 0.6383 -0.0585 0.0154 -0.0309 186 SER B N 2610 C CA . SER B 158 ? 0.5774 0.6509 0.6427 -0.0573 0.0135 -0.0281 186 SER B CA 2611 C C . SER B 158 ? 0.4904 0.5646 0.5564 -0.0543 0.0118 -0.0248 186 SER B C 2612 O O . SER B 158 ? 0.5539 0.6348 0.6229 -0.0530 0.0100 -0.0224 186 SER B O 2613 C CB . SER B 158 ? 0.5333 0.6065 0.6033 -0.0584 0.0143 -0.0287 186 SER B CB 2614 O OG . SER B 158 ? 0.5774 0.6578 0.6548 -0.0572 0.0123 -0.0262 186 SER B OG 2615 N N . ALA B 159 ? 0.4412 0.5086 0.5043 -0.0532 0.0124 -0.0245 187 ALA B N 2616 C CA . ALA B 159 ? 0.4653 0.5334 0.5292 -0.0506 0.0109 -0.0215 187 ALA B CA 2617 C C . ALA B 159 ? 0.5662 0.6362 0.6263 -0.0490 0.0102 -0.0209 187 ALA B C 2618 O O . ALA B 159 ? 0.4646 0.5398 0.5274 -0.0474 0.0086 -0.0180 187 ALA B O 2619 C CB . ALA B 159 ? 0.4179 0.4779 0.4790 -0.0499 0.0117 -0.0218 187 ALA B CB 2620 N N . ILE B 160 ? 0.6224 0.6880 0.6759 -0.0496 0.0116 -0.0237 188 ILE B N 2621 C CA . ILE B 160 ? 0.5048 0.5719 0.5541 -0.0478 0.0110 -0.0236 188 ILE B CA 2622 C C . ILE B 160 ? 0.4106 0.4871 0.4640 -0.0480 0.0097 -0.0222 188 ILE B C 2623 O O . ILE B 160 ? 0.4388 0.5204 0.4933 -0.0462 0.0085 -0.0198 188 ILE B O 2624 C CB . ILE B 160 ? 0.5173 0.5772 0.5584 -0.0485 0.0125 -0.0271 188 ILE B CB 2625 C CG1 . ILE B 160 ? 0.3502 0.4006 0.3859 -0.0474 0.0133 -0.0281 188 ILE B CG1 2626 C CG2 . ILE B 160 ? 0.4328 0.4957 0.4701 -0.0470 0.0119 -0.0275 188 ILE B CG2 2627 C CD1 . ILE B 160 ? 0.3390 0.3807 0.3661 -0.0486 0.0148 -0.0317 188 ILE B CD1 2628 N N . ALA B 161 ? 0.4780 0.5568 0.5334 -0.0504 0.0101 -0.0236 189 ALA B N 2629 C CA . ALA B 161 ? 0.4992 0.5868 0.5584 -0.0507 0.0088 -0.0224 189 ALA B CA 2630 C C . ALA B 161 ? 0.5145 0.6083 0.5801 -0.0494 0.0069 -0.0184 189 ALA B C 2631 O O . ALA B 161 ? 0.5211 0.6208 0.5876 -0.0482 0.0056 -0.0162 189 ALA B O 2632 C CB . ALA B 161 ? 0.4434 0.5326 0.5047 -0.0535 0.0093 -0.0246 189 ALA B CB 2633 N N . ALA B 162 ? 0.4462 0.5382 0.5158 -0.0497 0.0068 -0.0175 190 ALA B N 2634 C CA . ALA B 162 ? 0.5018 0.5986 0.5773 -0.0487 0.0049 -0.0138 190 ALA B CA 2635 C C . ALA B 162 ? 0.5524 0.6497 0.6262 -0.0467 0.0041 -0.0113 190 ALA B C 2636 O O . ALA B 162 ? 0.7115 0.8150 0.7881 -0.0460 0.0025 -0.0083 190 ALA B O 2637 C CB . ALA B 162 ? 0.4094 0.5032 0.4888 -0.0492 0.0049 -0.0135 190 ALA B CB 2638 N N . LYS B 163 ? 0.4594 0.5503 0.5286 -0.0458 0.0053 -0.0126 191 LYS B N 2639 C CA . LYS B 163 ? 0.4814 0.5730 0.5489 -0.0438 0.0047 -0.0107 191 LYS B CA 2640 C C . LYS B 163 ? 0.4981 0.5963 0.5643 -0.0428 0.0041 -0.0098 191 LYS B C 2641 O O . LYS B 163 ? 0.5979 0.7006 0.6654 -0.0416 0.0030 -0.0070 191 LYS B O 2642 C CB . LYS B 163 ? 0.5617 0.6451 0.6235 -0.0428 0.0060 -0.0129 191 LYS B CB 2643 C CG . LYS B 163 ? 0.7545 0.8391 0.8138 -0.0404 0.0055 -0.0117 191 LYS B CG 2644 C CD . LYS B 163 ? 0.8573 0.9336 0.9120 -0.0391 0.0064 -0.0134 191 LYS B CD 2645 C CE . LYS B 163 ? 0.7658 0.8344 0.8147 -0.0401 0.0081 -0.0173 191 LYS B CE 2646 N NZ . LYS B 163 ? 0.6323 0.6922 0.6756 -0.0387 0.0088 -0.0190 191 LYS B NZ 2647 N N . TYR B 164 ? 0.4897 0.5887 0.5531 -0.0436 0.0047 -0.0121 192 TYR B N 2648 C CA . TYR B 164 ? 0.6040 0.7090 0.6655 -0.0426 0.0042 -0.0116 192 TYR B CA 2649 C C . TYR B 164 ? 0.6315 0.7438 0.6970 -0.0438 0.0030 -0.0101 192 TYR B C 2650 O O . TYR B 164 ? 0.4717 0.5891 0.5355 -0.0432 0.0026 -0.0098 192 TYR B O 2651 C CB . TYR B 164 ? 0.5152 0.6157 0.5694 -0.0419 0.0056 -0.0151 192 TYR B CB 2652 C CG . TYR B 164 ? 0.4946 0.5898 0.5448 -0.0398 0.0062 -0.0157 192 TYR B CG 2653 C CD1 . TYR B 164 ? 0.3867 0.4864 0.4375 -0.0376 0.0054 -0.0134 192 TYR B CD1 2654 C CD2 . TYR B 164 ? 0.3395 0.4254 0.3854 -0.0401 0.0074 -0.0185 192 TYR B CD2 2655 C CE1 . TYR B 164 ? 0.4165 0.5121 0.4641 -0.0355 0.0057 -0.0139 192 TYR B CE1 2656 C CE2 . TYR B 164 ? 0.3888 0.4698 0.4310 -0.0379 0.0077 -0.0189 192 TYR B CE2 2657 C CZ . TYR B 164 ? 0.4700 0.5561 0.5132 -0.0355 0.0068 -0.0167 192 TYR B CZ 2658 O OH . TYR B 164 ? 0.6219 0.7038 0.6617 -0.0332 0.0069 -0.0172 192 TYR B OH 2659 N N . GLY B 165 ? 0.6709 0.7839 0.7416 -0.0452 0.0023 -0.0091 193 GLY B N 2660 C CA . GLY B 165 ? 0.6413 0.7610 0.7161 -0.0461 0.0008 -0.0075 193 GLY B CA 2661 C C . GLY B 165 ? 0.6310 0.7523 0.7036 -0.0472 0.0013 -0.0103 193 GLY B C 2662 O O . GLY B 165 ? 0.6168 0.7443 0.6900 -0.0472 0.0001 -0.0093 193 GLY B O 2663 N N . VAL B 166 ? 0.4572 0.5726 0.5269 -0.0483 0.0029 -0.0139 194 VAL B N 2664 C CA . VAL B 166 ? 0.4622 0.5784 0.5301 -0.0500 0.0034 -0.0169 194 VAL B CA 2665 C C . VAL B 166 ? 0.5382 0.6515 0.6089 -0.0521 0.0042 -0.0190 194 VAL B C 2666 O O . VAL B 166 ? 0.5829 0.6913 0.6545 -0.0521 0.0050 -0.0190 194 VAL B O 2667 C CB . VAL B 166 ? 0.5103 0.6224 0.5705 -0.0497 0.0047 -0.0198 194 VAL B CB 2668 C CG1 . VAL B 166 ? 0.3848 0.5001 0.4424 -0.0472 0.0041 -0.0179 194 VAL B CG1 2669 C CG2 . VAL B 166 ? 0.3953 0.4979 0.4513 -0.0500 0.0065 -0.0223 194 VAL B CG2 2670 N N . THR B 167 ? 0.5255 0.6423 0.5976 -0.0538 0.0039 -0.0207 195 THR B N 2671 C CA . THR B 167 ? 0.5893 0.7045 0.6640 -0.0560 0.0048 -0.0230 195 THR B CA 2672 C C . THR B 167 ? 0.6808 0.7876 0.7497 -0.0574 0.0072 -0.0264 195 THR B C 2673 O O . THR B 167 ? 0.6706 0.7742 0.7332 -0.0573 0.0078 -0.0278 195 THR B O 2674 C CB . THR B 167 ? 0.6397 0.7615 0.7171 -0.0575 0.0038 -0.0242 195 THR B CB 2675 O OG1 . THR B 167 ? 0.6594 0.7866 0.7440 -0.0570 0.0021 -0.0221 195 THR B OG1 2676 C CG2 . THR B 167 ? 0.6042 0.7230 0.6797 -0.0605 0.0056 -0.0283 195 THR B CG2 2677 N N . GLU B 168 ? 0.6656 0.7684 0.7362 -0.0586 0.0085 -0.0276 196 GLU B N 2678 C CA . GLU B 168 ? 0.6051 0.6995 0.6699 -0.0604 0.0108 -0.0307 196 GLU B CA 2679 C C . GLU B 168 ? 0.7032 0.7972 0.7640 -0.0630 0.0116 -0.0340 196 GLU B C 2680 O O . GLU B 168 ? 0.8378 0.9247 0.8913 -0.0637 0.0129 -0.0361 196 GLU B O 2681 C CB . GLU B 168 ? 0.5394 0.6308 0.6073 -0.0616 0.0120 -0.0315 196 GLU B CB 2682 C CG . GLU B 168 ? 0.5685 0.6511 0.6304 -0.0638 0.0146 -0.0347 196 GLU B CG 2683 C CD . GLU B 168 ? 0.6995 0.7791 0.7641 -0.0649 0.0159 -0.0354 196 GLU B CD 2684 O OE1 . GLU B 168 ? 0.7391 0.8226 0.8100 -0.0634 0.0149 -0.0333 196 GLU B OE1 2685 O OE2 . GLU B 168 ? 0.6559 0.7290 0.7159 -0.0672 0.0181 -0.0381 196 GLU B OE2 2686 N N . SER B 169 ? 0.6371 0.7384 0.7023 -0.0644 0.0107 -0.0345 197 SER B N 2687 C CA . SER B 169 ? 0.7116 0.8134 0.7736 -0.0671 0.0112 -0.0376 197 SER B CA 2688 C C . SER B 169 ? 0.6056 0.7066 0.6615 -0.0658 0.0104 -0.0375 197 SER B C 2689 O O . SER B 169 ? 0.6294 0.7254 0.6787 -0.0676 0.0114 -0.0403 197 SER B O 2690 C CB . SER B 169 ? 0.7901 0.9008 0.8590 -0.0687 0.0101 -0.0380 197 SER B CB 2691 O OG . SER B 169 ? 0.9200 1.0369 0.9890 -0.0680 0.0082 -0.0374 197 SER B OG 2692 N N . THR B 170 ? 0.5367 0.6425 0.5945 -0.0628 0.0086 -0.0344 198 THR B N 2693 C CA . THR B 170 ? 0.6290 0.7344 0.6813 -0.0610 0.0080 -0.0340 198 THR B CA 2694 C C . THR B 170 ? 0.6415 0.7372 0.6860 -0.0602 0.0096 -0.0355 198 THR B C 2695 O O . THR B 170 ? 0.6320 0.7239 0.6696 -0.0604 0.0099 -0.0377 198 THR B O 2696 C CB . THR B 170 ? 0.6214 0.7332 0.6773 -0.0579 0.0062 -0.0301 198 THR B CB 2697 O OG1 . THR B 170 ? 0.7247 0.8450 0.7860 -0.0585 0.0045 -0.0290 198 THR B OG1 2698 C CG2 . THR B 170 ? 0.6275 0.7382 0.6773 -0.0556 0.0060 -0.0297 198 THR B CG2 2699 N N . LEU B 171 ? 0.4645 0.5559 0.5100 -0.0593 0.0103 -0.0344 199 LEU B N 2700 C CA . LEU B 171 ? 0.5164 0.5983 0.5549 -0.0584 0.0117 -0.0357 199 LEU B CA 2701 C C . LEU B 171 ? 0.5463 0.6206 0.5791 -0.0616 0.0133 -0.0395 199 LEU B C 2702 O O . LEU B 171 ? 0.6165 0.6838 0.6411 -0.0612 0.0139 -0.0415 199 LEU B O 2703 C CB . LEU B 171 ? 0.5115 0.5906 0.5528 -0.0570 0.0120 -0.0338 199 LEU B CB 2704 C CG . LEU B 171 ? 0.4802 0.5499 0.5146 -0.0554 0.0130 -0.0346 199 LEU B CG 2705 C CD1 . LEU B 171 ? 0.4749 0.5458 0.5054 -0.0521 0.0120 -0.0337 199 LEU B CD1 2706 C CD2 . LEU B 171 ? 0.4298 0.4973 0.4679 -0.0547 0.0133 -0.0328 199 LEU B CD2 2707 N N . LEU B 172 ? 0.5351 0.6109 0.5720 -0.0648 0.0141 -0.0407 200 LEU B N 2708 C CA . LEU B 172 ? 0.5453 0.6142 0.5773 -0.0684 0.0159 -0.0442 200 LEU B CA 2709 C C . LEU B 172 ? 0.5327 0.6013 0.5596 -0.0703 0.0156 -0.0467 200 LEU B C 2710 O O . LEU B 172 ? 0.5374 0.5972 0.5562 -0.0720 0.0167 -0.0493 200 LEU B O 2711 C CB . LEU B 172 ? 0.6990 0.7710 0.7375 -0.0713 0.0169 -0.0447 200 LEU B CB 2712 C CG . LEU B 172 ? 0.6727 0.7423 0.7144 -0.0702 0.0176 -0.0432 200 LEU B CG 2713 C CD1 . LEU B 172 ? 0.6771 0.7523 0.7265 -0.0723 0.0181 -0.0434 200 LEU B CD1 2714 C CD2 . LEU B 172 ? 0.6082 0.6661 0.6420 -0.0710 0.0195 -0.0449 200 LEU B CD2 2715 N N . THR B 173 ? 0.3755 0.4533 0.4067 -0.0700 0.0140 -0.0458 201 THR B N 2716 C CA . THR B 173 ? 0.5971 0.6751 0.6237 -0.0718 0.0135 -0.0481 201 THR B CA 2717 C C . THR B 173 ? 0.5608 0.6344 0.5797 -0.0687 0.0129 -0.0482 201 THR B C 2718 O O . THR B 173 ? 0.4690 0.5357 0.4798 -0.0700 0.0133 -0.0509 201 THR B O 2719 C CB . THR B 173 ? 0.6556 0.7447 0.6890 -0.0726 0.0119 -0.0475 201 THR B CB 2720 O OG1 . THR B 173 ? 0.8251 0.9210 0.8626 -0.0688 0.0101 -0.0441 201 THR B OG1 2721 C CG2 . THR B 173 ? 0.5238 0.6173 0.5647 -0.0754 0.0125 -0.0480 201 THR B CG2 2722 N N . ARG B 174 ? 0.5804 0.6575 0.6014 -0.0646 0.0118 -0.0452 202 ARG B N 2723 C CA . ARG B 174 ? 0.6598 0.7339 0.6742 -0.0613 0.0113 -0.0452 202 ARG B CA 2724 C C . ARG B 174 ? 0.5879 0.6497 0.5933 -0.0614 0.0126 -0.0476 202 ARG B C 2725 O O . ARG B 174 ? 0.4844 0.5411 0.4818 -0.0606 0.0124 -0.0496 202 ARG B O 2726 C CB . ARG B 174 ? 0.6721 0.7515 0.6906 -0.0572 0.0104 -0.0415 202 ARG B CB 2727 C CG . ARG B 174 ? 0.6096 0.6875 0.6220 -0.0536 0.0098 -0.0414 202 ARG B CG 2728 C CD . ARG B 174 ? 0.5940 0.6766 0.6041 -0.0536 0.0087 -0.0424 202 ARG B CD 2729 N NE . ARG B 174 ? 0.6880 0.7666 0.6900 -0.0505 0.0085 -0.0437 202 ARG B NE 2730 C CZ . ARG B 174 ? 0.6921 0.7728 0.6900 -0.0499 0.0077 -0.0451 202 ARG B CZ 2731 N NH1 . ARG B 174 ? 0.6551 0.7422 0.6563 -0.0523 0.0069 -0.0452 202 ARG B NH1 2732 N NH2 . ARG B 174 ? 0.5909 0.6675 0.5812 -0.0467 0.0076 -0.0464 202 ARG B NH2 2733 N N . ASN B 175 ? 0.5573 0.6140 0.5637 -0.0625 0.0139 -0.0475 203 ASN B N 2734 C CA . ASN B 175 ? 0.4620 0.5065 0.4599 -0.0626 0.0151 -0.0495 203 ASN B CA 2735 C C . ASN B 175 ? 0.5781 0.6155 0.5718 -0.0674 0.0166 -0.0526 203 ASN B C 2736 O O . ASN B 175 ? 0.6296 0.6564 0.6166 -0.0681 0.0178 -0.0542 203 ASN B O 2737 C CB . ASN B 175 ? 0.4420 0.4841 0.4422 -0.0603 0.0156 -0.0474 203 ASN B CB 2738 C CG . ASN B 175 ? 0.5317 0.5780 0.5330 -0.0555 0.0143 -0.0450 203 ASN B CG 2739 O OD1 . ASN B 175 ? 0.6215 0.6623 0.6158 -0.0527 0.0140 -0.0458 203 ASN B OD1 2740 N ND2 . ASN B 175 ? 0.4300 0.4866 0.4401 -0.0544 0.0133 -0.0419 203 ASN B ND2 2741 N N . LYS B 176 ? 0.6231 0.6666 0.6207 -0.0708 0.0165 -0.0536 204 LYS B N 2742 C CA . LYS B 176 ? 0.5765 0.6151 0.5710 -0.0761 0.0178 -0.0566 204 LYS B CA 2743 C C . LYS B 176 ? 0.5718 0.6042 0.5663 -0.0781 0.0198 -0.0569 204 LYS B C 2744 O O . LYS B 176 ? 0.6698 0.6916 0.6563 -0.0804 0.0211 -0.0591 204 LYS B O 2745 C CB . LYS B 176 ? 0.5767 0.6063 0.5602 -0.0770 0.0177 -0.0595 204 LYS B CB 2746 C CG . LYS B 176 ? 0.6719 0.7077 0.6556 -0.0778 0.0162 -0.0605 204 LYS B CG 2747 C CD . LYS B 176 ? 0.7472 0.7773 0.7218 -0.0747 0.0151 -0.0615 204 LYS B CD 2748 C CE . LYS B 176 ? 0.8524 0.8878 0.8263 -0.0759 0.0137 -0.0629 204 LYS B CE 2749 N NZ . LYS B 176 ? 0.8631 0.9084 0.8458 -0.0797 0.0136 -0.0627 204 LYS B NZ 2750 N N . ILE B 177 ? 0.6822 0.7210 0.6854 -0.0772 0.0200 -0.0546 205 ILE B N 2751 C CA . ILE B 177 ? 0.7045 0.7386 0.7087 -0.0790 0.0219 -0.0548 205 ILE B CA 2752 C C . ILE B 177 ? 0.6406 0.6822 0.6524 -0.0829 0.0227 -0.0555 205 ILE B C 2753 O O . ILE B 177 ? 0.6371 0.6892 0.6580 -0.0816 0.0216 -0.0536 205 ILE B O 2754 C CB . ILE B 177 ? 0.6783 0.7134 0.6864 -0.0748 0.0214 -0.0517 205 ILE B CB 2755 C CG1 . ILE B 177 ? 0.6980 0.7258 0.6985 -0.0709 0.0207 -0.0513 205 ILE B CG1 2756 C CG2 . ILE B 177 ? 0.6899 0.7213 0.6999 -0.0766 0.0233 -0.0519 205 ILE B CG2 2757 C CD1 . ILE B 177 ? 0.6983 0.7296 0.7035 -0.0665 0.0197 -0.0480 205 ILE B CD1 2758 N N . ASP B 178 ? 0.7351 0.7715 0.7431 -0.0877 0.0245 -0.0583 206 ASP B N 2759 C CA . ASP B 178 ? 0.8777 0.9214 0.8928 -0.0917 0.0256 -0.0594 206 ASP B CA 2760 C C . ASP B 178 ? 0.8405 0.8862 0.8619 -0.0909 0.0266 -0.0579 206 ASP B C 2761 O O . ASP B 178 ? 0.8833 0.9391 0.9142 -0.0906 0.0262 -0.0570 206 ASP B O 2762 C CB . ASP B 178 ? 1.0224 1.0597 1.0310 -0.0975 0.0274 -0.0628 206 ASP B CB 2763 C CG . ASP B 178 ? 1.2099 1.2461 1.2130 -0.0990 0.0262 -0.0646 206 ASP B CG 2764 O OD1 . ASP B 178 ? 1.2901 1.3351 1.2978 -0.0970 0.0242 -0.0636 206 ASP B OD1 2765 O OD2 . ASP B 178 ? 1.2373 1.2635 1.2309 -0.1022 0.0272 -0.0670 206 ASP B OD2 2766 N N . ASP B 179 ? 0.7878 0.8236 0.8036 -0.0901 0.0279 -0.0577 207 ASP B N 2767 C CA . ASP B 179 ? 0.7027 0.7384 0.7228 -0.0897 0.0292 -0.0567 207 ASP B CA 2768 C C . ASP B 179 ? 0.6219 0.6541 0.6414 -0.0846 0.0282 -0.0540 207 ASP B C 2769 O O . ASP B 179 ? 0.6352 0.6570 0.6464 -0.0837 0.0286 -0.0543 207 ASP B O 2770 C CB . ASP B 179 ? 0.7392 0.7658 0.7530 -0.0941 0.0320 -0.0593 207 ASP B CB 2771 C CG . ASP B 179 ? 0.8031 0.8295 0.8209 -0.0941 0.0336 -0.0586 207 ASP B CG 2772 O OD1 . ASP B 179 ? 0.7849 0.8192 0.8114 -0.0911 0.0325 -0.0565 207 ASP B OD1 2773 O OD2 . ASP B 179 ? 0.8403 0.8580 0.8520 -0.0970 0.0358 -0.0602 207 ASP B OD2 2774 N N . PRO B 180 ? 0.6068 0.6475 0.6350 -0.0815 0.0267 -0.0514 208 PRO B N 2775 C CA . PRO B 180 ? 0.6121 0.6508 0.6407 -0.0769 0.0255 -0.0486 208 PRO B CA 2776 C C . PRO B 180 ? 0.7088 0.7370 0.7319 -0.0769 0.0271 -0.0490 208 PRO B C 2777 O O . PRO B 180 ? 0.7847 0.8067 0.8025 -0.0740 0.0264 -0.0480 208 PRO B O 2778 C CB . PRO B 180 ? 0.6357 0.6846 0.6749 -0.0753 0.0244 -0.0463 208 PRO B CB 2779 C CG . PRO B 180 ? 0.6613 0.7191 0.7052 -0.0775 0.0239 -0.0474 208 PRO B CG 2780 C CD . PRO B 180 ? 0.5945 0.6472 0.6326 -0.0822 0.0260 -0.0509 208 PRO B CD 2781 N N . THR B 181 ? 0.7240 0.7504 0.7479 -0.0801 0.0293 -0.0506 209 THR B N 2782 C CA . THR B 181 ? 0.6654 0.6822 0.6845 -0.0803 0.0309 -0.0509 209 THR B CA 2783 C C . THR B 181 ? 0.6578 0.6625 0.6652 -0.0808 0.0314 -0.0523 209 THR B C 2784 O O . THR B 181 ? 0.7021 0.6976 0.7040 -0.0802 0.0323 -0.0524 209 THR B O 2785 C CB . THR B 181 ? 0.6854 0.7024 0.7067 -0.0843 0.0334 -0.0528 209 THR B CB 2786 O OG1 . THR B 181 ? 0.6320 0.6464 0.6484 -0.0892 0.0351 -0.0557 209 THR B OG1 2787 C CG2 . THR B 181 ? 0.6064 0.6351 0.6391 -0.0837 0.0329 -0.0518 209 THR B CG2 2788 N N . LYS B 182 ? 0.6909 0.6949 0.6938 -0.0819 0.0308 -0.0536 210 LYS B N 2789 C CA . LYS B 182 ? 0.7342 0.7262 0.7254 -0.0821 0.0311 -0.0551 210 LYS B CA 2790 C C . LYS B 182 ? 0.6428 0.6324 0.6309 -0.0768 0.0289 -0.0534 210 LYS B C 2791 O O . LYS B 182 ? 0.6414 0.6213 0.6198 -0.0761 0.0287 -0.0546 210 LYS B O 2792 C CB . LYS B 182 ? 0.7981 0.7893 0.7850 -0.0860 0.0315 -0.0577 210 LYS B CB 2793 C CG . LYS B 182 ? 0.8528 0.8452 0.8411 -0.0920 0.0338 -0.0598 210 LYS B CG 2794 C CD . LYS B 182 ? 0.8904 0.8709 0.8709 -0.0944 0.0360 -0.0611 210 LYS B CD 2795 C CE . LYS B 182 ? 0.9431 0.9233 0.9225 -0.1010 0.0385 -0.0637 210 LYS B CE 2796 N NZ . LYS B 182 ? 0.9958 0.9713 0.9676 -0.1040 0.0382 -0.0658 210 LYS B NZ 2797 N N . LEU B 183 ? 0.5532 0.5513 0.5493 -0.0731 0.0273 -0.0507 211 LEU B N 2798 C CA . LEU B 183 ? 0.5928 0.5905 0.5872 -0.0681 0.0253 -0.0489 211 LEU B CA 2799 C C . LEU B 183 ? 0.6282 0.6142 0.6145 -0.0663 0.0256 -0.0492 211 LEU B C 2800 O O . LEU B 183 ? 0.6594 0.6415 0.6461 -0.0672 0.0268 -0.0490 211 LEU B O 2801 C CB . LEU B 183 ? 0.4354 0.4438 0.4399 -0.0652 0.0238 -0.0457 211 LEU B CB 2802 C CG . LEU B 183 ? 0.5920 0.6043 0.5972 -0.0606 0.0216 -0.0436 211 LEU B CG 2803 C CD1 . LEU B 183 ? 0.5184 0.5352 0.5223 -0.0604 0.0206 -0.0443 211 LEU B CD1 2804 C CD2 . LEU B 183 ? 0.6244 0.6452 0.6390 -0.0584 0.0204 -0.0403 211 LEU B CD2 2805 N N . GLN B 184 ? 0.6671 0.6470 0.6455 -0.0639 0.0246 -0.0500 212 GLN B N 2806 C CA . GLN B 184 ? 0.6286 0.5975 0.5990 -0.0617 0.0245 -0.0503 212 GLN B CA 2807 C C . GLN B 184 ? 0.4986 0.4706 0.4714 -0.0562 0.0226 -0.0480 212 GLN B C 2808 O O . GLN B 184 ? 0.6049 0.5852 0.5817 -0.0538 0.0211 -0.0467 212 GLN B O 2809 C CB . GLN B 184 ? 0.6466 0.6043 0.6051 -0.0627 0.0248 -0.0531 212 GLN B CB 2810 C CG . GLN B 184 ? 0.7574 0.7086 0.7117 -0.0684 0.0270 -0.0553 212 GLN B CG 2811 C CD . GLN B 184 ? 0.8480 0.7871 0.7898 -0.0698 0.0271 -0.0580 212 GLN B CD 2812 O OE1 . GLN B 184 ? 0.8551 0.7891 0.7904 -0.0659 0.0255 -0.0583 212 GLN B OE1 2813 N NE2 . GLN B 184 ? 0.8493 0.7846 0.7878 -0.0755 0.0290 -0.0600 212 GLN B NE2 2814 N N . MET B 185 ? 0.5029 0.4680 0.4728 -0.0545 0.0226 -0.0475 213 MET B N 2815 C CA . MET B 185 ? 0.5402 0.5063 0.5103 -0.0494 0.0207 -0.0458 213 MET B CA 2816 C C . MET B 185 ? 0.5445 0.5073 0.5072 -0.0467 0.0196 -0.0472 213 MET B C 2817 O O . MET B 185 ? 0.5411 0.4937 0.4943 -0.0479 0.0201 -0.0497 213 MET B O 2818 C CB . MET B 185 ? 0.5617 0.5185 0.5275 -0.0484 0.0210 -0.0458 213 MET B CB 2819 C CG . MET B 185 ? 0.6966 0.6548 0.6632 -0.0433 0.0190 -0.0441 213 MET B CG 2820 S SD . MET B 185 ? 1.1707 1.1154 1.1293 -0.0420 0.0191 -0.0449 213 MET B SD 2821 C CE . MET B 185 ? 0.9468 0.8903 0.9007 -0.0358 0.0166 -0.0448 213 MET B CE 2822 N N . GLY B 186 ? 0.5900 0.5612 0.5567 -0.0430 0.0179 -0.0457 214 GLY B N 2823 C CA . GLY B 186 ? 0.5469 0.5160 0.5071 -0.0397 0.0167 -0.0470 214 GLY B CA 2824 C C . GLY B 186 ? 0.5666 0.5392 0.5257 -0.0415 0.0168 -0.0484 214 GLY B C 2825 O O . GLY B 186 ? 0.6157 0.5876 0.5699 -0.0386 0.0157 -0.0495 214 GLY B O 2826 N N . GLN B 187 ? 0.4475 0.4244 0.4116 -0.0459 0.0180 -0.0483 215 GLN B N 2827 C CA . GLN B 187 ? 0.4741 0.4564 0.4391 -0.0476 0.0179 -0.0492 215 GLN B CA 2828 C C . GLN B 187 ? 0.5375 0.5316 0.5086 -0.0442 0.0163 -0.0472 215 GLN B C 2829 O O . GLN B 187 ? 0.5513 0.5531 0.5303 -0.0427 0.0158 -0.0444 215 GLN B O 2830 C CB . GLN B 187 ? 0.4099 0.3963 0.3807 -0.0528 0.0193 -0.0493 215 GLN B CB 2831 C CG . GLN B 187 ? 0.4428 0.4353 0.4152 -0.0551 0.0192 -0.0503 215 GLN B CG 2832 C CD . GLN B 187 ? 0.5337 0.5268 0.5090 -0.0606 0.0208 -0.0513 215 GLN B CD 2833 O OE1 . GLN B 187 ? 0.5876 0.5754 0.5624 -0.0628 0.0222 -0.0517 215 GLN B OE1 2834 N NE2 . GLN B 187 ? 0.4725 0.4731 0.4514 -0.0628 0.0206 -0.0518 215 GLN B NE2 2835 N N . ILE B 188 ? 0.5453 0.5403 0.5121 -0.0429 0.0156 -0.0485 216 ILE B N 2836 C CA . ILE B 188 ? 0.4738 0.4797 0.4453 -0.0398 0.0143 -0.0468 216 ILE B CA 2837 C C . ILE B 188 ? 0.4620 0.4773 0.4402 -0.0430 0.0144 -0.0461 216 ILE B C 2838 O O . ILE B 188 ? 0.5313 0.5439 0.5060 -0.0459 0.0149 -0.0483 216 ILE B O 2839 C CB . ILE B 188 ? 0.4338 0.4358 0.3966 -0.0362 0.0133 -0.0489 216 ILE B CB 2840 C CG1 . ILE B 188 ? 0.4014 0.3926 0.3565 -0.0330 0.0130 -0.0501 216 ILE B CG1 2841 C CG2 . ILE B 188 ? 0.3265 0.3402 0.2941 -0.0329 0.0121 -0.0471 216 ILE B CG2 2842 C CD1 . ILE B 188 ? 0.5330 0.5285 0.4937 -0.0300 0.0125 -0.0474 216 ILE B CD1 2843 N N . LEU B 189 ? 0.4256 0.4517 0.4133 -0.0425 0.0139 -0.0430 217 LEU B N 2844 C CA . LEU B 189 ? 0.4289 0.4642 0.4233 -0.0451 0.0137 -0.0421 217 LEU B CA 2845 C C . LEU B 189 ? 0.4220 0.4666 0.4184 -0.0425 0.0124 -0.0407 217 LEU B C 2846 O O . LEU B 189 ? 0.4630 0.5109 0.4602 -0.0388 0.0116 -0.0391 217 LEU B O 2847 C CB . LEU B 189 ? 0.4436 0.4844 0.4474 -0.0468 0.0139 -0.0395 217 LEU B CB 2848 C CG . LEU B 189 ? 0.4761 0.5107 0.4806 -0.0498 0.0153 -0.0403 217 LEU B CG 2849 C CD1 . LEU B 189 ? 0.3079 0.3504 0.3227 -0.0505 0.0150 -0.0373 217 LEU B CD1 2850 C CD2 . LEU B 189 ? 0.4198 0.4504 0.4207 -0.0539 0.0165 -0.0432 217 LEU B CD2 2851 N N . ASP B 190 ? 0.4105 0.4600 0.4081 -0.0445 0.0122 -0.0414 218 ASP B N 2852 C CA . ASP B 190 ? 0.3933 0.4524 0.3935 -0.0426 0.0110 -0.0399 218 ASP B CA 2853 C C . ASP B 190 ? 0.4903 0.5594 0.5008 -0.0441 0.0104 -0.0367 218 ASP B C 2854 O O . ASP B 190 ? 0.5792 0.6509 0.5930 -0.0473 0.0105 -0.0372 218 ASP B O 2855 C CB . ASP B 190 ? 0.3617 0.4196 0.3564 -0.0438 0.0108 -0.0427 218 ASP B CB 2856 C CG . ASP B 190 ? 0.3810 0.4491 0.3781 -0.0422 0.0096 -0.0414 218 ASP B CG 2857 O OD1 . ASP B 190 ? 0.2722 0.3488 0.2754 -0.0403 0.0089 -0.0381 218 ASP B OD1 2858 O OD2 . ASP B 190 ? 0.4565 0.5238 0.4492 -0.0432 0.0093 -0.0436 218 ASP B OD2 2859 N N . VAL B 191 ? 0.5122 0.5866 0.5273 -0.0416 0.0098 -0.0336 219 VAL B N 2860 C CA . VAL B 191 ? 0.4300 0.5131 0.4542 -0.0425 0.0090 -0.0302 219 VAL B CA 2861 C C . VAL B 191 ? 0.4226 0.5154 0.4492 -0.0413 0.0078 -0.0283 219 VAL B C 2862 O O . VAL B 191 ? 0.5091 0.6053 0.5350 -0.0384 0.0074 -0.0268 219 VAL B O 2863 C CB . VAL B 191 ? 0.3739 0.4569 0.4017 -0.0409 0.0089 -0.0277 219 VAL B CB 2864 C CG1 . VAL B 191 ? 0.3291 0.4197 0.3658 -0.0422 0.0080 -0.0243 219 VAL B CG1 2865 C CG2 . VAL B 191 ? 0.3836 0.4563 0.4082 -0.0417 0.0101 -0.0295 219 VAL B CG2 2866 N N . PRO B 192 ? 0.4361 0.5340 0.4657 -0.0435 0.0073 -0.0283 220 PRO B N 2867 C CA . PRO B 192 ? 0.4274 0.5342 0.4583 -0.0424 0.0061 -0.0266 220 PRO B CA 2868 C C . PRO B 192 ? 0.4650 0.5797 0.5034 -0.0420 0.0050 -0.0223 220 PRO B C 2869 O O . PRO B 192 ? 0.4751 0.5933 0.5190 -0.0440 0.0043 -0.0210 220 PRO B O 2870 C CB . PRO B 192 ? 0.4683 0.5763 0.4989 -0.0452 0.0059 -0.0286 220 PRO B CB 2871 C CG . PRO B 192 ? 0.4153 0.5173 0.4474 -0.0481 0.0068 -0.0303 220 PRO B CG 2872 C CD . PRO B 192 ? 0.3854 0.4816 0.4175 -0.0470 0.0077 -0.0296 220 PRO B CD 2873 N N . LEU B 193 ? 0.4765 0.5938 0.5149 -0.0394 0.0049 -0.0202 221 LEU B N 2874 C CA . LEU B 193 ? 0.5007 0.6251 0.5456 -0.0392 0.0038 -0.0159 221 LEU B CA 2875 C C . LEU B 193 ? 0.6054 0.7385 0.6528 -0.0398 0.0025 -0.0139 221 LEU B C 2876 O O . LEU B 193 ? 0.6196 0.7565 0.6635 -0.0384 0.0025 -0.0143 221 LEU B O 2877 C CB . LEU B 193 ? 0.4264 0.5520 0.4706 -0.0366 0.0039 -0.0142 221 LEU B CB 2878 C CG . LEU B 193 ? 0.4610 0.5803 0.5056 -0.0360 0.0045 -0.0142 221 LEU B CG 2879 C CD1 . LEU B 193 ? 0.4607 0.5702 0.5014 -0.0369 0.0056 -0.0178 221 LEU B CD1 2880 C CD2 . LEU B 193 ? 