data_51150 ####################### # Entry information # ####################### save_entry_information_1 _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information_1 _Entry.ID 51150 _Entry.Title ; Apo Thioredoxin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2021-10-21 _Entry.Accession_date 2021-10-21 _Entry.Last_release_date 2021-10-22 _Entry.Original_release_date 2021-10-22 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.14.0 _Entry.NMR_STAR_dict_location . _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _Entry.Details 'Backbone chemical shifts of apo Thioredoxin' _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 Ju-Sim Kim . . . . 51150 2 Alexandra Born . . . . 51150 3 James Till . . . . 51150 4 Lin Liu . . . . 51150 5 Sashi Kent . . . . 51150 6 Morkos Henen . . . . 51150 7 Beat Vogeli . . . . 51150 8 Andres Vazquez-Torres . . . . 51150 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 51150 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 197 51150 '15N chemical shifts' 99 51150 '1H chemical shifts' 99 51150 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2024-08-09 . original BMRB . 51150 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 51151 OmpR 51150 stop_ save_ ############### # Citations # ############### save_citations_1 _Citation.Sf_category citations _Citation.Sf_framecode citations_1 _Citation.Entry_ID 51150 _Citation.ID 1 _Citation.Name . _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 36266276 _Citation.DOI . _Citation.Full_citation . _Citation.Title ; Promiscuity of response regulators for thioredoxin steers bacterial virulence ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Commun.' _Citation.Journal_name_full 'Nature communications' _Citation.Journal_volume 13 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 2041-1723 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 6210 _Citation.Page_last 6210 _Citation.Year 2022 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Ju-Sim Kim . . . . 51150 1 2 Alexandra Born . . . . 51150 1 3 James Till . . . . 51150 1 4 Lin Liu . . . . 51150 1 5 Sashi Kent . . . . 51150 1 6 Morkos Henen . . . . 51150 1 7 Beat Vogeli . . . . 51150 1 8 Andres Vazquez-Torres . . . . 51150 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly_1 _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly_1 _Assembly.Entry_ID 51150 _Assembly.ID 1 _Assembly.Name 'Apo Thioredoxin' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states no _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange no _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 thioredoxin 1 $entity_1 . . yes native no no . . . 51150 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_asym_ID_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_asym_ID_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 32 32 SG . 1 . 1 CYS 35 35 SG . . . . . . . . . . . . 51150 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 51150 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity_1 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; SDKIIHLTDDSFDTDVLKAD GAILVDFWAEWCGPCKMIAP ILDEIADEYQGKLTVAKLNI DQNPGTAPKYGIRGIPTLLL FKNGEVAATKVGALSKGQLK EFLDANLA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 108 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 2 SER . 51150 1 2 3 ASP . 51150 1 3 4 LYS . 51150 1 4 5 ILE . 51150 1 5 6 ILE . 51150 1 6 7 HIS . 51150 1 7 8 LEU . 51150 1 8 9 THR . 51150 1 9 10 ASP . 51150 1 10 11 ASP . 51150 1 11 12 SER . 51150 1 12 13 PHE . 51150 1 13 14 ASP . 