0.3619 0.4828 0.4042 -0.0330 0.0047 -0.0136 221 LEU B CD2 2881 N N . PRO B 194 ? 0.7170 0.8534 0.7706 -0.0416 0.0014 -0.0116 222 PRO B N 2882 C CA . PRO B 194 ? 0.7280 0.8720 0.7848 -0.0426 -0.0001 -0.0095 222 PRO B CA 2883 C C . PRO B 194 ? 0.7059 0.8575 0.7621 -0.0412 -0.0009 -0.0067 222 PRO B C 2884 O O . PRO B 194 ? 0.9161 1.0727 0.9724 -0.0419 -0.0019 -0.0063 222 PRO B O 2885 C CB . PRO B 194 ? 0.6232 0.7677 0.6868 -0.0439 -0.0012 -0.0068 222 PRO B CB 2886 C CG . PRO B 194 ? 0.5718 0.7090 0.6356 -0.0439 -0.0001 -0.0080 222 PRO B CG 2887 C CD . PRO B 194 ? 0.6318 0.7635 0.6892 -0.0428 0.0016 -0.0113 222 PRO B CD 2888 N N . VAL B 195 ? 0.5323 0.6854 0.5881 -0.0395 -0.0005 -0.0049 223 VAL B N 2889 C CA . VAL B 195 ? 0.7034 0.8646 0.7586 -0.0384 -0.0009 -0.0022 223 VAL B CA 2890 C C . VAL B 195 ? 0.8154 0.9824 0.8759 -0.0399 -0.0027 0.0022 223 VAL B C 2891 O O . VAL B 195 ? 0.8260 0.9959 0.8875 -0.0411 -0.0038 0.0026 223 VAL B O 2892 C CB . VAL B 195 ? 0.7431 0.9070 0.7929 -0.0375 -0.0006 -0.0045 223 VAL B CB 2893 C CG1 . VAL B 195 ? 0.6396 0.8125 0.6893 -0.0368 -0.0012 -0.0015 223 VAL B CG1 2894 C CG2 . VAL B 195 ? 0.7662 0.9245 0.8099 -0.0355 0.0009 -0.0085 223 VAL B CG2 2895 N N . ALA C 1 ? 0.8862 0.9673 0.9693 -0.0445 -0.0895 0.0910 29 ALA C N 2896 C CA . ALA C 1 ? 0.8391 0.9261 0.9252 -0.0404 -0.0898 0.0870 29 ALA C CA 2897 C C . ALA C 1 ? 0.7620 0.8603 0.8508 -0.0417 -0.0848 0.0840 29 ALA C C 2898 O O . ALA C 1 ? 0.6547 0.7571 0.7401 -0.0452 -0.0834 0.0870 29 ALA C O 2899 C CB . ALA C 1 ? 0.8112 0.8958 0.8926 -0.0391 -0.0946 0.0903 29 ALA C CB 2900 N N . ASN C 2 ? 0.8121 0.9147 0.9067 -0.0390 -0.0822 0.0783 30 ASN C N 2901 C CA . ASN C 2 ? 0.7667 0.8794 0.8641 -0.0395 -0.0778 0.0746 30 ASN C CA 2902 C C . ASN C 2 ? 0.7378 0.8544 0.8322 -0.0441 -0.0746 0.0773 30 ASN C C 2903 O O . ASN C 2 ? 0.7939 0.9070 0.8877 -0.0467 -0.0733 0.0791 30 ASN C O 2904 C CB . ASN C 2 ? 0.8775 0.9961 0.9754 -0.0370 -0.0792 0.0727 30 ASN C CB 2905 C CG . ASN C 2 ? 0.8155 0.9391 0.9195 -0.0339 -0.0770 0.0662 30 ASN C CG 2906 O OD1 . ASN C 2 ? 0.8729 0.9974 0.9802 -0.0344 -0.0733 0.0630 30 ASN C OD1 2907 N ND2 . ASN C 2 ? 0.5312 0.6582 0.6366 -0.0308 -0.0794 0.0643 30 ASN C ND2 2908 N N . PHE C 3 ? 0.6640 0.7881 0.7567 -0.0451 -0.0734 0.0775 31 PHE C N 2909 C CA . PHE C 3 ? 0.5785 0.7062 0.6672 -0.0492 -0.0714 0.0810 31 PHE C CA 2910 C C . PHE C 3 ? 0.6191 0.7456 0.7021 -0.0503 -0.0751 0.0860 31 PHE C C 2911 O O . PHE C 3 ? 0.5933 0.7221 0.6758 -0.0480 -0.0772 0.0852 31 PHE C O 2912 C CB . PHE C 3 ? 0.4708 0.6078 0.5607 -0.0497 -0.0672 0.0777 31 PHE C CB 2913 C CG . PHE C 3 ? 0.5203 0.6588 0.6148 -0.0491 -0.0633 0.0730 31 PHE C CG 2914 C CD1 . PHE C 3 ? 0.5600 0.6921 0.6571 -0.0486 -0.0633 0.0723 31 PHE C CD1 2915 C CD2 . PHE C 3 ? 0.5889 0.7348 0.6848 -0.0490 -0.0596 0.0693 31 PHE C CD2 2916 C CE1 . PHE C 3 ? 0.6697 0.8028 0.7706 -0.0481 -0.0597 0.0680 31 PHE C CE1 2917 C CE2 . PHE C 3 ? 0.5469 0.6935 0.6464 -0.0485 -0.0561 0.0649 31 PHE C CE2 2918 C CZ . PHE C 3 ? 0.5727 0.7130 0.6747 -0.0481 -0.0561 0.0644 31 PHE C CZ 2919 N N . THR C 4 ? 0.6497 0.7734 0.7283 -0.0541 -0.0756 0.0912 32 THR C N 2920 C CA . THR C 4 ? 0.6542 0.7765 0.7267 -0.0557 -0.0789 0.0962 32 THR C CA 2921 C C . THR C 4 ? 0.6229 0.7546 0.6931 -0.0569 -0.0768 0.0963 32 THR C C 2922 O O . THR C 4 ? 0.5065 0.6453 0.5788 -0.0578 -0.0725 0.0936 32 THR C O 2923 C CB . THR C 4 ? 0.5773 0.6932 0.6454 -0.0598 -0.0803 0.1020 32 THR C CB 2924 O OG1 . THR C 4 ? 0.5500 0.6711 0.6188 -0.0635 -0.0759 0.1024 32 THR C OG1 2925 C CG2 . THR C 4 ? 0.4477 0.5531 0.5172 -0.0583 -0.0832 0.1022 32 THR C CG2 2926 N N . CYS C 5 ? 0.5316 0.6627 0.5971 -0.0568 -0.0802 0.0994 33 CYS C N 2927 C CA . CYS C 5 ? 0.5685 0.7076 0.6309 -0.0577 -0.0788 0.0998 33 CYS C CA 2928 C C . CYS C 5 ? 0.4834 0.6194 0.5383 -0.0600 -0.0824 0.1058 33 CYS C C 2929 O O . CYS C 5 ? 0.5826 0.7121 0.6355 -0.0579 -0.0870 0.1075 33 CYS C O 2930 C CB . CYS C 5 ? 0.6290 0.7725 0.6947 -0.0535 -0.0793 0.0948 33 CYS C CB 2931 S SG . CYS C 5 ? 0.5317 0.6854 0.5945 -0.0540 -0.0775 0.0940 33 CYS C SG 2932 N N . ALA C 6 ? 0.5041 0.6452 0.5549 -0.0639 -0.0802 0.1090 34 ALA C N 2933 C CA . ALA C 6 ? 0.5991 0.7364 0.6423 -0.0669 -0.0832 0.1153 34 ALA C CA 2934 C C . ALA C 6 ? 0.6466 0.7902 0.6852 -0.0670 -0.0836 0.1163 34 ALA C C 2935 O O . ALA C 6 ? 0.5615 0.7035 0.5932 -0.0701 -0.0852 0.1216 34 ALA C O 2936 C CB . ALA C 6 ? 0.4345 0.5711 0.4754 -0.0722 -0.0811 0.1194 34 ALA C CB 2937 N N . VAL C 7 ? 0.5644 0.7148 0.6062 -0.0639 -0.0820 0.1113 35 VAL C N 2938 C CA . VAL C 7 ? 0.4463 0.6023 0.4837 -0.0636 -0.0826 0.1119 35 VAL C CA 2939 C C . VAL C 7 ? 0.4849 0.6351 0.5200 -0.0604 -0.0882 0.1129 35 VAL C C 2940 O O . VAL C 7 ? 0.5487 0.6909 0.5857 -0.0584 -0.0914 0.1130 35 VAL C O 2941 C CB . VAL C 7 ? 0.4457 0.6112 0.4870 -0.0617 -0.0788 0.1062 35 VAL C CB 2942 C CG1 . VAL C 7 ? 0.3772 0.5479 0.4207 -0.0644 -0.0734 0.1051 35 VAL C CG1 2943 C CG2 . VAL C 7 ? 0.3883 0.5527 0.4363 -0.0570 -0.0799 0.1006 35 VAL C CG2 2944 N N . ALA C 8 ? 0.4518 0.6059 0.4825 -0.0598 -0.0896 0.1136 36 ALA C N 2945 C CA . ALA C 8 ? 0.5157 0.6649 0.5436 -0.0567 -0.0952 0.1147 36 ALA C CA 2946 C C . ALA C 8 ? 0.5749 0.7235 0.6099 -0.0516 -0.0966 0.1091 36 ALA C C 2947 O O . ALA C 8 ? 0.6355 0.7910 0.6761 -0.0501 -0.0934 0.1038 36 ALA C O 2948 C CB . ALA C 8 ? 0.5057 0.6603 0.5278 -0.0570 -0.0960 0.1160 36 ALA C CB 2949 N N . SER C 9 ? 0.5539 0.6941 0.5885 -0.0489 -0.1015 0.1104 37 SER C N 2950 C CA . SER C 9 ? 0.5689 0.7085 0.6099 -0.0438 -0.1035 0.1053 37 SER C CA 2951 C C . SER C 9 ? 0.5311 0.6794 0.5736 -0.0412 -0.1035 0.1014 37 SER C C 2952 O O . SER C 9 ? 0.4254 0.5758 0.4620 -0.0419 -0.1052 0.1039 37 SER C O 2953 C CB . SER C 9 ? 0.5469 0.6761 0.5853 -0.0412 -0.1096 0.1081 37 SER C CB 2954 O OG . SER C 9 ? 0.6194 0.7489 0.6636 -0.0358 -0.1119 0.1033 37 SER C OG 2955 N N . GLY C 10 ? 0.4944 0.6476 0.5445 -0.0385 -0.1015 0.0953 38 GLY C N 2956 C CA . GLY C 10 ? 0.3912 0.5524 0.4432 -0.0362 -0.1015 0.0912 38 GLY C CA 2957 C C . GLY C 10 ? 0.3818 0.5515 0.4345 -0.0388 -0.0960 0.0888 38 GLY C C 2958 O O . GLY C 10 ? 0.4632 0.6399 0.5178 -0.0374 -0.0952 0.0848 38 GLY C O 2959 N N . THR C 11 ? 0.3962 0.5652 0.4469 -0.0427 -0.0925 0.0914 39 THR C N 2960 C CA . THR C 11 ? 0.4761 0.6525 0.5279 -0.0450 -0.0871 0.0889 39 THR C CA 2961 C C . THR C 11 ? 0.5735 0.7524 0.6333 -0.0431 -0.0842 0.0828 39 THR C C 2962 O O . THR C 11 ? 0.5546 0.7283 0.6186 -0.0420 -0.0847 0.0820 39 THR C O 2963 C CB . THR C 11 ? 0.5040 0.6790 0.5522 -0.0493 -0.0841 0.0931 39 THR C CB 2964 O OG1 . THR C 11 ? 0.6646 0.8377 0.7051 -0.0515 -0.0866 0.0989 39 THR C OG1 2965 C CG2 . THR C 11 ? 0.2982 0.4809 0.3477 -0.0512 -0.0786 0.0902 39 THR C CG2 2966 N N . THR C 12 ? 0.5636 0.7499 0.6251 -0.0428 -0.0813 0.0784 40 THR C N 2967 C CA . THR C 12 ? 0.4603 0.6492 0.5286 -0.0419 -0.0779 0.0727 40 THR C CA 2968 C C . THR C 12 ? 0.4095 0.6034 0.4768 -0.0445 -0.0727 0.0714 40 THR C C 2969 O O . THR C 12 ? 0.4740 0.6718 0.5361 -0.0462 -0.0718 0.0733 40 THR C O 2970 C CB . THR C 12 ? 0.3873 0.5805 0.4598 -0.0388 -0.0791 0.0674 40 THR C CB 2971 O OG1 . THR C 12 ? 0.4694 0.6691 0.5384 -0.0394 -0.0785 0.0665 40 THR C OG1 2972 C CG2 . THR C 12 ? 0.3437 0.5330 0.4177 -0.0355 -0.0844 0.0680 40 THR C CG2 2973 N N . CYS C 13 ? 0.3296 0.5229 0.4016 -0.0447 -0.0693 0.0682 41 CYS C N 2974 C CA . CYS C 13 ? 0.3339 0.5317 0.4056 -0.0465 -0.0644 0.0660 41 CYS C CA 2975 C C . CYS C 13 ? 0.4397 0.6376 0.5174 -0.0453 -0.0617 0.0604 41 CYS C C 2976 O O . CYS C 13 ? 0.4074 0.6025 0.4898 -0.0432 -0.0634 0.0583 41 CYS C O 2977 C CB . CYS C 13 ? 0.2632 0.4592 0.3318 -0.0494 -0.0624 0.0702 41 CYS C CB 2978 S SG . CYS C 13 ? 0.5354 0.7233 0.6077 -0.0497 -0.0630 0.0720 41 CYS C SG 2979 N N . LYS C 14 ? 0.4895 0.6907 0.5670 -0.0465 -0.0574 0.0579 42 LYS C N 2980 C CA . LYS C 14 ? 0.4470 0.6478 0.5293 -0.0458 -0.0545 0.0529 42 LYS C CA 2981 C C . LYS C 14 ? 0.5248 0.7205 0.6091 -0.0468 -0.0529 0.0543 42 LYS C C 2982 O O . LYS C 14 ? 0.4971 0.6928 0.5785 -0.0487 -0.0514 0.0575 42 LYS C O 2983 C CB . LYS C 14 ? 0.4192 0.6251 0.4997 -0.0465 -0.0509 0.0494 42 LYS C CB 2984 C CG . LYS C 14 ? 0.6647 0.8759 0.7416 -0.0462 -0.0523 0.0487 42 LYS C CG 2985 C CD . LYS C 14 ? 0.7226 0.9383 0.7965 -0.0470 -0.0488 0.0460 42 LYS C CD 2986 C CE . LYS C 14 ? 0.8054 1.0261 0.8747 -0.0469 -0.0503 0.0463 42 LYS C CE 2987 N NZ . LYS C 14 ? 0.8283 1.0532 0.8938 -0.0476 -0.0471 0.0439 42 LYS C NZ 2988 N N . SER C 15 ? 0.6179 0.8097 0.7072 -0.0454 -0.0532 0.0519 43 SER C N 2989 C CA . SER C 15 ? 0.6336 0.8206 0.7251 -0.0461 -0.0513 0.0523 43 SER C CA 2990 C C . SER C 15 ? 0.6859 0.8724 0.7821 -0.0450 -0.0490 0.0468 43 SER C C 2991 O O . SER C 15 ? 0.7016 0.8916 0.7991 -0.0439 -0.0489 0.0430 43 SER C O 2992 C CB . SER C 15 ? 0.6156 0.7965 0.7080 -0.0457 -0.0546 0.0560 43 SER C CB 2993 O OG . SER C 15 ? 0.7861 0.9666 0.8738 -0.0473 -0.0565 0.0615 43 SER C OG 2994 N N . ALA C 16 ? 0.7079 0.8901 0.8064 -0.0453 -0.0472 0.0463 44 ALA C N 2995 C CA . ALA C 16 ? 0.7233 0.9043 0.8258 -0.0444 -0.0449 0.0412 44 ALA C CA 2996 C C . ALA C 16 ? 0.6433 0.8180 0.7487 -0.0441 -0.0448 0.0417 44 ALA C C 2997 O O . ALA C 16 ? 0.5848 0.7561 0.6888 -0.0450 -0.0458 0.0458 44 ALA C O 2998 C CB . ALA C 16 ? 0.6588 0.8428 0.7595 -0.0455 -0.0409 0.0381 44 ALA C CB 2999 N N . ILE C 17 ? 0.6179 0.7912 0.7273 -0.0430 -0.0436 0.0374 45 ILE C N 3000 C CA . ILE C 17 ? 0.5969 0.7644 0.7088 -0.0428 -0.0425 0.0368 45 ILE C CA 3001 C C . ILE C 17 ? 0.6410 0.8088 0.7532 -0.0436 -0.0383 0.0328 45 ILE C C 3002 O O . ILE C 17 ? 0.5240 0.6958 0.6360 -0.0436 -0.0368 0.0293 45 ILE C O 3003 C CB . ILE C 17 ? 0.6107 0.7754 0.7270 -0.0406 -0.0447 0.0351 45 ILE C CB 3004 C CG1 . ILE C 17 ? 0.6435 0.8125 0.7626 -0.0396 -0.0437 0.0300 45 ILE C CG1 3005 C CG2 . ILE C 17 ? 0.5761 0.7392 0.6918 -0.0394 -0.0492 0.0391 45 ILE C CG2 3006 C CD1 . ILE C 17 ? 0.5843 0.7517 0.7083 -0.0373 -0.0455 0.0278 45 ILE C CD1 3007 N N . LEU C 18 ? 0.6926 0.8559 0.8048 -0.0442 -0.0366 0.0333 46 LEU C N 3008 C CA . LEU C 18 ? 0.6528 0.8148 0.7654 -0.0446 -0.0330 0.0294 46 LEU C CA 3009 C C . LEU C 18 ? 0.6960 0.8546 0.8128 -0.0433 -0.0331 0.0265 46 LEU C C 3010 O O . LEU C 18 ? 0.6736 0.8272 0.7920 -0.0428 -0.0339 0.0278 46 LEU C O 3011 C CB . LEU C 18 ? 0.6744 0.8336 0.7850 -0.0458 -0.0311 0.0312 46 LEU C CB 3012 C CG . LEU C 18 ? 0.6411 0.7985 0.7513 -0.0460 -0.0275 0.0273 46 LEU C CG 3013 C CD1 . LEU C 18 ? 0.6415 0.8036 0.7492 -0.0464 -0.0257 0.0246 46 LEU C CD1 3014 C CD2 . LEU C 18 ? 0.5156 0.6701 0.6242 -0.0469 -0.0262 0.0293 46 LEU C CD2 3015 N N . TYR C 19 ? 0.7749 0.9366 0.8934 -0.0428 -0.0324 0.0224 47 TYR C N 3016 C CA . TYR C 19 ? 0.6763 0.8365 0.7990 -0.0416 -0.0326 0.0193 47 TYR C CA 3017 C C . TYR C 19 ? 0.5648 0.7219 0.6878 -0.0423 -0.0290 0.0157 47 TYR C C 3018 O O . TYR C 19 ? 0.4740 0.6327 0.5945 -0.0436 -0.0264 0.0134 47 TYR C O 3019 C CB . TYR C 19 ? 0.6432 0.8090 0.7679 -0.0409 -0.0339 0.0169 47 TYR C CB 3020 C CG . TYR C 19 ? 0.7264 0.8917 0.8561 -0.0393 -0.0346 0.0140 47 TYR C CG 3021 C CD1 . TYR C 19 ? 0.6515 0.8141 0.7836 -0.0373 -0.0375 0.0161 47 TYR C CD1 3022 C CD2 . TYR C 19 ? 0.7858 0.9534 0.9175 -0.0399 -0.0322 0.0091 47 TYR C CD2 3023 C CE1 . TYR C 19 ? 0.7327 0.8953 0.8694 -0.0355 -0.0382 0.0133 47 TYR C CE1 3024 C CE2 . TYR C 19 ? 0.7251 0.8931 0.8615 -0.0385 -0.0327 0.0063 47 TYR C CE2 3025 C CZ . TYR C 19 ? 0.7043 0.8701 0.8433 -0.0362 -0.0356 0.0084 47 TYR C CZ 3026 O OH . TYR C 19 ? 0.7240 0.8906 0.8677 -0.0345 -0.0360 0.0055 47 TYR C OH 3027 N N . THR C 20 ? 0.5647 0.7170 0.6902 -0.0415 -0.0289 0.0152 48 THR C N 3028 C CA . THR C 20 ? 0.6433 0.7923 0.7692 -0.0421 -0.0257 0.0116 48 THR C CA 3029 C C . THR C 20 ? 0.5866 0.7376 0.7166 -0.0413 -0.0256 0.0076 48 THR C C 3030 O O . THR C 20 ? 0.4015 0.5521 0.5349 -0.0395 -0.0278 0.0081 48 THR C O 3031 C CB . THR C 20 ? 0.5815 0.7238 0.7072 -0.0418 -0.0255 0.0135 48 THR C CB 3032 O OG1 . THR C 20 ? 0.6966 0.8370 0.8259 -0.0400 -0.0281 0.0143 48 THR C OG1 3033 C CG2 . THR C 20 ? 0.3888 0.5304 0.5112 -0.0426 -0.0263 0.0179 48 THR C CG2 3034 N N . SER C 21 ? 0.6789 0.8323 0.8083 -0.0426 -0.0230 0.0037 49 SER C N 3035 C CA . SER C 21 ? 0.7053 0.8617 0.8386 -0.0424 -0.0226 -0.0002 49 SER C CA 3036 C C . SER C 21 ? 0.6448 0.7966 0.7804 -0.0419 -0.0211 -0.0023 49 SER C C 3037 O O . SER C 21 ? 0.6647 0.8119 0.7978 -0.0432 -0.0182 -0.0034 49 SER C O 3038 C CB . SER C 21 ? 0.6782 0.8383 0.8099 -0.0444 -0.0204 -0.0038 49 SER C CB 3039 O OG . SER C 21 ? 0.7680 0.9320 0.9037 -0.0444 -0.0202 -0.0075 49 SER C OG 3040 N N . PRO C 22 ? 0.6662 0.8190 0.8063 -0.0399 -0.0230 -0.0027 50 PRO C N 3041 C CA . PRO C 22 ? 0.7623 0.9111 0.9047 -0.0391 -0.0217 -0.0046 50 PRO C CA 3042 C C . PRO C 22 ? 0.8052 0.9545 0.9475 -0.0412 -0.0179 -0.0093 50 PRO C C 3043 O O . PRO C 22 ? 0.8158 0.9599 0.9572 -0.0417 -0.0156 -0.0105 50 PRO C O 3044 C CB . PRO C 22 ? 0.7627 0.9148 0.9101 -0.0364 -0.0248 -0.0048 50 PRO C CB 3045 C CG . PRO C 22 ? 0.6957 0.8511 0.8425 -0.0355 -0.0283 -0.0014 50 PRO C CG 3046 C CD . PRO C 22 ? 0.6777 0.8359 0.8209 -0.0380 -0.0266 -0.0016 50 PRO C CD 3047 N N . ASN C 23 ? 0.8737 1.0290 1.0166 -0.0425 -0.0173 -0.0118 51 ASN C N 3048 C CA . ASN C 23 ? 0.8535 1.0101 0.9965 -0.0449 -0.0140 -0.0163 51 ASN C CA 3049 C C . ASN C 23 ? 0.7935 0.9521 0.9324 -0.0474 -0.0127 -0.0171 51 ASN C C 3050 O O . ASN C 23 ? 0.7675 0.9273 0.9041 -0.0470 -0.0145 -0.0143 51 ASN C O 3051 C CB . ASN C 23 ? 0.8648 1.0278 1.0136 -0.0441 -0.0147 -0.0193 51 ASN C CB 3052 C CG . ASN C 23 ? 1.0263 1.1874 1.1790 -0.0413 -0.0159 -0.0190 51 ASN C CG 3053 O OD1 . ASN C 23 ? 1.0615 1.2271 1.2187 -0.0388 -0.0188 -0.0188 51 ASN C OD1 3054 N ND2 . ASN C 23 ? 1.0739 1.2279 1.2247 -0.0415 -0.0139 -0.0189 51 ASN C ND2 3055 N N . ALA C 24 ? 0.6553 0.8137 0.7929 -0.0500 -0.0096 -0.0210 52 ALA C N 3056 C CA . ALA C 24 ? 0.6428 0.8035 0.7768 -0.0524 -0.0086 -0.0224 52 ALA C CA 3057 C C . ALA C 24 ? 0.6144 0.7837 0.7521 -0.0521 -0.0109 -0.0233 52 ALA C C 3058 O O . ALA C 24 ? 0.5541 0.7280 0.6974 -0.0512 -0.0119 -0.0249 52 ALA C O 3059 C CB . ALA C 24 ? 0.5201 0.6778 0.6516 -0.0554 -0.0048 -0.0264 52 ALA C CB 3060 N N . THR C 25 ? 0.6145 0.7862 0.7491 -0.0527 -0.0120 -0.0221 53 THR C N 3061 C CA . THR C 25 ? 0.6998 0.8794 0.8370 -0.0526 -0.0144 -0.0228 53 THR C CA 3062 C C . THR C 25 ? 0.6855 0.8657 0.8174 -0.0546 -0.0137 -0.0232 53 THR C C 3063 O O . THR C 25 ? 0.7342 0.9091 0.8611 -0.0564 -0.0111 -0.0243 53 THR C O 3064 C CB . THR C 25 ? 0.5426 0.7254 0.6826 -0.0494 -0.0185 -0.0190 53 THR C CB 3065 O OG1 . THR C 25 ? 0.5701 0.7476 0.7063 -0.0483 -0.0190 -0.0149 53 THR C OG1 3066 C CG2 . THR C 25 ? 0.5080 0.6927 0.6542 -0.0472 -0.0199 -0.0195 53 THR C CG2 3067 N N . THR C 26 ? 0.6462 0.8324 0.7789 -0.0540 -0.0164 -0.0225 54 THR C N 3068 C CA . THR C 26 ? 0.5325 0.7198 0.6601 -0.0555 -0.0163 -0.0227 54 THR C CA 3069 C C . THR C 26 ? 0.6437 0.8338 0.7706 -0.0532 -0.0196 -0.0186 54 THR C C 3070 O O . THR C 26 ? 0.7045 0.8961 0.8350 -0.0508 -0.0221 -0.0161 54 THR C O 3071 C CB . THR C 26 ? 0.6008 0.7937 0.7297 -0.0578 -0.0162 -0.0267 54 THR C CB 3072 O OG1 . THR C 26 ? 0.6165 0.8168 0.7512 -0.0561 -0.0193 -0.0264 54 THR C OG1 3073 C CG2 . THR C 26 ? 0.6186 0.8094 0.7484 -0.0605 -0.0129 -0.0308 54 THR C CG2 3074 N N . TYR C 27 ? 0.5481 0.7383 0.6697 -0.0540 -0.0195 -0.0180 55 TYR C N 3075 C CA . TYR C 27 ? 0.5610 0.7543 0.6811 -0.0524 -0.0224 -0.0145 55 TYR C CA 3076 C C . TYR C 27 ? 0.6197 0.8201 0.7444 -0.0515 -0.0255 -0.0149 55 TYR C C 3077 O O . TYR C 27 ? 0.7162 0.9184 0.8425 -0.0492 -0.0285 -0.0115 55 TYR C O 3078 C CB . TYR C 27 ? 0.6029 0.7956 0.7164 -0.0535 -0.0214 -0.0146 55 TYR C CB 3079 C CG . TYR C 27 ? 0.6510 0.8372 0.7600 -0.0536 -0.0189 -0.0134 55 TYR C CG 3080 C CD1 . TYR C 27 ? 0.6247 0.8090 0.7331 -0.0518 -0.0198 -0.0091 55 TYR C CD1 3081 C CD2 . TYR C 27 ? 0.6190 0.8009 0.7241 -0.0555 -0.0159 -0.0165 55 TYR C CD2 3082 C CE1 . TYR C 27 ? 0.7049 0.8839 0.8094 -0.0518 -0.0176 -0.0081 55 TYR C CE1 3083 C CE2 . TYR C 27 ? 0.4968 0.6728 0.5976 -0.0552 -0.0138 -0.0156 55 TYR C CE2 3084 C CZ . TYR C 27 ? 0.6882 0.8631 0.7890 -0.0533 -0.0147 -0.0114 55 TYR C CZ 3085 O OH . TYR C 27 ? 0.7660 0.9357 0.8629 -0.0529 -0.0128 -0.0105 55 TYR C OH 3086 N N . GLY C 28 ? 0.5783 0.7826 0.7048 -0.0533 -0.0250 -0.0190 56 GLY C N 3087 C CA . GLY C 28 ? 0.5807 0.7925 0.7119 -0.0525 -0.0279 -0.0201 56 GLY C CA 3088 C C . GLY C 28 ? 0.5900 0.8031 0.7275 -0.0499 -0.0298 -0.0189 56 GLY C C 3089 O O . GLY C 28 ? 0.6049 0.8223 0.7449 -0.0477 -0.0334 -0.0172 56 GLY C O 3090 N N . ASN C 29 ? 0.5759 0.7848 0.7154 -0.0501 -0.0275 -0.0200 57 ASN C N 3091 C CA . ASN C 29 ? 0.7315 0.9407 0.8766 -0.0475 -0.0291 -0.0191 57 ASN C CA 3092 C C . ASN C 29 ? 0.6437 0.8497 0.7875 -0.0447 -0.0317 -0.0139 57 ASN C C 3093 O O . ASN C 29 ? 0.5722 0.7803 0.7198 -0.0419 -0.0348 -0.0125 57 ASN C O 3094 C CB . ASN C 29 ? 0.9125 1.1172 1.0590 -0.0485 -0.0257 -0.0214 57 ASN C CB 3095 C CG . ASN C 29 ? 1.0891 1.2927 1.2404 -0.0456 -0.0271 -0.0202 57 ASN C CG 3096 O OD1 . ASN C 29 ? 1.1641 1.3621 1.3137 -0.0439 -0.0277 -0.0166 57 ASN C OD1 3097 N ND2 . ASN C 29 ? 1.1425 1.3514 1.2997 -0.0450 -0.0275 -0.0233 57 ASN C ND2 3098 N N . LEU C 30 ? 0.5366 0.7373 0.6748 -0.0454 -0.0305 -0.0112 58 LEU C N 3099 C CA . LEU C 30 ? 0.4657 0.6634 0.6021 -0.0434 -0.0327 -0.0061 58 LEU C CA 3100 C C . LEU C 30 ? 0.4756 0.6783 0.6114 -0.0421 -0.0364 -0.0039 58 LEU C C 3101 O O . LEU C 30 ? 0.5676 0.7699 0.7047 -0.0398 -0.0396 -0.0007 58 LEU C O 3102 C CB . LEU C 30 ? 0.6095 0.8017 0.7402 -0.0447 -0.0303 -0.0041 58 LEU C CB 3103 C CG . LEU C 30 ? 0.6215 0.8071 0.7523 -0.0451 -0.0275 -0.0046 58 LEU C CG 3104 C CD1 . LEU C 30 ? 0.6139 0.7952 0.7391 -0.0462 -0.0254 -0.0029 58 LEU C CD1 3105 C CD2 . LEU C 30 ? 0.5636 0.7467 0.6979 -0.0427 -0.0296 -0.0020 58 LEU C CD2 3106 N N . VAL C 31 ? 0.5228 0.7296 0.6561 -0.0437 -0.0361 -0.0056 59 VAL C N 3107 C CA . VAL C 31 ? 0.6214 0.8335 0.7540 -0.0427 -0.0396 -0.0041 59 VAL C CA 3108 C C . VAL C 31 ? 0.6392 0.8555 0.7778 -0.0403 -0.0429 -0.0048 59 VAL C C 3109 O O . VAL C 31 ? 0.7575 0.9752 0.8960 -0.0382 -0.0467 -0.0017 59 VAL C O 3110 C CB . VAL C 31 ? 0.5214 0.7376 0.6511 -0.0449 -0.0386 -0.0070 59 VAL C CB 3111 C CG1 . VAL C 31 ? 0.4194 0.6416 0.5489 -0.0438 -0.0424 -0.0060 59 VAL C CG1 3112 C CG2 . VAL C 31 ? 0.5830 0.7951 0.7061 -0.0466 -0.0359 -0.0060 59 VAL C CG2 3113 N N . ALA C 32 ? 0.5524 0.7708 0.6959 -0.0407 -0.0416 -0.0090 60 ALA C N 3114 C CA . ALA C 32 ? 0.6400 0.8632 0.7898 -0.0382 -0.0445 -0.0103 60 ALA C CA 3115 C C . ALA C 32 ? 0.5654 0.7845 0.7175 -0.0350 -0.0466 -0.0074 60 ALA C C 3116 O O . ALA C 32 ? 0.5969 0.8188 0.7515 -0.0321 -0.0505 -0.0063 60 ALA C O 3117 C CB . ALA C 32 ? 0.5902 0.8176 0.7447 -0.0398 -0.0423 -0.0159 60 ALA C CB 3118 N N . ARG C 33 ? 0.5500 0.7624 0.7012 -0.0354 -0.0441 -0.0066 61 ARG C N 3119 C CA . ARG C 33 ? 0.7148 0.9226 0.8680 -0.0326 -0.0458 -0.0041 61 ARG C CA 3120 C C . ARG C 33 ? 0.7204 0.9254 0.8699 -0.0310 -0.0494 0.0014 61 ARG C C 3121 O O . ARG C 33 ? 0.7298 0.9332 0.8810 -0.0280 -0.0527 0.0035 61 ARG C O 3122 C CB . ARG C 33 ? 0.8663 1.0673 1.0186 -0.0338 -0.0422 -0.0042 61 ARG C CB 3123 C CG . ARG C 33 ? 0.9723 1.1674 1.1256 -0.0313 -0.0439 -0.0014 61 ARG C CG 3124 C CD . ARG C 33 ? 1.0897 1.2782 1.2418 -0.0326 -0.0404 -0.0017 61 ARG C CD 3125 N NE . ARG C 33 ? 1.2333 1.4238 1.3866 -0.0351 -0.0364 -0.0063 61 ARG C NE 3126 C CZ . ARG C 33 ? 1.3090 1.4943 1.4602 -0.0369 -0.0328 -0.0071 61 ARG C CZ 3127 N NH1 . ARG C 33 ? 1.3130 1.4914 1.4614 -0.0365 -0.0327 -0.0038 61 ARG C NH1 3128 N NH2 . ARG C 33 ? 1.2861 1.4729 1.4378 -0.0393 -0.0294 -0.0113 61 ARG C NH2 3129 N N . PHE C 34 ? 0.6124 0.8165 0.7563 -0.0330 -0.0486 0.0037 62 PHE C N 3130 C CA . PHE C 34 ? 0.6366 0.8382 0.7764 -0.0322 -0.0514 0.0090 62 PHE C CA 3131 C C . PHE C 34 ? 0.6332 0.8403 0.7719 -0.0312 -0.0550 0.0099 62 PHE C C 3132 O O . PHE C 34 ? 0.6694 0.8755 0.8076 -0.0289 -0.0589 0.0132 62 PHE C O 3133 C CB . PHE C 34 ? 0.5896 0.7868 0.7240 -0.0345 -0.0487 0.0116 62 PHE C CB 3134 C CG . PHE C 34 ? 0.7347 0.9249 0.8694 -0.0344 -0.0473 0.0131 62 PHE C CG 3135 C CD1 . PHE C 34 ? 0.8137 1.0017 0.9499 -0.0357 -0.0435 0.0099 62 PHE C CD1 3136 C CD2 . PHE C 34 ? 0.6820 0.8675 0.8153 -0.0331 -0.0499 0.0177 62 PHE C CD2 3137 C CE1 . PHE C 34 ? 0.8246 1.0061 0.9610 -0.0354 -0.0424 0.0112 62 PHE C CE1 3138 C CE2 . PHE C 34 ? 0.6447 0.8236 0.7782 -0.0331 -0.0488 0.0190 62 PHE C CE2 3139 C CZ . PHE C 34 ? 0.7505 0.9276 0.8857 -0.0341 -0.0451 0.0157 62 PHE C CZ 3140 N N . ASN C 35 ? 0.5956 0.8083 0.7336 -0.0329 -0.0537 0.0070 63 ASN C N 3141 C CA . ASN C 35 ? 0.5943 0.8128 0.7314 -0.0322 -0.0570 0.0072 63 ASN C CA 3142 C C . ASN C 35 ? 0.6180 0.8342 0.7494 -0.0318 -0.0594 0.0127 63 ASN C C 3143 O O . ASN C 35 ? 0.6164 0.8350 0.7472 -0.0300 -0.0634 0.0144 63 ASN C O 3144 C CB . ASN C 35 ? 0.5506 0.7734 0.6935 -0.0292 -0.0604 0.0052 63 ASN C CB 3145 C CG . ASN C 35 ? 0.6089 0.8392 0.7521 -0.0290 -0.0629 0.0036 63 ASN C CG 3146 O OD1 . ASN C 35 ? 0.6443 0.8775 0.7847 -0.0315 -0.0611 0.0020 63 ASN C OD1 3147 N ND2 . ASN C 35 ? 0.6601 0.8934 0.8064 -0.0258 -0.0672 0.0038 63 ASN C ND2 3148 N N . THR C 36 ? 0.5522 0.7637 0.6793 -0.0337 -0.0569 0.0152 64 THR C N 3149 C CA . THR C 36 ? 0.5311 0.7403 0.6526 -0.0339 -0.0585 0.0205 64 THR C CA 3150 C C . THR C 36 ? 0.5614 0.7731 0.6778 -0.0363 -0.0560 0.0202 64 THR C C 3151 O O . THR C 36 ? 0.5834 0.7951 0.6949 -0.0369 -0.0570 0.0240 64 THR C O 3152 C CB . THR C 36 ? 0.5262 0.7282 0.6465 -0.0341 -0.0575 0.0240 64 THR C CB 3153 O OG1 . THR C 36 ? 0.6278 0.8278 0.7482 -0.0361 -0.0530 0.0218 64 THR C OG1 3154 C CG2 . THR C 36 ? 0.4040 0.6025 0.5285 -0.0315 -0.0601 0.0246 64 THR C CG2 3155 N N . THR C 37 ? 0.5714 0.7855 0.6891 -0.0378 -0.0529 0.0156 65 THR C N 3156 C CA . THR C 37 ? 0.5463 0.7618 0.6590 -0.0400 -0.0503 0.0149 65 THR C CA 3157 C C . THR C 37 ? 0.6878 0.9072 0.8021 -0.0413 -0.0484 0.0094 65 THR C C 3158 O O . THR C 37 ? 0.7675 0.9875 0.8869 -0.0410 -0.0479 0.0060 65 THR C O 3159 C CB . THR C 37 ? 0.5681 0.7786 0.6784 -0.0414 -0.0468 0.0163 65 THR C CB 3160 O OG1 . THR C 37 ? 0.7490 0.9610 0.8543 -0.0431 -0.0443 0.0153 65 THR C OG1 3161 C CG2 . THR C 37 ? 0.5048 0.7120 0.6192 -0.0416 -0.0442 0.0132 65 THR C CG2 3162 N N . THR C 38 ? 0.5858 0.8077 0.6955 -0.0427 -0.0473 0.0085 66 THR C N 3163 C CA . THR C 38 ? 0.4583 0.6830 0.5684 -0.0443 -0.0455 0.0033 66 THR C CA 3164 C C . THR C 38 ? 0.5924 0.8125 0.7009 -0.0460 -0.0411 0.0016 66 THR C C 3165 O O . THR C 38 ? 0.6511 0.8670 0.7571 -0.0459 -0.0397 0.0045 66 THR C O 3166 C CB . THR C 38 ? 0.5307 0.7597 0.6360 -0.0450 -0.0465 0.0028 66 THR C CB 3167 O OG1 . THR C 38 ? 0.6423 0.8690 0.7414 -0.0458 -0.0444 0.0048 66 THR C OG1 3168 C CG2 . THR C 38 ? 0.4645 0.6976 0.5703 -0.0432 -0.0510 0.0052 66 THR C CG2 3169 N N . LEU C 39 ? 0.5995 0.8202 0.7091 -0.0476 -0.0391 -0.0032 67 LEU C N 3170 C CA . LEU C 39 ? 0.5852 0.8011 0.6925 -0.0493 -0.0350 -0.0053 67 LEU C CA 3171 C C . LEU C 39 ? 0.6398 0.8538 0.7402 -0.0497 -0.0334 -0.0036 67 LEU C C 3172 O O . LEU C 39 ? 0.6386 0.8480 0.7374 -0.0496 -0.0313 -0.0021 67 LEU C O 3173 C CB . LEU C 39 ? 0.5689 0.7860 0.6779 -0.0514 -0.0334 -0.0107 67 LEU C CB 3174 C CG . LEU C 39 ? 0.5898 0.8016 0.6955 -0.0533 -0.0294 -0.0134 67 LEU C CG 3175 C CD1 . LEU C 39 ? 0.5066 0.7129 0.6144 -0.0528 -0.0275 -0.0123 67 LEU C CD1 3176 C CD2 . LEU C 39 ? 0.5752 0.7889 0.6825 -0.0557 -0.0284 -0.0185 67 LEU C CD2 3177 N N . PRO C 40 ? 0.6673 0.8850 0.7636 -0.0500 -0.0345 -0.0039 68 PRO C N 3178 C CA . PRO C 40 ? 0.6051 0.8211 0.6948 -0.0502 -0.0327 -0.0027 68 PRO C CA 3179 C C . PRO C 40 ? 0.6368 0.8514 0.7255 -0.0489 -0.0331 0.0025 68 PRO C C 3180 O O . PRO C 40 ? 0.6278 0.8398 0.7127 -0.0490 -0.0308 0.0034 68 PRO C O 3181 C CB . PRO C 40 ? 0.5848 0.8056 0.6706 -0.0505 -0.0344 -0.0035 68 PRO C CB 3182 C CG . PRO C 40 ? 0.5219 0.7470 0.6124 -0.0505 -0.0371 -0.0053 68 PRO C CG 3183 C CD . PRO C 40 ? 0.5955 0.8189 0.6927 -0.0504 -0.0370 -0.0060 68 PRO C CD 3184 N N . ASP C 41 ? 0.6025 0.8187 0.6943 -0.0477 -0.0361 0.0058 69 ASP C N 3185 C CA . ASP C 41 ? 0.5421 0.7565 0.6331 -0.0468 -0.0367 0.0108 69 ASP C CA 3186 C C . ASP C 41 ? 0.5384 0.7474 0.6322 -0.0469 -0.0347 0.0112 69 ASP C C 3187 O O . ASP C 41 ? 0.4994 0.7061 0.5909 -0.0469 -0.0333 0.0139 69 ASP C O 3188 C CB . ASP C 41 ? 0.5659 0.7828 0.6588 -0.0456 -0.0408 0.0142 69 ASP C CB 3189 C CG . ASP C 41 ? 0.6474 0.8692 0.7363 -0.0455 -0.0428 0.0149 69 ASP C CG 3190 O OD1 . ASP C 41 ? 0.5763 0.7995 0.6603 -0.0463 -0.0410 0.0138 69 ASP C OD1 3191 O OD2 . ASP C 41 ? 0.7267 0.9510 0.8171 -0.0445 -0.0464 0.0165 69 ASP C OD2 3192 N N . LEU C 42 ? 0.5031 0.7106 0.6019 -0.0469 -0.0345 0.0083 70 LEU C N 3193 C CA . LEU C 42 ? 0.6044 0.8065 0.7055 -0.0470 -0.0323 0.0079 70 LEU C CA 3194 C C . LEU C 42 ? 0.5210 0.7202 0.6182 -0.0481 -0.0286 0.0060 70 LEU C C 3195 O O . LEU C 42 ? 0.4779 0.6734 0.5740 -0.0480 -0.0270 0.0078 70 LEU C O 3196 C CB . LEU C 42 ? 0.6414 0.8431 0.7482 -0.0469 -0.0325 0.0047 70 LEU C CB 3197 C CG . LEU C 42 ? 0.6254 0.8216 0.7348 -0.0470 -0.0304 0.0040 70 LEU C CG 3198 C CD1 . LEU C 42 ? 0.5968 0.7898 0.7065 -0.0459 -0.0314 0.0086 70 LEU C CD1 3199 C CD2 . LEU C 42 ? 0.5942 0.7911 0.7093 -0.0468 -0.0308 0.0008 70 LEU C CD2 3200 N N . LEU C 43 ? 0.5025 0.7032 0.5972 -0.0491 -0.0274 0.0022 71 LEU C N 3201 C CA . LEU C 43 ? 0.6991 0.8967 0.7893 -0.0499 -0.0243 0.0000 71 LEU C CA 3202 C C . LEU C 43 ? 0.7180 0.9163 0.8034 -0.0492 -0.0238 0.0032 71 LEU C C 3203 O O . LEU C 43 ? 0.6717 0.8665 0.7551 -0.0490 -0.0216 0.0037 71 LEU C O 3204 C CB . LEU C 43 ? 0.7652 0.9644 0.8531 -0.0512 -0.0236 -0.0045 71 LEU C CB 3205 C CG . LEU C 43 ? 0.6706 0.8699 0.7629 -0.0524 -0.0237 -0.0083 71 LEU C CG 3206 C CD1 . LEU C 43 ? 0.5140 0.7157 0.6037 -0.0540 -0.0235 -0.0123 71 LEU C CD1 3207 C CD2 . LEU C 43 ? 0.6992 0.8927 0.7933 -0.0530 -0.0211 -0.0099 71 LEU C CD2 3208 N N . GLY C 44 ? 0.7065 0.9096 0.7900 -0.0488 -0.0260 0.0055 72 GLY C N 3209 C CA . GLY C 44 ? 0.7123 0.9171 0.7913 -0.0483 -0.0255 0.0086 72 GLY C CA 3210 C C . GLY C 44 ? 0.7599 0.9627 0.8405 -0.0479 -0.0255 0.0128 72 GLY C C 3211 O O . GLY C 44 ? 0.7898 0.9918 0.8675 -0.0477 -0.0236 0.0140 72 GLY C O 3212 N N . ALA C 45 ? 0.7977 0.9998 0.8829 -0.0476 -0.0277 0.0150 73 ALA C N 3213 C CA . ALA C 45 ? 0.7224 0.9219 0.8093 -0.0474 -0.0281 0.0190 73 ALA C CA 3214 C C . ALA C 45 ? 0.7391 0.9336 0.8269 -0.0476 -0.0253 0.0176 73 ALA C C 3215 O O . ALA C 45 ? 0.7268 0.9196 0.8144 -0.0476 -0.0249 0.0206 73 ALA C O 3216 C CB . ALA C 45 ? 0.6886 0.8875 0.7802 -0.0469 -0.0312 0.0209 73 ALA C CB 3217 N N . ASN C 46 ? 0.7655 0.9575 0.8540 -0.0478 -0.0235 0.0130 74 ASN C N 3218 C CA . ASN C 46 ? 0.7373 0.9241 0.8261 -0.0479 -0.0210 0.0116 74 ASN C CA 3219 C C . ASN C 46 ? 0.8266 1.0125 0.9105 -0.0480 -0.0182 0.0090 74 ASN C C 3220 O O . ASN C 46 ? 0.9573 1.1386 1.0409 -0.0480 -0.0160 0.0067 74 ASN C O 3221 C CB . ASN C 46 ? 0.5758 0.7591 0.6689 -0.0482 -0.0207 0.0086 74 ASN C CB 3222 C CG . ASN C 46 ? 0.5703 0.7529 0.6684 -0.0476 -0.0231 0.0112 74 ASN C CG 3223 O OD1 . ASN C 46 ? 0.6621 0.8408 0.7619 -0.0474 -0.0228 0.0129 74 ASN C OD1 3224 N ND2 . ASN C 46 ? 0.5217 0.7080 0.6218 -0.0473 -0.0257 0.0116 74 ASN C ND2 3225 N N . GLY C 47 ? 0.7871 0.9773 0.8668 -0.0478 -0.0184 0.0093 75 GLY C N 3226 C CA . GLY C 47 ? 0.7793 0.9689 0.8537 -0.0474 -0.0160 0.0069 75 GLY C CA 3227 C C . GLY C 47 ? 0.8073 0.9930 0.8804 -0.0480 -0.0144 0.0018 75 GLY C C 3228 O O . GLY C 47 ? 0.8946 1.0766 0.9644 -0.0476 -0.0122 -0.0004 75 GLY C O 3229 N N . LEU C 48 ? 0.8082 0.9948 0.8839 -0.0489 -0.0157 -0.0001 76 LEU C N 3230 C CA . LEU C 48 ? 0.7883 0.9716 0.8632 -0.0500 -0.0144 -0.0049 76 LEU C CA 3231 C C . LEU C 48 ? 0.7850 0.9714 0.8558 -0.0505 -0.0149 -0.0073 76 LEU C C 3232 O O . LEU C 48 ? 0.6968 0.8886 0.7673 -0.0501 -0.0169 -0.0053 76 LEU C O 3233 C CB . LEU C 48 ? 0.7652 0.9475 0.8461 -0.0509 -0.0153 -0.0058 76 LEU C CB 3234 C CG . LEU C 48 ? 0.6928 0.8715 0.7778 -0.0505 -0.0149 -0.0038 76 LEU C CG 3235 C CD1 . LEU C 48 ? 0.6148 0.7945 0.7058 -0.0509 -0.0165 -0.0041 76 LEU C CD1 3236 C CD2 . LEU C 48 ? 0.6583 0.8304 0.7410 -0.0507 -0.0121 -0.0060 76 LEU C CD2 3237 N N . PRO C 49 ? 0.8452 1.0278 0.9124 -0.0514 -0.0132 -0.0116 77 PRO C N 3238 C CA . PRO C 49 ? 0.8472 1.0319 0.9101 -0.0520 -0.0136 -0.0143 77 PRO C CA 3239 C C . PRO C 49 ? 0.8934 1.0831 0.9598 -0.0532 -0.0160 -0.0148 77 PRO C C 3240 O O . PRO C 49 ? 0.8047 0.9949 0.8769 -0.0540 -0.0168 -0.0147 77 PRO C O 3241 C CB . PRO C 49 ? 0.7551 0.9332 0.8141 -0.0532 -0.0113 -0.0188 77 PRO C CB 3242 C CG . PRO C 49 ? 0.7942 0.9669 0.8548 -0.0528 -0.0096 -0.0182 77 PRO C CG 3243 C CD . PRO C 49 ? 0.8384 1.0139 0.9047 -0.0519 -0.0107 -0.0139 77 PRO C CD 3244 N N . ASP C 50 ? 0.9493 1.1428 1.0120 -0.0532 -0.0172 -0.0154 78 ASP C N 3245 C CA . ASP C 50 ? 1.0020 1.2009 1.0673 -0.0541 -0.0198 -0.0160 78 ASP C CA 3246 C C . ASP C 50 ? 0.9291 1.1265 0.9975 -0.0563 -0.0195 -0.0199 78 ASP C C 3247 O O . ASP C 50 ? 0.9042 1.1056 0.9779 -0.0569 -0.0215 -0.0199 78 ASP C O 3248 C CB . ASP C 50 ? 1.1072 1.3091 1.1665 -0.0539 -0.0206 -0.0169 78 ASP C CB 3249 C CG . ASP C 50 ? 1.2467 1.4504 1.3020 -0.0518 -0.0204 -0.0135 78 ASP C CG 3250 O OD1 . ASP C 50 ? 1.3031 1.5123 1.3580 -0.0511 -0.0225 -0.0111 78 ASP C OD1 3251 O OD2 . ASP C 50 ? 1.3276 1.5276 1.3805 -0.0508 -0.0182 -0.0131 78 ASP C OD2 3252 N N . GLY C 51 ? 0.8268 1.0184 0.8917 -0.0576 -0.0171 -0.0234 79 GLY C N 3253 C CA . GLY C 51 ? 0.7305 0.9203 0.7970 -0.0603 -0.0165 -0.0275 79 GLY C CA 3254 C C . GLY C 51 ? 0.7007 0.8880 0.7729 -0.0612 -0.0154 -0.0278 79 GLY C C 3255 O O . GLY C 51 ? 0.7477 0.9337 0.8213 -0.0637 -0.0146 -0.0313 79 GLY C O 3256 N N . THR C 52 ? 0.5947 0.7815 0.6703 -0.0593 -0.0154 -0.0243 80 THR C N 3257 C CA . THR C 52 ? 0.5162 0.7005 0.5971 -0.0599 -0.0144 -0.0246 80 THR C CA 3258 C C . THR C 52 ? 0.5829 0.7726 0.6701 -0.0611 -0.0161 -0.0260 80 THR C C 3259 O O . THR C 52 ? 0.5735 0.7693 0.6634 -0.0600 -0.0188 -0.0241 80 THR C O 3260 C CB . THR C 52 ? 0.5422 0.7256 0.6257 -0.0576 -0.0146 -0.0204 80 THR C CB 3261 O OG1 . THR C 52 ? 0.6443 0.8238 0.7223 -0.0564 -0.0131 -0.0191 80 THR C OG1 3262 C CG2 . THR C 52 ? 0.5273 0.7074 0.6157 -0.0581 -0.0134 -0.0210 80 THR C CG2 3263 N N . LEU C 53 ? 0.5502 0.7378 0.6394 -0.0634 -0.0145 -0.0293 81 LEU C N 3264 C CA . LEU C 53 ? 0.6458 0.8392 0.7411 -0.0647 -0.0160 -0.0312 81 LEU C CA 3265 C C . LEU C 53 ? 0.5597 0.7559 0.6619 -0.0626 -0.0174 -0.0285 81 LEU C C 3266 O O . LEU C 53 ? 0.5423 0.7343 0.6449 -0.0611 -0.0165 -0.0262 81 LEU C O 3267 C CB . LEU C 53 ? 0.5581 0.7488 0.6536 -0.0681 -0.0136 -0.0357 81 LEU C CB 3268 C CG . LEU C 53 ? 0.5412 0.7275 0.6295 -0.0709 -0.0119 -0.0391 81 LEU C CG 3269 C CD1 . LEU C 53 ? 0.5819 0.7655 0.6713 -0.0744 -0.0096 -0.0430 81 LEU C CD1 3270 C CD2 . LEU C 53 ? 0.4855 0.6769 0.5715 -0.0715 -0.0141 -0.0401 81 LEU C CD2 3271 N N . SER C 54 ? 0.5178 0.7211 0.6255 -0.0623 -0.0200 -0.0288 82 SER C N 3272 C CA . SER C 54 ? 0.5611 0.7669 0.6753 -0.0600 -0.0216 -0.0265 82 SER C CA 3273 C C . SER C 54 ? 0.5560 0.7586 0.6736 -0.0611 -0.0192 -0.0286 82 SER C C 3274 O O . SER C 54 ? 0.5539 0.7554 0.6754 -0.0592 -0.0196 -0.0267 82 SER C O 3275 C CB . SER C 54 ? 0.5980 0.8122 0.7170 -0.0593 -0.0251 -0.0268 82 SER C CB 3276 O OG . SER C 54 ? 0.7035 0.9214 0.8271 -0.0613 -0.0245 -0.0309 82 SER C OG 3277 N N . SER C 55 ? 0.5692 0.7695 0.6847 -0.0643 -0.0166 -0.0325 83 SER C N 3278 C CA . SER C 55 ? 0.5736 0.7707 0.6916 -0.0658 -0.0140 -0.0349 83 SER C CA 3279 C C . SER C 55 ? 0.6723 0.8601 0.7854 -0.0658 -0.0112 -0.0339 83 SER C C 3280 O O . SER C 55 ? 0.7895 0.9735 0.9036 -0.0671 -0.0088 -0.0356 83 SER C O 3281 C CB . SER C 55 ? 0.5406 0.7399 0.6586 -0.0697 -0.0126 -0.0397 83 SER C CB 3282 O OG . SER C 55 ? 0.6468 0.8416 0.7572 -0.0719 -0.0112 -0.0411 83 SER C OG 3283 N N . ALA C 56 ? 0.5819 0.7664 0.6896 -0.0644 -0.0114 -0.0314 84 ALA C N 3284 C CA . ALA C 56 ? 0.6055 0.7820 0.7090 -0.0638 -0.0092 -0.0301 84 ALA C CA 3285 C C . ALA C 56 ? 0.7324 0.9073 0.8405 -0.0618 -0.0093 -0.0277 84 ALA C C 3286 O O . ALA C 56 ? 0.7328 0.9121 0.8453 -0.0596 -0.0119 -0.0251 84 ALA C O 3287 C CB . ALA C 56 ? 0.4919 0.6668 0.5895 -0.0623 -0.0098 -0.0276 84 ALA C CB 3288 N N . PRO C 57 ? 0.7271 0.8952 0.8336 -0.0624 -0.0067 -0.0286 85 PRO C N 3289 C CA . PRO C 57 ? 0.6643 0.8302 0.7750 -0.0609 -0.0065 -0.0270 85 PRO C CA 3290 C C . PRO C 57 ? 0.6544 0.8180 0.7644 -0.0581 -0.0077 -0.0225 85 PRO C C 3291 O O . PRO C 57 ? 0.7555 0.9166 0.8604 -0.0576 -0.0074 -0.0211 85 PRO C O 3292 C CB . PRO C 57 ? 0.6706 0.8294 0.7783 -0.0630 -0.0031 -0.0298 85 PRO C CB 3293 C CG . PRO C 57 ? 0.6659 0.8210 0.7662 -0.0643 -0.0019 -0.0309 85 PRO C CG 3294 C CD . PRO C 57 ? 0.6135 0.7753 0.7139 -0.0648 -0.0039 -0.0314 85 PRO C CD 3295 N N . VAL C 58 ? 0.5939 0.7586 0.7089 -0.0562 -0.0093 -0.0204 86 VAL C N 3296 C CA . VAL C 58 ? 0.6641 0.8253 0.7786 -0.0540 -0.0100 -0.0164 86 VAL C CA 3297 C C . VAL C 58 ? 0.5991 0.7554 0.7160 -0.0537 -0.0087 -0.0168 86 VAL C C 3298 O O . VAL C 58 ? 0.4887 0.6475 0.6107 -0.0534 -0.0092 -0.0182 86 VAL C O 3299 C CB . VAL C 58 ? 0.4793 0.6452 0.5968 -0.0519 -0.0135 -0.0125 86 VAL C CB 3300 C CG1 . VAL C 58 ? 0.5266 0.6949 0.6398 -0.0518 -0.0145 -0.0107 86 VAL C CG1 3301 C CG2 . VAL C 58 ? 0.6146 0.7864 0.7376 -0.0515 -0.0155 -0.0139 86 VAL C CG2 3302 N N . ALA C 59 ? 0.6083 0.7582 0.7216 -0.0535 -0.0071 -0.0158 87 ALA C N 3303 C CA . ALA C 59 ? 0.6164 0.7608 0.7309 -0.0533 -0.0056 -0.0164 87 ALA C CA 3304 C C . ALA C 59 ? 0.6638 0.8086 0.7828 -0.0510 -0.0079 -0.0133 87 ALA C C 3305 O O . ALA C 59 ? 0.7347 0.8817 0.8541 -0.0496 -0.0103 -0.0098 87 ALA C O 3306 C CB . ALA C 59 ? 0.5048 0.6422 0.6137 -0.0536 -0.0035 -0.0162 87 ALA C CB 3307 N N . ALA C 60 ? 0.6525 0.7950 0.7747 -0.0508 -0.0072 -0.0147 88 ALA C N 3308 C CA . ALA C 60 ? 0.6191 0.7605 0.7450 -0.0485 -0.0092 -0.0121 88 ALA C CA 3309 C C . ALA C 60 ? 0.7437 0.8805 0.8665 -0.0477 -0.0098 -0.0085 88 ALA C C 3310 O O . ALA C 60 ? 0.7358 0.8679 0.8543 -0.0486 -0.0076 -0.0090 88 ALA C O 3311 C CB . ALA C 60 ? 0.5084 0.6472 0.6371 -0.0484 -0.0078 -0.0146 88 ALA C CB 3312 N N . ASN C 61 ? 0.8496 0.9875 0.9744 -0.0460 -0.0127 -0.0047 89 ASN C N 3313 C CA . ASN C 61 ? 0.8502 0.9846 0.9726 -0.0454 -0.0136 -0.0008 89 ASN C CA 3314 C C . ASN C 61 ? 0.7202 0.8566 0.8384 -0.0462 -0.0133 0.0007 89 ASN C C 3315 O O . ASN C 61 ? 0.7228 0.8571 0.8389 -0.0459 -0.0137 0.0037 89 ASN C O 3316 C CB . ASN C 61 ? 0.9197 1.0470 1.0410 -0.0453 -0.0119 -0.0012 89 ASN C CB 3317 C CG . ASN C 61 ? 0.9718 1.0970 1.0972 -0.0441 -0.0127 -0.0020 89 ASN C CG 3318 O OD1 . ASN C 61 ? 0.9538 1.0832 1.0830 -0.0433 -0.0140 -0.0031 89 ASN C OD1 3319 N ND2 . ASN C 61 ? 1.0292 1.1482 1.1538 -0.0437 -0.0120 -0.0016 89 ASN C ND2 3320 N N . SER C 62 ? 0.6795 0.8200 0.7963 -0.0472 -0.0126 -0.0014 90 SER C N 3321 C CA . SER C 62 ? 0.6732 0.8162 0.7860 -0.0476 -0.0126 0.0000 90 SER C CA 3322 C C . SER C 62 ? 0.7280 0.8760 0.8426 -0.0467 -0.0158 0.0035 90 SER C C 3323 O O . SER C 62 ? 0.7750 0.9251 0.8935 -0.0459 -0.0178 0.0038 90 SER C O 3324 C CB . SER C 62 ? 0.5582 0.7031 0.6682 -0.0490 -0.0107 -0.0036 90 SER C CB 3325 O OG . SER C 62 ? 0.5256 0.6764 0.6383 -0.0491 -0.0123 -0.0045 90 SER C OG 3326 N N . THR C 63 ? 0.7452 0.8951 0.8567 -0.0468 -0.0163 0.0063 91 THR C N 3327 C CA . THR C 63 ? 0.7794 0.9334 0.8918 -0.0462 -0.0193 0.0101 91 THR C CA 3328 C C . THR C 63 ? 0.7866 0.9464 0.8970 -0.0466 -0.0197 0.0095 91 THR C C 3329 O O . THR C 63 ? 0.7978 0.9581 0.9045 -0.0474 -0.0177 0.0075 91 THR C O 3330 C CB . THR C 63 ? 0.6389 0.7913 0.7494 -0.0461 -0.0199 0.0144 91 THR C CB 3331 O OG1 . THR C 63 ? 0.6336 0.7869 0.7398 -0.0468 -0.0178 0.0139 91 THR C OG1 3332 C CG2 . THR C 63 ? 0.5598 0.7063 0.6722 -0.0458 -0.0198 0.0151 91 THR C CG2 3333 N N . VAL C 64 ? 0.7738 0.9375 0.8862 -0.0460 -0.0226 0.0112 92 VAL C N 3334 C CA . VAL C 64 ? 0.7092 0.8787 0.8196 -0.0463 -0.0235 0.0111 92 VAL C CA 3335 C C . VAL C 64 ? 0.7175 0.8896 0.8279 -0.0456 -0.0267 0.0157 92 VAL C C 3336 O O . VAL C 64 ? 0.6073 0.7782 0.7209 -0.0446 -0.0291 0.0176 92 VAL C O 3337 C CB . VAL C 64 ? 0.6267 0.7994 0.7397 -0.0463 -0.0239 0.0074 92 VAL C CB 3338 C CG1 . VAL C 64 ? 0.5560 0.7344 0.6665 -0.0467 -0.0249 0.0073 92 VAL C CG1 3339 C CG2 . VAL C 64 ? 0.6352 0.8049 0.7481 -0.0474 -0.0208 0.0028 92 VAL C CG2 3340 N N . LYS C 65 ? 0.6917 0.8673 0.7982 -0.0461 -0.0267 0.0175 93 LYS C N 3341 C CA . LYS C 65 ? 0.6802 0.8587 0.7858 -0.0458 -0.0297 0.0218 93 LYS C CA 3342 C C . LYS C 65 ? 0.6413 0.8238 0.7486 -0.0451 -0.0320 0.0205 93 LYS C C 3343 O O . LYS C 65 ? 0.5489 0.7346 0.6552 -0.0455 -0.0310 0.0172 93 LYS C O 3344 C CB . LYS C 65 ? 0.6338 0.8152 0.7346 -0.0466 -0.0287 0.0239 93 LYS C CB 3345 C CG . LYS C 65 ? 0.6560 0.8343 0.7555 -0.0472 -0.0276 0.0268 93 LYS C CG 3346 C CD . LYS C 65 ? 0.6826 0.8643 0.7776 -0.0479 -0.0258 0.0276 93 LYS C CD 3347 C CE . LYS C 65 ? 0.8533 1.0404 0.9456 -0.0481 -0.0276 0.0301 93 LYS C CE 3348 N NZ . LYS C 65 ? 0.9395 1.1302 1.0274 -0.0487 -0.0260 0.0316 93 LYS C NZ 3349 N N . ILE C 66 ? 0.6282 0.8104 0.7380 -0.0440 -0.0353 0.0230 94 ILE C N 3350 C CA . ILE C 66 ? 0.5891 0.7753 0.7008 -0.0430 -0.0380 0.0220 94 ILE C CA 3351 C C . ILE C 66 ? 0.5806 0.7690 0.6898 -0.0426 -0.0412 0.0264 94 ILE C C 3352 O O . ILE C 66 ? 0.5976 0.7830 0.7075 -0.0419 -0.0436 0.0301 94 ILE C O 3353 C CB . ILE C 66 ? 0.5455 0.7298 0.6626 -0.0415 -0.0393 0.0202 94 ILE C CB 3354 C CG1 . ILE C 66 ? 0.5909 0.7732 0.7102 -0.0421 -0.0360 0.0157 94 ILE C CG1 3355 C CG2 . ILE C 66 ? 0.4619 0.6510 0.5813 -0.0402 -0.0423 0.0190 94 ILE C CG2 3356 C CD1 . ILE C 66 ? 0.5624 0.7436 0.6870 -0.0407 -0.0368 0.0134 94 ILE C CD1 3357 N N . PRO C 67 ? 0.5427 0.7360 0.6487 -0.0431 -0.0414 0.0261 95 PRO C N 3358 C CA . PRO C 67 ? 0.4514 0.6470 0.5543 -0.0430 -0.0443 0.0303 95 PRO C CA 3359 C C . PRO C 67 ? 0.4726 0.6692 0.5783 -0.0412 -0.0483 0.0306 95 PRO C C 3360 O O . PRO C 67 ? 0.4236 0.6220 0.5332 -0.0402 -0.0486 0.0267 95 PRO C O 3361 C CB . PRO C 67 ? 0.5039 0.7045 0.6027 -0.0439 -0.0430 0.0289 95 PRO C CB 3362 C CG . PRO C 67 ? 0.5262 0.7274 0.6266 -0.0443 -0.0401 0.0234 95 PRO C CG 3363 C CD . PRO C 67 ? 0.5271 0.7239 0.6323 -0.0439 -0.0393 0.0216 95 PRO C CD 3364 N N . PHE C 68 ? 0.4869 0.6825 0.5904 -0.0407 -0.0515 0.0353 96 PHE C N 3365 C CA . PHE C 68 ? 0.4272 0.6237 0.5325 -0.0387 -0.0557 0.0360 96 PHE C CA 3366 C C . PHE C 68 ? 0.4646 0.6614 0.5650 -0.0390 -0.0586 0.0411 96 PHE C C 3367 O O . PHE C 68 ? 0.4856 0.6813 0.5819 -0.0408 -0.0573 0.0444 96 PHE C O 3368 C CB . PHE C 68 ? 0.2765 0.4683 0.3866 -0.0369 -0.0573 0.0358 96 PHE C CB 3369 C CG . PHE C 68 ? 0.4363 0.6216 0.5449 -0.0376 -0.0573 0.0400 96 PHE C CG 3370 C CD1 . PHE C 68 ? 0.4374 0.6196 0.5432 -0.0372 -0.0610 0.0451 96 PHE C CD1 3371 C CD2 . PHE C 68 ? 0.4430 0.6250 0.5527 -0.0387 -0.0539 0.0389 96 PHE C CD2 3372 C CE1 . PHE C 68 ? 0.5258 0.7020 0.6302 -0.0382 -0.0611 0.0489 96 PHE C CE1 3373 C CE2 . PHE C 68 ? 0.5242 0.7006 0.6328 -0.0395 -0.0541 0.0427 96 PHE C CE2 3374 C CZ . PHE C 68 ? 0.6033 0.7768 0.7092 -0.0394 -0.0576 0.0477 96 PHE C CZ 3375 N N . ARG C 69 ? 0.4727 0.6712 0.5735 -0.0371 -0.0625 0.0416 97 ARG C N 3376 C CA . ARG C 69 ? 0.4759 0.6740 0.5719 -0.0370 -0.0660 0.0464 97 ARG C CA 3377 C C . ARG C 69 ? 0.5042 0.6952 0.6005 -0.0364 -0.0682 0.0503 97 ARG C C 3378 O O . ARG C 69 ? 0.4158 0.6040 0.5165 -0.0342 -0.0700 0.0489 97 ARG C O 3379 C CB . ARG C 69 ? 0.4088 0.6112 0.5058 -0.0348 -0.0695 0.0445 97 ARG C CB 3380 C CG . ARG C 69 ? 0.6818 0.8849 0.7740 -0.0341 -0.0737 0.0485 97 ARG C CG 3381 C CD . ARG C 69 ? 1.4984 1.7042 1.5942 -0.0310 -0.0777 0.0459 97 ARG C CD 3382 N NE . ARG C 69 ? 1.6139 1.8255 1.7139 -0.0310 -0.0753 0.0399 97 ARG C NE 3383 C CZ . ARG C 69 ? 1.7375 1.9530 1.8422 -0.0288 -0.0773 0.0361 97 ARG C CZ 3384 N NH1 . ARG C 69 ? 1.7607 1.9751 1.8667 -0.0258 -0.0821 0.0373 97 ARG C NH1 3385 N NH2 . ARG C 69 ? 1.8398 2.0603 1.9479 -0.0296 -0.0746 0.0308 97 ARG C NH2 3386 N N . CYS C 70 ? 0.3947 0.5829 0.4864 -0.0386 -0.0678 0.0551 98 CYS C N 3387 C CA . CYS C 70 ? 0.3930 0.5741 0.4838 -0.0386 -0.0702 0.0594 98 CYS C CA 3388 C C . CYS C 70 ? 0.4507 0.6301 0.5368 -0.0380 -0.0749 0.0640 98 CYS C C 3389 O O . CYS C 70 ? 0.4742 0.6573 0.5556 -0.0394 -0.0750 0.0659 98 CYS C O 3390 C CB . CYS C 70 ? 0.3876 0.5666 0.4759 -0.0417 -0.0670 0.0621 98 CYS C CB 3391 S SG . CYS C 70 ? 0.5203 0.6904 0.6063 -0.0428 -0.0697 0.0683 98 CYS C SG 3392 N N . ARG C 71 ? 0.4009 0.5743 0.4878 -0.0360 -0.0788 0.0659 99 ARG C N 3393 C CA . ARG C 71 ? 0.4237 0.5940 0.5053 -0.0356 -0.0835 0.0707 99 ARG C CA 3394 C C . ARG C 71 ? 0.4574 0.6190 0.5360 -0.0369 -0.0853 0.0759 99 ARG C C 3395 O O . ARG C 71 ? 0.5529 0.7091 0.6350 -0.0355 -0.0859 0.0751 99 ARG C O 3396 C CB . ARG C 71 ? 0.4271 0.5979 0.5110 -0.0315 -0.0879 0.0687 99 ARG C CB 3397 C CG . ARG C 71 ? 0.3982 0.5648 0.4763 -0.0306 -0.0931 0.0736 99 ARG C CG 3398 C CD . ARG C 71 ? 0.5001 0.6687 0.5803 -0.0264 -0.0974 0.0712 99 ARG C CD 3399 N NE . ARG C 71 ? 0.6400 0.8046 0.7136 -0.0258 -0.1024 0.0761 99 ARG C NE 3400 C CZ . ARG C 71 ? 0.6552 0.8108 0.7260 -0.0248 -0.1062 0.0800 99 ARG C CZ 3401 N NH1 . ARG C 71 ? 0.5687 0.7186 0.6431 -0.0240 -0.1058 0.0795 99 ARG C NH1 3402 N NH2 . ARG C 71 ? 0.6594 0.8114 0.7234 -0.0245 -0.1106 0.0845 99 ARG C NH2 3403 N N . CYS C 72 ? 0.4580 0.6181 0.5299 -0.0396 -0.0863 0.0812 100 CYS C N 3404 C CA . CYS C 72 ? 0.4787 0.6304 0.5471 -0.0413 -0.0882 0.0864 100 CYS C CA 3405 C C . CYS C 72 ? 0.5096 0.6552 0.5741 -0.0393 -0.0941 0.0898 100 CYS C C 3406 O O . CYS C 72 ? 0.5900 0.7383 0.6507 -0.0387 -0.0965 0.0911 100 CYS C O 3407 C CB . CYS C 72 ? 0.4545 0.6078 0.5178 -0.0461 -0.0856 0.0906 100 CYS C CB 3408 S SG . CYS C 72 ? 0.6008 0.7594 0.6680 -0.0485 -0.0789 0.0874 100 CYS C SG 3409 N N . ASN C 73 ? 0.5229 0.6600 0.5882 -0.0381 -0.0968 0.0913 101 ASN C N 3410 C CA . ASN C 73 ? 0.5900 0.7195 0.6501 -0.0367 -0.1026 0.0954 101 ASN C CA 3411 C C . ASN C 73 ? 0.7488 0.8731 0.8027 -0.0416 -0.1022 0.1016 101 ASN C C 3412 O O . ASN C 73 ? 0.9658 1.0941 1.0202 -0.0453 -0.0976 0.1017 101 ASN C O 3413 C CB . ASN C 73 ? 0.6074 0.7307 0.6714 -0.0321 -0.1062 0.0932 101 ASN C CB 3414 C CG . ASN C 73 ? 0.6967 0.8142 0.7639 -0.0328 -0.1045 0.0927 101 ASN C CG 3415 O OD1 . ASN C 73 ? 0.7176 0.8334 0.7828 -0.0371 -0.1017 0.0955 101 ASN C OD1 3416 N ND2 . ASN C 73 ? 0.5715 0.6866 0.6441 -0.0286 -0.1059 0.0888 101 ASN C ND2 3417 N N . GLY C 74 ? 0.6843 0.8000 0.7321 -0.0418 -0.1070 0.1065 102 GLY C N 3418 C CA . GLY C 74 ? 0.6993 0.8106 0.7408 -0.0470 -0.1066 0.1125 102 GLY C CA 3419 C C . GLY C 74 ? 0.6632 0.7732 0.7075 -0.0501 -0.1027 0.1125 102 GLY C C 3420 O O . GLY C 74 ? 0.6539 0.7646 0.6945 -0.0551 -0.1005 0.1163 102 GLY C O 3421 N N . ASP C 75 ? 0.6950 0.8041 0.7463 -0.0473 -0.1016 0.1079 103 ASP C N 3422 C CA . ASP C 75 ? 0.7121 0.8173 0.7660 -0.0494 -0.0993 0.1080 103 ASP C CA 3423 C C . ASP C 75 ? 0.6919 0.8041 0.7530 -0.0490 -0.0940 0.1026 103 ASP C C 3424 O O . ASP C 75 ? 0.6599 0.7728 0.7218 -0.0524 -0.0906 0.1033 103 ASP C O 3425 C CB . ASP C 75 ? 0.7960 0.8905 0.8504 -0.0463 -0.1037 0.1081 103 ASP C CB 3426 C CG . ASP C 75 ? 0.9526 1.0381 0.9991 -0.0471 -0.1091 0.1140 103 ASP C CG 3427 O OD1 . ASP C 75 ? 0.9359 1.0203 0.9766 -0.0521 -0.1085 0.1191 103 ASP C OD1 3428 O OD2 . ASP C 75 ? 1.0505 1.1304 1.0963 -0.0427 -0.1138 0.1134 103 ASP C OD2 3429 N N . VAL C 76 ? 0.6652 0.7826 0.7314 -0.0450 -0.0933 0.0972 104 VAL C N 3430 C CA . VAL C 76 ? 0.5625 0.6844 0.6356 -0.0440 -0.0891 0.0917 104 VAL C CA 3431 C C . VAL C 76 ? 0.5767 0.7086 0.6527 -0.0424 -0.0868 0.0872 104 VAL C C 3432 O O . VAL C 76 ? 0.5914 0.7253 0.6656 -0.0404 -0.0895 0.0872 104 VAL C O 3433 C CB . VAL C 76 ? 0.7844 0.8998 0.8620 -0.0402 -0.0911 0.0888 104 VAL C CB 3434 C CG1 . VAL C 76 ? 0.6607 0.7771 0.7402 -0.0353 -0.0946 0.0861 104 VAL C CG1 3435 C CG2 . VAL C 76 ? 