51150 1 14 15 THR . 51150 1 15 16 ASP . 51150 1 16 17 VAL . 51150 1 17 18 LEU . 51150 1 18 19 LYS . 51150 1 19 20 ALA . 51150 1 20 21 ASP . 51150 1 21 22 GLY . 51150 1 22 23 ALA . 51150 1 23 24 ILE . 51150 1 24 25 LEU . 51150 1 25 26 VAL . 51150 1 26 27 ASP . 51150 1 27 28 PHE . 51150 1 28 29 TRP . 51150 1 29 30 ALA . 51150 1 30 31 GLU . 51150 1 31 32 TRP . 51150 1 32 33 CYS . 51150 1 33 34 GLY . 51150 1 34 35 PRO . 51150 1 35 36 CYS . 51150 1 36 37 LYS . 51150 1 37 38 MET . 51150 1 38 39 ILE . 51150 1 39 40 ALA . 51150 1 40 41 PRO . 51150 1 41 42 ILE . 51150 1 42 43 LEU . 51150 1 43 44 ASP . 51150 1 44 45 GLU . 51150 1 45 46 ILE . 51150 1 46 47 ALA . 51150 1 47 48 ASP . 51150 1 48 49 GLU . 51150 1 49 50 TYR . 51150 1 50 51 GLN . 51150 1 51 52 GLY . 51150 1 52 53 LYS . 51150 1 53 54 LEU . 51150 1 54 55 THR . 51150 1 55 56 VAL . 51150 1 56 57 ALA . 51150 1 57 58 LYS . 51150 1 58 59 LEU . 51150 1 59 60 ASN . 51150 1 60 61 ILE . 51150 1 61 62 ASP . 51150 1 62 63 GLN . 51150 1 63 64 ASN . 51150 1 64 65 PRO . 51150 1 65 66 GLY . 51150 1 66 67 THR . 51150 1 67 68 ALA . 51150 1 68 69 PRO . 51150 1 69 70 LYS . 51150 1 70 71 TYR . 51150 1 71 72 GLY . 51150 1 72 73 ILE . 51150 1 73 74 ARG . 51150 1 74 75 GLY . 51150 1 75 76 ILE . 51150 1 76 77 PRO . 51150 1 77 78 THR . 51150 1 78 79 LEU . 51150 1 79 80 LEU . 51150 1 80 81 LEU . 51150 1 81 82 PHE . 51150 1 82 83 LYS . 51150 1 83 84 ASN . 51150 1 84 85 GLY . 51150 1 85 86 GLU . 51150 1 86 87 VAL . 51150 1 87 88 ALA . 51150 1 88 89 ALA . 51150 1 89 90 THR . 51150 1 90 91 LYS . 51150 1 91 92 VAL . 51150 1 92 93 GLY . 51150 1 93 94 ALA . 51150 1 94 95 LEU . 51150 1 95 96 SER . 51150 1 96 97 LYS . 51150 1 97 98 GLY . 51150 1 98 99 GLN . 51150 1 99 100 LEU . 51150 1 100 101 LYS . 51150 1 101 102 GLU . 51150 1 102 103 PHE . 51150 1 103 104 LEU . 51150 1 104 105 ASP . 51150 1 105 106 ALA . 51150 1 106 107 ASN . 51150 1 107 108 LEU . 51150 1 108 109 ALA . 51150 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . SER 1 1 51150 1 . ASP 2 2 51150 1 . LYS 3 3 51150 1 . ILE 4 4 51150 1 . ILE 5 5 51150 1 . HIS 6 6 51150 1 . LEU 7 7 51150 1 . THR 8 8 51150 1 . ASP 9 9 51150 1 . ASP 10 10 51150 1 . SER 11 11 51150 1 . PHE 12 12 51150 1 . ASP 13 13 51150 1 . THR 14 14 51150 1 . ASP 15 15 51150 1 . VAL 16 16 51150 1 . LEU 17 17 51150 1 . LYS 18 18 51150 1 . ALA 19 19 51150 1 . ASP 20 20 51150 1 . GLY 21 21 51150 1 . ALA 22 22 51150 1 . ILE 23 23 51150 1 . LEU 24 24 51150 1 . VAL 25 25 51150 1 . ASP 26 26 51150 1 . PHE 27 27 51150 1 . TRP 28 28 51150 1 . ALA 29 29 51150 1 . GLU 30 30 51150 1 . TRP 31 31 51150 1 . CYS 32 32 51150 1 . GLY 33 33 51150 1 . PRO 34 34 51150 1 . CYS 35 35 51150 1 . LYS 36 36 51150 1 . MET 37 37 51150 1 . ILE 38 38 51150 1 . ALA 39 39 51150 1 . PRO 40 40 51150 1 . ILE 41 41 51150 1 . LEU 42 42 51150 1 . ASP 43 43 51150 1 . GLU 44 44 51150 1 . ILE 45 45 51150 1 . ALA 46 46 51150 1 . ASP 47 47 51150 1 . GLU 48 48 51150 1 . TYR 49 49 51150 1 . GLN 50 50 51150 1 . GLY 51 51 51150 1 . LYS 52 52 51150 1 . LEU 53 53 51150 1 . THR 54 54 51150 1 . VAL 55 55 51150 1 . ALA 56 56 51150 1 . LYS 57 57 51150 1 . LEU 58 58 51150 1 . ASN 59 59 51150 1 . ILE 60 60 51150 1 . ASP 61 61 51150 1 . GLN 62 62 51150 1 . ASN 63 63 51150 1 . PRO 64 64 51150 1 . GLY 65 65 51150 1 . THR 66 66 51150 1 . ALA 67 67 51150 1 . PRO 68 68 51150 1 . LYS 69 69 51150 1 . TYR 70 70 51150 1 . GLY 71 71 51150 1 . ILE 72 72 51150 1 . ARG 73 73 51150 1 . GLY 74 74 51150 1 . ILE 75 75 51150 1 . PRO 76 76 51150 1 . THR 77 77 51150 1 . LEU 78 78 51150 1 . LEU 79 79 51150 1 . LEU 80 80 51150 1 . PHE 81 81 51150 1 . LYS 82 82 51150 1 . ASN 83 83 51150 1 . GLY 84 84 51150 1 . GLU 85 85 51150 1 . VAL 86 86 51150 1 . ALA 87 87 51150 1 . ALA 88 88 51150 1 . THR 89 89 51150 1 . LYS 90 90 51150 1 . VAL 91 91 51150 1 . GLY 92 92 51150 1 . ALA 93 93 51150 1 . LEU 94 94 51150 1 . SER 95 95 51150 1 . LYS 96 96 51150 1 . GLY 97 97 51150 1 . GLN 98 98 51150 1 . LEU 99 99 51150 1 . LYS 100 100 51150 1 . GLU 101 101 51150 1 . PHE 102 102 51150 1 . LEU 103 103 51150 1 . ASP 104 104 51150 1 . ALA 105 105 51150 1 . ASN 106 106 51150 1 . LEU 107 107 51150 1 . ALA 108 108 51150 1 stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source_1 _Entity_natural_src_list.Entry_ID 51150 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $entity_1 . 28901 organism . 'Salmonella enterica' 'Salmonella enterica' . . Bacteria . Salmonella enterica . . . . . . . . . . . . . 51150 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source_1 _Entity_experimental_src_list.Entry_ID 51150 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $entity_1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . plasmid . . pET22b . . . 51150 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 51150 _Sample.ID 1 _Sample.Name '15N,13C Apo Thioredoxin' _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number 1 _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Thioredoxin '[U-98% 13C; U-98% 15N]' . . 1 $entity_1 . . 1.5 . . mM . . . . 51150 1 2 'potassium phosphate' 'natural abundance' . . . . . . 20 . . mM . . . . 51150 1 3 'sodium chloride' 'natural abundance' . . . . . . 50 . . mM . . . . 51150 1 4 D2O '[U-99% 2H]' . . . . . . 3 . . % . . . . 51150 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 51150 _Sample_condition_list.ID 1 _Sample_condition_list.Name Standard _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 50 . mM 51150 1 pH 6.5 . pH 51150 1 pressure 1 . atm 51150 1 temperature 298 . K 51150 1 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 51150 _Software.ID 1 _Software.Type . _Software.Name NMRPipe _Software.Version . _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID processing . 51150 1 stop_ save_ save_software_2 _Software.Sf_category software _Software.Sf_framecode software_2 _Software.Entry_ID 51150 _Software.ID 2 _Software.Type . _Software.Name NMRDraw _Software.Version . _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID processing . 51150 2 stop_ save_ save_software_3 _Software.Sf_category software _Software.Sf_framecode software_3 _Software.Entry_ID 51150 _Software.ID 3 _Software.Type . _Software.Name CcpNMR _Software.Version . _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' . 51150 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 51150 _NMR_spectrometer.ID 1 _NMR_spectrometer.Name 'Varian 600' _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_experiment_list_1 _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list_1 _Experiment_list.Entry_ID 51150 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NUS_flag _Experiment.Interleaved_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Details _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no no no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 51150 1 2 '3D HN(CO)CACB' no no no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 51150 1 3 '3D CBCA(CO)NH' no no no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 51150 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_1 _Chem_shift_reference.Entry_ID 51150 _Chem_shift_reference.ID 1 _Chem_shift_reference.Name Thioredoxin _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 na na . . . . na 0 na direct 1 . . . . . 