0.8120 0.9300 0.8957 -0.0400 -0.0867 0.0842 104 VAL C CG2 3436 N N . GLY C 77 ? 0.5687 0.7061 0.6487 -0.0433 -0.0819 0.0834 105 GLY C N 3437 C CA . GLY C 77 ? 0.5486 0.6947 0.6314 -0.0419 -0.0795 0.0788 105 GLY C CA 3438 C C . GLY C 77 ? 0.5417 0.6886 0.6314 -0.0386 -0.0784 0.0729 105 GLY C C 3439 O O . GLY C 77 ? 0.5916 0.7357 0.6844 -0.0390 -0.0762 0.0714 105 GLY C O 3440 N N . GLN C 78 ? 0.4624 0.6134 0.5543 -0.0356 -0.0800 0.0697 106 GLN C N 3441 C CA . GLN C 78 ? 0.4822 0.6347 0.5806 -0.0326 -0.0793 0.0641 106 GLN C CA 3442 C C . GLN C 78 ? 0.5232 0.6847 0.6234 -0.0320 -0.0775 0.0600 106 GLN C C 3443 O O . GLN C 78 ? 0.4468 0.6121 0.5433 -0.0325 -0.0789 0.0616 106 GLN C O 3444 C CB . GLN C 78 ? 0.4373 0.5848 0.5372 -0.0287 -0.0841 0.0642 106 GLN C CB 3445 C CG . GLN C 78 ? 0.5529 0.6905 0.6504 -0.0290 -0.0866 0.0683 106 GLN C CG 3446 C CD . GLN C 78 ? 0.5639 0.6963 0.6607 -0.0251 -0.0923 0.0695 106 GLN C CD 3447 O OE1 . GLN C 78 ? 0.5390 0.6745 0.6341 -0.0234 -0.0953 0.0699 106 GLN C OE1 3448 N NE2 . GLN C 78 ? 0.5767 0.7012 0.6744 -0.0236 -0.0941 0.0701 106 GLN C NE2 3449 N N . SER C 79 ? 0.4495 0.6142 0.5551 -0.0312 -0.0746 0.0547 107 SER C N 3450 C CA . SER C 79 ? 0.4450 0.6177 0.5526 -0.0307 -0.0731 0.0504 107 SER C CA 3451 C C . SER C 79 ? 0.5333 0.7079 0.6413 -0.0276 -0.0777 0.0502 107 SER C C 3452 O O . SER C 79 ? 0.5779 0.7486 0.6882 -0.0248 -0.0809 0.0503 107 SER C O 3453 C CB . SER C 79 ? 0.5237 0.6983 0.6369 -0.0304 -0.0694 0.0449 107 SER C CB 3454 O OG . SER C 79 ? 0.4866 0.6578 0.6044 -0.0276 -0.0711 0.0431 107 SER C OG 3455 N N . ASP C 80 ? 0.4773 0.6578 0.5829 -0.0281 -0.0783 0.0500 108 ASP C N 3456 C CA . ASP C 80 ? 0.3807 0.5625 0.4848 -0.0256 -0.0832 0.0513 108 ASP C CA 3457 C C . ASP C 80 ? 0.4719 0.6577 0.5821 -0.0222 -0.0849 0.0463 108 ASP C C 3458 O O . ASP C 80 ? 0.5366 0.7295 0.6486 -0.0222 -0.0839 0.0427 108 ASP C O 3459 C CB . ASP C 80 ? 0.4466 0.6333 0.5455 -0.0276 -0.0830 0.0529 108 ASP C CB 3460 C CG . ASP C 80 ? 0.4365 0.6234 0.5321 -0.0255 -0.0882 0.0554 108 ASP C CG 3461 O OD1 . ASP C 80 ? 0.5119 0.6943 0.6086 -0.0226 -0.0923 0.0564 108 ASP C OD1 3462 O OD2 . ASP C 80 ? 0.5751 0.7661 0.6664 -0.0268 -0.0884 0.0565 108 ASP C OD2 3463 N N . ARG C 81 ? 0.6464 0.8275 0.7597 -0.0192 -0.0875 0.0462 109 ARG C N 3464 C CA . ARG C 81 ? 0.7287 0.9135 0.8484 -0.0155 -0.0893 0.0415 109 ARG C CA 3465 C C . ARG C 81 ? 0.6806 0.8717 0.8063 -0.0162 -0.0850 0.0354 109 ARG C C 3466 O O . ARG C 81 ? 0.6517 0.8482 0.7826 -0.0138 -0.0860 0.0312 109 ARG C O 3467 C CB . ARG C 81 ? 0.8759 1.0641 0.9944 -0.0127 -0.0943 0.0420 109 ARG C CB 3468 C CG . ARG C 81 ? 1.0616 1.2422 1.1746 -0.0111 -0.0993 0.0477 109 ARG C CG 3469 C CD . ARG C 81 ? 1.2519 1.4261 1.3679 -0.0076 -0.1018 0.0475 109 ARG C CD 3470 N NE . ARG C 81 ? 1.4033 1.5678 1.5132 -0.0072 -0.1055 0.0534 109 ARG C NE 3471 C CZ . ARG C 81 ? 1.5405 1.6985 1.6511 -0.0036 -0.1094 0.0542 109 ARG C CZ 3472 N NH1 . ARG C 81 ? 1.5945 1.7432 1.6987 -0.0038 -0.1127 0.0597 109 ARG C NH1 3473 N NH2 . ARG C 81 ? 1.5672 1.7279 1.6846 0.0003 -0.1100 0.0494 109 ARG C NH2 3474 N N . LEU C 82 ? 0.5765 0.7669 0.7013 -0.0197 -0.0801 0.0351 110 LEU C N 3475 C CA . LEU C 82 ? 0.5522 0.7461 0.6816 -0.0209 -0.0757 0.0299 110 LEU C CA 3476 C C . LEU C 82 ? 0.5817 0.7693 0.7102 -0.0229 -0.0723 0.0313 110 LEU C C 3477 O O . LEU C 82 ? 0.5615 0.7443 0.6852 -0.0244 -0.0726 0.0360 110 LEU C O 3478 C CB . LEU C 82 ? 0.5435 0.7442 0.6714 -0.0235 -0.0731 0.0278 110 LEU C CB 3479 C CG . LEU C 82 ? 0.5234 0.7314 0.6526 -0.0220 -0.0759 0.0255 110 LEU C CG 3480 C CD1 . LEU C 82 ? 0.4954 0.7081 0.6208 -0.0249 -0.0738 0.0250 110 LEU C CD1 3481 C CD2 . LEU C 82 ? 0.3246 0.5375 0.4612 -0.0202 -0.0756 0.0199 110 LEU C CD2 3482 N N . PRO C 83 ? 0.6879 0.8757 0.8209 -0.0232 -0.0689 0.0272 111 PRO C N 3483 C CA . PRO C 83 ? 0.5849 0.7783 0.7240 -0.0220 -0.0679 0.0215 111 PRO C CA 3484 C C . PRO C 83 ? 0.5529 0.7456 0.6965 -0.0179 -0.0713 0.0203 111 PRO C C 3485 O O . PRO C 83 ? 0.6316 0.8179 0.7739 -0.0161 -0.0740 0.0237 111 PRO C O 3486 C CB . PRO C 83 ? 0.5560 0.7474 0.6964 -0.0243 -0.0628 0.0190 111 PRO C CB 3487 C CG . PRO C 83 ? 0.4655 0.6487 0.6028 -0.0248 -0.0627 0.0232 111 PRO C CG 3488 C CD . PRO C 83 ? 0.5765 0.7583 0.7084 -0.0251 -0.0657 0.0284 111 PRO C CD 3489 N N . ILE C 84 ? 0.6532 0.8528 0.8022 -0.0166 -0.0712 0.0155 112 ILE C N 3490 C CA . ILE C 84 ? 0.7083 0.9089 0.8625 -0.0125 -0.0740 0.0134 112 ILE C CA 3491 C C . ILE C 84 ? 0.7155 0.9163 0.8746 -0.0128 -0.0703 0.0092 112 ILE C C 3492 O O . ILE C 84 ? 0.7537 0.9581 0.9139 -0.0158 -0.0662 0.0060 112 ILE C O 3493 C CB . ILE C 84 ? 0.7431 0.9523 0.9004 -0.0104 -0.0771 0.0108 112 ILE C CB 3494 C CG1 . ILE C 84 ? 0.8270 1.0438 0.9850 -0.0138 -0.0738 0.0073 112 ILE C CG1 3495 C CG2 . ILE C 84 ? 0.7783 0.9858 0.9311 -0.0085 -0.0822 0.0153 112 ILE C CG2 3496 C CD1 . ILE C 84 ? 0.8614 1.0847 1.0263 -0.0138 -0.0713 0.0012 112 ILE C CD1 3497 N N . TYR C 85 ? 0.6769 0.8731 0.8383 -0.0099 -0.0718 0.0093 113 TYR C N 3498 C CA . TYR C 85 ? 0.6607 0.8572 0.8268 -0.0097 -0.0686 0.0052 113 TYR C CA 3499 C C . TYR C 85 ? 0.7169 0.9180 0.8890 -0.0053 -0.0714 0.0020 113 TYR C C 3500 O O . TYR C 85 ? 0.8229 1.0206 0.9945 -0.0014 -0.0759 0.0043 113 TYR C O 3501 C CB . TYR C 85 ? 0.6116 0.7985 0.7754 -0.0102 -0.0671 0.0076 113 TYR C CB 3502 C CG . TYR C 85 ? 0.6590 0.8460 0.8271 -0.0103 -0.0634 0.0034 113 TYR C CG 3503 C CD1 . TYR C 85 ? 0.6782 0.8661 0.8459 -0.0142 -0.0583 0.0012 113 TYR C CD1 3504 C CD2 . TYR C 85 ? 0.5655 0.7515 0.7377 -0.0064 -0.0651 0.0015 113 TYR C CD2 3505 C CE1 . TYR C 85 ? 0.5584 0.7460 0.7295 -0.0146 -0.0549 -0.0026 113 TYR C CE1 3506 C CE2 . TYR C 85 ? 0.6698 0.8562 0.8457 -0.0066 -0.0615 -0.0025 113 TYR C CE2 3507 C CZ . TYR C 85 ? 0.6279 0.8150 0.8032 -0.0109 -0.0564 -0.0044 113 TYR C CZ 3508 O OH . TYR C 85 ? 0.6865 0.8736 0.8648 -0.0113 -0.0528 -0.0082 113 TYR C OH 3509 N N . VAL C 86 ? 0.6330 0.8417 0.8106 -0.0057 -0.0688 -0.0034 114 VAL C N 3510 C CA . VAL C 86 ? 0.6490 0.8629 0.8331 -0.0015 -0.0709 -0.0071 114 VAL C CA 3511 C C . VAL C 86 ? 0.6531 0.8625 0.8398 -0.0001 -0.0689 -0.0088 114 VAL C C 3512 O O . VAL C 86 ? 0.5787 0.7873 0.7658 -0.0033 -0.0641 -0.0109 114 VAL C O 3513 C CB . VAL C 86 ? 0.6081 0.8340 0.7976 -0.0024 -0.0697 -0.0122 114 VAL C CB 3514 C CG1 . VAL C 86 ? 0.5660 0.7981 0.7612 0.0027 -0.0738 -0.0147 114 VAL C CG1 3515 C CG2 . VAL C 86 ? 0.5272 0.7567 0.7131 -0.0055 -0.0699 -0.0109 114 VAL C CG2 3516 N N . VAL C 87 ? 0.7190 0.9248 0.9068 0.0047 -0.0727 -0.0078 115 VAL C N 3517 C CA . VAL C 87 ? 0.8711 1.0719 1.0609 0.0067 -0.0715 -0.0092 115 VAL C CA 3518 C C . VAL C 87 ? 1.0199 1.2287 1.2163 0.0063 -0.0677 -0.0154 115 VAL C C 3519 O O . VAL C 87 ? 1.0191 1.2376 1.2208 0.0083 -0.0689 -0.0190 115 VAL C O 3520 C CB . VAL C 87 ? 0.7267 0.9233 0.9169 0.0127 -0.0769 -0.0077 115 VAL C CB 3521 C CG1 . VAL C 87 ? 0.6203 0.8117 0.8124 0.0148 -0.0755 -0.0094 115 VAL C CG1 3522 C CG2 . VAL C 87 ? 0.6418 0.8297 0.8250 0.0129 -0.0809 -0.0015 115 VAL C CG2 3523 N N . GLN C 88 ? 1.0655 1.2701 1.2615 0.0040 -0.0633 -0.0165 116 GLN C N 3524 C CA . GLN C 88 ? 1.0411 1.2523 1.2425 0.0029 -0.0592 -0.0221 116 GLN C CA 3525 C C . GLN C 88 ? 1.1348 1.3443 1.3398 0.0079 -0.0606 -0.0240 116 GLN C C 3526 O O . GLN C 88 ? 1.1325 1.3336 1.3345 0.0110 -0.0639 -0.0206 116 GLN C O 3527 C CB . GLN C 88 ? 0.9600 1.1672 1.1584 -0.0023 -0.0536 -0.0223 116 GLN C CB 3528 C CG . GLN C 88 ? 0.9542 1.1603 1.1475 -0.0068 -0.0525 -0.0196 116 GLN C CG 3529 C CD . GLN C 88 ? 1.0375 1.2539 1.2333 -0.0090 -0.0517 -0.0224 116 GLN C CD 3530 O OE1 . GLN C 88 ? 1.0627 1.2879 1.2644 -0.0076 -0.0518 -0.0267 116 GLN C OE1 3531 N NE2 . GLN C 88 ? 1.0561 1.2717 1.2473 -0.0125 -0.0510 -0.0202 116 GLN C NE2 3532 N N . PRO C 89 ? 1.2071 1.4247 1.4183 0.0085 -0.0582 -0.0294 117 PRO C N 3533 C CA . PRO C 89 ? 1.1995 1.4169 1.4146 0.0135 -0.0592 -0.0319 117 PRO C CA 3534 C C . PRO C 89 ? 1.1936 1.3983 1.4044 0.0152 -0.0598 -0.0289 117 PRO C C 3535 O O . PRO C 89 ? 1.1787 1.3797 1.3897 0.0205 -0.0641 -0.0279 117 PRO C O 3536 C CB . PRO C 89 ? 1.1755 1.4011 1.3957 0.0109 -0.0540 -0.0376 117 PRO C CB 3537 C CG . PRO C 89 ? 1.1435 1.3775 1.3646 0.0065 -0.0523 -0.0388 117 PRO C CG 3538 C CD . PRO C 89 ? 1.1757 1.4040 1.3907 0.0048 -0.0547 -0.0336 117 PRO C CD 3539 N N . GLN C 90 ? 1.1828 1.3806 1.3896 0.0110 -0.0558 -0.0276 118 GLN C N 3540 C CA . GLN C 90 ? 1.2647 1.4506 1.4675 0.0122 -0.0562 -0.0250 118 GLN C CA 3541 C C . GLN C 90 ? 1.2669 1.4431 1.4626 0.0093 -0.0569 -0.0192 118 GLN C C 3542 O O . GLN C 90 ? 1.2921 1.4614 1.4843 0.0064 -0.0539 -0.0180 118 GLN C O 3543 C CB . GLN C 90 ? 1.3276 1.5126 1.5320 0.0109 -0.0513 -0.0285 118 GLN C CB 3544 C CG . GLN C 90 ? 1.3882 1.5758 1.5975 0.0162 -0.0524 -0.0323 118 GLN C CG 3545 C CD . GLN C 90 ? 1.4618 1.6385 1.6678 0.0206 -0.0563 -0.0293 118 GLN C CD 3546 O OE1 . GLN C 90 ? 1.5005 1.6668 1.7006 0.0188 -0.0569 -0.0249 118 GLN C OE1 3547 N NE2 . GLN C 90 ? 1.4564 1.6355 1.6663 0.0264 -0.0590 -0.0319 118 GLN C NE2 3548 N N . ASP C 91 ? 1.1912 1.3677 1.3847 0.0099 -0.0609 -0.0158 119 ASP C N 3549 C CA . ASP C 91 ? 1.0618 1.2303 1.2487 0.0072 -0.0618 -0.0103 119 ASP C CA 3550 C C . ASP C 91 ? 0.9281 1.0865 1.1112 0.0104 -0.0665 -0.0059 119 ASP C C 3551 O O . ASP C 91 ? 0.8655 1.0241 1.0505 0.0154 -0.0706 -0.0065 119 ASP C O 3552 C CB . ASP C 91 ? 1.0763 1.2508 1.2622 0.0051 -0.0629 -0.0088 119 ASP C CB 3553 C CG . ASP C 91 ? 1.1061 1.2846 1.2915 -0.0003 -0.0578 -0.0103 119 ASP C CG 3554 O OD1 . ASP C 91 ? 1.1959 1.3713 1.3807 -0.0026 -0.0537 -0.0117 119 ASP C OD1 3555 O OD2 . ASP C 91 ? 1.0213 1.2058 1.2064 -0.0021 -0.0582 -0.0101 119 ASP C OD2 3556 N N . GLY C 92 ? 0.8048 0.9545 0.9822 0.0075 -0.0659 -0.0016 120 GLY C N 3557 C CA . GLY C 92 ? 0.7614 0.9014 0.9341 0.0092 -0.0703 0.0033 120 GLY C CA 3558 C C . GLY C 92 ? 0.7955 0.9336 0.9630 0.0051 -0.0705 0.0081 120 GLY C C 3559 O O . GLY C 92 ? 0.8186 0.9594 0.9853 0.0008 -0.0664 0.0077 120 GLY C O 3560 N N . LEU C 93 ? 0.7502 0.8835 0.9139 0.0066 -0.0753 0.0126 121 LEU C N 3561 C CA . LEU C 93 ? 0.7720 0.9040 0.9307 0.0030 -0.0760 0.0173 121 LEU C CA 3562 C C . LEU C 93 ? 0.7681 0.8952 0.9235 -0.0015 -0.0722 0.0192 121 LEU C C 3563 O O . LEU C 93 ? 0.6344 0.7649 0.7880 -0.0054 -0.0696 0.0203 121 LEU C O 3564 C CB . LEU C 93 ? 0.7265 0.8514 0.8806 0.0052 -0.0818 0.0222 121 LEU C CB 3565 C CG . LEU C 93 ? 0.7487 0.8753 0.9051 0.0108 -0.0867 0.0210 121 LEU C CG 3566 C CD1 . LEU C 93 ? 0.8539 0.9710 1.0094 0.0145 -0.0896 0.0214 121 LEU C CD1 3567 C CD2 . LEU C 93 ? 0.6608 0.7876 0.8133 0.0110 -0.0909 0.0250 121 LEU C CD2 3568 N N . ASP C 94 ? 0.8550 0.9742 1.0096 -0.0007 -0.0720 0.0195 122 ASP C N 3569 C CA . ASP C 94 ? 0.8283 0.9418 0.9798 -0.0045 -0.0690 0.0215 122 ASP C CA 3570 C C . ASP C 94 ? 0.7394 0.8589 0.8934 -0.0073 -0.0634 0.0176 122 ASP C C 3571 O O . ASP C 94 ? 0.7406 0.8597 0.8919 -0.0113 -0.0606 0.0192 122 ASP C O 3572 C CB . ASP C 94 ? 0.9137 1.0177 1.0642 -0.0025 -0.0705 0.0220 122 ASP C CB 3573 C CG . ASP C 94 ? 1.0152 1.1119 1.1615 -0.0063 -0.0689 0.0253 122 ASP C CG 3574 O OD1 . ASP C 94 ? 1.0247 1.1246 1.1707 -0.0099 -0.0647 0.0248 122 ASP C OD1 3575 O OD2 . ASP C 94 ? 1.0599 1.1477 1.2030 -0.0056 -0.0720 0.0286 122 ASP C OD2 3576 N N . ALA C 95 ? 0.6499 0.7750 0.8090 -0.0053 -0.0617 0.0124 123 ALA C N 3577 C CA . ALA C 95 ? 0.6719 0.8022 0.8331 -0.0080 -0.0564 0.0085 123 ALA C CA 3578 C C . ALA C 95 ? 0.7194 0.8572 0.8802 -0.0107 -0.0551 0.0086 123 ALA C C 3579 O O . ALA C 95 ? 0.6848 0.8240 0.8442 -0.0143 -0.0513 0.0079 123 ALA C O 3580 C CB . ALA C 95 ? 0.6603 0.7950 0.8270 -0.0053 -0.0551 0.0030 123 ALA C CB 3581 N N . ILE C 96 ? 0.7687 0.9110 0.9303 -0.0089 -0.0586 0.0095 124 ILE C N 3582 C CA . ILE C 96 ? 0.7818 0.9308 0.9424 -0.0112 -0.0581 0.0099 124 ILE C CA 3583 C C . ILE C 96 ? 0.6841 0.8284 0.8388 -0.0144 -0.0579 0.0148 124 ILE C C 3584 O O . ILE C 96 ? 0.6364 0.7835 0.7894 -0.0179 -0.0547 0.0146 124 ILE C O 3585 C CB . ILE C 96 ? 0.7318 0.8858 0.8941 -0.0081 -0.0625 0.0101 124 ILE C CB 3586 C CG1 . ILE C 96 ? 0.7149 0.8755 0.8835 -0.0052 -0.0623 0.0048 124 ILE C CG1 3587 C CG2 . ILE C 96 ? 0.7432 0.9028 0.9033 -0.0105 -0.0625 0.0115 124 ILE C CG2 3588 C CD1 . ILE C 96 ? 0.7060 0.8697 0.8767 -0.0007 -0.0674 0.0049 124 ILE C CD1 3589 N N . ALA C 97 ? 0.5541 0.6913 0.7058 -0.0133 -0.0614 0.0192 125 ALA C N 3590 C CA . ALA C 97 ? 0.6066 0.7390 0.7529 -0.0162 -0.0617 0.0242 125 ALA C CA 3591 C C . ALA C 97 ? 0.7137 0.8444 0.8588 -0.0196 -0.0570 0.0234 125 ALA C C 3592 O O . ALA C 97 ? 0.7053 0.8382 0.8477 -0.0227 -0.0550 0.0249 125 ALA C O 3593 C CB . ALA C 97 ? 0.5565 0.6803 0.7001 -0.0146 -0.0658 0.0283 125 ALA C CB 3594 N N . ARG C 98 ? 0.7976 0.9245 0.9448 -0.0187 -0.0552 0.0209 126 ARG C N 3595 C CA . ARG C 98 ? 0.6981 0.8222 0.8439 -0.0216 -0.0512 0.0203 126 ARG C CA 3596 C C . ARG C 98 ? 0.7064 0.8364 0.8542 -0.0233 -0.0466 0.0157 126 ARG C C 3597 O O . ARG C 98 ? 0.6237 0.7538 0.7688 -0.0263 -0.0437 0.0161 126 ARG C O 3598 C CB . ARG C 98 ? 0.5861 0.7024 0.7322 -0.0202 -0.0514 0.0201 126 ARG C CB 3599 C CG . ARG C 98 ? 0.5741 0.6833 0.7175 -0.0191 -0.0558 0.0247 126 ARG C CG 3600 C CD . ARG C 98 ? 0.5885 0.6893 0.7312 -0.0185 -0.0558 0.0249 126 ARG C CD 3601 N NE . ARG C 98 ? 0.5948 0.6892 0.7331 -0.0204 -0.0579 0.0302 126 ARG C NE 3602 C CZ . ARG C 98 ? 0.6608 0.7501 0.7971 -0.0189 -0.0625 0.0337 126 ARG C CZ 3603 N NH1 . ARG C 98 ? 0.7567 0.8464 0.8951 -0.0150 -0.0655 0.0323 126 ARG C NH1 3604 N NH2 . ARG C 98 ? 0.4623 0.5460 0.5944 -0.0213 -0.0641 0.0386 126 ARG C NH2 3605 N N . ASN C 99 ? 0.7057 0.8406 0.8578 -0.0214 -0.0461 0.0114 127 ASN C N 3606 C CA . ASN C 99 ? 0.7945 0.9340 0.9483 -0.0232 -0.0418 0.0069 127 ASN C CA 3607 C C . ASN C 99 ? 0.8462 0.9935 0.9999 -0.0249 -0.0409 0.0058 127 ASN C C 3608 O O . ASN C 99 ? 0.8795 1.0290 1.0325 -0.0275 -0.0373 0.0034 127 ASN C O 3609 C CB . ASN C 99 ? 0.7374 0.8786 0.8958 -0.0210 -0.0408 0.0024 127 ASN C CB 3610 C CG . ASN C 99 ? 0.6950 0.8286 0.8535 -0.0193 -0.0413 0.0027 127 ASN C CG 3611 O OD1 . ASN C 99 ? 0.6933 0.8204 0.8484 -0.0209 -0.0402 0.0050 127 ASN C OD1 3612 N ND2 . ASN C 99 ? 0.6844 0.8190 0.8467 -0.0158 -0.0429 0.0005 127 ASN C ND2 3613 N N . VAL C 100 ? 0.8311 0.9820 0.9851 -0.0235 -0.0445 0.0077 128 VAL C N 3614 C CA . VAL C 100 ? 0.6735 0.8318 0.8273 -0.0250 -0.0440 0.0066 128 VAL C CA 3615 C C . VAL C 100 ? 0.6401 0.7975 0.7889 -0.0270 -0.0446 0.0108 128 VAL C C 3616 O O . VAL C 100 ? 0.6695 0.8302 0.8164 -0.0296 -0.0422 0.0098 128 VAL C O 3617 C CB . VAL C 100 ? 0.6902 0.8546 0.8477 -0.0222 -0.0473 0.0052 128 VAL C CB 3618 C CG1 . VAL C 100 ? 0.6703 0.8426 0.8278 -0.0240 -0.0466 0.0036 128 VAL C CG1 3619 C CG2 . VAL C 100 ? 0.7187 0.8847 0.8816 -0.0199 -0.0468 0.0010 128 VAL C CG2 3620 N N . PHE C 101 ? 0.6072 0.7600 0.7537 -0.0260 -0.0478 0.0154 129 PHE C N 3621 C CA . PHE C 101 ? 0.5700 0.7227 0.7118 -0.0279 -0.0487 0.0196 129 PHE C CA 3622 C C . PHE C 101 ? 0.6430 0.7890 0.7811 -0.0297 -0.0477 0.0231 129 PHE C C 3623 O O . PHE C 101 ? 0.7075 0.8520 0.8421 -0.0306 -0.0497 0.0275 129 PHE C O 3624 C CB . PHE C 101 ? 0.5148 0.6692 0.6561 -0.0260 -0.0534 0.0224 129 PHE C CB 3625 C CG . PHE C 101 ? 0.4806 0.6427 0.6250 -0.0245 -0.0544 0.0192 129 PHE C CG 3626 C CD1 . PHE C 101 ? 0.4624 0.6307 0.6055 -0.0266 -0.0528 0.0179 129 PHE C CD1 3627 C CD2 . PHE C 101 ? 0.4752 0.6386 0.6238 -0.0211 -0.0571 0.0173 129 PHE C CD2 3628 C CE1 . PHE C 101 ? 0.4370 0.6125 0.5831 -0.0254 -0.0538 0.0149 129 PHE C CE1 3629 C CE2 . PHE C 101 ? 0.3770 0.5481 0.5288 -0.0198 -0.0581 0.0142 129 PHE C CE2 3630 C CZ . PHE C 101 ? 0.3967 0.5739 0.5473 -0.0221 -0.0566 0.0130 129 PHE C CZ 3631 N N . ASN C 102 ? 0.5566 0.6990 0.6954 -0.0304 -0.0447 0.0210 130 ASN C N 3632 C CA . ASN C 102 ? 0.4838 0.6211 0.6194 -0.0325 -0.0430 0.0235 130 ASN C CA 3633 C C . ASN C 102 ? 0.4711 0.6022 0.6047 -0.0321 -0.0463 0.0284 130 ASN C C 3634 O O . ASN C 102 ? 0.4429 0.5714 0.5733 -0.0342 -0.0457 0.0315 130 ASN C O 3635 C CB . ASN C 102 ? 0.5321 0.6730 0.6642 -0.0352 -0.0409 0.0244 130 ASN C CB 3636 C CG . ASN C 102 ? 0.5625 0.7078 0.6955 -0.0362 -0.0373 0.0197 130 ASN C CG 3637 O OD1 . ASN C 102 ? 0.6581 0.8058 0.7881 -0.0381 -0.0353 0.0198 130 ASN C OD1 3638 N ND2 . ASN C 102 ? 0.5662 0.7125 0.7028 -0.0349 -0.0365 0.0157 130 ASN C ND2 3639 N N . ALA C 103 ? 0.5199 0.6487 0.6554 -0.0294 -0.0498 0.0290 131 ALA C N 3640 C CA . ALA C 103 ? 0.5715 0.6941 0.7045 -0.0290 -0.0535 0.0337 131 ALA C CA 3641 C C . ALA C 103 ? 0.6773 0.8014 0.8061 -0.0312 -0.0549 0.0384 131 ALA C C 3642 O O . ALA C 103 ? 0.7039 0.8228 0.8297 -0.0325 -0.0565 0.0426 131 ALA C O 3643 C CB . ALA C 103 ? 0.4104 0.5255 0.5428 -0.0296 -0.0526 0.0344 131 ALA C CB 3644 N N . PHE C 104 ? 0.7034 0.8345 0.8317 -0.0318 -0.0542 0.0377 132 PHE C N 3645 C CA . PHE C 104 ? 0.6412 0.7745 0.7656 -0.0335 -0.0559 0.0420 132 PHE C CA 3646 C C . PHE C 104 ? 0.5919 0.7221 0.7151 -0.0316 -0.0609 0.0452 132 PHE C C 3647 O O . PHE C 104 ? 0.6181 0.7473 0.7372 -0.0331 -0.0629 0.0498 132 PHE C O 3648 C CB . PHE C 104 ? 0.5613 0.7027 0.6853 -0.0344 -0.0540 0.0400 132 PHE C CB 3649 C CG . PHE C 104 ? 0.5687 0.7124 0.6913 -0.0370 -0.0496 0.0388 132 PHE C CG 3650 C CD1 . PHE C 104 ? 0.5040 0.6458 0.6231 -0.0394 -0.0489 0.0424 132 PHE C CD1 3651 C CD2 . PHE C 104 ? 0.5926 0.7404 0.7172 -0.0370 -0.0464 0.0340 132 PHE C CD2 3652 C CE1 . PHE C 104 ? 0.5647 0.7087 0.6825 -0.0414 -0.0450 0.0412 132 PHE C CE1 3653 C CE2 . PHE C 104 ? 0.6011 0.7504 0.7238 -0.0391 -0.0427 0.0328 132 PHE C CE2 3654 C CZ . PHE C 104 ? 0.5672 0.7146 0.6866 -0.0411 -0.0420 0.0363 132 PHE C CZ 3655 N N . VAL C 105 ? 0.5335 0.6623 0.6601 -0.0282 -0.0630 0.0428 133 VAL C N 3656 C CA . VAL C 105 ? 0.5314 0.6557 0.6568 -0.0258 -0.0680 0.0456 133 VAL C CA 3657 C C . VAL C 105 ? 0.6349 0.7522 0.7625 -0.0234 -0.0692 0.0444 133 VAL C C 3658 O O . VAL C 105 ? 0.5079 0.6257 0.6390 -0.0229 -0.0662 0.0404 133 VAL C O 3659 C CB . VAL C 105 ? 0.6222 0.7524 0.7495 -0.0231 -0.0704 0.0438 133 VAL C CB 3660 C CG1 . VAL C 105 ? 0.5618 0.6989 0.6867 -0.0253 -0.0694 0.0447 133 VAL C CG1 3661 C CG2 . VAL C 105 ? 0.4746 0.6089 0.6078 -0.0205 -0.0688 0.0378 133 VAL C CG2 3662 N N . THR C 106 ? 0.7662 0.8765 0.8914 -0.0220 -0.0735 0.0479 134 THR C N 3663 C CA . THR C 106 ? 0.7456 0.8492 0.8728 -0.0191 -0.0752 0.0465 134 THR C CA 3664 C C . THR C 106 ? 0.7264 0.8322 0.8563 -0.0145 -0.0784 0.0441 134 THR C C 3665 O O . THR C 106 ? 0.7856 0.8960 0.9146 -0.0139 -0.0804 0.0451 134 THR C O 3666 C CB . THR C 106 ? 0.7465 0.8399 0.8691 -0.0199 -0.0784 0.0515 134 THR C CB 3667 O OG1 . THR C 106 ? 0.7120 0.8030 0.8313 -0.0184 -0.0834 0.0549 134 THR C OG1 3668 C CG2 . THR C 106 ? 0.6585 0.7507 0.7778 -0.0248 -0.0759 0.0548 134 THR C CG2 3669 N N . TYR C 107 ? 0.6582 0.7606 0.7912 -0.0110 -0.0792 0.0412 135 TYR C N 3670 C CA . TYR C 107 ? 0.5950 0.7002 0.7313 -0.0062 -0.0823 0.0384 135 TYR C CA 3671 C C . TYR C 107 ? 0.6292 0.7291 0.7614 -0.0043 -0.0881 0.0427 135 TYR C C 3672 O O . TYR C 107 ? 0.6578 0.7614 0.7914 -0.0009 -0.0911 0.0415 135 TYR C O 3673 C CB . TYR C 107 ? 0.7585 0.8617 0.8991 -0.0029 -0.0815 0.0341 135 TYR C CB 3674 C CG . TYR C 107 ? 0.8712 0.9632 1.0091 -0.0010 -0.0848 0.0364 135 TYR C CG 3675 C CD1 . TYR C 107 ? 0.8035 0.8916 0.9410 0.0037 -0.0900 0.0368 135 TYR C CD1 3676 C CD2 . TYR C 107 ? 0.9399 1.0250 1.0757 -0.0037 -0.0828 0.0379 135 TYR C CD2 3677 C CE1 . TYR C 107 ? 0.8479 0.9252 0.9825 0.0056 -0.0932 0.0388 135 TYR C CE1 3678 C CE2 . TYR C 107 ? 0.9728 1.0473 1.1058 -0.0021 -0.0860 0.0399 135 TYR C CE2 3679 C CZ . TYR C 107 ? 0.9380 1.0084 1.0704 0.0025 -0.0911 0.0403 135 TYR C CZ 3680 O OH . TYR C 107 ? 0.9940 1.0532 1.1232 0.0042 -0.0944 0.0422 135 TYR C OH 3681 N N . GLN C 108 ? 0.6961 0.7871 0.8229 -0.0064 -0.0898 0.0476 136 GLN C N 3682 C CA . GLN C 108 ? 0.7562 0.8412 0.8777 -0.0056 -0.0952 0.0525 136 GLN C CA 3683 C C . GLN C 108 ? 0.7044 0.7959 0.8237 -0.0076 -0.0956 0.0547 136 GLN C C 3684 O O . GLN C 108 ? 0.5345 0.6256 0.6517 -0.0051 -0.0999 0.0563 136 GLN C O 3685 C CB . GLN C 108 ? 0.8954 0.9698 1.0115 -0.0086 -0.0963 0.0575 136 GLN C CB 3686 C CG . GLN C 108 ? 0.9657 1.0320 1.0829 -0.0066 -0.0968 0.0559 136 GLN C CG 3687 C CD . GLN C 108 ? 1.0059 1.0740 1.1261 -0.0093 -0.0913 0.0534 136 GLN C CD 3688 O OE1 . GLN C 108 ? 0.9690 1.0459 1.0924 -0.0110 -0.0870 0.0506 136 GLN C OE1 3689 N NE2 . GLN C 108 ? 1.0329 1.0921 1.1515 -0.0098 -0.0918 0.0544 136 GLN C NE2 3690 N N . GLU C 109 ? 0.8249 0.9222 0.9442 -0.0119 -0.0911 0.0548 137 GLU C N 3691 C CA . GLU C 109 ? 0.7094 0.8135 0.8266 -0.0139 -0.0909 0.0565 137 GLU C CA 3692 C C . GLU C 109 ? 0.7723 0.8850 0.8937 -0.0106 -0.0914 0.0522 137 GLU C C 3693 O O . GLU C 109 ? 0.8543 0.9696 0.9734 -0.0098 -0.0944 0.0540 137 GLU C O 3694 C CB . GLU C 109 ? 0.5582 0.6663 0.6745 -0.0189 -0.0859 0.0571 137 GLU C CB 3695 C CG . GLU C 109 ? 0.4912 0.5921 0.6023 -0.0226 -0.0862 0.0624 137 GLU C CG 3696 C CD . GLU C 109 ? 0.6533 0.7580 0.7643 -0.0269 -0.0811 0.0623 137 GLU C CD 3697 O OE1 . GLU C 109 ? 0.6488 0.7592 0.7641 -0.0267 -0.0772 0.0577 137 GLU C OE1 3698 O OE2 . GLU C 109 ? 0.7712 0.8731 0.8778 -0.0305 -0.0810 0.0668 137 GLU C OE2 3699 N N . ILE C 110 ? 0.7130 0.8302 0.8405 -0.0087 -0.0887 0.0467 138 ILE C N 3700 C CA . ILE C 110 ? 0.6579 0.7824 0.7901 -0.0049 -0.0899 0.0423 138 ILE C CA 3701 C C . ILE C 110 ? 0.7534 0.8714 0.8846 -0.0003 -0.0956 0.0436 138 ILE C C 3702 O O . ILE C 110 ? 0.9134 1.0217 1.0404 -0.0006 -0.0978 0.0474 138 ILE C O 3703 C CB . ILE C 110 ? 0.6474 0.7776 0.7862 -0.0043 -0.0855 0.0361 138 ILE C CB 3704 C CG1 . ILE C 110 ? 0.6040 0.7377 0.7426 -0.0091 -0.0800 0.0354 138 ILE C CG1 3705 C CG2 . ILE C 110 ? 0.5958 0.7350 0.7398 -0.0010 -0.0865 0.0316 138 ILE C CG2 3706 C CD1 . ILE C 110 ? 0.5489 0.6877 0.6931 -0.0090 -0.0757 0.0296 138 ILE C CD1 3707 N N . ALA C 111 ? 0.7699 0.8928 0.9046 0.0041 -0.0983 0.0406 139 ALA C N 3708 C CA . ALA C 111 ? 