51150 1 H 1 water protons . . . . ppm 4.77 internal direct 1 . . . . . 51150 1 N 15 na na . . . . na 0 na direct 1 . . . . . 51150 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_1 _Assigned_chem_shift_list.Entry_ID 51150 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Name 'Apo Trxa' _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 51150 1 2 '3D HN(CO)CACB' . . . 51150 1 3 '3D CBCA(CO)NH' . . . 51150 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 3 $software_3 . . 51150 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_assembly_asym_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 . 1 2 2 ASP CA C 13 54.702 0.000 . 1 . . . . . 3 ASP CA . 51150 1 2 . 1 . 1 2 2 ASP CB C 13 40.846 0.000 . 1 . . . . . 3 ASP CB . 51150 1 3 . 1 . 1 3 3 LYS H H 1 8.368 0.005 . 1 . . . . . 4 LYS H . 51150 1 4 . 1 . 1 3 3 LYS CA C 13 56.611 0.010 . 1 . . . . . 4 LYS CA . 51150 1 5 . 1 . 1 3 3 LYS CB C 13 33.475 0.007 . 1 . . . . . 4 LYS CB . 51150 1 6 . 1 . 1 3 3 LYS N N 15 118.894 0.097 . 1 . . . . . 4 LYS N . 51150 1 7 . 1 . 1 4 4 ILE H H 1 7.328 0.018 . 1 . . . . . 5 ILE H . 51150 1 8 . 1 . 1 4 4 ILE CA C 13 60.604 0.039 . 1 . . . . . 5 ILE CA . 51150 1 9 . 1 . 1 4 4 ILE CB C 13 38.406 0.038 . 1 . . . . . 5 ILE CB . 51150 1 10 . 1 . 1 4 4 ILE N N 15 121.013 0.070 . 1 . . . . . 5 ILE N . 51150 1 11 . 1 . 1 5 5 ILE H H 1 8.241 0.007 . 1 . . . . . 6 ILE H . 51150 1 12 . 1 . 1 5 5 ILE CA C 13 60.183 0.050 . 1 . . . . . 6 ILE CA . 51150 1 13 . 1 . 1 5 5 ILE CB C 13 39.350 0.048 . 1 . . . . . 6 ILE CB . 51150 1 14 . 1 . 1 5 5 ILE N N 15 125.777 0.087 . 1 . . . . . 6 ILE N . 51150 1 15 . 1 . 1 6 6 HIS H H 1 8.816 0.007 . 1 . . . . . 7 HIS H . 51150 1 16 . 1 . 1 6 6 HIS CA C 13 56.103 0.041 . 1 . . . . . 7 HIS CA . 51150 1 17 . 1 . 1 6 6 HIS CB C 13 31.375 0.048 . 1 . . . . . 7 HIS CB . 51150 1 18 . 1 . 1 6 6 HIS N N 15 125.895 0.100 . 1 . . . . . 7 HIS N . 51150 1 19 . 1 . 1 7 7 LEU H H 1 8.868 0.014 . 1 . . . . . 8 LEU H . 51150 1 20 . 1 . 1 7 7 LEU CA C 13 53.751 0.032 . 1 . . . . . 8 LEU CA . 51150 1 21 . 1 . 1 7 7 LEU CB C 13 46.023 0.072 . 1 . . . . . 8 LEU CB . 51150 1 22 . 1 . 1 7 7 LEU N N 15 124.626 0.078 . 1 . . . . . 8 LEU N . 51150 1 23 . 1 . 1 8 8 THR H H 1 8.128 0.004 . 1 . . . . . 9 THR H . 51150 1 24 . 1 . 1 8 8 THR CA C 13 58.876 0.009 . 1 . . . . . 9 THR CA . 51150 1 25 . 1 . 1 8 8 THR CB C 13 72.930 0.057 . 1 . . . . . 9 THR CB . 51150 1 26 . 1 . 1 8 8 THR N N 15 108.103 0.043 . 1 . . . . . 9 THR N . 51150 1 27 . 1 . 1 9 9 ASP H H 1 8.199 0.012 . 1 . . . . . 10 ASP H . 51150 1 28 . 1 . 1 9 9 ASP CA C 13 58.090 0.050 . 1 . . . . . 10 ASP CA . 51150 1 29 . 1 . 1 9 9 ASP CB C 13 40.347 0.036 . 1 . . . . . 10 ASP CB . 51150 1 30 . 1 . 1 9 9 ASP N N 15 119.810 0.066 . 1 . . . . . 10 ASP N . 51150 1 31 . 1 . 1 10 10 ASP H H 1 8.205 0.003 . 1 . . . . . 11 ASP H . 51150 1 32 . 1 . 1 10 10 ASP CA C 13 56.420 0.048 . 1 . . . . . 11 ASP CA . 51150 1 33 . 1 . 1 10 10 ASP CB C 13 41.265 0.061 . 1 . . . . . 11 ASP CB . 51150 1 34 . 1 . 1 10 10 ASP N N 15 116.382 0.063 . 1 . . . . . 11 ASP N . 51150 1 35 . 1 . 1 11 11 SER H H 1 8.257 0.005 . 1 . . . . . 12 SER H . 51150 1 36 . 1 . 1 11 11 SER CA C 13 59.355 0.023 . 1 . . . . . 12 SER CA . 51150 1 37 . 1 . 1 11 11 SER CB C 13 64.352 0.042 . 1 . . . . . 12 SER CB . 51150 1 38 . 1 . 1 11 11 SER N N 15 117.877 0.055 . 1 . . . . . 12 SER N . 51150 1 39 . 1 . 1 12 12 PHE H H 1 7.688 0.011 . 