0.7326 0.8492 0.8661 0.0091 -0.1040 0.0417 139 ALA C CA 3709 C C . ALA C 111 ? 0.6772 0.7877 0.8033 0.0084 -0.1086 0.0478 139 ALA C C 3710 O O . ALA C 111 ? 0.7744 0.8862 0.8996 0.0118 -0.1130 0.0481 139 ALA C O 3711 C CB . ALA C 111 ? 0.6643 0.7722 0.7984 0.0108 -0.1041 0.0410 139 ALA C CB 3712 N N . ALA C 112 ? 0.6823 0.7860 0.8028 0.0040 -0.1077 0.0526 140 ALA C N 3713 C CA . ALA C 112 ? 0.7587 0.8571 0.8717 0.0026 -0.1116 0.0586 140 ALA C CA 3714 C C . ALA C 112 ? 0.7756 0.8837 0.8886 0.0014 -0.1111 0.0583 140 ALA C C 3715 O O . ALA C 112 ? 0.8710 0.9784 0.9803 0.0031 -0.1154 0.0607 140 ALA C O 3716 C CB . ALA C 112 ? 0.6819 0.7730 0.7896 -0.0026 -0.1101 0.0635 140 ALA C CB 3717 N N . ALA C 113 ? 0.6499 0.7666 0.7666 -0.0014 -0.1057 0.0552 141 ALA C N 3718 C CA . ALA C 113 ? 0.6041 0.7304 0.7212 -0.0028 -0.1044 0.0542 141 ALA C CA 3719 C C . ALA C 113 ? 0.7197 0.8527 0.8414 0.0020 -0.1069 0.0500 141 ALA C C 3720 O O . ALA C 113 ? 0.8273 0.9659 0.9478 0.0022 -0.1085 0.0503 141 ALA C O 3721 C CB . ALA C 113 ? 0.6464 0.7790 0.7663 -0.0068 -0.0981 0.0517 141 ALA C CB 3722 N N . ASN C 114 ? 0.6904 0.8232 0.8176 0.0058 -0.1073 0.0459 142 ASN C N 3723 C CA . ASN C 114 ? 0.7580 0.8983 0.8905 0.0104 -0.1094 0.0414 142 ASN C CA 3724 C C . ASN C 114 ? 0.9159 1.0504 1.0471 0.0161 -0.1158 0.0424 142 ASN C C 3725 O O . ASN C 114 ? 0.8303 0.9705 0.9667 0.0207 -0.1178 0.0383 142 ASN C O 3726 C CB . ASN C 114 ? 0.6730 0.8203 0.8135 0.0108 -0.1048 0.0351 142 ASN C CB 3727 C CG . ASN C 114 ? 0.7318 0.8863 0.8734 0.0058 -0.0992 0.0335 142 ASN C CG 3728 O OD1 . ASN C 114 ? 0.6795 0.8431 0.8235 0.0056 -0.0985 0.0309 142 ASN C OD1 3729 N ND2 . ASN C 114 ? 0.7797 0.9298 0.9195 0.0019 -0.0952 0.0349 142 ASN C ND2 3730 N N . ASN C 115 ? 1.0710 1.1944 1.1953 0.0156 -0.1191 0.0480 143 ASN C N 3731 C CA . ASN C 115 ? 1.2062 1.3221 1.3271 0.0206 -0.1258 0.0501 143 ASN C CA 3732 C C . ASN C 115 ? 1.3696 1.4846 1.4956 0.0269 -0.1282 0.0458 143 ASN C C 3733 O O . ASN C 115 ? 1.4410 1.5454 1.5640 0.0291 -0.1312 0.0478 143 ASN C O 3734 C CB . ASN C 115 ? 1.2818 1.4009 1.3991 0.0218 -0.1299 0.0521 143 ASN C CB 3735 C CG . ASN C 115 ? 1.3792 1.4905 1.4871 0.0179 -0.1317 0.0592 143 ASN C CG 3736 O OD1 . ASN C 115 ? 1.4173 1.5171 1.5199 0.0176 -0.1342 0.0632 143 ASN C OD1 3737 N ND2 . ASN C 115 ? 1.3995 1.5171 1.5051 0.0146 -0.1304 0.0606 143 ASN C ND2 3738 N N . ILE C 116 ? 1.5055 1.6317 1.6392 0.0295 -0.1268 0.0400 144 ILE C N 3739 C CA . ILE C 116 ? 1.5997 1.7272 1.7389 0.0358 -0.1290 0.0354 144 ILE C CA 3740 C C . ILE C 116 ? 1.6247 1.7454 1.7656 0.0362 -0.1268 0.0342 144 ILE C C 3741 O O . ILE C 116 ? 1.6581 1.7727 1.7990 0.0414 -0.1306 0.0334 144 ILE C O 3742 C CB . ILE C 116 ? 1.5933 1.7357 1.7412 0.0375 -0.1269 0.0290 144 ILE C CB 3743 C CG1 . ILE C 116 ? 1.5645 1.7138 1.7108 0.0371 -0.1291 0.0301 144 ILE C CG1 3744 C CG2 . ILE C 116 ? 1.6041 1.7487 1.7578 0.0444 -0.1295 0.0243 144 ILE C CG2 3745 C CD1 . ILE C 116 ? 1.5132 1.6771 1.6676 0.0384 -0.1274 0.0240 144 ILE C CD1 3746 N N . PRO C 117 ? 1.5557 1.6768 1.6974 0.0309 -0.1209 0.0340 145 PRO C N 3747 C CA . PRO C 117 ? 1.5110 1.6247 1.6536 0.0319 -0.1197 0.0330 145 PRO C CA 3748 C C . PRO C 117 ? 1.4581 1.5572 1.5927 0.0308 -0.1226 0.0389 145 PRO C C 3749 O O . PRO C 117 ? 1.4307 1.5260 1.5597 0.0258 -0.1219 0.0437 145 PRO C O 3750 C CB . PRO C 117 ? 1.4782 1.5973 1.6245 0.0270 -0.1125 0.0305 145 PRO C CB 3751 C CG . PRO C 117 ? 1.4618 1.5898 1.6082 0.0231 -0.1101 0.0308 145 PRO C CG 3752 C CD . PRO C 117 ? 1.5005 1.6289 1.6432 0.0250 -0.1153 0.0336 145 PRO C CD 3753 N N . ASP C 118 ? 1.3941 1.4852 1.5282 0.0355 -0.1261 0.0383 146 ASP C N 3754 C CA . ASP C 118 ? 1.3353 1.4122 1.4629 0.0345 -0.1282 0.0427 146 ASP C CA 3755 C C . ASP C 118 ? 1.3507 1.4246 1.4817 0.0350 -0.1250 0.0395 146 ASP C C 3756 O O . ASP C 118 ? 1.3521 1.4183 1.4796 0.0310 -0.1232 0.0423 146 ASP C O 3757 C CB . ASP C 118 ? 1.3029 1.3703 1.4251 0.0394 -0.1356 0.0455 146 ASP C CB 3758 C CG . ASP C 118 ? 1.2983 1.3612 1.4126 0.0364 -0.1388 0.0518 146 ASP C CG 3759 O OD1 . ASP C 118 ? 1.2263 1.2779 1.3336 0.0331 -0.1400 0.0570 146 ASP C OD1 3760 O OD2 . ASP C 118 ? 1.3303 1.4010 1.4453 0.0371 -0.1400 0.0515 146 ASP C OD2 3761 N N . PRO C 119 ? 1.3474 1.4278 1.4855 0.0399 -0.1243 0.0334 147 PRO C N 3762 C CA . PRO C 119 ? 1.3192 1.3978 1.4604 0.0394 -0.1202 0.0303 147 PRO C CA 3763 C C . PRO C 119 ? 1.2794 1.3686 1.4261 0.0350 -0.1131 0.0269 147 PRO C C 3764 O O . PRO C 119 ? 1.1674 1.2645 1.3148 0.0317 -0.1112 0.0275 147 PRO C O 3765 C CB . PRO C 119 ? 1.3328 1.4126 1.4785 0.0469 -0.1229 0.0255 147 PRO C CB 3766 C CG . PRO C 119 ? 1.3800 1.4649 1.5262 0.0511 -0.1276 0.0252 147 PRO C CG 3767 C CD . PRO C 119 ? 1.3793 1.4674 1.5222 0.0461 -0.1272 0.0293 147 PRO C CD 3768 N N . ASN C 120 ? 1.3542 1.4432 1.5045 0.0353 -0.1096 0.0234 148 ASN C N 3769 C CA . ASN C 120 ? 1.3253 1.4224 1.4802 0.0314 -0.1028 0.0199 148 ASN C CA 3770 C C . ASN C 120 ? 1.2737 1.3839 1.4365 0.0344 -0.1011 0.0137 148 ASN C C 3771 O O . ASN C 120 ? 1.2242 1.3394 1.3917 0.0336 -0.0965 0.0094 148 ASN C O 3772 C CB . ASN C 120 ? 1.2729 1.3625 1.4271 0.0302 -0.1000 0.0193 148 ASN C CB 3773 C CG . ASN C 120 ? 1.2744 1.3665 1.4287 0.0238 -0.0940 0.0195 148 ASN C CG 3774 O OD1 . ASN C 120 ? 1.3036 1.4050 1.4602 0.0209 -0.0910 0.0185 148 ASN C OD1 3775 N ND2 . ASN C 120 ? 1.2360 1.3197 1.3878 0.0218 -0.0923 0.0207 148 ASN C ND2 3776 N N . LYS C 121 ? 1.2930 1.4086 1.4571 0.0376 -0.1049 0.0134 149 LYS C N 3777 C CA . LYS C 121 ? 1.2438 1.3718 1.4156 0.0411 -0.1041 0.0074 149 LYS C CA 3778 C C . LYS C 121 ? 1.1175 1.2563 1.2911 0.0392 -0.1037 0.0071 149 LYS C C 3779 O O . LYS C 121 ? 1.0407 1.1779 1.2107 0.0404 -0.1083 0.0104 149 LYS C O 3780 C CB . LYS C 121 ? 1.3081 1.4337 1.4809 0.0487 -0.1097 0.0059 149 LYS C CB 3781 C CG . LYS C 121 ? 1.3987 1.5092 1.5653 0.0510 -0.1135 0.0095 149 LYS C CG 3782 C CD . LYS C 121 ? 1.4865 1.5922 1.6542 0.0506 -0.1100 0.0074 149 LYS C CD 3783 C CE . LYS C 121 ? 1.5492 1.6390 1.7095 0.0514 -0.1138 0.0119 149 LYS C CE 3784 N NZ . LYS C 121 ? 1.5930 1.6771 1.7519 0.0471 -0.1093 0.0124 149 LYS C NZ 3785 N N . ILE C 122 ? 1.0884 1.2380 1.2675 0.0365 -0.0987 0.0029 150 ILE C N 3786 C CA . ILE C 122 ? 1.0226 1.1828 1.2037 0.0342 -0.0979 0.0021 150 ILE C CA 3787 C C . ILE C 122 ? 0.9904 1.1640 1.1798 0.0357 -0.0956 -0.0044 150 ILE C C 3788 O O . ILE C 122 ? 1.0692 1.2446 1.2629 0.0369 -0.0928 -0.0084 150 ILE C O 3789 C CB . ILE C 122 ? 0.9548 1.1147 1.1326 0.0271 -0.0933 0.0045 150 ILE C CB 3790 C CG1 . ILE C 122 ? 0.7727 0.9346 0.9539 0.0241 -0.0871 0.0008 150 ILE C CG1 3791 C CG2 . ILE C 122 ? 1.0117 1.1597 1.1817 0.0250 -0.0952 0.0109 150 ILE C CG2 3792 C CD1 . ILE C 122 ? 0.5961 0.7570 0.7740 0.0175 -0.0825 0.0029 150 ILE C CD1 3793 N N . ASN C 123 ? 0.9560 1.1392 1.1476 0.0355 -0.0967 -0.0055 151 ASN C N 3794 C CA . ASN C 123 ? 0.9181 1.1148 1.1178 0.0369 -0.0951 -0.0116 151 ASN C CA 3795 C C . ASN C 123 ? 0.9703 1.1752 1.1720 0.0308 -0.0895 -0.0137 151 ASN C C 3796 O O . ASN C 123 ? 0.9906 1.1939 1.1878 0.0265 -0.0888 -0.0104 151 ASN C O 3797 C CB . ASN C 123 ? 0.9686 1.1717 1.1703 0.0417 -0.1007 -0.0123 151 ASN C CB 3798 C CG . ASN C 123 ? 1.0143 1.2136 1.2172 0.0491 -0.1056 -0.0131 151 ASN C CG 3799 O OD1 . ASN C 123 ? 0.9949 1.1873 1.1931 0.0525 -0.1112 -0.0094 151 ASN C OD1 3800 N ND2 . ASN C 123 ? 1.0242 1.2281 1.2332 0.0517 -0.1035 -0.0182 151 ASN C ND2 3801 N N . VAL C 124 ? 0.9599 1.1731 1.1681 0.0303 -0.0856 -0.0193 152 VAL C N 3802 C CA . VAL C 124 ? 0.9680 1.1895 1.1785 0.0248 -0.0806 -0.0219 152 VAL C CA 3803 C C . VAL C 124 ? 0.9733 1.2028 1.1843 0.0244 -0.0832 -0.0217 152 VAL C C 3804 O O . VAL C 124 ? 0.9431 1.1769 1.1567 0.0293 -0.0881 -0.0224 152 VAL C O 3805 C CB . VAL C 124 ? 1.0113 1.2414 1.2291 0.0248 -0.0765 -0.0282 152 VAL C CB 3806 C CG1 . VAL C 124 ? 0.9679 1.2049 1.1870 0.0185 -0.0712 -0.0305 152 VAL C CG1 3807 C CG2 . VAL C 124 ? 1.0009 1.2228 1.2179 0.0259 -0.0743 -0.0284 152 VAL C CG2 3808 N N . SER C 125 ? 0.9228 1.1539 1.1312 0.0187 -0.0802 -0.0206 153 SER C N 3809 C CA . SER C 125 ? 0.9322 1.1702 1.1400 0.0174 -0.0821 -0.0202 153 SER C CA 3810 C C . SER C 125 ? 0.9352 1.1661 1.1363 0.0187 -0.0869 -0.0143 153 SER C C 3811 O O . SER C 125 ? 0.9690 1.2043 1.1685 0.0176 -0.0887 -0.0134 153 SER C O 3812 C CB . SER C 125 ? 0.9230 1.1739 1.1384 0.0204 -0.0840 -0.0252 153 SER C CB 3813 O OG . SER C 125 ? 0.9986 1.2589 1.2176 0.0158 -0.0797 -0.0292 153 SER C OG 3814 N N . GLN C 126 ? 0.8939 1.1135 1.0907 0.0209 -0.0890 -0.0104 154 GLN C N 3815 C CA . GLN C 126 ? 0.8444 1.0563 1.0341 0.0211 -0.0930 -0.0045 154 GLN C CA 3816 C C . GLN C 126 ? 0.8939 1.1028 1.0781 0.0150 -0.0895 -0.0014 154 GLN C C 3817 O O . GLN C 126 ? 0.8533 1.0599 1.0371 0.0113 -0.0846 -0.0021 154 GLN C O 3818 C CB . GLN C 126 ? 0.7910 0.9911 0.9772 0.0245 -0.0958 -0.0012 154 GLN C CB 3819 C CG . GLN C 126 ? 0.8377 1.0287 1.0159 0.0241 -0.0995 0.0053 154 GLN C CG 3820 C CD . GLN C 126 ? 0.9461 1.1251 1.1207 0.0268 -0.1022 0.0084 154 GLN C CD 3821 O OE1 . GLN C 126 ? 0.9829 1.1600 1.1609 0.0290 -0.1009 0.0058 154 GLN C OE1 3822 N NE2 . GLN C 126 ? 0.9848 1.1553 1.1522 0.0266 -0.1058 0.0142 154 GLN C NE2 3823 N N . THR C 127 ? 0.9373 1.1463 1.1170 0.0142 -0.0923 0.0021 155 THR C N 3824 C CA . THR C 127 ? 0.8102 1.0169 0.9843 0.0089 -0.0896 0.0051 155 THR C CA 3825 C C . THR C 127 ? 0.6885 0.8835 0.8555 0.0084 -0.0913 0.0112 155 THR C C 3826 O O . THR C 127 ? 0.8108 1.0012 0.9751 0.0118 -0.0964 0.0143 155 THR C O 3827 C CB . THR C 127 ? 0.7734 0.9873 0.9462 0.0079 -0.0914 0.0053 155 THR C CB 3828 O OG1 . THR C 127 ? 0.7991 1.0117 0.9703 0.0123 -0.0976 0.0077 155 THR C OG1 3829 C CG2 . THR C 127 ? 0.7502 0.9759 0.9298 0.0072 -0.0891 -0.0007 155 THR C CG2 3830 N N . LEU C 128 ? 0.5678 0.7579 0.7319 0.0042 -0.0871 0.0128 156 LEU C N 3831 C CA . LEU C 128 ? 0.5829 0.7626 0.7405 0.0030 -0.0881 0.0185 156 LEU C CA 3832 C C . LEU C 128 ? 0.5807 0.7606 0.7331 -0.0018 -0.0858 0.0215 156 LEU C C 3833 O O . LEU C 128 ? 0.5885 0.7732 0.7422 -0.0051 -0.0813 0.0189 156 LEU C O 3834 C CB . LEU C 128 ? 0.6288 0.8016 0.7871 0.0025 -0.0853 0.0182 156 LEU C CB 3835 C CG . LEU C 128 ? 0.6588 0.8307 0.8221 0.0072 -0.0870 0.0150 156 LEU C CG 3836 C CD1 . LEU C 128 ? 0.7117 0.8774 0.8754 0.0059 -0.0834 0.0144 156 LEU C CD1 3837 C CD2 . LEU C 128 ? 0.4960 0.6625 0.6571 0.0119 -0.0933 0.0180 156 LEU C CD2 3838 N N . TRP C 129 ? 0.5568 0.7314 0.7030 -0.0022 -0.0890 0.0269 157 TRP C N 3839 C CA . TRP C 129 ? 0.5939 0.7673 0.7344 -0.0066 -0.0870 0.0305 157 TRP C CA 3840 C C . TRP C 129 ? 0.5719 0.7379 0.7102 -0.0092 -0.0839 0.0326 157 TRP C C 3841 O O . TRP C 129 ? 0.5934 0.7513 0.7303 -0.0078 -0.0860 0.0351 157 TRP C O 3842 C CB . TRP C 129 ? 0.6493 0.8199 0.7839 -0.0060 -0.0916 0.0356 157 TRP C CB 3843 C CG . TRP C 129 ? 0.5374 0.7055 0.6655 -0.0104 -0.0898 0.0401 157 TRP C CG 3844 C CD1 . TRP C 129 ? 0.4971 0.6691 0.6247 -0.0144 -0.0849 0.0390 157 TRP C CD1 3845 C CD2 . TRP C 129 ? 0.5385 0.6998 0.6598 -0.0113 -0.0927 0.0462 157 TRP C CD2 3846 N NE1 . TRP C 129 ? 0.4331 0.6018 0.5544 -0.0174 -0.0846 0.0439 157 TRP C NE1 3847 C CE2 . TRP C 129 ? 0.4843 0.6465 0.6016 -0.0159 -0.0892 0.0485 157 TRP C CE2 3848 C CE3 . TRP C 129 ? 0.5119 0.6662 0.6297 -0.0088 -0.0980 0.0500 157 TRP C CE3 3849 C CZ2 . TRP C 129 ? 0.4760 0.6333 0.5864 -0.0182 -0.0907 0.0543 157 TRP C CZ2 3850 C CZ3 . TRP C 129 ? 0.4967 0.6452 0.6073 -0.0113 -0.0995 0.0560 157 TRP C CZ3 3851 C CH2 . TRP C 129 ? 0.5181 0.6685 0.6252 -0.0160 -0.0958 0.0581 157 TRP C CH2 3852 N N . ILE C 130 ? 0.5901 0.7587 0.7282 -0.0131 -0.0790 0.0314 158 ILE C N 3853 C CA . ILE C 130 ? 0.6022 0.7647 0.7381 -0.0159 -0.0758 0.0333 158 ILE C CA 3854 C C . ILE C 130 ? 0.6203 0.7805 0.7497 -0.0190 -0.0759 0.0384 158 ILE C C 3855 O O . ILE C 130 ? 0.5572 0.7226 0.6848 -0.0215 -0.0737 0.0381 158 ILE C O 3856 C CB . ILE C 130 ? 0.5383 0.7047 0.6775 -0.0180 -0.0704 0.0288 158 ILE C CB 3857 C CG1 . ILE C 130 ? 0.5515 0.7210 0.6972 -0.0152 -0.0701 0.0235 158 ILE C CG1 3858 C CG2 . ILE C 130 ? 0.4970 0.6572 0.6339 -0.0207 -0.0673 0.0305 158 ILE C CG2 3859 C CD1 . ILE C 130 ? 0.5465 0.7093 0.6938 -0.0122 -0.0721 0.0240 158 ILE C CD1 3860 N N . PRO C 131 ? 0.6271 0.7794 0.7526 -0.0190 -0.0785 0.0432 159 PRO C N 3861 C CA . PRO C 131 ? 0.5966 0.7469 0.7158 -0.0221 -0.0789 0.0485 159 PRO C CA 3862 C C . PRO C 131 ? 0.5053 0.6539 0.6230 -0.0259 -0.0745 0.0494 159 PRO C C 3863 O O . PRO C 131 ? 0.4934 0.6351 0.6085 -0.0271 -0.0750 0.0530 159 PRO C O 3864 C CB . PRO C 131 ? 0.5567 0.6988 0.6727 -0.0205 -0.0837 0.0530 159 PRO C CB 3865 C CG . PRO C 131 ? 0.5488 0.6863 0.6689 -0.0179 -0.0840 0.0504 159 PRO C CG 3866 C CD . PRO C 131 ? 0.5812 0.7262 0.7078 -0.0161 -0.0816 0.0441 159 PRO C CD 3867 N N . LEU C 132 ? 0.3873 0.5420 0.5064 -0.0277 -0.0703 0.0462 160 LEU C N 3868 C CA . LEU C 132 ? 0.4930 0.6469 0.6103 -0.0311 -0.0662 0.0470 160 LEU C CA 3869 C C . LEU C 132 ? 0.6209 0.7724 0.7324 -0.0336 -0.0674 0.0528 160 LEU C C 3870 O O . LEU C 132 ? 0.5678 0.7218 0.6760 -0.0337 -0.0697 0.0551 160 LEU C O 3871 C CB . LEU C 132 ? 0.4050 0.5660 0.5234 -0.0325 -0.0621 0.0431 160 LEU C CB 3872 C CG . LEU C 132 ? 0.6081 0.7726 0.7319 -0.0307 -0.0607 0.0372 160 LEU C CG 3873 C CD1 . LEU C 132 ? 0.4914 0.6624 0.6149 -0.0326 -0.0572 0.0339 160 LEU C CD1 3874 C CD2 . LEU C 132 ? 0.6781 0.8375 0.8051 -0.0302 -0.0589 0.0353 160 LEU C CD2 3875 N N . PRO C 133 ? 0.6258 0.7725 0.7359 -0.0357 -0.0658 0.0551 161 PRO C N 3876 C CA . PRO C 133 ? 0.5518 0.6964 0.6566 -0.0386 -0.0666 0.0606 161 PRO C CA 3877 C C . PRO C 133 ? 0.5724 0.7238 0.6743 -0.0411 -0.0637 0.0610 161 PRO C C 3878 O O . PRO C 133 ? 0.5945 0.7500 0.6982 -0.0417 -0.0599 0.0574 161 PRO C O 3879 C CB . PRO C 133 ? 0.6015 0.7403 0.7068 -0.0401 -0.0650 0.0616 161 PRO C CB 3880 C CG . PRO C 133 ? 0.5746 0.7154 0.6845 -0.0391 -0.0613 0.0561 161 PRO C CG 3881 C CD . PRO C 133 ? 0.5827 0.7268 0.6960 -0.0360 -0.0626 0.0522 161 PRO C CD 3882 N N . CYS C 134 ? 0.4765 0.6288 0.5736 -0.0426 -0.0657 0.0654 162 CYS C N 3883 C CA . CYS C 134 ? 0.5141 0.6729 0.6079 -0.0449 -0.0633 0.0660 162 CYS C CA 3884 C C . CYS C 134 ? 0.5722 0.7295 0.6604 -0.0472 -0.0656 0.0721 162 CYS C C 3885 O O . CYS C 134 ? 0.5256 0.6763 0.6124 -0.0470 -0.0690 0.0755 162 CYS C O 3886 C CB . CYS C 134 ? 0.2868 0.4521 0.3814 -0.0432 -0.0633 0.0625 162 CYS C CB 3887 S SG . CYS C 134 ? 0.4952 0.6595 0.5887 -0.0404 -0.0690 0.0641 162 CYS C SG 3888 N N . SER C 135 ? 0.6030 0.7660 0.6876 -0.0493 -0.0636 0.0735 163 SER C N 3889 C CA . SER C 135 ? 0.5967 0.7593 0.6755 -0.0519 -0.0654 0.0792 163 SER C CA 3890 C C . SER C 135 ? 0.5922 0.7628 0.6677 -0.0529 -0.0636 0.0789 163 SER C C 3891 O O . SER C 135 ? 0.4900 0.6659 0.5676 -0.0523 -0.0603 0.0746 163 SER C O 3892 C CB . SER C 135 ? 0.5893 0.7487 0.6668 -0.0551 -0.0640 0.0826 163 SER C CB 3893 O OG . SER C 135 ? 0.5641 0.7237 0.6359 -0.0580 -0.0654 0.0882 163 SER C OG 3894 N N . CYS C 136 ? 0.5940 0.7651 0.6641 -0.0545 -0.0658 0.0835 164 CYS C N 3895 C CA . CYS C 136 ? 0.5008 0.6793 0.5669 -0.0558 -0.0640 0.0839 164 CYS C CA 3896 C C . CYS C 136 ? 0.5189 0.6983 0.5805 -0.0598 -0.0627 0.0889 164 CYS C C 3897 O O . CYS C 136 ? 0.5142 0.6994 0.5716 -0.0614 -0.0614 0.0903 164 CYS C O 3898 C CB . CYS C 136 ? 0.4986 0.6783 0.5618 -0.0541 -0.0675 0.0845 164 CYS C CB 3899 S SG . CYS C 136 ? 0.6267 0.8069 0.6954 -0.0495 -0.0694 0.0785 164 CYS C SG 3900 N N . ASP C 137 ? 0.4994 0.6732 0.5619 -0.0615 -0.0629 0.0914 165 ASP C N 3901 C CA . ASP C 137 ? 0.5113 0.6859 0.5700 -0.0657 -0.0618 0.0962 165 ASP C CA 3902 C C . ASP C 137 ? 0.5443 0.7270 0.6034 -0.0670 -0.0569 0.0942 165 ASP C C 3903 O O . ASP C 137 ? 0.5363 0.7210 0.5997 -0.0651 -0.0542 0.0893 165 ASP C O 3904 C CB . ASP C 137 ? 0.4724 0.6398 0.5329 -0.0673 -0.0625 0.0985 165 ASP C CB 3905 C CG . ASP C 137 ? 0.5568 0.7153 0.6153 -0.0668 -0.0676 0.1019 165 ASP C CG 3906 O OD1 . ASP C 137 ? 0.4714 0.6297 0.5254 -0.0666 -0.0705 0.1044 165 ASP C OD1 3907 O OD2 . ASP C 137 ? 0.6221 0.7736 0.6833 -0.0664 -0.0689 0.1019 165 ASP C OD2 3908 N N . LYS C 138 ? 0.6727 0.8601 0.7271 -0.0701 -0.0559 0.0979 166 LYS C N 3909 C CA . LYS C 138 ? 0.6539 0.8487 0.7084 -0.0717 -0.0513 0.0968 166 LYS C CA 3910 C C . LYS C 138 ? 0.6176 0.8094 0.6751 -0.0736 -0.0501 0.0978 166 LYS C C 3911 O O . LYS C 138 ? 0.5409 0.7252 0.5986 -0.0747 -0.0528 0.1007 166 LYS C O 3912 C CB . LYS C 138 ? 0.5713 0.7720 0.6198 -0.0746 -0.0507 0.1008 166 LYS C CB 3913 C CG . LYS C 138 ? 0.5324 0.7380 0.5777 -0.0729 -0.0510 0.0992 166 LYS C CG 3914 C CD . LYS C 138 ? 0.5705 0.7805 0.6092 -0.0762 -0.0510 0.1042 166 LYS C CD 3915 C CE . LYS C 138 ? 0.6124 0.8273 0.6472 -0.0746 -0.0513 0.1029 166 LYS C CE 3916 N NZ . LYS C 138 ? 0.6117 0.8362 0.6449 -0.0754 -0.0469 0.1013 166 LYS C NZ 3917 N N . GLU C 139 ? 0.6816 0.8791 0.7411 -0.0739 -0.0460 0.0953 167 GLU C N 3918 C CA . GLU C 139 ? 0.7878 0.9836 0.8498 -0.0760 -0.0446 0.0963 167 GLU C CA 3919 C C . GLU C 139 ? 0.7451 0.9482 0.8040 -0.0796 -0.0423 0.0996 167 GLU C C 3920 O O . GLU C 139 ? 0.6792 0.8903 0.7378 -0.0791 -0.0389 0.0972 167 GLU C O 3921 C CB . GLU C 139 ? 0.7562 0.9520 0.8233 -0.0733 -0.0419 0.0908 167 GLU C CB 3922 C CG . GLU C 139 ? 0.6407 0.8338 0.7107 -0.0750 -0.0409 0.0915 167 GLU C CG 3923 C CD . GLU C 139 ? 0.7296 0.9139 0.7997 -0.0767 -0.0446 0.0954 167 GLU C CD 3924 O OE1 . GLU C 139 ? 0.7284 0.9115 0.7987 -0.0797 -0.0444 0.0983 167 GLU C OE1 3925 O OE2 . GLU C 139 ? 0.8272 1.0056 0.8971 -0.0749 -0.0478 0.0954 167 GLU C OE2 3926 N N . GLU C 140 ? 0.8167 1.0169 0.8730 -0.0834 -0.0442 0.1052 168 GLU C N 3927 C CA . GLU C 140 ? 0.9527 1.1596 1.0059 -0.0876 -0.0423 0.1090 168 GLU C CA 3928 C C . GLU C 140 ? 0.9295 1.1458 0.9789 -0.0873 -0.0403 0.1085 168 GLU C C 3929 O O . GLU C 140 ? 0.8547 1.0796 0.9041 -0.0881 -0.0366 0.1074 168 GLU C O 3930 C CB . GLU C 140 ? 1.0050 1.2152 1.0623 -0.0886 -0.0392 0.1075 168 GLU C CB 3931 C CG . GLU C 140 ? 1.1091 1.3118 1.1682 -0.0912 -0.0411 0.1104 168 GLU C CG 3932 C CD . GLU C 140 ? 1.2765 1.4762 1.3308 -0.0959 -0.0439 0.1170 168 GLU C CD 3933 O OE1 . GLU C 140 ? 1.3233 1.5293 1.3757 -0.1000 -0.0421 0.1202 168 GLU C OE1 3934 O OE2 . GLU C 140 ? 1.3298 1.5208 1.3821 -0.0954 -0.0478 0.1190 168 GLU C OE2 3935 N N . GLY C 141 ? 0.9187 1.1330 0.9646 -0.0860 -0.0427 0.1091 169 GLY C N 3936 C CA . GLY C 141 ? 0.7896 1.0117 0.8312 -0.0858 -0.0413 0.1090 169 GLY C CA 3937 C C . GLY C 141 ? 0.8144 1.0408 0.8580 -0.0814 -0.0392 0.1027 169 GLY C C 3938 O O . GLY C 141 ? 0.9049 1.1368 0.9449 -0.0806 -0.0385 0.1020 169 GLY C O 3939 N N . SER C 142 ? 0.7079 0.9312 0.7570 -0.0787 -0.0383 0.0983 170 SER C N 3940 C CA . SER C 142 ? 0.6942 0.9210 0.7450 -0.0750 -0.0361 0.0923 170 SER C CA 3941 C C . SER C 142 ? 0.7450 0.9656 0.7979 -0.0717 -0.0387 0.0891 170 SER C C 3942 O O . SER C 142 ? 0.8286 1.0416 0.8840 -0.0715 -0.0414 0.0901 170 SER C O 3943 C CB . SER C 142 ? 0.7465 0.9752 0.8016 -0.0742 -0.0328 0.0890 170 SER C CB 3944 O OG . SER C 142 ? 0.9220 1.1569 0.9757 -0.0772 -0.0305 0.0917 170 SER C OG 3945 N N . ASN C 143 ? 0.6404 0.8647 0.6925 -0.0691 -0.0377 0.0851 171 ASN C N 3946 C CA . ASN C 143 ? 0.5920 0.8120 0.6464 -0.0660 -0.0398 0.0816 171 ASN C CA 3947 C C . ASN C 143 ? 0.6905 0.9075 0.7503 -0.0640 -0.0380 0.0768 171 ASN C C 3948 O O . ASN C 143 ? 0.6556 0.8764 0.7160 -0.0633 -0.0346 0.0737 171 ASN C O 3949 C CB . ASN C 143 ? 0.5212 0.7462 0.5723 -0.0643 -0.0395 0.0791 171 ASN C CB 3950 C CG . ASN C 143 ? 0.5736 0.8002 0.6192 -0.0659 -0.0420 0.0836 171 ASN C CG 3951 O OD1 . ASN C 143 ? 0.6701 0.8922 0.7146 -0.0677 -0.0448 0.0882 171 ASN C OD1 3952 N ND2 . ASN C 143 ? 0.5654 0.7981 0.6071 -0.0652 -0.0411 0.0822 171 ASN C ND2 3953 N N . VAL C 144 ? 0.7439 0.9538 0.8073 -0.0628 -0.0405 0.0761 172 VAL C N 3954 C CA . VAL C 144 ? 0.7085 0.9148 0.7769 -0.0611 -0.0391 0.0720 172 VAL C CA 3955 C C . VAL C 144 ? 0.6569 0.8594 0.7279 -0.0585 -0.0412 0.0688 172 VAL C C 3956 O O . VAL C 144 ? 0.6042 0.8056 0.6737 -0.0581 -0.0444 0.0706 172 VAL C O 3957 C CB . VAL C 144 ? 0.7798 0.9807 0.8506 -0.0628 -0.0396 0.0748 172 VAL C CB 3958 C CG1 . VAL C 144 ? 0.7009 0.9063 0.7704 -0.0651 -0.0368 0.0767 172 VAL C CG1 3959 C CG2 . VAL C 144 ? 0.7472 0.9431 0.8167 -0.0640 -0.0437 0.0795 172 VAL C CG2 3960 N N . MET C 145 ? 0.5839 0.7848 0.6586 -0.0567 -0.0395 0.0639 173 MET C N 3961 C CA . MET C 145 ? 0.4760 0.6727 0.5542 -0.0545 -0.0415 0.0611 173 MET C CA 3962 C C . MET C 145 ? 0.5422 0.7325 0.6245 -0.0545 -0.0420 0.0614 173 MET C C 3963 O O . MET C 145 ? 0.6773 0.8666 0.7613 -0.0546 -0.0392 0.0594 173 MET C O 3964 C CB . MET C 145 ? 0.4755 0.6747 0.5550 -0.0527 -0.0396 0.0553 173 MET C CB 3965 C CG . MET C 145 ? 0.4058 0.6026 0.4885 -0.0507 -0.0421 0.0528 173 MET C CG 3966 S SD . MET C 145 ? 1.0349 1.2319 1.1209 -0.0491 -0.0396 0.0457 173 MET C SD 3967 C CE . MET C 145 ? 1.3268 1.5255 1.4106 -0.0501 -0.0351 0.0444 173 MET C CE 3968 N N . HIS C 146 ? 0.4108 0.5962 0.4942 -0.0540 -0.0455 0.0637 174 HIS C N 3969 C CA . HIS C 146 ? 0.5062 0.6849 0.5930 -0.0538 -0.0462 0.0640 174 HIS C CA 3970 C C . HIS C 146 ? 0.6199 0.7970 0.7112 -0.0516 -0.0449 0.0584 174 HIS C C 3971 O O . HIS C 146 ? 0.6645 0.8432 0.7570 -0.0498 -0.0457 0.0554 174 HIS C O 3972 C CB . HIS C 146 ? 0.5784 0.7520 0.6647 -0.0537 -0.0506 0.0679 174 HIS C CB 3973 C CG . HIS C 146 ? 0.6944 0.8682 0.7761 -0.0566 -0.0518 0.0737 174 HIS C CG 3974 N ND1 . HIS C 146 ? 0.6801 0.8501 0.7615 -0.0588 -0.0518 0.0771 174 HIS C ND1 3975 C CD2 . HIS C 146 ? 0.7663 0.9439 0.8435 -0.0577 -0.0531 0.0768 174 HIS C CD2 3976 C CE1 . HIS C 146 ? 0.7922 0.9637 0.8691 -0.0614 -0.0529 0.0820 174 HIS C CE1 3977 N NE2 . HIS C 146 ? 0.7963 0.9723 0.8705 -0.0608 -0.0536 0.0820 174 HIS C NE2 3978 N N . LEU C 147 ? 0.6817 0.8558 0.7752 -0.0519 -0.0426 0.0570 175 LEU C N 3979 C CA . LEU C 147 ? 0.5934 0.7650 0.6908 -0.0501 -0.0412 0.0521 175 LEU C CA 3980 C C . LEU C 147 ? 