1 . . . . . 13 PHE H . 51150 1 40 . 1 . 1 12 12 PHE CA C 13 63.352 0.031 . 1 . . . . . 13 PHE CA . 51150 1 41 . 1 . 1 12 12 PHE CB C 13 40.790 0.058 . 1 . . . . . 13 PHE CB . 51150 1 42 . 1 . 1 12 12 PHE N N 15 125.402 0.058 . 1 . . . . . 13 PHE N . 51150 1 43 . 1 . 1 13 13 ASP H H 1 8.686 0.007 . 1 . . . . . 14 ASP H . 51150 1 44 . 1 . 1 13 13 ASP CA C 13 58.047 0.005 . 1 . . . . . 14 ASP CA . 51150 1 45 . 1 . 1 13 13 ASP CB C 13 40.866 0.006 . 1 . . . . . 14 ASP CB . 51150 1 46 . 1 . 1 13 13 ASP N N 15 117.241 0.052 . 1 . . . . . 14 ASP N . 51150 1 47 . 1 . 1 14 14 THR H H 1 7.750 0.006 . 1 . . . . . 15 THR H . 51150 1 48 . 1 . 1 14 14 THR CA C 13 65.753 0.005 . 1 . . . . . 15 THR CA . 51150 1 49 . 1 . 1 14 14 THR CB C 13 69.199 0.003 . 1 . . . . . 15 THR CB . 51150 1 50 . 1 . 1 14 14 THR N N 15 112.492 0.062 . 1 . . . . . 15 THR N . 51150 1 51 . 1 . 1 15 15 ASP H H 1 8.424 0.007 . 1 . . . . . 16 ASP H . 51150 1 52 . 1 . 1 15 15 ASP CA C 13 56.600 0.017 . 1 . . . . . 16 ASP CA . 51150 1 53 . 1 . 1 15 15 ASP CB C 13 41.871 0.003 . 1 . . . . . 16 ASP CB . 51150 1 54 . 1 . 1 15 15 ASP N N 15 118.932 0.053 . 1 . . . . . 16 ASP N . 51150 1 55 . 1 . 1 16 16 VAL H H 1 7.551 0.003 . 1 . . . . . 17 VAL H . 51150 1 56 . 1 . 1 16 16 VAL CA C 13 63.254 0.007 . 1 . . . . . 17 VAL CA . 51150 1 57 . 1 . 1 16 16 VAL CB C 13 32.319 0.070 . 1 . . . . . 17 VAL CB . 51150 1 58 . 1 . 1 16 16 VAL N N 15 113.022 0.054 . 1 . . . . . 17 VAL N . 51150 1 59 . 1 . 1 17 17 LEU H H 1 6.980 0.008 . 1 . . . . . 18 LEU H . 51150 1 60 . 1 . 1 17 17 LEU CA C 13 58.147 0.013 . 1 . . . . . 18 LEU CA . 51150 1 61 . 1 . 1 17 17 LEU CB C 13 39.582 0.041 . 1 . . . . . 18 LEU CB . 51150 1 62 . 1 . 1 17 17 LEU N N 15 116.402 0.049 . 1 . . . . . 18 LEU N . 51150 1 63 . 1 . 1 18 18 LYS H H 1 7.378 0.007 . 1 . . . . . 19 LYS H . 51150 1 64 . 1 . 1 18 18 LYS CA C 13 54.998 0.041 . 1 . . . . . 19 LYS CA . 51150 1 65 . 1 . 1 18 18 LYS CB C 13 32.164 0.027 . 1 . . . . . 19 LYS CB . 51150 1 66 . 1 . 1 18 18 LYS N N 15 115.262 0.060 . 1 . . . . . 19 LYS N . 51150 1 67 . 1 . 1 19 19 ALA H H 1 6.597 0.008 . 1 . . . . . 20 ALA H . 51150 1 68 . 1 . 1 19 19 ALA CA C 13 52.239 0.000 . 1 . . . . . 20 ALA CA . 51150 1 69 . 1 . 1 19 19 ALA CB C 13 20.332 0.012 . 1 . . . . . 20 ALA CB . 51150 1 70 . 1 . 1 19 19 ALA N N 15 122.436 0.049 . 1 . . . . . 20 ALA N . 51150 1 71 . 1 . 1 20 20 ASP H H 1 8.508 0.008 . 1 . . . . . 21 ASP H . 51150 1 72 . 1 . 1 20 20 ASP CA C 13 54.323 0.022 . 1 . . . . . 21 ASP CA . 51150 1 73 . 1 . 1 20 20 ASP CB C 13 42.039 0.013 . 1 . . . . . 21 ASP CB . 51150 1 74 . 1 . 1 20 20 ASP N N 15 121.334 0.050 . 1 . . . . . 21 ASP N . 51150 1 75 . 1 . 1 21 21 GLY H H 1 8.122 0.009 . 1 . . . . . 22 GLY H . 51150 1 76 . 1 . 1 21 21 GLY CA C 13 44.509 0.003 . 1 . . . . . 22 GLY CA . 51150 1 77 . 1 . 1 21 21 GLY N N 15 108.591 0.061 . 1 . . . . . 22 GLY N . 51150 1 78 . 1 . 1 22 22 ALA H H 1 8.465 0.007 . 1 . . . . . 23 ALA H . 51150 1 79 . 1 . 1 22 22 ALA CA C 13 51.679 0.018 . 1 . . . . . 23 ALA CA . 51150 1 80 . 1 . 1 22 22 ALA CB C 13 20.318 0.009 . 1 . . . . . 23 ALA CB . 51150 1 81 . 1 . 1 22 22 ALA N N 15 123.283 0.047 . 1 . . . . . 23 ALA N . 51150 1 82 . 1 . 1 23 23 ILE H H 1 8.940 0.004 . 1 . . . . . 24 ILE H . 51150 1 83 . 1 . 1 23 23 ILE CA C 13 59.014 0.016 . 1 . . . . . 24 ILE CA . 51150 1 84 . 1 . 1 23 23 ILE CB C 13 41.071 0.033 . 1 . . . . . 24 ILE CB . 51150 1 85 . 1 . 1 23 23 ILE N N 15 123.808 0.063 . 1 . . . . . 24 ILE N . 51150 1 86 . 1 . 1 24 24 LEU H H 1 9.231 0.004 . 1 . . . . . 25 LEU H . 51150 1 87 . 1 . 1 24 24 LEU CA C 13 53.013 0.003 . 1 . . . . . 25 LEU CA . 51150 1 88 . 1 . 1 24 24 LEU CB C 13 45.534 0.021 . 1 . . . . . 25 LEU CB . 51150 1 89 . 1 . 1 24 24 LEU N N 15 130.682 0.056 . 1 . . . . . 25 LEU N . 51150 1 90 . 1 . 1 25 25 VAL H H 1 9.741 0.006 . 1 . . . . . 26 VAL H . 51150 1 91 . 1 . 1 25 25 VAL CA C 13 61.623 0.003 . 1 . . . . . 26 VAL CA . 51150 1 92 . 1 . 1 25 25 VAL CB C 13 33.707 0.008 . 1 . . . . . 26 VAL CB . 51150 1 93 . 1 . 1 25 25 VAL N N 15 126.686 0.044 . 1 . . . . . 26 VAL N . 51150 1 94 . 1 . 1 26 26 ASP H H 1 8.850 0.015 . 1 . . . . . 27 ASP H . 51150 1 95 . 1 . 1 26 26 ASP CA C 13 52.237 0.042 . 1 . . . . . 27 ASP CA . 51150 1 96 . 1 . 1 26 26 ASP CB C 13 40.878 0.029 . 1 . . . . . 27 ASP CB . 51150 1 97 . 1 . 1 26 26 ASP N N 15 125.204 0.149 . 1 . . . . . 27 ASP N . 51150 1 98 . 1 . 1 27 27 PHE H H 1 8.693 0.049 . 1 . . . . . 28 PHE H . 51150 1 99 . 1 . 1 27 27 PHE CA C 13 58.267 0.054 . 1 . . . . . 28 PHE CA . 51150 1 100 . 1 . 1 27 27 PHE CB C 13 39.772 0.019 . 1 . . . . . 28 PHE CB . 51150 1 101 . 1 . 1 27 27 PHE N N 15 128.019 0.160 . 1 . . . . . 28 PHE N . 51150 1 102 . 1 . 1 28 28 TRP H H 1 8.634 0.019 . 1 . . . . . 29 TRP H . 51150 1 103 . 1 . 1 28 28 TRP HE1 H 1 10.898 0.016 . 1 . . . . . 29 TRP HE1 . 51150 1 104 . 1 . 1 28 28 TRP CA C 13 55.257 0.053 . 1 . . . . . 29 TRP CA . 51150 1 105 . 1 . 1 28 28 TRP CB C 13 33.262 0.052 . 1 . . . . . 29 TRP CB . 51150 1 106 . 1 . 1 28 28 TRP N N 15 120.310 0.059 . 1 . . . . . 29 TRP N . 51150 1 107 . 1 . 1 28 28 TRP NE1 N 15 131.937 0.186 . 1 . . . . . 29 TRP NE1 . 51150 1 108 . 1 . 1 29 29 ALA H H 1 6.471 0.009 . 1 . . . . . 30 ALA H . 51150 1 109 . 1 . 1 29 29 ALA CA C 13 51.601 0.048 . 1 . . . . . 30 ALA CA . 51150 1 110 . 1 . 1 29 29 ALA CB C 13 21.781 0.078 . 1 . . . . . 30 ALA CB . 51150 1 111 . 1 . 1 29 29 ALA N N 15 116.073 0.083 . 1 . . . . . 30 ALA N . 51150 1 112 . 1 . 1 30 30 GLU H H 1 9.352 0.083 . 1 . . . . . 31 GLU H . 51150 1 113 . 1 . 1 30 30 GLU CA C 13 59.612 0.079 . 1 . . . . . 31 GLU CA . 51150 1 114 . 1 . 1 30 30 GLU CB C 13 29.811 0.025 . 1 . . . . . 31 GLU CB . 51150 1 115 . 1 . 1 30 30 GLU N N 15 121.753 0.339 . 1 . . . . . 31 GLU N . 51150 1 116 . 1 . 1 31 31 TRP H H 1 6.593 0.017 . 1 . . . . . 32 TRP H . 51150 1 117 . 1 . 1 31 31 TRP HE1 H 1 11.555 0.074 . 1 . . . . . 32 TRP HE1 . 51150 1 118 . 1 . 1 31 31 TRP CA C 13 53.961 0.000 . 1 . . . . . 32 TRP CA . 51150 1 119 . 1 . 1 31 31 TRP CB C 13 28.913 0.000 . 1 . . . . . 32 TRP CB . 51150 1 120 . 1 . 1 31 31 TRP N N 15 111.340 0.105 . 1 . . . . . 32 TRP N . 51150 1 121 . 1 . 1 31 31 TRP NE1 N 15 120.124 16.411 . 1 . . . . . 32 TRP NE1 . 51150 1 122 . 1 . 1 35 35 CYS CA C 13 63.358 0.051 . 1 . . . . . 36 CYS CA . 51150 1 123 . 1 . 1 35 35 CYS CB C 13 34.641 0.094 . 1 . . . . . 36 CYS CB . 51150 1 124 . 1 . 1 36 36 LYS H H 1 7.917 0.005 . 1 . . . . . 37 LYS H . 51150 1 125 . 1 . 1 36 36 LYS CA C 13 59.077 0.032 . 1 . . . . . 37 LYS CA . 51150 1 126 . 1 . 1 36 36 LYS CB C 13 31.550 0.056 . 1 . . . . . 37 LYS CB . 51150 1 127 . 1 . 1 36 36 LYS N N 15 121.102 0.204 . 1 . . . . . 37 LYS N . 51150 1 128 . 1 . 1 37 37 MET H H 1 7.595 0.012 . 1 . . . . . 38 MET H . 51150 1 129 . 1 . 1 37 37 MET CA C 13 57.992 0.050 . 1 . . . . . 38 MET CA . 51150 1 130 . 1 . 1 37 37 MET CB C 13 32.359 0.101 . 1 . . . . . 38 MET CB . 51150 1 131 . 1 . 1 37 37 MET N N 15 117.433 0.121 . 1 . . . . . 38 MET N . 51150 1 132 . 1 . 1 38 38 ILE H H 1 7.222 0.025 . 1 . . . . . 39 ILE H . 51150 1 133 . 1 . 1 38 38 ILE CA C 13 61.906 0.043 . 