0.5788 0.7434 0.6791 -0.0497 -0.0426 0.0530 175 LEU C C 3981 O O . LEU C 147 ? 0.6042 0.7661 0.7039 -0.0513 -0.0421 0.0556 175 LEU C O 3982 C CB . LEU C 147 ? 0.5785 0.7524 0.6755 -0.0506 -0.0370 0.0490 175 LEU C CB 3983 C CG . LEU C 147 ? 0.6399 0.8108 0.7402 -0.0493 -0.0351 0.0441 175 LEU C CG 3984 C CD1 . LEU C 147 ? 0.6507 0.8237 0.7524 -0.0478 -0.0354 0.0402 175 LEU C CD1 3985 C CD2 . LEU C 147 ? 0.6387 0.8105 0.7376 -0.0499 -0.0314 0.0422 175 LEU C CD2 3986 N N . ALA C 148 ? 0.6054 0.7673 0.7089 -0.0476 -0.0443 0.0508 176 ALA C N 3987 C CA . ALA C 148 ? 0.6424 0.7975 0.7486 -0.0469 -0.0457 0.0512 176 ALA C CA 3988 C C . ALA C 148 ? 0.6716 0.8247 0.7803 -0.0466 -0.0423 0.0473 176 ALA C C 3989 O O . ALA C 148 ? 0.6832 0.8388 0.7932 -0.0457 -0.0402 0.0429 176 ALA C O 3990 C CB . ALA C 148 ? 0.6057 0.7589 0.7143 -0.0444 -0.0489 0.0504 176 ALA C CB 3991 N N . TYR C 149 ? 0.6737 0.8222 0.7825 -0.0476 -0.0418 0.0490 177 TYR C N 3992 C CA . TYR C 149 ? 0.7279 0.8742 0.8381 -0.0477 -0.0386 0.0459 177 TYR C CA 3993 C C . TYR C 149 ? 0.8170 0.9562 0.9297 -0.0469 -0.0398 0.0459 177 TYR C C 3994 O O . TYR C 149 ? 0.8009 0.9361 0.9126 -0.0477 -0.0420 0.0498 177 TYR C O 3995 C CB . TYR C 149 ? 0.8305 0.9790 0.9381 -0.0498 -0.0364 0.0477 177 TYR C CB 3996 C CG . TYR C 149 ? 0.8888 1.0359 0.9970 -0.0497 -0.0331 0.0443 177 TYR C CG 3997 C CD1 . TYR C 149 ? 0.9676 1.1088 1.0773 -0.0498 -0.0329 0.0444 177 TYR C CD1 3998 C CD2 . TYR C 149 ? 0.8899 1.0412 0.9967 -0.0496 -0.0301 0.0412 177 TYR C CD2 3999 C CE1 . TYR C 149 ? 0.9776 1.1172 1.0874 -0.0497 -0.0300 0.0414 177 TYR C CE1 4000 C CE2 . TYR C 149 ? 0.9465 1.0960 1.0533 -0.0494 -0.0272 0.0382 177 TYR C CE2 4001 C CZ . TYR C 149 ? 0.9674 1.1112 1.0757 -0.0494 -0.0272 0.0384 177 TYR C CZ 4002 O OH . TYR C 149 ? 0.9151 1.0568 1.0229 -0.0492 -0.0244 0.0354 177 TYR C OH 4003 N N . SER C 150 ? 0.8425 0.9797 0.9579 -0.0453 -0.0384 0.0415 178 SER C N 4004 C CA . SER C 150 ? 0.7963 0.9268 0.9138 -0.0444 -0.0389 0.0409 178 SER C CA 4005 C C . SER C 150 ? 0.7906 0.9193 0.9072 -0.0458 -0.0359 0.0402 178 SER C C 4006 O O . SER C 150 ? 0.6039 0.7347 0.7203 -0.0458 -0.0328 0.0368 178 SER C O 4007 C CB . SER C 150 ? 0.7878 0.9174 0.9087 -0.0422 -0.0386 0.0366 178 SER C CB 4008 O OG . SER C 150 ? 0.7234 0.8465 0.8461 -0.0412 -0.0392 0.0360 178 SER C OG 4009 N N . VAL C 151 ? 0.8634 0.9878 0.9791 -0.0469 -0.0371 0.0436 179 VAL C N 4010 C CA . VAL C 151 ? 0.9249 1.0479 1.0396 -0.0483 -0.0349 0.0436 179 VAL C CA 4011 C C . VAL C 151 ? 0.8304 0.9496 0.9466 -0.0471 -0.0325 0.0392 179 VAL C C 4012 O O . VAL C 151 ? 0.7156 0.8298 0.8338 -0.0458 -0.0336 0.0381 179 VAL C O 4013 C CB . VAL C 151 ? 0.9896 1.1081 1.1035 -0.0498 -0.0372 0.0480 179 VAL C CB 4014 C CG1 . VAL C 151 ? 1.0006 1.1172 1.1140 -0.0510 -0.0350 0.0476 179 VAL C CG1 4015 C CG2 . VAL C 151 ? 0.9967 1.1188 1.1083 -0.0517 -0.0391 0.0527 179 VAL C CG2 4016 N N . GLY C 152 ? 0.8148 0.9365 0.9298 -0.0475 -0.0293 0.0368 180 GLY C N 4017 C CA . GLY C 152 ? 0.9712 1.0889 1.0867 -0.0468 -0.0269 0.0330 180 GLY C CA 4018 C C . GLY C 152 ? 1.0989 1.2122 1.2137 -0.0477 -0.0269 0.0347 180 GLY C C 4019 O O . GLY C 152 ? 1.0677 1.1833 1.1811 -0.0492 -0.0274 0.0380 180 GLY C O 4020 N N . LYS C 153 ? 1.2022 1.3096 1.3180 -0.0468 -0.0262 0.0324 181 LYS C N 4021 C CA . LYS C 153 ? 1.1738 1.2765 1.2889 -0.0475 -0.0263 0.0338 181 LYS C CA 4022 C C . LYS C 153 ? 1.0839 1.1888 1.1967 -0.0482 -0.0236 0.0327 181 LYS C C 4023 O O . LYS C 153 ? 1.0430 1.1483 1.1548 -0.0474 -0.0211 0.0290 181 LYS C O 4024 C CB . LYS C 153 ? 1.1342 1.2299 1.2507 -0.0462 -0.0263 0.0314 181 LYS C CB 4025 C CG . LYS C 153 ? 1.1716 1.2614 1.2879 -0.0469 -0.0281 0.0339 181 LYS C CG 4026 C CD . LYS C 153 ? 1.2021 1.2907 1.3193 -0.0474 -0.0318 0.0380 181 LYS C CD 4027 C CE . LYS C 153 ? 1.1883 1.2756 1.3042 -0.0497 -0.0334 0.0421 181 LYS C CE 4028 N NZ . LYS C 153 ? 1.1478 1.2410 1.2622 -0.0513 -0.0315 0.0428 181 LYS C NZ 4029 N N . ASN C 156 ? 1.5323 1.6478 1.6430 -0.0568 -0.0313 0.0517 184 ASN C N 4030 C CA . ASN C 156 ? 1.5685 1.6915 1.6778 -0.0585 -0.0301 0.0535 184 ASN C CA 4031 C C . ASN C 156 ? 1.5980 1.7268 1.7061 -0.0591 -0.0308 0.0556 184 ASN C C 4032 O O . ASN C 156 ? 1.6792 1.8073 1.7876 -0.0576 -0.0313 0.0542 184 ASN C O 4033 C CB . ASN C 156 ? 1.5579 1.6836 1.6666 -0.0571 -0.0268 0.0497 184 ASN C CB 4034 C CG . ASN C 156 ? 1.5458 1.6800 1.6528 -0.0571 -0.0250 0.0495 184 ASN C CG 4035 O OD1 . ASN C 156 ? 1.5367 1.6766 1.6430 -0.0589 -0.0249 0.0522 184 ASN C OD1 4036 N ND2 . ASN C 156 ? 1.5345 1.6700 1.6409 -0.0552 -0.0236 0.0462 184 ASN C ND2 4037 N N . THR C 157 ? 1.5120 1.6470 1.6189 -0.0614 -0.0306 0.0588 185 THR C N 4038 C CA . THR C 157 ? 1.4021 1.5425 1.5073 -0.0623 -0.0314 0.0612 185 THR C CA 4039 C C . THR C 157 ? 1.3842 1.5335 1.4880 -0.0626 -0.0287 0.0606 185 THR C C 4040 O O . THR C 157 ? 1.4129 1.5672 1.5151 -0.0623 -0.0284 0.0607 185 THR C O 4041 C CB . THR C 157 ? 1.3300 1.4691 1.4344 -0.0653 -0.0344 0.0667 185 THR C CB 4042 O OG1 . THR C 157 ? 1.3439 1.4843 1.4484 -0.0678 -0.0340 0.0688 185 THR C OG1 4043 C CG2 . THR C 157 ? 1.2925 1.4227 1.3978 -0.0646 -0.0374 0.0673 185 THR C CG2 4044 N N . SER C 158 ? 1.3060 1.4572 1.4101 -0.0630 -0.0270 0.0598 186 SER C N 4045 C CA . SER C 158 ? 1.2351 1.3946 1.3377 -0.0629 -0.0245 0.0591 186 SER C CA 4046 C C . SER C 158 ? 1.1904 1.3518 1.2919 -0.0600 -0.0224 0.0546 186 SER C C 4047 O O . SER C 158 ? 1.1731 1.3409 1.2727 -0.0599 -0.0215 0.0548 186 SER C O 4048 C CB . SER C 158 ? 1.2225 1.3828 1.3261 -0.0633 -0.0233 0.0586 186 SER C CB 4049 O OG . SER C 158 ? 1.1951 1.3642 1.2975 -0.0632 -0.0211 0.0581 186 SER C OG 4050 N N . ALA C 159 ? 1.1592 1.3148 1.2616 -0.0578 -0.0215 0.0506 187 ALA C N 4051 C CA . ALA C 159 ? 1.1442 1.3008 1.2451 -0.0554 -0.0194 0.0462 187 ALA C CA 4052 C C . ALA C 159 ? 1.0759 1.2338 1.1763 -0.0550 -0.0203 0.0461 187 ALA C C 4053 O O . ALA C 159 ? 1.0560 1.2180 1.1545 -0.0539 -0.0188 0.0440 187 ALA C O 4054 C CB . ALA C 159 ? 1.1292 1.2788 1.2309 -0.0535 -0.0184 0.0422 187 ALA C CB 4055 N N . ILE C 160 ? 1.0420 1.1962 1.1440 -0.0558 -0.0229 0.0485 188 ILE C N 4056 C CA . ILE C 160 ? 0.9883 1.1436 1.0899 -0.0554 -0.0243 0.0486 188 ILE C CA 4057 C C . ILE C 160 ? 0.9999 1.1628 1.0992 -0.0567 -0.0243 0.0513 188 ILE C C 4058 O O . ILE C 160 ? 0.9467 1.1135 1.0444 -0.0557 -0.0236 0.0496 188 ILE C O 4059 C CB . ILE C 160 ? 0.8711 1.0207 0.9746 -0.0559 -0.0274 0.0509 188 ILE C CB 4060 C CG1 . ILE C 160 ? 0.7746 0.9171 0.8803 -0.0542 -0.0272 0.0476 188 ILE C CG1 4061 C CG2 . ILE C 160 ? 0.8600 1.0121 0.9628 -0.0557 -0.0292 0.0521 188 ILE C CG2 4062 C CD1 . ILE C 160 ? 0.7129 0.8493 0.8205 -0.0543 -0.0302 0.0497 188 ILE C CD1 4063 N N . ALA C 161 ? 0.9836 1.1486 1.0825 -0.0590 -0.0252 0.0556 189 ALA C N 4064 C CA . ALA C 161 ? 0.9967 1.1693 1.0931 -0.0606 -0.0251 0.0586 189 ALA C CA 4065 C C . ALA C 161 ? 1.0200 1.1989 1.1147 -0.0593 -0.0220 0.0555 189 ALA C C 4066 O O . ALA C 161 ? 0.9825 1.1670 1.0748 -0.0591 -0.0214 0.0555 189 ALA C O 4067 C CB . ALA C 161 ? 0.9381 1.1117 1.0346 -0.0637 -0.0262 0.0634 189 ALA C CB 4068 N N . ALA C 162 ? 1.0627 1.2405 1.1582 -0.0583 -0.0201 0.0530 190 ALA C N 4069 C CA . ALA C 162 ? 1.1093 1.2919 1.2028 -0.0566 -0.0173 0.0498 190 ALA C CA 4070 C C . ALA C 162 ? 1.0471 1.2285 1.1392 -0.0543 -0.0164 0.0455 190 ALA C C 4071 O O . ALA C 162 ? 0.9729 1.1597 1.0623 -0.0533 -0.0150 0.0441 190 ALA C O 4072 C CB . ALA C 162 ? 1.1527 1.3332 1.2473 -0.0558 -0.0159 0.0479 190 ALA C CB 4073 N N . LYS C 163 ? 1.1066 1.2810 1.2005 -0.0534 -0.0172 0.0435 191 LYS C N 4074 C CA . LYS C 163 ? 1.1649 1.3376 1.2579 -0.0517 -0.0164 0.0395 191 LYS C CA 4075 C C . LYS C 163 ? 1.2243 1.4021 1.3155 -0.0519 -0.0172 0.0405 191 LYS C C 4076 O O . LYS C 163 ? 1.2445 1.4244 1.3335 -0.0506 -0.0159 0.0373 191 LYS C O 4077 C CB . LYS C 163 ? 1.1059 1.2711 1.2017 -0.0512 -0.0176 0.0381 191 LYS C CB 4078 C CG . LYS C 163 ? 1.0706 1.2345 1.1661 -0.0500 -0.0174 0.0345 191 LYS C CG 4079 C CD . LYS C 163 ? 1.0251 1.1819 1.1233 -0.0494 -0.0177 0.0323 191 LYS C CD 4080 C CE . LYS C 163 ? 1.0092 1.1660 1.1077 -0.0486 -0.0176 0.0289 191 LYS C CE 4081 N NZ . LYS C 163 ? 0.9521 1.1028 1.0531 -0.0480 -0.0175 0.0263 191 LYS C NZ 4082 N N . TYR C 164 ? 1.1863 1.3658 1.2780 -0.0537 -0.0194 0.0449 192 TYR C N 4083 C CA . TYR C 164 ? 1.0992 1.2833 1.1891 -0.0541 -0.0206 0.0464 192 TYR C CA 4084 C C . TYR C 164 ? 1.0946 1.2860 1.1818 -0.0555 -0.0202 0.0498 192 TYR C C 4085 O O . TYR C 164 ? 1.0345 1.2291 1.1201 -0.0564 -0.0217 0.0523 192 TYR C O 4086 C CB . TYR C 164 ? 0.9961 1.1763 1.0880 -0.0547 -0.0238 0.0486 192 TYR C CB 4087 C CG . TYR C 164 ? 0.8985 1.0734 0.9927 -0.0530 -0.0241 0.0449 192 TYR C CG 4088 C CD1 . TYR C 164 ? 0.8283 1.0050 0.9214 -0.0516 -0.0233 0.0413 192 TYR C CD1 4089 C CD2 . TYR C 164 ? 0.8533 1.0216 0.9505 -0.0528 -0.0251 0.0448 192 TYR C CD2 4090 C CE1 . TYR C 164 ? 0.8480 1.0207 0.9435 -0.0504 -0.0235 0.0378 192 TYR C CE1 4091 C CE2 . TYR C 164 ? 0.8139 0.9781 0.9134 -0.0513 -0.0251 0.0413 192 TYR C CE2 4092 C CZ . TYR C 164 ? 0.8351 1.0016 0.9337 -0.0503 -0.0243 0.0378 192 TYR C CZ 4093 O OH . TYR C 164 ? 0.8650 1.0280 0.9660 -0.0491 -0.0242 0.0343 192 TYR C OH 4094 N N . GLY C 165 ? 1.0894 1.2835 1.1763 -0.0558 -0.0184 0.0499 193 GLY C N 4095 C CA . GLY C 165 ? 1.0709 1.2731 1.1554 -0.0570 -0.0175 0.0525 193 GLY C CA 4096 C C . GLY C 165 ? 0.9931 1.1969 1.0774 -0.0600 -0.0197 0.0581 193 GLY C C 4097 O O . GLY C 165 ? 1.0254 1.2350 1.1070 -0.0610 -0.0198 0.0602 193 GLY C O 4098 N N . VAL C 166 ? 0.9670 1.1651 1.0539 -0.0614 -0.0216 0.0605 194 VAL C N 4099 C CA . VAL C 166 ? 0.9985 1.1968 1.0848 -0.0644 -0.0239 0.0660 194 VAL C CA 4100 C C . VAL C 166 ? 1.0176 1.2148 1.1057 -0.0666 -0.0240 0.0685 194 VAL C C 4101 O O . VAL C 166 ? 1.0395 1.2328 1.1300 -0.0655 -0.0232 0.0660 194 VAL C O 4102 C CB . VAL C 166 ? 0.9499 1.1417 1.0369 -0.0642 -0.0272 0.0671 194 VAL C CB 4103 C CG1 . VAL C 166 ? 0.9308 1.1154 1.0201 -0.0656 -0.0293 0.0695 194 VAL C CG1 4104 C CG2 . VAL C 166 ? 0.9259 1.1214 1.0096 -0.0656 -0.0288 0.0704 194 VAL C CG2 4105 N N . THR C 167 ? 0.9685 1.1692 1.0552 -0.0699 -0.0249 0.0733 195 THR C N 4106 C CA . THR C 167 ? 1.0148 1.2151 1.1032 -0.0725 -0.0251 0.0761 195 THR C CA 4107 C C . THR C 167 ? 1.0904 1.2805 1.1810 -0.0728 -0.0278 0.0769 195 THR C C 4108 O O . THR C 167 ? 1.0983 1.2834 1.1882 -0.0726 -0.0303 0.0781 195 THR C O 4109 C CB . THR C 167 ? 1.0287 1.2353 1.1147 -0.0764 -0.0255 0.0813 195 THR C CB 4110 O OG1 . THR C 167 ? 1.0838 1.2999 1.1694 -0.0765 -0.0224 0.0803 195 THR C OG1 4111 C CG2 . THR C 167 ? 0.9751 1.1769 1.0620 -0.0800 -0.0279 0.0857 195 THR C CG2 4112 N N . GLU C 168 ? 1.1121 1.2991 1.2052 -0.0730 -0.0274 0.0761 196 GLU C N 4113 C CA . GLU C 168 ? 1.1231 1.3003 1.2182 -0.0731 -0.0298 0.0765 196 GLU C CA 4114 C C . GLU C 168 ? 0.9921 1.1658 1.0858 -0.0764 -0.0331 0.0820 196 GLU C C 4115 O O . GLU C 168 ? 0.8523 1.0178 0.9463 -0.0757 -0.0358 0.0825 196 GLU C O 4116 C CB . GLU C 168 ? 1.1640 1.3391 1.2617 -0.0730 -0.0287 0.0749 196 GLU C CB 4117 C CG . GLU C 168 ? 1.1825 1.3473 1.2821 -0.0729 -0.0311 0.0751 196 GLU C CG 4118 C CD . GLU C 168 ? 1.2155 1.3781 1.3172 -0.0724 -0.0299 0.0729 196 GLU C CD 4119 O OE1 . GLU C 168 ? 1.1948 1.3636 1.2968 -0.0715 -0.0272 0.0707 196 GLU C OE1 4120 O OE2 . GLU C 168 ? 1.2337 1.3884 1.3369 -0.0727 -0.0317 0.0733 196 GLU C OE2 4121 N N . SER C 169 ? 0.9527 1.1325 1.0446 -0.0799 -0.0328 0.0859 197 SER C N 4122 C CA . SER C 169 ? 0.9501 1.1270 1.0396 -0.0835 -0.0358 0.0914 197 SER C CA 4123 C C . SER C 169 ? 0.9424 1.1175 1.0292 -0.0824 -0.0378 0.0924 197 SER C C 4124 O O . SER C 169 ? 0.9161 1.0838 1.0016 -0.0833 -0.0412 0.0952 197 SER C O 4125 C CB . SER C 169 ? 0.8656 1.0504 0.9536 -0.0877 -0.0348 0.0953 197 SER C CB 4126 O OG . SER C 169 ? 0.8630 1.0442 0.9483 -0.0916 -0.0378 0.1008 197 SER C OG 4127 N N . THR C 170 ? 0.8814 1.0629 0.9672 -0.0802 -0.0358 0.0898 198 THR C N 4128 C CA . THR C 170 ? 0.9171 1.0976 1.0006 -0.0787 -0.0374 0.0899 198 THR C CA 4129 C C . THR C 170 ? 0.9179 1.0890 1.0033 -0.0761 -0.0400 0.0881 198 THR C C 4130 O O . THR C 170 ? 0.8936 1.0598 0.9771 -0.0764 -0.0433 0.0907 198 THR C O 4131 C CB . THR C 170 ? 0.9799 1.1678 1.0628 -0.0760 -0.0346 0.0859 198 THR C CB 4132 O OG1 . THR C 170 ? 1.0205 1.2177 1.1012 -0.0780 -0.0324 0.0876 198 THR C OG1 4133 C CG2 . THR C 170 ? 0.9785 1.1646 1.0597 -0.0740 -0.0365 0.0853 198 THR C CG2 4134 N N . LEU C 171 ? 0.8558 1.0242 0.9446 -0.0734 -0.0386 0.0836 199 LEU C N 4135 C CA . LEU C 171 ? 0.8388 0.9990 0.9298 -0.0707 -0.0405 0.0812 199 LEU C CA 4136 C C . LEU C 171 ? 0.9471 1.0986 1.0383 -0.0723 -0.0439 0.0846 199 LEU C C 4137 O O . LEU C 171 ? 0.9683 1.1139 1.0591 -0.0709 -0.0468 0.0851 199 LEU C O 4138 C CB . LEU C 171 ? 0.7579 0.9175 0.8521 -0.0681 -0.0378 0.0759 199 LEU C CB 4139 C CG . LEU C 171 ? 0.8434 0.9960 0.9401 -0.0650 -0.0390 0.0725 199 LEU C CG 4140 C CD1 . LEU C 171 ? 0.9222 1.0767 1.0182 -0.0630 -0.0398 0.0710 199 LEU C CD1 4141 C CD2 . LEU C 171 ? 0.8306 0.9823 0.9299 -0.0632 -0.0362 0.0679 199 LEU C CD2 4142 N N . LEU C 172 ? 0.9206 1.0714 1.0121 -0.0751 -0.0435 0.0868 200 LEU C N 4143 C CA . LEU C 172 ? 0.7944 0.9364 0.8858 -0.0767 -0.0467 0.0898 200 LEU C CA 4144 C C . LEU C 172 ? 0.7728 0.9122 0.8603 -0.0790 -0.0501 0.0950 200 LEU C C 4145 O O . LEU C 172 ? 0.7327 0.8633 0.8196 -0.0787 -0.0536 0.0965 200 LEU C O 4146 C CB . LEU C 172 ? 0.8395 0.9819 0.9319 -0.0796 -0.0456 0.0911 200 LEU C CB 4147 C CG . LEU C 172 ? 0.8437 0.9855 0.9397 -0.0774 -0.0432 0.0866 200 LEU C CG 4148 C CD1 . LEU C 172 ? 0.8710 1.0154 0.9677 -0.0806 -0.0420 0.0883 200 LEU C CD1 4149 C CD2 . LEU C 172 ? 0.7089 0.8408 0.8067 -0.0749 -0.0452 0.0845 200 LEU C CD2 4150 N N . THR C 173 ? 0.7546 0.9013 0.8392 -0.0813 -0.0492 0.0976 201 THR C N 4151 C CA . THR C 173 ? 0.9014 1.0458 0.9816 -0.0837 -0.0524 0.1027 201 THR C CA 4152 C C . THR C 173 ? 0.9165 1.0585 0.9957 -0.0802 -0.0545 0.1013 201 THR C C 4153 O O . THR C 173 ? 0.8817 1.0162 0.9587 -0.0802 -0.0584 0.1039 201 THR C O 4154 C CB . THR C 173 ? 0.9956 1.1489 1.0726 -0.0875 -0.0507 0.1061 201 THR C CB 4155 O OG1 . THR C 173 ? 1.0787 1.2408 1.1561 -0.0852 -0.0476 0.1028 201 THR C OG1 4156 C CG2 . THR C 173 ? 1.0055 1.1618 1.0838 -0.0911 -0.0489 0.1076 201 THR C CG2 4157 N N . ARG C 174 ? 0.8659 1.0140 0.9466 -0.0772 -0.0520 0.0970 202 ARG C N 4158 C CA . ARG C 174 ? 0.7478 0.8950 0.8282 -0.0738 -0.0536 0.0951 202 ARG C CA 4159 C C . ARG C 174 ? 0.7378 0.8757 0.8207 -0.0710 -0.0563 0.0933 202 ARG C C 4160 O O . ARG C 174 ? 0.7559 0.8895 0.8375 -0.0693 -0.0596 0.0941 202 ARG C O 4161 C CB . ARG C 174 ? 0.7372 0.8922 0.8193 -0.0713 -0.0502 0.0902 202 ARG C CB 4162 C CG . ARG C 174 ? 0.7650 0.9202 0.8470 -0.0681 -0.0517 0.0880 202 ARG C CG 4163 C CD . ARG C 174 ? 0.7244 0.8811 0.8015 -0.0695 -0.0542 0.0922 202 ARG C CD 4164 N NE . ARG C 174 ? 0.6135 0.7677 0.6907 -0.0663 -0.0569 0.0907 202 ARG C NE 4165 C CZ . ARG C 174 ? 0.6367 0.7902 0.7098 -0.0666 -0.0600 0.0939 202 ARG C CZ 4166 N NH1 . ARG C 174 ? 0.5592 0.7139 0.6276 -0.0703 -0.0606 0.0991 202 ARG C NH1 4167 N NH2 . ARG C 174 ? 0.6243 0.7758 0.6981 -0.0633 -0.0626 0.0920 202 ARG C NH2 4168 N N . ASN C 175 ? 0.7039 0.8388 0.7903 -0.0704 -0.0549 0.0908 203 ASN C N 4169 C CA . ASN C 175 ? 0.7563 0.8826 0.8451 -0.0677 -0.0572 0.0889 203 ASN C CA 4170 C C . ASN C 175 ? 0.8893 1.0071 0.9767 -0.0701 -0.0600 0.0928 203 ASN C C 4171 O O . ASN C 175 ? 0.8825 0.9928 0.9719 -0.0681 -0.0616 0.0913 203 ASN C O 4172 C CB . ASN C 175 ? 0.6847 0.8122 0.7780 -0.0649 -0.0541 0.0831 203 ASN C CB 4173 C CG . ASN C 175 ? 0.6319 0.7655 0.7263 -0.0622 -0.0523 0.0791 203 ASN C CG 4174 O OD1 . ASN C 175 ? 0.6027 0.7341 0.6982 -0.0593 -0.0542 0.0772 203 ASN C OD1 4175 N ND2 . ASN C 175 ? 0.4525 0.5939 0.5466 -0.0630 -0.0488 0.0777 203 ASN C ND2 4176 N N . LYS C 176 ? 0.9874 1.1069 1.0714 -0.0744 -0.0604 0.0977 204 LYS C N 4177 C CA . LYS C 176 ? 1.0278 1.1399 1.1094 -0.0777 -0.0632 0.1022 204 LYS C CA 4178 C C . LYS C 176 ? 1.0197 1.1258 1.1043 -0.0774 -0.0630 0.1004 204 LYS C C 4179 O O . LYS C 176 ? 1.0313 1.1278 1.1151 -0.0769 -0.0663 0.1017 204 LYS C O 4180 C CB . LYS C 176 ? 1.0837 1.1879 1.1614 -0.0773 -0.0680 0.1056 204 LYS C CB 4181 C CG . LYS C 176 ? 1.2183 1.3216 1.2906 -0.0824 -0.0699 0.1120 204 LYS C CG 4182 C CD . LYS C 176 ? 1.2466 1.3378 1.3153 -0.0830 -0.0751 0.1157 204 LYS C CD 4183 C CE . LYS C 176 ? 1.2184 1.3085 1.2814 -0.0888 -0.0766 0.1222 204 LYS C CE 4184 N NZ . LYS C 176 ? 1.2119 1.2895 1.2704 -0.0896 -0.0819 0.1260 204 LYS C NZ 4185 N N . ILE C 177 ? 0.9933 1.1049 1.0811 -0.0776 -0.0591 0.0976 205 ILE C N 4186 C CA . ILE C 177 ? 0.9898 1.0962 1.0803 -0.0773 -0.0587 0.0957 205 ILE C CA 4187 C C . ILE C 177 ? 1.0144 1.1228 1.1043 -0.0819 -0.0578 0.0987 205 ILE C C 4188 O O . ILE C 177 ? 1.0128 1.1302 1.1023 -0.0842 -0.0552 0.0996 205 ILE C O 4189 C CB . ILE C 177 ? 0.8862 0.9960 0.9808 -0.0736 -0.0553 0.0896 205 ILE C CB 4190 C CG1 . ILE C 177 ? 0.8633 0.9712 0.9590 -0.0693 -0.0564 0.0865 205 ILE C CG1 4191 C CG2 . ILE C 177 ? 0.7929 0.8979 0.8900 -0.0735 -0.0546 0.0877 205 ILE C CG2 4192 C CD1 . ILE C 177 ? 0.8563 0.9693 0.9551 -0.0661 -0.0528 0.0808 205 ILE C CD1 4193 N N . ASP C 179 ? 1.0773 1.1837 1.1724 -0.0842 -0.0547 0.0959 207 ASP C N 4194 C CA . ASP C 179 ? 1.0722 1.1763 1.1703 -0.0829 -0.0533 0.0925 207 ASP C CA 4195 C C . ASP C 179 ? 1.0284 1.1327 1.1291 -0.0779 -0.0511 0.0867 207 ASP C C 4196 O O . ASP C 179 ? 1.1030 1.2002 1.2040 -0.0750 -0.0529 0.0850 207 ASP C O 4197 C CB . ASP C 179 ? 1.1798 1.2727 1.2771 -0.0840 -0.0567 0.0943 207 ASP C CB 4198 C CG . ASP C 179 ? 1.2987 1.3890 1.3987 -0.0833 -0.0555 0.0913 207 ASP C CG 4199 O OD1 . ASP C 179 ? 1.3489 1.4464 1.4510 -0.0828 -0.0521 0.0887 207 ASP C OD1 4200 O OD2 . ASP C 179 ? 1.3475 1.4281 1.4471 -0.0830 -0.0581 0.0915 207 ASP C OD2 4201 N N . PRO C 180 ? 0.9241 1.0365 1.0265 -0.0768 -0.0474 0.0837 208 PRO C N 4202 C CA . PRO C 180 ? 0.8825 0.9959 0.9870 -0.0726 -0.0449 0.0782 208 PRO C CA 4203 C C . PRO C 180 ? 0.9807 1.0858 1.0870 -0.0701 -0.0453 0.0749 208 PRO C C 4204 O O . PRO C 180 ? 1.0650 1.1681 1.1724 -0.0667 -0.0447 0.0713 208 PRO C O 4205 C CB . PRO C 180 ? 0.8033 0.9255 0.9085 -0.0731 -0.0413 0.0765 208 PRO C CB 4206 C CG . PRO C 180 ? 0.8600 0.9886 0.9633 -0.0769 -0.0416 0.0811 208 PRO C CG 4207 C CD . PRO C 180 ? 0.8819 1.0035 0.9838 -0.0799 -0.0453 0.0856 208 PRO C CD 4208 N N . THR C 181 ? 1.0014 1.1019 1.1080 -0.0718 -0.0462 0.0760 209 THR C N 4209 C CA . THR C 181 ? 1.0271 1.1203 1.1352 -0.0696 -0.0462 0.0727 209 THR C CA 4210 C C . THR C 181 ? 1.1096 1.1946 1.2178 -0.0669 -0.0486 0.0717 209 THR C C 4211 O O . THR C 181 ? 1.1231 1.2034 1.2327 -0.0642 -0.0480 0.0680 209 THR C O 4212 C CB . THR C 181 ? 0.8813 0.9707 0.9893 -0.0723 -0.0474 0.0747 209 THR C CB 4213 O OG1 . THR C 181 ? 0.8588 0.9439 0.9649 -0.0752 -0.0510 0.0795 209 THR C OG1 4214 C CG2 . THR C 181 ? 0.7513 0.8494 0.8598 -0.0744 -0.0448 0.0751 209 THR C CG2 4215 N N . LYS C 182 ? 1.1591 1.2426 1.2656 -0.0676 -0.0514 0.0749 210 LYS C N 4216 C CA . LYS C 182 ? 1.2817 1.3578 1.3882 -0.0648 -0.0540 0.0740 210 LYS C CA 4217 C C . LYS C 182 ? 1.3317 1.4120 1.4396 -0.0614 -0.0525 0.0705 210 LYS C C 4218 O O . LYS C 182 ? 1.3170 1.3934 1.4252 -0.0589 -0.0545 0.0696 210 LYS C O 4219 C CB . LYS C 182 ? 1.3481 1.4194 1.4517 -0.0669 -0.0582 0.0790 210 LYS C CB 4220 C CG . LYS C 182 ? 1.3993 1.4651 1.5013 -0.0704 -0.0603 0.0824 210 LYS C CG 4221 C CD . LYS C 182 ? 1.3877 1.4445 1.4908 -0.0684 -0.0612 0.0799 210 LYS C CD 4222 C CE . LYS C 182 ? 1.3654 1.4151 1.4663 -0.0718 -0.0642 0.0836 210 LYS C CE 4223 N NZ . LYS C 182 ? 1.3500 1.4057 1.4510 -0.0761 -0.0625 0.0857 210 LYS C NZ 4224 N N . LEU C 183 ? 1.3143 1.4030 1.4230 -0.0615 -0.0490 0.0685 211 LEU C N 4225 C CA . LEU C 183 ? 1.2445 1.3377 1.3543 -0.0587 -0.0472 0.0650 211 LEU C CA 4226 C C . LEU C 183 ? 1.3007 1.3896 1.4128 -0.0553 -0.0464 0.0603 211 LEU C C 4227 O O . LEU C 183 ? 1.3420 1.4286 1.4551 -0.0549 -0.0445 0.0578 211 LEU C O 4228 C CB . LEU C 183 ? 1.1298 1.2318 1.2395 -0.0595 -0.0436 0.0637 211 LEU C CB 4229 C CG . LEU C 183 ? 1.0938 1.2012 1.2039 -0.0575 -0.0424 0.0613 211 LEU C CG 4230 C CD1 . LEU C 183 ? 1.0382 1.1475 1.1465 -0.0584 -0.0450 0.0650 211 LEU C CD1 4231 C CD2 . LEU C 183 ? 1.0681 1.1829 1.1779 -0.0576 -0.0386 0.0590 211 LEU C CD2 4232 N N . GLN C 184 ? 1.3041 1.3922 1.4171 -0.0528 -0.0477 0.0589 212 GLN C N 4233 C CA . GLN C 184 ? 1.3106 1.3961 1.4260 -0.0496 -0.0467 0.0542 212 GLN C CA 4234 C C . GLN C 184 ? 1.3566 1.4493 1.4731 -0.0484 -0.0435 0.0506 212 GLN C C 4235 O O . GLN C 184 ? 1.4010 1.4998 1.5166 -0.0492 -0.0435 0.0519 212 GLN C O 4236 C CB . GLN C 184 ? 1.2936 1.3740 1.4096 -0.0473 -0.0502 0.0546 212 GLN C CB 4237 C CG . GLN C 184 ? 1.2917 1.3630 1.4068 -0.0475 -0.0531 0.0567 212 GLN C CG 4238 C CD . GLN C 184 ? 1.3035 1.3697 1.4188 -0.0448 -0.0567 0.0570 212 GLN C CD 4239 O OE1 . GLN C 184 ? 1.2837 1.3537 1.4000 -0.0428 -0.0573 0.0558 212 GLN C OE1 4240 N NE2 . GLN C 184 ? 1.3281 1.3857 1.4424 -0.0445 -0.0594 0.0583 212 GLN C NE2 4241 N N . MET C 185 ? 1.3535 1.4453 1.4717 -0.0468 -0.0409 0.0461 213 MET C N 4242 C CA . MET C 185 ? 1.3397 1.4371 1.4588 -0.0457 -0.0382 0.0423 213 MET C CA 4243 C C . MET C 185 ? 1.3226 1.4220 1.4432 -0.0438 -0.0403 0.0419 213 MET C C 4244 O O . MET C 185 ? 1.3481 1.4427 1.4699 -0.0421 -0.0427 0.0420 213 MET C O 4245 C CB . MET C 185 ? 1.2720 1.3668 1.3924 -0.0444 -0.0354 0.0376 213 MET C CB 4246 C CG . MET C 185 ? 1.3173 1.4174 1.4380 -0.0439 -0.0322 0.0337 213 MET C CG 4247 S SD . MET C 185 ? 1.7099 1.8064 1.8318 -0.0425 -0.0292 0.0282 213 MET C SD 4248 C CE . MET C 185 ? 0.7009 0.7970 0.8262 -0.0400 -0.0310 0.0263 213 MET C CE 4249 N N . GLY C 186 ? 1.2107 1.3169 1.3309 -0.0441 -0.0395 0.0415 214 GLY C N 4250 C CA . GLY C 186 ? 1.1753 1.2840 1.2969 -0.0423 -0.0413 0.0408 214 GLY C CA 4251 C C . GLY C 186 ? 