1 . . . . . 39 ILE CA . 51150 1 134 . 1 . 1 38 38 ILE CB C 13 39.333 0.030 . 1 . . . . . 39 ILE CB . 51150 1 135 . 1 . 1 38 38 ILE N N 15 110.820 0.393 . 1 . . . . . 39 ILE N . 51150 1 136 . 1 . 1 39 39 ALA H H 1 7.244 0.022 . 1 . . . . . 40 ALA H . 51150 1 137 . 1 . 1 39 39 ALA CA C 13 57.550 0.000 . 1 . . . . . 40 ALA CA . 51150 1 138 . 1 . 1 39 39 ALA CB C 13 15.365 0.000 . 1 . . . . . 40 ALA CB . 51150 1 139 . 1 . 1 39 39 ALA N N 15 125.234 0.141 . 1 . . . . . 40 ALA N . 51150 1 140 . 1 . 1 40 40 PRO CA C 13 65.015 0.067 . 1 . . . . . 41 PRO CA . 51150 1 141 . 1 . 1 40 40 PRO CB C 13 31.869 0.000 . 1 . . . . . 41 PRO CB . 51150 1 142 . 1 . 1 41 41 ILE H H 1 8.213 0.004 . 1 . . . . . 42 ILE H . 51150 1 143 . 1 . 1 41 41 ILE CA C 13 63.285 0.062 . 1 . . . . . 42 ILE CA . 51150 1 144 . 1 . 1 41 41 ILE CB C 13 34.788 0.150 . 1 . . . . . 42 ILE CB . 51150 1 145 . 1 . 1 41 41 ILE N N 15 111.090 0.054 . 1 . . . . . 42 ILE N . 51150 1 146 . 1 . 1 42 42 LEU H H 1 7.862 0.031 . 1 . . . . . 43 LEU H . 51150 1 147 . 1 . 1 42 42 LEU CA C 13 57.805 0.020 . 1 . . . . . 43 LEU CA . 51150 1 148 . 1 . 1 42 42 LEU CB C 13 40.799 0.079 . 1 . . . . . 43 LEU CB . 51150 1 149 . 1 . 1 42 42 LEU N N 15 119.683 0.279 . 1 . . . . . 43 LEU N . 51150 1 150 . 1 . 1 43 43 ASP H H 1 7.294 0.008 . 1 . . . . . 44 ASP H . 51150 1 151 . 1 . 1 43 43 ASP CA C 13 58.035 0.029 . 1 . . . . . 44 ASP CA . 51150 1 152 . 1 . 1 43 43 ASP CB C 13 40.683 0.007 . 1 . . . . . 44 ASP CB . 51150 1 153 . 1 . 1 43 43 ASP N N 15 118.588 0.062 . 1 . . . . . 44 ASP N . 51150 1 154 . 1 . 1 44 44 GLU H H 1 7.218 0.004 . 1 . . . . . 45 GLU H . 51150 1 155 . 1 . 1 44 44 GLU CA C 13 59.419 0.008 . 1 . . . . . 45 GLU CA . 51150 1 156 . 1 . 1 44 44 GLU CB C 13 29.577 0.063 . 1 . . . . . 45 GLU CB . 51150 1 157 . 1 . 1 44 44 GLU N N 15 118.201 0.045 . 1 . . . . . 45 GLU N . 51150 1 158 . 1 . 1 45 45 ILE H H 1 8.511 0.006 . 1 . . . . . 46 ILE H . 51150 1 159 . 1 . 1 45 45 ILE CA C 13 62.341 0.044 . 1 . . . . . 46 ILE CA . 51150 1 160 . 1 . 1 45 45 ILE CB C 13 36.464 0.001 . 1 . . . . . 46 ILE CB . 51150 1 161 . 1 . 1 45 45 ILE N N 15 120.972 0.053 . 1 . . . . . 46 ILE N . 51150 1 162 . 1 . 1 46 46 ALA H H 1 8.583 0.007 . 1 . . . . . 47 ALA H . 51150 1 163 . 1 . 1 46 46 ALA CA C 13 55.186 0.049 . 1 . . . . . 47 ALA CA . 51150 1 164 . 1 . 1 46 46 ALA CB C 13 18.141 0.048 . 1 . . . . . 47 ALA CB . 51150 1 165 . 1 . 1 46 46 ALA N N 15 122.461 0.043 . 1 . . . . . 47 ALA N . 51150 1 166 . 1 . 1 47 47 ASP H H 1 7.116 0.005 . 1 . . . . . 48 ASP H . 51150 1 167 . 1 . 1 47 47 ASP CA C 13 57.026 0.037 . 1 . . . . . 48 ASP CA . 51150 1 168 . 1 . 1 47 47 ASP CB C 13 41.327 0.054 . 1 . . . . . 48 ASP CB . 51150 1 169 . 1 . 1 47 47 ASP N N 15 115.054 0.055 . 1 . . . . . 48 ASP N . 51150 1 170 . 1 . 1 48 48 GLU H H 1 8.582 0.006 . 1 . . . . . 49 GLU H . 51150 1 171 . 1 . 1 48 48 GLU CA C 13 59.263 0.039 . 1 . . . . . 49 GLU CA . 51150 1 172 . 1 . 1 48 48 GLU CB C 13 30.194 0.076 . 1 . . . . . 49 GLU CB . 51150 1 173 . 1 . 1 48 48 GLU N N 15 120.827 0.065 . 1 . . . . . 49 GLU N . 51150 1 174 . 1 . 1 49 49 TYR H H 1 8.746 0.003 . 1 . . . . . 50 TYR H . 51150 1 175 . 1 . 1 49 49 TYR CA C 13 58.231 0.034 . 1 . . . . . 50 TYR CA . 51150 1 176 . 1 . 1 49 49 TYR CB C 13 37.183 0.074 . 1 . . . . . 50 TYR CB . 51150 1 177 . 1 . 1 49 49 TYR N N 15 115.366 0.049 . 1 . . . . . 50 TYR N . 51150 1 178 . 1 . 1 50 50 GLN H H 1 7.069 0.006 . 1 . . . . . 51 GLN H . 51150 1 179 . 1 . 1 50 50 GLN CA C 13 58.435 0.039 . 1 . . . . . 51 GLN CA . 51150 1 180 . 1 . 