1.1075 1.2155 1.2277 -0.0426 -0.0453 0.0454 214 GLY C C 4252 O O . GLY C 186 ? 1.0521 1.1620 1.1731 -0.0409 -0.0474 0.0452 214 GLY C O 4253 N N . GLN C 187 ? 1.0229 1.1282 1.1407 -0.0448 -0.0465 0.0496 215 GLN C N 4254 C CA . GLN C 187 ? 0.9744 1.0792 1.0898 -0.0458 -0.0499 0.0544 215 GLN C CA 4255 C C . GLN C 187 ? 0.8532 0.9660 0.9675 -0.0464 -0.0491 0.0546 215 GLN C C 4256 O O . GLN C 187 ? 0.8393 0.9571 0.9531 -0.0475 -0.0458 0.0530 215 GLN C O 4257 C CB . GLN C 187 ? 0.9571 1.0587 1.0699 -0.0489 -0.0506 0.0587 215 GLN C CB 4258 C CG . GLN C 187 ? 0.9608 1.0606 1.0708 -0.0503 -0.0544 0.0639 215 GLN C CG 4259 C CD . GLN C 187 ? 1.0265 1.1216 1.1343 -0.0533 -0.0555 0.0679 215 GLN C CD 4260 O OE1 . GLN C 187 ? 0.9909 1.0838 1.0997 -0.0540 -0.0538 0.0667 215 GLN C OE1 4261 N NE2 . GLN C 187 ? 1.1052 1.1984 1.2099 -0.0552 -0.0587 0.0728 215 GLN C NE2 4262 N N . ILE C 188 ? 0.7071 0.8208 0.8205 -0.0455 -0.0521 0.0564 216 ILE C N 4263 C CA . ILE C 188 ? 0.6368 0.7580 0.7491 -0.0458 -0.0514 0.0563 216 ILE C CA 4264 C C . ILE C 188 ? 0.6148 0.7386 0.7231 -0.0489 -0.0518 0.0611 216 ILE C C 4265 O O . ILE C 188 ? 0.6548 0.7749 0.7608 -0.0501 -0.0549 0.0655 216 ILE C O 4266 C CB . ILE C 188 ? 0.5595 0.6815 0.6726 -0.0433 -0.0545 0.0558 216 ILE C CB 4267 C CG1 . ILE C 188 ? 0.5906 0.7105 0.7079 -0.0401 -0.0543 0.0512 216 ILE C CG1 4268 C CG2 . ILE C 188 ? 0.5173 0.6472 0.6291 -0.0437 -0.0536 0.0554 216 ILE C CG2 4269 C CD1 . ILE C 188 ? 0.5891 0.7132 0.7087 -0.0400 -0.0500 0.0462 216 ILE C CD1 4270 N N . LEU C 189 ? 0.5413 0.6715 0.6488 -0.0503 -0.0485 0.0601 217 LEU C N 4271 C CA . LEU C 189 ? 0.5954 0.7293 0.6993 -0.0532 -0.0483 0.0641 217 LEU C CA 4272 C C . LEU C 189 ? 0.7309 0.8715 0.8329 -0.0531 -0.0485 0.0643 217 LEU C C 4273 O O . LEU C 189 ? 0.8241 0.9682 0.9276 -0.0512 -0.0473 0.0604 217 LEU C O 4274 C CB . LEU C 189 ? 0.6654 0.8022 0.7692 -0.0549 -0.0446 0.0630 217 LEU C CB 4275 C CG . LEU C 189 ? 0.6522 0.7835 0.7575 -0.0555 -0.0440 0.0630 217 LEU C CG 4276 C CD1 . LEU C 189 ? 0.5591 0.6947 0.6637 -0.0571 -0.0405 0.0622 217 LEU C CD1 4277 C CD2 . LEU C 189 ? 0.6946 0.8201 0.7985 -0.0573 -0.0475 0.0679 217 LEU C CD2 4278 N N . ASP C 190 ? 0.5818 0.7239 0.6802 -0.0553 -0.0501 0.0691 218 ASP C N 4279 C CA . ASP C 190 ? 0.5723 0.7210 0.6680 -0.0557 -0.0501 0.0699 218 ASP C CA 4280 C C . ASP C 190 ? 0.6609 0.8158 0.7550 -0.0578 -0.0465 0.0700 218 ASP C C 4281 O O . ASP C 190 ? 0.6942 0.8495 0.7861 -0.0606 -0.0464 0.0739 218 ASP C O 4282 C CB . ASP C 190 ? 0.6661 0.8125 0.7583 -0.0569 -0.0540 0.0751 218 ASP C CB 4283 C CG . ASP C 190 ? 0.6131 0.7661 0.7016 -0.0577 -0.0540 0.0766 218 ASP C CG 4284 O OD1 . ASP C 190 ? 0.5991 0.7588 0.6878 -0.0573 -0.0511 0.0737 218 ASP C OD1 4285 O OD2 . ASP C 190 ? 0.6797 0.8309 0.7648 -0.0588 -0.0572 0.0810 218 ASP C OD2 4286 N N . VAL C 191 ? 0.6367 0.7964 0.7317 -0.0565 -0.0435 0.0656 219 VAL C N 4287 C CA . VAL C 191 ? 0.5973 0.7629 0.6908 -0.0578 -0.0400 0.0650 219 VAL C CA 4288 C C . VAL C 191 ? 0.6352 0.8080 0.7253 -0.0583 -0.0396 0.0658 219 VAL C C 4289 O O . VAL C 191 ? 0.7121 0.8876 0.8023 -0.0565 -0.0392 0.0625 219 VAL C O 4290 C CB . VAL C 191 ? 0.5567 0.7226 0.6527 -0.0560 -0.0369 0.0594 219 VAL C CB 4291 C CG1 . VAL C 191 ? 0.4877 0.6590 0.5820 -0.0569 -0.0334 0.0585 219 VAL C CG1 4292 C CG2 . VAL C 191 ? 0.5863 0.7449 0.6856 -0.0552 -0.0373 0.0581 219 VAL C CG2 4293 N N . PRO C 192 ? 0.6617 0.8377 0.7485 -0.0609 -0.0398 0.0702 220 PRO C N 4294 C CA . PRO C 192 ? 0.6876 0.8701 0.7706 -0.0613 -0.0397 0.0713 220 PRO C CA 4295 C C . PRO C 192 ? 0.6786 0.8681 0.7606 -0.0610 -0.0359 0.0683 220 PRO C C 4296 O O . PRO C 192 ? 0.6800 0.8738 0.7602 -0.0629 -0.0340 0.0702 220 PRO C O 4297 C CB . PRO C 192 ? 0.7750 0.9576 0.8549 -0.0645 -0.0415 0.0774 220 PRO C CB 4298 C CG . PRO C 192 ? 0.8124 0.9902 0.8945 -0.0661 -0.0415 0.0791 220 PRO C CG 4299 C CD . PRO C 192 ? 0.7562 0.9303 0.8425 -0.0637 -0.0401 0.0742 220 PRO C CD 4300 N N . LEU C 193 ? 0.7214 0.9121 0.8042 -0.0586 -0.0349 0.0636 221 LEU C N 4301 C CA . LEU C 193 ? 0.6952 0.8911 0.7768 -0.0577 -0.0315 0.0599 221 LEU C CA 4302 C C . LEU C 193 ? 0.8336 1.0367 0.9107 -0.0586 -0.0309 0.0617 221 LEU C C 4303 O O . LEU C 193 ? 0.8161 1.0207 0.8913 -0.0582 -0.0328 0.0622 221 LEU C O 4304 C CB . LEU C 193 ? 0.6601 0.8546 0.7433 -0.0552 -0.0312 0.0548 221 LEU C CB 4305 C CG . LEU C 193 ? 0.6888 0.8769 0.7763 -0.0540 -0.0314 0.0520 221 LEU C CG 4306 C CD1 . LEU C 193 ? 0.5349 0.7232 0.6233 -0.0521 -0.0304 0.0467 221 LEU C CD1 4307 C CD2 . LEU C 193 ? 0.7429 0.9285 0.8318 -0.0546 -0.0294 0.0518 221 LEU C CD2 4308 N N . PRO C 194 ? 0.9348 1.1427 1.0102 -0.0597 -0.0284 0.0625 222 PRO C N 4309 C CA . PRO C 194 ? 0.9394 1.1549 1.0104 -0.0604 -0.0275 0.0639 222 PRO C CA 4310 C C . PRO C 194 ? 0.8539 1.0716 0.9231 -0.0582 -0.0271 0.0599 222 PRO C C 4311 O O . PRO C 194 ? 0.8873 1.1034 0.9581 -0.0563 -0.0255 0.0552 222 PRO C O 4312 C CB . PRO C 194 ? 0.9145 1.1345 0.9850 -0.0609 -0.0242 0.0634 222 PRO C CB 4313 C CG . PRO C 194 ? 0.9571 1.1718 1.0318 -0.0609 -0.0239 0.0627 222 PRO C CG 4314 C CD . PRO C 194 ? 0.9691 1.1759 1.0465 -0.0605 -0.0266 0.0627 222 PRO C CD 4315 N N . VAL C 195 ? 0.8208 1.0418 0.8866 -0.0586 -0.0287 0.0618 223 VAL C N 4316 C CA . VAL C 195 ? 0.7827 1.0061 0.8464 -0.0568 -0.0286 0.0582 223 VAL C CA 4317 C C . VAL C 195 ? 0.8569 1.0855 0.9180 -0.0557 -0.0251 0.0549 223 VAL C C 4318 O O . VAL C 195 ? 0.9004 1.1351 0.9579 -0.0565 -0.0239 0.0568 223 VAL C O 4319 C CB . VAL C 195 ? 0.7320 0.9580 0.7921 -0.0576 -0.0312 0.0614 223 VAL C CB 4320 C C1 . NAG D . ? 0.6406 0.6892 0.6961 -0.0270 -0.0032 -0.0043 301 NAG A C1 4321 C C2 . NAG D . ? 0.6226 0.6827 0.6821 -0.0266 -0.0042 -0.0019 301 NAG A C2 4322 C C3 . NAG D . ? 0.6522 0.7187 0.7178 -0.0294 -0.0046 0.0011 301 NAG A C3 4323 C C4 . NAG D . ? 0.7360 0.8005 0.7998 -0.0303 -0.0029 -0.0006 301 NAG A C4 4324 C C5 . NAG D . ? 0.7644 0.8183 0.8250 -0.0307 -0.0019 -0.0030 301 NAG A C5 4325 C C6 . NAG D . ? 0.7711 0.8230 0.8304 -0.0321 -0.0001 -0.0048 301 NAG A C6 4326 C C7 . NAG D . ? 0.7378 0.8013 0.7949 -0.0223 -0.0059 -0.0025 301 NAG A C7 4327 C C8 . NAG D . ? 0.6617 0.7267 0.7200 -0.0211 -0.0077 -0.0016 301 NAG A C8 4328 N N2 . NAG D . ? 0.6573 0.7199 0.7181 -0.0254 -0.0059 -0.0007 301 NAG A N2 4329 O O3 . NAG D . ? 0.7901 0.8670 0.8592 -0.0294 -0.0055 0.0035 301 NAG A O3 4330 O O4 . NAG D . ? 0.8127 0.8831 0.8817 -0.0326 -0.0033 0.0019 301 NAG A O4 4331 O O5 . NAG D . ? 0.7578 0.8052 0.8126 -0.0285 -0.0016 -0.0055 301 NAG A O5 4332 O O6 . NAG D . ? 0.8166 0.8688 0.8712 -0.0308 0.0011 -0.0071 301 NAG A O6 4333 O O7 . NAG D . ? 0.6608 0.7237 0.7135 -0.0206 -0.0047 -0.0048 301 NAG A O7 4334 C C1 . NAG E . ? 0.4918 0.4518 0.4709 -0.0678 0.0301 -0.0490 302 NAG A C1 4335 C C2 . NAG E . ? 0.5541 0.5126 0.5288 -0.0639 0.0279 -0.0485 302 NAG A C2 4336 C C3 . NAG E . ? 0.5559 0.5061 0.5204 -0.0657 0.0284 -0.0511 302 NAG A C3 4337 C C4 . NAG E . ? 0.6071 0.5446 0.5626 -0.0689 0.0304 -0.0531 302 NAG A C4 4338 C C5 . NAG E . ? 0.6072 0.5481 0.5683 -0.0730 0.0326 -0.0532 302 NAG A C5 4339 C C6 . NAG E . ? 0.6151 0.5432 0.5670 -0.0757 0.0346 -0.0549 302 NAG A C6 4340 C C7 . NAG E . ? 0.4620 0.4379 0.4507 -0.0581 0.0245 -0.0441 302 NAG A C7 4341 C C8 . NAG E . ? 0.4077 0.3964 0.4055 -0.0570 0.0232 -0.0422 302 NAG A C8 4342 N N2 . NAG E . ? 0.5577 0.5284 0.5410 -0.0619 0.0262 -0.0466 302 NAG A N2 4343 O O3 . NAG E . ? 0.5926 0.5396 0.5523 -0.0612 0.0263 -0.0507 302 NAG A O3 4344 O O4 . NAG E . ? 0.7303 0.6604 0.6767 -0.0715 0.0309 -0.0555 302 NAG A O4 4345 O O5 . NAG E . ? 0.6361 0.5845 0.6065 -0.0705 0.0320 -0.0509 302 NAG A O5 4346 O O6 . NAG E . ? 0.6723 0.6039 0.6289 -0.0799 0.0370 -0.0554 302 NAG A O6 4347 O O7 . NAG E . ? 0.4417 0.4124 0.4281 -0.0557 0.0240 -0.0433 302 NAG A O7 4348 C C1 . NAG F . ? 0.7416 0.8899 0.7011 0.0550 0.0036 -0.0550 301 NAG B C1 4349 C C2 . NAG F . ? 0.7333 0.8783 0.6875 0.0624 0.0022 -0.0587 301 NAG B C2 4350 C C3 . NAG F . ? 0.8670 1.0259 0.8213 0.0679 0.0027 -0.0604 301 NAG B C3 4351 C C4 . NAG F . ? 0.9196 1.0763 0.8671 0.0687 0.0032 -0.0627 301 NAG B C4 4352 C C5 . NAG F . ? 0.9035 1.0629 0.8558 0.0612 0.0045 -0.0590 301 NAG B C5 4353 C C7 . NAG F . ? 0.8663 0.9959 0.8208 0.0621 0.0002 -0.0583 301 NAG B C7 4354 C C8 . NAG F . ? 0.8439 0.9570 0.7861 0.0649 -0.0008 -0.0626 301 NAG B C8 4355 N N2 . NAG F . ? 0.7663 0.9111 0.7255 0.0621 0.0015 -0.0570 301 NAG B N2 4356 O O3 . NAG F . ? 0.8696 1.0268 0.8197 0.0751 0.0013 -0.0638 301 NAG B O3 4357 O O4 . NAG F . ? 1.0292 1.1989 0.9765 0.0741 0.0037 -0.0644 301 NAG B O4 4358 O O5 . NAG F . ? 0.8994 1.0488 0.8540 0.0555 0.0042 -0.0566 301 NAG B O5 4359 O O7 . NAG F . ? 0.7925 0.9208 0.7520 0.0598 -0.0002 -0.0560 301 NAG B O7 4360 C C1 . NAG G . ? 0.6884 0.7325 0.7465 -0.0544 0.0165 -0.0276 302 NAG B C1 4361 C C2 . NAG G . ? 0.8080 0.8534 0.8711 -0.0557 0.0173 -0.0282 302 NAG B C2 4362 C C3 . NAG G . ? 0.8576 0.9062 0.9268 -0.0536 0.0152 -0.0252 302 NAG B C3 4363 C C4 . NAG G . ? 0.9479 0.9915 1.0143 -0.0514 0.0142 -0.0233 302 NAG B C4 4364 C C5 . NAG G . ? 0.8588 0.8996 0.9191 -0.0505 0.0142 -0.0234 302 NAG B C5 4365 C C6 . NAG G . ? 0.8304 0.8627 0.8860 -0.0493 0.0145 -0.0235 302 NAG B C6 4366 C C7 . NAG G . ? 0.7917 0.8409 0.8556 -0.0605 0.0200 -0.0328 302 NAG B C7 4367 C C8 . NAG G . ? 0.7662 0.8230 0.8340 -0.0625 0.0202 -0.0341 302 NAG B C8 4368 N N2 . NAG G . ? 0.7902 0.8419 0.8568 -0.0577 0.0177 -0.0296 302 NAG B N2 4369 O O3 . NAG G . ? 0.9164 0.9644 0.9889 -0.0544 0.0160 -0.0262 302 NAG B O3 4370 O O4 . NAG G . ? 1.0349 1.0839 1.1072 -0.0498 0.0118 -0.0201 302 NAG B O4 4371 O O5 . NAG G . ? 0.7689 0.8081 0.8244 -0.0522 0.0158 -0.0261 302 NAG B O5 4372 O O6 . NAG G . ? 0.7550 0.7874 0.8089 -0.0469 0.0129 -0.0216 302 NAG B O6 4373 O O7 . NAG G . ? 0.7528 0.7938 0.8111 -0.0616 0.0219 -0.0345 302 NAG B O7 4374 O O . HOH H . ? 0.7215 0.6065 0.6445 -0.0948 0.0479 -0.0609 401 HOH A O 4375 O O . HOH H . ? 0.5959 0.6059 0.6530 -0.0622 0.0307 -0.0398 402 HOH A O 4376 O O . HOH H . ? 0.6366 0.5352 0.5844 -0.0376 0.0185 -0.0409 403 HOH A O 4377 O O . HOH H . ? 0.4858 0.3954 0.4879 -0.0213 -0.0141 -0.0180 404 HOH A O 4378 O O . HOH H . ? 0.5860 0.5214 0.6035 -0.0212 -0.0171 -0.0132 405 HOH A O 4379 O O . HOH H . ? 0.5737 0.4291 0.4950 -0.0885 0.0610 -0.0591 406 HOH A O 4380 O O . HOH H . ? 0.4362 0.3300 0.4308 -0.0374 0.0137 -0.0314 407 HOH A O 4381 O O . HOH H . ? 0.6461 0.5241 0.6092 -0.0625 0.0463 -0.0511 408 HOH A O 4382 O O . HOH H . ? 0.5839 0.5248 0.6412 -0.0332 -0.0071 -0.0132 409 HOH A O 4383 O O . HOH H . ? 0.6295 0.5216 0.6362 -0.0308 -0.0009 -0.0240 410 HOH A O 4384 O O . HOH H . ? 0.7136 0.5226 0.6382 -0.0132 -0.0157 -0.0330 411 HOH A O 4385 O O . HOH H . ? 0.5110 0.3449 0.4228 -0.0340 0.0169 -0.0422 412 HOH A O 4386 O O . HOH H . ? 0.4561 0.4673 0.4824 -0.0140 -0.0058 -0.0149 413 HOH A O 4387 O O . HOH H . ? 0.6475 0.4539 0.5554 -0.0543 0.0426 -0.0527 414 HOH A O 4388 O O . HOH H . ? 0.4717 0.4848 0.4920 -0.0129 -0.0030 -0.0180 415 HOH A O 4389 O O . HOH H . ? 0.6451 0.4333 0.4968 -0.0343 0.0175 -0.0527 416 HOH A O 4390 O O . HOH H . ? 0.3853 0.3127 0.3645 -0.0473 0.0232 -0.0381 417 HOH A O 4391 O O . HOH H . ? 0.4939 0.3975 0.4962 -0.0261 -0.0069 -0.0203 418 HOH A O 4392 O O . HOH H . ? 0.5783 0.5802 0.6024 -0.0631 0.0266 -0.0400 419 HOH A O 4393 O O . HOH H . ? 0.4088 0.3007 0.3864 -0.0393 0.0174 -0.0340 420 HOH A O 4394 O O . HOH H . ? 0.6015 0.4381 0.5118 -0.0149 0.0020 -0.0396 421 HOH A O 4395 O O . HOH H . ? 0.5913 0.5011 0.5556 -0.0123 -0.0022 -0.0306 422 HOH A O 4396 O O . HOH H . ? 0.4782 0.4738 0.4918 -0.0817 0.0366 -0.0515 423 HOH A O 4397 O O . HOH H . ? 0.6862 0.5161 0.6336 -0.0391 0.0257 -0.0458 424 HOH A O 4398 O O . HOH H . ? 0.8374 0.7963 0.8327 0.0098 -0.0304 -0.0225 425 HOH A O 4399 O O . HOH H . ? 0.7316 0.7565 0.7997 -0.0328 -0.0126 0.0038 426 HOH A O 4400 O O . HOH H . ? 0.4415 0.3833 0.4375 -0.0430 0.0190 -0.0329 427 HOH A O 4401 O O . HOH H . ? 0.4242 0.4248 0.4632 -0.0545 0.0224 -0.0321 428 HOH A O 4402 O O . HOH H . ? 0.5005 0.3857 0.4403 -0.0176 0.0052 -0.0373 429 HOH A O 4403 O O . HOH H . ? 0.7932 0.5773 0.6653 -0.0336 0.0171 -0.0458 430 HOH A O 4404 O O . HOH H . ? 0.3768 0.3372 0.3836 -0.0418 0.0169 -0.0304 431 HOH A O 4405 O O . HOH H . ? 0.8888 0.5915 0.6606 -0.0407 0.0177 -0.0616 432 HOH A O 4406 O O . HOH H . ? 0.6162 0.5035 0.5447 -0.0956 0.0506 -0.0604 433 HOH A O 4407 O O . HOH H . ? 0.7483 0.7549 0.7984 -0.0556 0.0232 -0.0322 434 HOH A O 4408 O O . HOH H . ? 0.8087 0.5242 0.5932 -0.0517 0.0242 -0.0608 435 HOH A O 4409 O O . HOH H . ? 0.5489 0.5289 0.5715 -0.0417 0.0148 -0.0265 436 HOH A O 4410 O O . HOH H . ? 0.4604 0.3820 0.4272 -0.0453 0.0223 -0.0402 437 HOH A O 4411 O O . HOH I . ? 0.6646 0.7729 0.7456 -0.0521 0.0040 -0.0166 401 HOH B O 4412 O O . HOH I . ? 0.6769 0.6955 0.7011 -0.0383 0.0123 -0.0259 402 HOH B O 4413 O O . HOH I . ? 0.5585 0.6550 0.5971 -0.0104 0.0005 -0.0123 403 HOH B O 4414 O O . HOH I . ? 0.9487 0.9446 0.8287 -0.0342 -0.0001 -0.0829 404 HOH B O 4415 O O . HOH I . ? 0.5842 0.6773 0.6308 -0.0305 0.0049 -0.0117 405 HOH B O 4416 O O . HOH I . ? 0.5109 0.4874 0.4071 -0.0140 0.0053 -0.0702 406 HOH B O 4417 O O . HOH I . ? 0.5851 0.6131 0.5728 0.0206 -0.0083 -0.0334 407 HOH B O 4418 O O . HOH I . ? 0.8405 0.6965 0.6894 -0.0265 0.0098 -0.0709 408 HOH B O 4419 O O . HOH I . ? 0.5758 0.7459 0.6054 0.0343 -0.0041 -0.0272 409 HOH B O 4420 O O . HOH I . ? 0.5958 0.4896 0.4648 -0.0153 0.0072 -0.0688 410 HOH B O 4421 O O . HOH I . ? 0.8110 0.6072 0.5971 0.0003 -0.0021 -0.0835 411 HOH B O 4422 O O . HOH I . ? 0.6196 0.5694 0.4909 -0.0068 0.0030 -0.0766 412 HOH B O 4423 O O . HOH I . ? 0.5565 0.6404 0.5021 0.0486 -0.0005 -0.0570 413 HOH B O 4424 O O . HOH I . ? 0.7423 0.5631 0.5315 0.0302 -0.0097 -0.0871 414 HOH B O 4425 O O . HOH I . ? 0.5413 0.7403 0.5790 0.0351 -0.0024 -0.0253 415 HOH B O 4426 O O . HOH I . ? 0.6067 0.7382 0.5815 0.0155 0.0067 -0.0411 416 HOH B O 4427 O O . HOH I . ? 0.4848 0.5641 0.4259 0.0428 0.0010 -0.0576 417 HOH B O 4428 O O . HOH I . ? 0.4780 0.7234 0.5473 0.0006 0.0037 0.0011 418 HOH B O 4429 O O . HOH I . ? 0.6438 0.5199 0.5012 -0.0289 0.0099 -0.0721 419 HOH B O 4430 O O . HOH I . ? 0.5781 0.6551 0.5682 -0.0224 0.0080 -0.0375 420 HOH B O 4431 O O . HOH I . ? 0.5257 0.6220 0.5698 -0.0224 0.0033 -0.0102 421 HOH B O 4432 O O . HOH I . ? 0.6417 0.7185 0.7136 -0.0459 0.0061 -0.0125 422 HOH B O 4433 O O . HOH I . ? 0.7699 0.8653 0.8153 -0.0092 -0.0030 -0.0092 423 HOH B O 4434 O O . HOH I . ? 0.6829 0.7493 0.7211 -0.0210 0.0026 -0.0133 424 HOH B O 4435 O O . HOH I . ? 0.5793 0.6493 0.6211 -0.0334 0.0069 -0.0163 425 HOH B O 4436 O O . HOH I . ? 0.4382 0.6845 0.5038 0.0103 0.0029 -0.0054 426 HOH B O 4437 O O . HOH I . ? 0.4715 0.5950 0.4679 -0.0442 0.0006 -0.0422 427 HOH B O 4438 O O . HOH I . ? 0.6107 0.7316 0.6598 -0.0138 0.0007 -0.0065 428 HOH B O 4439 O O . HOH I . ? 0.7061 0.7554 0.6866 0.0196 -0.0016 -0.0379 429 HOH B O 4440 O O . HOH I . ? 0.4754 0.5087 0.4843 -0.0281 0.0098 -0.0290 430 HOH B O 4441 O O . HOH I . ? 0.6314 0.5513 0.5253 -0.0182 0.0091 -0.0630 431 HOH B O 4442 O O . HOH I . ? 0.6375 0.4619 0.4423 0.0098 -0.0032 -0.0811 432 HOH B O 4443 O O . HOH I . ? 0.7147 0.8202 0.7439 0.0180 -0.0088 -0.0214 433 HOH B O 4444 O O . HOH I . ? 0.5155 0.6450 0.6031 -0.0653 0.0053 -0.0327 434 HOH B O 4445 O O . HOH I . ? 0.6941 0.7090 0.6577 -0.0528 0.0139 -0.0553 435 HOH B O 4446 O O . HOH I . ? 0.7709 0.7183 0.6297 -0.0045 0.0010 -0.0817 436 HOH B O 4447 O O . HOH I . ? 0.5851 0.7201 0.6732 -0.0707 0.0062 -0.0385 437 HOH B O 4448 O O . HOH I . ? 0.5334 0.5502 0.5644 -0.0847 0.0372 -0.0525 438 HOH B O 4449 O O . HOH J . ? 0.6720 0.8760 0.7407 -0.0473 -0.0204 0.0099 301 HOH C O 4450 O O . HOH J . ? 0.6409 0.8265 0.7077 -0.0679 -0.0146 -0.0378 302 HOH C O 4451 O O . HOH J . ? 0.7101 0.8008 0.8179 -0.0322 -0.0790 0.0668 303 HOH C O 4452 O O . HOH J . ? 0.5592 0.7273 0.6579 -0.0192 -0.0965 0.0596 304 HOH C O 4453 O O . HOH J . ? 0.5425 0.7487 0.6293 -0.0598 -0.0233 -0.0241 305 HOH C O 4454 O O . HOH J . ? 0.4451 0.6122 0.4880 -0.0733 -0.0689 0.1120 306 HOH C O 4455 O O . HOH J . ? 0.6568 0.7863 0.7153 -0.0683 -0.0764 0.1094 307 HOH C O 4456 O O . HOH J . ? 0.6362 0.8480 0.7388 -0.0645 -0.0230 -0.0320 308 HOH C O 4457 O O . HOH J . ? 0.6760 0.8058 0.7860 -0.0493 -0.0243 0.0359 309 HOH C O # 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 ALA 1 29 29 ALA ALA A . n A 1 2 ASN 2 30 30 ASN ASN A . n A 1 3 PHE 3 31 31 PHE PHE A . n A 1 4 THR 4 32 32 THR THR A . n A 1 5 CYS 5 33 33 CYS CYS A . n A 1 6 ALA 6 34 34 ALA ALA A . n A 1 7 VAL 7 35 35 VAL VAL A . n A 1 8 ALA 8 36 36 ALA ALA A . n A 1 9 SER 9 37 37 SER SER A . n A 1 10 GLY 10 38 38 GLY GLY A . n A 1 11 THR 11 39 39 THR THR A . n A 1 12 THR 12 40 40 THR THR A . n A 1 13 CYS 13 41 41 CYS CYS A . n A 1 14 LYS 14 42 42 LYS LYS A . n A 1 15 SER 15 43 43 SER SER A . n A 1 16 ALA 16 44 44 ALA ALA A . n A 1 17 ILE 17 45 45 ILE ILE A . n A 1 18 LEU 18 46 46 LEU LEU A . n A 1 19 TYR 19 47 47 TYR TYR A . n A 1 20 THR 20 48 48 THR THR A . n A 1 21 SER 21 49 49 SER SER A . n A 1 22 PRO 22 50 50 PRO PRO A . n A 1 23 ASN 23 51 51 ASN ASN A . n A 1 24 ALA 24 52 52 ALA ALA A . n A 1 25 THR 25 53 53 THR THR A . n A 1 26 THR 26 54 54 THR THR A . n A 1 27 TYR 27 55 55 TYR TYR A . n A 1 28 GLY 28 56 56 GLY GLY A . n A 1 29 ASN 29 57 57 ASN ASN A . n A 1 30 LEU 30 58 58 LEU LEU A . n A 1 31 VAL 31 59 59 VAL VAL A . n A 1 32 ALA 32 60 60 ALA ALA A . n A 1 33 ARG 33 61 61 ARG ARG A . n A 1 34 PHE 34 62 62 PHE PHE A . n A 1 35 ASN 35 63 63 ASN ASN A . n A 1 36 THR 36 64 64 THR THR A . n A 1 37 THR 37 65 65 THR THR A . n A 1 38 THR 38 66 66 THR THR A . n A 1 39 LEU 39 67 67 LEU LEU A . n A 1 40 PRO 40 68 68 PRO PRO A . n A 1 41 ASP 41 69 69 ASP ASP A . n A 1 42 LEU 42 70 70 LEU LEU A . n A 1 43 LEU 43 71 71 LEU LEU A . n A 1 44 GLY 44 72 72 GLY GLY A . n A 1 45 ALA 45 73 73 ALA ALA A . n A 1 46 ASN 46 74 74 ASN ASN A . n A 1 47 GLY 47 75 75 GLY GLY A . n A 1 48 LEU 48 76 76 LEU LEU A . n A 1 49 PRO 49 77 77 PRO PRO A . n A 1 50 ASP 50 78 78 ASP ASP A . n A 1 51 GLY 51 79 79 GLY GLY A . n A 1 52 THR 52 80 80 THR THR A . n A 1 53 LEU 53 81 81 LEU LEU A . n A 1 54 SER 54 82 82 SER SER A . n A 1 55 SER 55 83 83 SER SER A . n A 1 56 ALA 56 84 84 ALA ALA A . n A 1 57 PRO 57 85 85 PRO PRO A . n A 1 58 VAL 58 86 86 VAL VAL A . n A 1 59 ALA 59 87 87 ALA ALA A . n A 1 60 ALA 60 88 88 ALA ALA A . n A 1 61 ASN 61 89 89 ASN ASN A . n A 1 62 SER 62 90 90 SER SER A . n A 1 63 THR 63 91 91 THR THR A . n A 1 64 VAL 64 92 92 VAL VAL A . n A 1 65 LYS 65 93 93 LYS LYS A . n A 1 66 ILE 66 94 94 ILE ILE A . n A 1 67 PRO 67 95 95 PRO PRO A . n A 1 68 PHE 68 96 96 PHE PHE A . n A 1 69 ARG 69 97 97 ARG ARG A . n A 1 70 CYS 70 98 98 CYS CYS A . n A 1 71 ARG 71 99 99 ARG ARG A . n A 1 72 CYS 72 100 100 CYS CYS A . n A 1 73 ASN 73 101 101 ASN ASN A . n A 1 74 GLY 74 102 102 GLY GLY A . n A 1 75 ASP 75 103 103 ASP ASP A . n A 1 76 VAL 76 104 104 VAL VAL A . n A 1 77 GLY 77 105 105 GLY GLY A . n A 1 78 GLN 78 106 106 GLN GLN A . n A 1 79 SER 79 107 107 SER SER A . n A 1 80 ASP 80 108 108 ASP ASP A . n A 1 81 ARG 81 109 109 ARG ARG A . n A 1 82 LEU 82 110 110 LEU LEU A . n A 1 83 PRO 83 111 111 PRO PRO A . n A 1 84 ILE 84 112 112 ILE ILE A . n A 1 85 TYR 85 113 113 TYR TYR A . n A 1 86 VAL 86 114 114 VAL VAL A . n A 1 87 VAL 87 115 115 VAL VAL A . n A 1 88 GLN 88 116 116 GLN GLN A . n A 1 89 PRO 89 117 117 PRO PRO A . n A 1 90 GLN 90 118 118 GLN GLN A . n A 1 91 ASP 91 119 119 ASP ASP A . n A 1 92 GLY 92 120 120 GLY GLY A . n A 1 93 LEU 93 121 121 LEU LEU A . n A 1 94 ASP 94 122 122 ASP ASP A . n A 1 95 ALA 95 123 123 ALA ALA A . n A 1 96 ILE 96 124 124 ILE ILE A . n A 1 97 ALA 97 125 125 ALA ALA A . n A 1 98 ARG 98 126 126 ARG ARG A . n A 1 99 ASN 99 127 127 ASN ASN A . n A 1 100 VAL 100 128 128 VAL VAL A . n A 1 101 PHE 101 129 129 PHE PHE A . n A 1 102 ASN 102 130 130 ASN ASN A . n A 1 103 ALA 103 131 131 ALA ALA A . n A 1 104 PHE 104 132 132 PHE PHE A . n A 1 105 VAL 105 133 133 VAL VAL A . n A 1 106 THR 106 134 134 THR THR A . n A 1 107 TYR 107 135 135 TYR TYR A . n A 1 108 GLN 108 136 136 GLN GLN A . n A 1 109 GLU 109 137 137 GLU GLU A . n A 1 110 ILE 110 138 138 ILE ILE A . n A 1 111 ALA 111 139 139 ALA ALA A . n A 1 112 ALA 112 140 140 ALA ALA A . n A 1 113 ALA 113 141 141 ALA ALA A . n A 1 114 ASN 114 142 142 ASN ASN A . n A 1 115 ASN 115 143 143 ASN ASN A . n A 1 116 ILE 116 144 144 ILE ILE A . n A 1 117 PRO 117 145 145 PRO PRO A . n A 1 118 ASP 118 146 146 ASP ASP A . n A 1 119 PRO 119 147 147 PRO PRO A . n A 1 120 ASN 120 148 148 ASN ASN A . n A 1 121 LYS 121 149 149 LYS LYS A . n A 1 122 ILE 122 150 150 ILE ILE A . n A 1 123 ASN 123 151 151 ASN ASN A . n A 1 124 VAL 124 152 152 VAL VAL A . n A 1 125 SER 125 153 153 SER SER A . n A 1 126 GLN 126 154 154 GLN GLN A . n A 1 127 THR 127 155 155 THR THR A . n A 1 128 LEU 128 156 156 LEU LEU A . n A 1 129 TRP 129 157 157 TRP TRP A . n A 1 130 ILE 130 158 158 ILE ILE A . n A 1 131 PRO 131 159 159 PRO PRO A . n A 1 132 LEU 132 160 160 LEU LEU A . n A 1 133 PRO 133 161 161 PRO PRO A . n A 1 134 CYS 134 162 162 CYS CYS A . n A 1 135 SER 135 163 163 SER SER A . n A 1 136 CYS 136 164 164 CYS CYS A . n A 1 137 ASP 137 165 165 ASP ASP A . n A 1 138 LYS 138 166 166 LYS LYS A . n A 1 139 GLU 139 167 167 GLU GLU A . n A 1 140 GLU 140 168 168 GLU GLU A . n A 1 141 GLY 141 169 169 GLY GLY A . n A 1 142 SER 142 170 170 SER SER A . n A 1 143 ASN 143 171 171 ASN ASN A . n A 1 144 VAL 144 172 172 VAL VAL A . n A 1 145 MET 145 173 173 MET MET A . n A 1 146 HIS 146 174 174 HIS HIS A . n A 1 147 LEU 147 175 175 LEU LEU A . n A 1 148 ALA 148 176 176 ALA ALA A . n A 1 149 TYR 149 177 177 TYR TYR A . n A 1 150 SER 150 178 178 SER SER A . n A 1 151 VAL 151 179 179 VAL VAL A . n A 1 152 GLY 152 180 180 GLY GLY A . n A 1 153 LYS 153 181 181 LYS LYS A . n A 1 154 GLY 154 182 182 GLY GLY A . n A 1 155 GLU 155 183 183 GLU GLU A . n A 1 156 ASN 156 184 184 ASN ASN A . n A 1 157 THR 157 185 185 THR THR A . n A 1 158 SER 158 186 186 SER SER A . n A 1 159 ALA 159 187 187 ALA ALA A . n A 1 160 ILE 160 188 188 ILE ILE A . n A 1 161 ALA 161 189 189 ALA ALA A . n A 1 162 ALA 162 190 190 ALA ALA A . n A 1 163 LYS 163 191 191 LYS LYS A . n A 1 164 TYR 164 192 192 TYR TYR A . n A 1 165 GLY 165 193 193 GLY GLY A . n A 1 166 VAL 166 194 194 VAL VAL A . n A 1 167 THR 167 195 195 THR THR A . n A 1 168 GLU 168 196 196 GLU GLU A . n A 1 169 SER 169 197 197 SER SER A . n A 1 170 THR 170 198 198 THR THR A . n A 1 171 LEU 171 199 199 LEU LEU A . n A 1 172 LEU 172 200 200 LEU LEU A . n A 1 173 THR 173 201 201 THR THR A . n A 1 174 ARG 174 202 202 ARG ARG A . n A 1 175 ASN 175 203 203 ASN ASN A . n A 1 176 LYS 176 204 204 LYS LYS A . n A 1 177 ILE 177 205 205 ILE ILE A . n A 1 178 ASP 178 206 206 ASP ASP A . n A 1 179 ASP 179 207 207 ASP ASP A . n A 1 180 PRO 180 208 208 PRO PRO A . n A 1 181 THR 181 209 209 THR THR A . n A 1 182 LYS 182 210 210 LYS LYS A . n A 1 183 LEU 183 211 211 LEU LEU A . n A 1 184 GLN 184 212 212 GLN GLN A . n A 1 185 MET 185 213 213 MET MET A . n A 1 186 GLY 186 214 214 GLY GLY A . n A 1 187 GLN 187 215 215 GLN GLN A . n A 1 188 ILE 188 216 216 ILE ILE A . n A 1 189 LEU 189 217 217 LEU LEU A . n A 1 190 ASP 190 218 218 ASP ASP A . n A 1 191 VAL 191 219 219 VAL VAL A . n A 1 192 PRO 192 220 220 PRO PRO A . n A 1 193 LEU 193 221 221 LEU LEU A . n A 1 194 PRO 194 222 222 PRO PRO A . n A 1 195 VAL 195 223 223 VAL VAL A . n B 1 1 ALA 1 29 29 ALA ALA B . n B 1 2 ASN 2 30 30 ASN ASN B . n B 1 3 PHE 3 31 31 PHE PHE B . n B 1 4 THR 4 32 32 THR THR B . n B 1 5 CYS 5 33 33 CYS CYS B . n B 1 6 ALA 6 34 34 ALA ALA B . n B 1 7 VAL 7 35 35 VAL VAL B . n B 1 8 ALA 8 36 36 ALA ALA B . n B 1 9 SER 9 37 37 SER SER B . n B 1 10 GLY 10 38 38 GLY GLY B . n B 1 11 THR 11 39 39 THR THR B . n B 1 12 THR 12 40 40 THR THR B . n B 1 13 CYS 13 41 41 CYS CYS B . n B 1 14 LYS 14 42 42 LYS LYS B . n B 1 15 SER 15 43 43 SER SER B . n B 1 16 ALA 16 44 44 ALA ALA B . n B 1 17 ILE 17 45 45 ILE ILE B . n B 1 18 LEU 18 46 46 LEU LEU B . n B 1 19 TYR 19 47 47 TYR TYR B . n B 1 20 THR 20 48 48 THR THR B . n B 1 21 SER 21 49 49 SER SER B . n B 1 22 PRO 22 50 50 PRO PRO B . n B 1 23 ASN 23 51 51 ASN ASN B . n B 1 24 ALA 24 52 52 ALA ALA B . n B 1 25 THR 25 53 53 THR THR B . n B 1 26 THR 26 54 54 THR THR B . n B 1 27 TYR 27 55 55 TYR TYR B . n B 1 28 GLY 28 56 56 GLY GLY B . n B 1 29 ASN 29 57 57 ASN ASN B . n B 1 30 LEU 30 58 58 LEU LEU B . n B 1 31 VAL 31 59 59 VAL VAL B . n B 1 32 ALA 32 60 60 ALA ALA B . n B 1 33 ARG 33 61 61 ARG ARG B . n B 1 34 PHE 34 62 62 PHE PHE B . n B 1 35 ASN 35 63 63 ASN ASN B . n B 1 36 THR 36 64 64 THR THR B . n B 1 37 THR 37 65 65 THR THR B . n B 1 38 THR 38 66 66 THR THR B . n B 1 39 LEU 39 67 67 LEU LEU B . n B 1 40 PRO 40 68 68 PRO PRO B . n B 1 41 ASP 41 69 69 ASP ASP B . n B 1 42 LEU 42 70 70 LEU LEU B . n B 1 43 LEU 43 71 71 LEU LEU B . n B 1 44 GLY 44 72 72 GLY GLY B . n B 1 45 ALA 45 73 73 ALA ALA B . n B 1 46 ASN 46 74 74 ASN ASN B . n B 1 47 GLY 47 75 75 GLY GLY B . n B 1 48 LEU 48 76 76 LEU LEU B . n B 1 49 PRO 49 77 77 PRO PRO B . n B 1 50 ASP 50 78 78 ASP ASP B . n B 1 51 GLY 51 79 79 GLY GLY B . n B 1 52 THR 52 80 80 THR THR B . n B 1 53 LEU 53 81 81 LEU LEU B . n B 1 54 SER 54 82 82 SER SER B . n B 1 55 SER 55 83 83 SER SER B . n B 1 56 ALA 56 84 84 ALA ALA B . n B 1 57 PRO 57 85 85 PRO PRO B . n B 1 58 VAL 58 86 86 VAL VAL B . n B 1 59 ALA 59 87 87 ALA ALA B . n B 1 60 ALA 60 88 88 ALA ALA B . n B 1 61 ASN 61 89 89 ASN ASN B . n B 1 62 SER 62 90 90 SER SER B . n B 1 63 THR 63 91 91 THR THR B . n B 1 64 VAL 64 92 92 VAL VAL B . n B 1 65 LYS 65 93 93 LYS LYS B . n B 1 66 ILE 66 94 94 ILE ILE B . n B 1 67 PRO 67 95 95 PRO PRO B . n B 1 68 PHE 68 96 96 PHE PHE B . n B 1 69 ARG 69 97 97 ARG ARG B . n B 1 70 CYS 70 98 98 CYS CYS B . n B 1 71 ARG 71 99 99 ARG ARG B . n B 1 72 CYS 72 100 100 CYS CYS B . n B 1 73 ASN 73 101 101 ASN ASN B . n B 1 74 GLY 74 102 102 GLY GLY B . n B 1 75 ASP 75 103 103 ASP ASP B . n B 1 76 VAL 76 104 104 VAL VAL B . n B 1 77 GLY 77 105 105 GLY GLY B . n B 1 78 GLN 78 106 106 GLN GLN B . n B 1 79 SER 79 107 107 SER SER B . n B 1 80 ASP 80 108 108 ASP ASP B . n B 1 81 ARG 81 109 109 ARG ARG B . n B 1 82 LEU 82 110 110 LEU LEU B . n B 1 83 PRO 83 111 111 PRO PRO B . n B 1 84 ILE 84 112 112 ILE ILE B . n B 1 85 TYR 85 113 113 TYR TYR B . n B 1 86 VAL 86 114 114 VAL VAL B . n B 1 87 VAL 87 115 115 VAL VAL B . n B 1 88 GLN 88 116 116 GLN GLN B . n B 1 89 PRO 89 117 117 PRO PRO B . n B 1 90 GLN 90 118 118 GLN GLN B . n B 1 91 ASP 91 119 119 ASP ASP B . n B 1 92 GLY 92 120 120 GLY GLY B . n B 1 93 LEU 93 121 121 LEU LEU B . n B 1 94 ASP 94 122 122 ASP ASP B . n B 1 95 ALA 95 123 123 ALA ALA B . n B 1 96 ILE 96 124 124 ILE ILE B . n B 1 97 ALA 97 125 125 ALA ALA B . n B 1 98 ARG 98 126 126 ARG ARG B . n B 1 99 ASN 99 127 127 ASN ASN B . n B 1 100 VAL 100 128 128 VAL VAL B . n B 1 101 PHE 101 129 129 PHE PHE B . n B 1 102 ASN 102 130 130 ASN ASN B . n B 1 103 ALA 103 131 131 ALA ALA B . n B 1 104 PHE 104 132 132 PHE PHE B . n B 1 105 VAL 105 133 133 VAL VAL B . n B 1 106 THR 106 134 134 THR THR B . n B 1 107 TYR 107 135 135 TYR TYR B . n B 1 108 GLN 108 136 136 GLN GLN B . n B 1 109 GLU 109 137 137 GLU GLU B . n B 1 110 ILE 110 138 138 ILE ILE B . n B 1 111 ALA 111 139 139 ALA ALA B . n B 1 112 ALA 112 140 140 ALA ALA B . n B 1 113 ALA 113 141 141 ALA ALA B . n B 1 114 ASN 114 142 142 ASN ASN B . n B 1 115 ASN 115 143 143 ASN ASN B . n B 1 116 ILE 116 144 144 ILE ILE B . n B 1 117 PRO 117 145 145 PRO PRO B . n B 1 118 ASP 118 146 146 ASP ASP B . n B 1 119 PRO 119 147 147 PRO PRO B . n B 1 120 ASN 120 148 148 ASN ASN B . n B 1 121 LYS 121 149 149 LYS LYS B . n B 1 122 ILE 122 150 150 ILE ILE B . n B 1 123 ASN 123 151 151 ASN ASN B . n B 1 124 VAL 124 152 152 VAL VAL B . n B 1 125 SER 125 153 153 SER SER B . n B 1 126 GLN 126 154 154 GLN GLN B . n B 1 127 THR 127 155 155 THR THR B . n B 1 128 LEU 128 156 156 LEU LEU B . n B 1 129 TRP 129 157 157 TRP TRP B . n B 1 130 ILE 130 158 158 ILE ILE B . n B 1 131 PRO 131 159 159 PRO PRO B . n B 1 132 LEU 132 160 160 LEU LEU B . n B 1 133 PRO 133 161 161 PRO PRO B . n B 1 134 CYS 134 162 162 CYS CYS B . n B 1 135 SER 135 163 163 SER SER B . n B 1 136 CYS 136 164 164 CYS CYS B . n B 1 137 ASP 137 165 165 ASP ASP B . n B 1 138 LYS 138 166 166 LYS LYS B . n B 1 139 GLU 139 167 167 GLU GLU B . n B 1 140 GLU 140 168 168 GLU GLU B . n B 1 141 GLY 141 169 169 GLY GLY B . n B 1 142 SER 142 170 170 SER SER B . n B 1 143 ASN 143 171 171 ASN ASN B . n B 1 144 VAL 144 172 172 VAL VAL B . n B 1 145 MET 145 173 173 MET MET B . n B 1 146 HIS 146 174 174 HIS HIS B . n B 1 147 LEU 147 175 175 LEU LEU B . n B 1 148 ALA 148 176 176 ALA ALA B . n B 1 149 TYR 149 177 177 TYR TYR B . n B 1 150 SER 150 178 178 SER SER B . n B 1 151 VAL 151 179 179 VAL VAL B . n B 1 152 GLY 152 180 180 GLY GLY B . n B 1 153 LYS 153 181 181 LYS LYS B . n B 1 154 GLY 154 182 182 GLY GLY B . n B 1 155 GLU 155 183 183 GLU GLU B . n B 1 156 ASN 156 184 184 ASN ASN B . n B 1 157 THR 157 185 185 THR THR B . n B 1 158 SER 158 186 186 SER SER B . n B 1 159 ALA 159 187 187 ALA ALA B . n B 1 160 ILE 160 188 188 ILE ILE B . n B 1 161 ALA 161 189 189 ALA ALA B . n B 1 162 ALA 162 190 190 ALA ALA B . n B 1 163 LYS 163 191 191 LYS LYS B . n B 1 164 TYR 164 192 192 TYR TYR B . n B 1 165 GLY 165 193 193 GLY GLY B . n B 1 166 VAL 166 194 194 VAL VAL B . n B 1 167 THR 167 195 195 THR THR B . n B 1 168 GLU 168 196 196 GLU GLU B . n B 1 169 SER 169 197 197 SER SER B . n B 1 170 THR 170 198 198 THR THR B . n B 1 171 LEU 171 199 199 LEU LEU B . n B 1 172 LEU 172 200 200 LEU LEU B . n B 1 173 THR 173 201 201 THR THR B . n B 1 174 ARG 174 202 202 ARG ARG B . n B 1 175 ASN 175 203 203 ASN ASN B . n B 1 176 LYS 176 204 204 LYS LYS B . n B 1 177 ILE 177 205 205 ILE ILE B . n B 1 178 ASP 178 206 206 ASP ASP B . n B 1 179 ASP 179 207 207 ASP ASP B . n B 1 180 PRO 180 208 208 PRO PRO B . n B 1 181 THR 181 209 209 THR THR B . n B 1 182 LYS 182 210 210 LYS LYS B . n B 1 183 LEU 183 211 211 LEU LEU B . n B 1 184 GLN 184 212 212 GLN GLN B . n B 1 185 MET 185 213 213 MET MET B . n B 1 186 GLY 186 214 214 GLY GLY B . n B 1 187 GLN 187 215 215 GLN GLN B . n B 1 188 ILE 188 216 216 ILE ILE B . n B 1 189 LEU 189 217 217 LEU LEU B . n B 1 190 ASP 190 218 218 ASP ASP B . n B 1 191 VAL 191 219 219 VAL VAL B . n B 1 192 PRO 192 220 220 PRO PRO B . n B 1 193 LEU 193 221 221 LEU LEU B . n B 1 194 PRO 194 222 222 PRO PRO B . n B 1 195 VAL 195 223 223 VAL VAL B . n C 1 1 ALA 1 29 29 ALA ALA C . n C 1 2 ASN 2 30 30 ASN ASN C . n C 1 3 PHE 3 31 31 PHE PHE C . n C 1 4 THR 4 32 32 THR THR C . n C 1 5 CYS 5 33 33 CYS CYS C . n C 1 6 ALA 6 34 34 ALA ALA C . n C 1 7 VAL 7 35 35 VAL VAL C . n C 1 8 ALA 8 36 36 ALA ALA C . n C 1 9 SER 9 37 37 SER SER C . n C 1 10 GLY 10 38 38 GLY GLY C . n C 1 11 THR 11 39 39 THR THR C . n C 1 12 THR 12 40 40 THR THR C . n C 1 13 CYS 13 41 41 CYS CYS C . n C 1 14 LYS 14 42 42 LYS LYS C . n C 1 15 SER 15 43 43 SER SER C . n C 1 16 ALA 16 44 44 ALA ALA C . n C 1 17 ILE 17 45 45 ILE ILE C . n C 1 18 LEU 18 46 46 LEU LEU C . n C 1 19 TYR 19 47 47 TYR TYR C . n C 1 20 THR 20 48 48 THR THR C . n C 1 21 SER 21 49 49 SER SER C . n C 1 22 PRO 22 50 50 PRO PRO C . n C 1 23 ASN 23 51 51 ASN ASN C . n C 1 24 ALA 24 52 52 ALA ALA C . n C 1 25 THR 25 53 53 THR THR C . n C 1 26 THR 26 54 54 THR THR C . n C 1 27 TYR 27 55 55 TYR TYR C . n C 1 28 GLY 28 56 56 GLY GLY C . n C 1 29 ASN 29 57 57 ASN ASN C . n C 1 30 LEU 30 58 58 LEU LEU C . n C 1 31 VAL 31 59 59 VAL VAL C . n C 1 32 ALA 32 60 60 ALA ALA C . n C 1 33 ARG 33 61 61 ARG ARG C . n C 1 34 PHE 34 62 62 PHE PHE C . n C 1 35 ASN 35 63 63 ASN ASN C . n C 1 36 THR 36 64 64 THR THR C . n C 1 37 THR 37 65 65 THR THR C . n C 1 38 THR 38 66 66 THR THR C . n C 1 39 LEU 39 67 67 LEU LEU C . n C 1 40 PRO 40 68 68 PRO PRO C . n C 1 41 ASP 41 69 69 ASP ASP C . n C 1 42 LEU 42 70 70 LEU LEU C . n C 1 43 LEU 43 71 71 LEU LEU C . n C 1 44 GLY 44 72 72 GLY GLY C . n C 1 45 ALA 45 73 73 ALA ALA C . n C 1 46 ASN 46 74 74 ASN ASN C . n C 1 47 GLY 47 75 75 GLY GLY C . n C 1 48 LEU 48 76 76 LEU LEU C . n C 1 49 PRO 49 77 77 PRO PRO C . n C 1 50 ASP 50 78 78 ASP ASP C . n C 1 51 GLY 51 79 79 GLY GLY C . n C 1 52 THR 52 80 80 THR THR C . n C 1 53 LEU 53 81 81 LEU LEU C . n C 1 54 SER 54 82 82 SER SER C . n C 1 55 SER 55 83 83 SER SER C . n C 1 56 ALA 56 84 84 ALA ALA C . n C 1 57 PRO 57 85 85 PRO PRO C . n C 1 58 VAL 58 86 86 VAL VAL C . n C 1 59 ALA 59 87 87 ALA ALA C . n C 1 60 ALA 60 88 88 ALA ALA C . n C 1 61 ASN 61 89 89 ASN ASN C . n C 1 62 SER 62 90 90 SER SER C . n C 1 63 THR 63 91 91 THR THR C . n C 1 64 VAL 64 92 92 VAL VAL C . n C 1 65 LYS 65 93 93 LYS LYS C . n C 1 66 ILE 66 94 94 ILE ILE C . n C 1 67 PRO 67 95 95 PRO PRO C . n C 1 68 PHE 68 96 96 PHE PHE C . n C 1 69 ARG 69 97 97 ARG ARG C . n C 1 70 CYS 70 98 98 CYS CYS C . n C 1 71 ARG 71 99 99 ARG ARG C . n C 1 72 CYS 72 100 100 CYS CYS C . n C 1 73 ASN 73 101 101 ASN ASN C . n C 1 74 GLY 74 102 102 GLY GLY C . n C 1 75 ASP 75 103 103 ASP ASP C . n C 1 76 VAL 76 104 104 VAL VAL C . n C 1 77 GLY 77 105 105 GLY GLY C . n C 1 78 GLN 78 106 106 GLN GLN C . n C 1 79 SER 79 107 107 SER SER C . n C 1 80 ASP 80 108 108 ASP ASP C . n C 1 81 ARG 81 109 109 ARG ARG C . n C 1 82 LEU 82 110 110 LEU LEU C . n C 1 83 PRO 83 111 111 PRO PRO C . n C 1 84 ILE 84 112 112 ILE ILE C . n C 1 85 TYR 85 113 113 TYR TYR C . n C 1 86 VAL 86 114 114 VAL VAL C . n C 1 87 VAL 87 115 115 VAL VAL C . n C 1 88 GLN 88 116 116 GLN GLN C . n C 1 89 PRO 89 117 117 PRO PRO C . n C 1 90 GLN 90 118 118 GLN GLN C . n C 1 91 ASP 91 119 119 ASP ASP C . n C 1 92 GLY 92 120 120 GLY GLY C . n C 1 93 LEU 93 121 121 LEU LEU C . n C 1 94 ASP 94 122 122 ASP ASP C . n C 1 95 ALA 95 123 123 ALA ALA C . n C 1 96 ILE 96 124 124 ILE ILE C . n C 1 97 ALA 97 125 125 ALA ALA C . n C 1 98 ARG 98 126 126 ARG ARG C . n C 1 99 ASN 99 127 127 ASN ASN C . n C 1 100 VAL 100 128 128 VAL VAL C . n C 1 101 PHE 101 129 129 PHE PHE C . n C 1 102 ASN 102 130 130 ASN ASN C . n C 1 103 ALA 103 131 131 ALA ALA C . n C 1 104 PHE 104 132 132 PHE PHE C . n C 1 105 VAL 105 133 133 VAL VAL C . n C 1 106 THR 106 134 134 THR THR C . n C 1 107 TYR 107 135 135 TYR TYR C . n C 1 108 GLN 108 136 136 GLN GLN C . n C 1 109 GLU 109 137 137 GLU GLU C . n C 1 110 ILE 110 138 138 ILE ILE C . n C 1 111 ALA 111 139 139 ALA ALA C . n C 1 112 ALA 112 140 140 ALA ALA C . n C 1 113 ALA 113 141 141 ALA ALA C . n C 1 114 ASN 114 142 142 ASN ASN C . n C 1 115 ASN 115 143 143 ASN ASN C . n C 1 116 ILE 116 144 144 ILE ILE C . n C 1 117 PRO 117 145 145 PRO PRO C . n C 1 118 ASP 118 146 146 ASP ASP C . n C 1 119 PRO 119 147 147 PRO PRO C . n C 1 120 ASN 120 148 148 ASN ASN C . n C 1 121 LYS 121 149 149 LYS LYS C . n C 1 122 ILE 122 150 150 ILE ILE C . n C 1 123 ASN 123 151 151 ASN ASN C . n C 1 124 VAL 124 152 152 VAL VAL C . n C 1 125 SER 125 153 153 SER SER C . n C 1 126 GLN 126 154 154 GLN GLN C . n C 1 127 THR 127 155 155 THR THR C . n C 1 128 LEU 128 156 156 LEU LEU C . n C 1 129 TRP 129 157 157 TRP TRP C . n C 1 130 ILE 130 158 158 ILE ILE C . n C 1 131 PRO 131 159 159 PRO PRO C . n C 1 132 LEU 132 160 160 LEU LEU C . n C 1 133 PRO 133 161 161 PRO PRO C . n C 1 134 CYS 134 162 162 CYS CYS C . n C 1 135 SER 135 163 163 SER SER C . n C 1 136 CYS 136 164 164 CYS CYS C . n C 1 137 ASP 137 165 165 ASP ASP C . n C 1 138 LYS 138 166 166 LYS LYS C . n C 1 139 GLU 139 167 167 GLU GLU C . n C 1 140 GLU 140 168 168 GLU GLU C . n C 1 141 GLY 141 169 169 GLY GLY C . n C 1 142 SER 142 170 170 SER SER C . n C 1 143 ASN 143 171 171 ASN ASN C . n C 1 144 VAL 144 172 172 VAL VAL C . n C 1 145 MET 145 173 173 MET MET C . n C 1 146 HIS 146 174 174 HIS HIS C . n C 1 147 LEU 147 175 175 LEU LEU C . n C 1 148 ALA 148 176 176 ALA ALA C . n C 1 149 TYR 149 177 177 TYR TYR C . n C 1 150 SER 150 178 178 SER SER C . n C 1 151 VAL 151 179 179 VAL VAL C . n C 1 152 GLY 152 180 180 GLY GLY C . n C 1 153 LYS 153 181 181 LYS LYS C . n C 1 154 GLY 154 182 ? ? ? C . n C 1 155 GLU 155 183 ? ? ? C . n C 1 156 ASN 156 184 184 ASN ASN C . n C 1 157 THR 157 185 185 THR THR C . n C 1 158 SER 158 186 186 SER SER C . n C 1 159 ALA 159 187 187 ALA ALA C . n C 1 160 ILE 160 188 188 ILE ILE C . n C 1 161 ALA 161 189 189 ALA ALA C . n C 1 162 ALA 162 190 190 ALA ALA C . n C 1 163 LYS 163 191 191 LYS LYS C . n C 1 164 TYR 164 192 192 TYR TYR C . n C 1 165 GLY 165 193 193 GLY GLY C . n C 1 166 VAL 166 194 194 VAL VAL C . n C 1 167 THR 167 195 195 THR THR C . n C 1 168 GLU 168 196 196 GLU GLU C . n C 1 169 SER 169 197 197 SER SER C . n C 1 170 THR 170 198 198 THR THR C . n C 1 171 LEU 171 199 199 LEU LEU C . n C 1 172 LEU 172 200 200 LEU LEU C . n C 1 173 THR 173 201 201 THR THR C . n C 1 174 ARG 174 202 202 ARG ARG C . n C 1 175 ASN 175 203 203 ASN ASN C . n C 1 176 LYS 176 204 204 LYS LYS C . n C 1 177 ILE 177 205 205 ILE ILE C . n C 1 178 ASP 178 206 ? ? ? C . n C 1 179 ASP 179 207 207 ASP ASP C . n C 1 180 PRO 180 208 208 PRO PRO C . n C 1 181 THR 181 209 209 THR THR C . n C 1 182 LYS 182 210 210 LYS LYS C . n C 1 183 LEU 183 211 211 LEU LEU C . n C 1 184 GLN 184 212 212 GLN GLN C . n C 1 185 MET 185 213 213 MET MET C . n C 1 186 GLY 186 214 214 GLY GLY C . n C 1 187 GLN 187 215 215 GLN GLN C . n C 1 188 ILE 188 216 216 ILE ILE C . n C 1 189 LEU 189 217 217 LEU LEU C . n C 1 190 ASP 190 218 218 ASP ASP C . n C 1 191 VAL 191 219 219 VAL VAL C . n C 1 192 PRO 192 220 220 PRO PRO C . n C 1 193 LEU 193 221 221 LEU LEU C . n C 1 194 PRO 194 222 222 PRO PRO C . n C 1 195 VAL 195 223 223 VAL VAL C . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code D 2 NAG 1 301 301 NAG NAG A . E 2 NAG 1 302 302 NAG NAG A . F 2 NAG 1 301 302 NAG NAG B . G 2 NAG 1 302 303 NAG NAG B . H 3 HOH 1 401 401 HOH HOH A . H 3 HOH 2 402 402 HOH HOH A . H 3 HOH 3 403 403 HOH HOH A . H 3 HOH 4 404 404 HOH HOH A . H 3 HOH 5 405 405 HOH HOH A . H 3 HOH 6 406 406 HOH HOH A . H 3 HOH 7 407 407 HOH HOH A . H 3 HOH 8 408 408 HOH HOH A . H 3 HOH 9 409 409 HOH HOH A . H 3 HOH 10 410 410 HOH HOH A . H 3 HOH 11 411 411 HOH HOH A . H 3 HOH 12 412 412 HOH HOH A . H 3 HOH 13 413 413 HOH HOH A . H 3 HOH 14 414 414 HOH HOH A . H 3 HOH 15 415 415 HOH HOH A . H 3 HOH 16 416 416 HOH HOH A . H 3 HOH 17 417 417 HOH HOH A . H 3 HOH 18 418 418 HOH HOH A . H 3 HOH 19 419 419 HOH HOH A . H 3 HOH 20 420 420 HOH HOH A . H 3 HOH 21 421 421 HOH HOH A . H 3 HOH 22 422 422 HOH HOH A . H 3 HOH 23 423 423 HOH HOH A . H 3 HOH 24 424 424 HOH HOH A . H 3 HOH 25 425 425 HOH HOH A . H 3 HOH 26 426 426 HOH HOH A . H 3 HOH 27 427 427 HOH HOH A . H 3 HOH 28 428 428 HOH HOH A . H 3 HOH 29 429 429 HOH HOH A . H 3 HOH 30 430 430 HOH HOH A . H 3 HOH 31 431 431 HOH HOH A . H 3 HOH 32 432 432 HOH HOH A . H 3 HOH 33 433 433 HOH HOH A . H 3 HOH 34 434 434 HOH HOH A . H 3 HOH 35 435 435 HOH HOH A . H 3 HOH 36 436 436 HOH HOH A . H 3 HOH 37 437 437 HOH HOH A . I 3 HOH 1 401 401 HOH HOH B . I 3 HOH 2 402 402 HOH HOH B . I 3 HOH 3 403 403 HOH HOH B . I 3 HOH 4 404 404 HOH HOH B . I 3 HOH 5 405 405 HOH HOH B . I 3 HOH 6 406 406 HOH HOH B . I 3 HOH 7 407 407 HOH HOH B . I 3 HOH 8 408 408 HOH HOH B . I 3 HOH 9 409 409 HOH HOH B . I 3 HOH 10 410 410 HOH HOH B . I 3 HOH 11 411 411 HOH HOH B . I 3 HOH 12 412 412 HOH HOH B . I 3 HOH 13 413 413 HOH HOH B . I 3 HOH 14 414 414 HOH HOH B . I 3 HOH 15 415 415 HOH HOH B . I 3 HOH 16 416 416 HOH HOH B . I 3 HOH 17 417 417 HOH HOH B . I 3 HOH 18 418 418 HOH HOH B . I 3 HOH 19 419 419 HOH HOH B . I 3 HOH 20 420 420 HOH HOH B . I 3 HOH 21 421 421 HOH HOH B . I 3 HOH 22 422 422 HOH HOH B . I 3 HOH 23 423 423 HOH HOH B . I 3 HOH 24 424 424 HOH HOH B . I 3 HOH 25 425 425 HOH HOH B . I 3 HOH 26 426 426 HOH HOH B . I 3 HOH 27 427 427 HOH HOH B . I 3 HOH 28 428 428 HOH HOH B . I 3 HOH 29 429 429 HOH HOH B . I 3 HOH 30 430 430 HOH HOH B . I 3 HOH 31 431 431 HOH HOH B . I 3 HOH 32 432 432 HOH HOH B . I 3 HOH 33 433 433 HOH HOH B . I 3 HOH 34 434 434 HOH HOH B . I 3 HOH 35 435 435 HOH HOH B . I 3 HOH 36 436 436 HOH HOH B . I 3 HOH 37 437 437 HOH HOH B . I 3 HOH 38 438 438 HOH HOH B . J 3 HOH 1 301 301 HOH HOH C . J 3 HOH 2 302 302 HOH HOH C . J 3 HOH 3 303 303 HOH HOH C . J 3 HOH 4 304 304 HOH HOH C . J 3 HOH 5 305 305 HOH HOH C . J 3 HOH 6 306 306 HOH HOH C . J 3 HOH 7 307 307 HOH HOH C . J 3 HOH 8 308 308 HOH HOH C . J 3 HOH 9 309 309 HOH HOH C . # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_defined_assembly ? monomeric 1 2 author_defined_assembly ? monomeric 1 3 author_defined_assembly ? monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,D,E,H 2 1 B,F,G,I 3 1 C,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 2017-02-22 # _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 16.3691 _pdbx_refine_tls.origin_y 43.1120 _pdbx_refine_tls.origin_z 86.2985 _pdbx_refine_tls.T[1][1] 0.2082 _pdbx_refine_tls.T[2][2] 0.2764 _pdbx_refine_tls.T[3][3] 0.2705 _pdbx_refine_tls.T[1][2] -0.0445 _pdbx_refine_tls.T[1][3] 0.0078 _pdbx_refine_tls.T[2][3] -0.0152 _pdbx_refine_tls.L[1][1] 0.1304 _pdbx_refine_tls.L[2][2] 0.1979 _pdbx_refine_tls.L[3][3] 0.4488 _pdbx_refine_tls.L[1][2] 0.0001 _pdbx_refine_tls.L[1][3] 0.1062 _pdbx_refine_tls.L[2][3] 0.0763 _pdbx_refine_tls.S[1][1] -0.0188 _pdbx_refine_tls.S[1][2] 0.1231 _pdbx_refine_tls.S[1][3] 0.0464 _pdbx_refine_tls.S[2][1] 0.0345 _pdbx_refine_tls.S[2][2] -0.0242 _pdbx_refine_tls.S[2][3] 0.0366 _pdbx_refine_tls.S[3][1] 0.0880 _pdbx_refine_tls.S[3][2] -0.0013 _pdbx_refine_tls.S[3][3] 0.0000 # _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 ? _pdbx_refine_tls_group.beg_auth_seq_id ? _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id ? _pdbx_refine_tls_group.end_auth_seq_id ? _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 ALL # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.8_1069 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? SHELXD ? ? ? . 4 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OD1 B ASP 122 ? ? NH1 B ARG 126 ? ? 2.13 2 1 O A HOH 401 ? ? O A HOH 433 ? ? 2.14 3 1 NH1 A ARG 97 ? ? OD2 A ASP 108 ? ? 2.18 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 C _pdbx_validate_rmsd_angle.auth_asym_id_1 B _pdbx_validate_rmsd_angle.auth_comp_id_1 LEU _pdbx_validate_rmsd_angle.auth_seq_id_1 221 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 N _pdbx_validate_rmsd_angle.auth_asym_id_2 B _pdbx_validate_rmsd_angle.auth_comp_id_2 PRO _pdbx_validate_rmsd_angle.auth_seq_id_2 222 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 CA _pdbx_validate_rmsd_angle.auth_asym_id_3 B _pdbx_validate_rmsd_angle.auth_comp_id_3 PRO _pdbx_validate_rmsd_angle.auth_seq_id_3 222 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 129.72 _pdbx_validate_rmsd_angle.angle_target_value 119.30 _pdbx_validate_rmsd_angle.angle_deviation 10.42 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.50 _pdbx_validate_rmsd_angle.linker_flag Y # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 30 ? ? 51.04 -137.92 2 1 ASN A 89 ? ? 74.27 -6.12 3 1 ARG A 109 ? ? 56.91 13.86 4 1 ASN A 143 ? ? 54.31 -38.67 5 1 SER A 153 ? ? 74.75 -1.74 6 1 ASN B 30 ? ? 51.91 -132.30 7 1 ASN B 89 ? ? 75.25 -3.75 8 1 ARG B 109 ? ? 56.46 14.81 9 1 ASN C 30 ? ? 36.23 -128.42 10 1 THR C 53 ? ? -153.45 -158.08 11 1 ARG C 109 ? ? 55.88 16.91 12 1 GLN C 118 ? ? -115.39 51.19 13 1 ALA C 139 ? ? 68.34 -57.64 14 1 ASN C 143 ? ? 52.02 -55.86 15 1 ASN C 148 ? ? -86.50 35.34 16 1 SER C 153 ? ? 78.02 -2.50 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A VAL 223 ? CG1 ? A VAL 195 CG1 2 1 Y 1 A VAL 223 ? CG2 ? A VAL 195 CG2 3 1 Y 1 C VAL 223 ? CG1 ? C VAL 195 CG1 4 1 Y 1 C VAL 223 ? CG2 ? C VAL 195 CG2 5 1 N 1 B NAG 301 ? C6 ? F NAG 1 C6 6 1 N 1 B NAG 301 ? O6 ? F NAG 1 O6 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 C GLY 182 ? C GLY 154 2 1 Y 1 C GLU 183 ? C GLU 155 3 1 Y 1 C ASP 206 ? C ASP 178 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 water HOH #