1 50 50 GLN CB C 13 28.801 0.060 . 1 . . . . . 51 GLN CB . 51150 1 181 . 1 . 1 50 50 GLN N N 15 121.370 0.050 . 1 . . . . . 51 GLN N . 51150 1 182 . 1 . 1 51 51 GLY H H 1 9.259 0.003 . 1 . . . . . 52 GLY H . 51150 1 183 . 1 . 1 51 51 GLY CA C 13 45.703 0.057 . 1 . . . . . 52 GLY CA . 51150 1 184 . 1 . 1 51 51 GLY N N 15 115.719 0.041 . 1 . . . . . 52 GLY N . 51150 1 185 . 1 . 1 52 52 LYS H H 1 8.202 0.007 . 1 . . . . . 53 LYS H . 51150 1 186 . 1 . 1 52 52 LYS CA C 13 56.387 0.027 . 1 . . . . . 53 LYS CA . 51150 1 187 . 1 . 1 52 52 LYS CB C 13 35.083 0.077 . 1 . . . . . 53 LYS CB . 51150 1 188 . 1 . 1 52 52 LYS N N 15 117.920 0.059 . 1 . . . . . 53 LYS N . 51150 1 189 . 1 . 1 53 53 LEU H H 1 7.811 0.006 . 1 . . . . . 54 LEU H . 51150 1 190 . 1 . 1 53 53 LEU CA C 13 54.274 0.031 . 1 . . . . . 54 LEU CA . 51150 1 191 . 1 . 1 53 53 LEU CB C 13 47.289 0.040 . 1 . . . . . 54 LEU CB . 51150 1 192 . 1 . 1 53 53 LEU N N 15 119.125 0.096 . 1 . . . . . 54 LEU N . 51150 1 193 . 1 . 1 54 54 THR H H 1 8.085 0.007 . 1 . . . . . 55 THR H . 51150 1 194 . 1 . 1 54 54 THR CA C 13 62.045 0.030 . 1 . . . . . 55 THR CA . 51150 1 195 . 1 . 1 54 54 THR CB C 13 70.427 0.025 . 1 . . . . . 55 THR CB . 51150 1 196 . 1 . 1 54 54 THR N N 15 123.409 0.045 . 1 . . . . . 55 THR N . 51150 1 197 . 1 . 1 55 55 VAL H H 1 9.927 0.003 . 1 . . . . . 56 VAL H . 51150 1 198 . 1 . 1 55 55 VAL CA C 13 62.118 0.067 . 1 . . . . . 56 VAL CA . 51150 1 199 . 1 . 1 55 55 VAL CB C 13 32.423 0.066 . 1 . . . . . 56 VAL CB . 51150 1 200 . 1 . 1 55 55 VAL N N 15 129.942 0.036 . 1 . . . . . 56 VAL N . 51150 1 201 . 1 . 1 56 56 ALA H H 1 9.295 0.011 . 1 . . . . . 57 ALA H . 51150 1 202 . 1 . 1 56 56 ALA CA C 13 49.260 0.009 . 1 . . . . . 57 ALA CA . 51150 1 203 . 1 . 1 56 56 ALA CB C 13 24.171 0.026 . 1 . . . . . 57 ALA CB . 51150 1 204 . 1 . 1 56 56 ALA N N 15 129.597 0.069 . 1 . . . . . 57 ALA N . 51150 1 205 . 1 . 1 57 57 LYS H H 1 8.649 0.010 . 1 . . . . . 58 LYS H . 51150 1 206 . 1 . 1 57 57 LYS CA C 13 54.815 0.001 . 1 . . . . . 58 LYS CA . 51150 1 207 . 1 . 1 57 57 LYS CB C 13 37.397 0.011 . 1 . . . . . 58 LYS CB . 51150 1 208 . 1 . 1 57 57 LYS N N 15 118.344 0.077 . 1 . . . . . 58 LYS N . 51150 1 209 . 1 . 1 58 58 LEU H H 1 8.891 0.044 . 1 . . . . . 59 LEU H . 51150 1 210 . 1 . 1 58 58 LEU CA C 13 54.223 0.028 . 1 . . . . . 59 LEU CA . 51150 1 211 . 1 . 1 58 58 LEU CB C 13 44.624 0.061 . 1 . . . . . 59 LEU CB . 51150 1 212 . 1 . 1 58 58 LEU N N 15 123.189 0.161 . 1 . . . . . 59 LEU N . 51150 1 213 . 1 . 1 59 59 ASN H H 1 9.061 0.004 . 1 . . . . . 60 ASN H . 51150 1 214 . 1 . 1 59 59 ASN CA C 13 51.879 0.022 . 1 . . . . . 60 ASN CA . 51150 1 215 . 1 . 1 59 59 ASN CB C 13 38.290 0.001 . 1 . . . . . 60 ASN CB . 51150 1 216 . 1 . 1 59 59 ASN N N 15 126.659 0.065 . 1 . . . . . 60 ASN N . 51150 1 217 . 1 . 1 60 60 ILE H H 1 8.507 0.025 . 1 . . . . . 61 ILE H . 51150 1 218 . 1 . 1 60 60 ILE CA C 13 63.382 0.094 . 1 . . . . . 61 ILE CA . 51150 1 219 . 1 . 1 60 60 ILE CB C 13 37.940 0.011 . 1 . . . . . 61 ILE CB . 51150 1 220 . 1 . 1 60 60 ILE N N 15 122.161 0.202 . 1 . . . . . 61 ILE N . 51150 1 221 . 1 . 1 61 61 ASP H H 1 7.887 0.011 . 1 . . . . . 62 ASP H . 51150 1 222 . 1 . 1 61 61 ASP CA C 13 55.153 0.006 . 1 . . . . . 62 ASP CA . 51150 1 223 . 1 . 1 61 61 ASP CB C 13 42.588 0.049 . 1 . . . . . 62 ASP CB . 51150 1 224 . 1 . 1 61 61 ASP N N 15 119.799 0.103 . 1 . . . . . 62 ASP N . 51150 1 225 . 1 . 1 62 62 GLN H H 1 8.355 0.005 . 1 . . . . . 63 GLN H . 51150 1 226 . 1 . 1 62 62 GLN CA C 13 56.417 0.074 . 1 . . . . . 63 GLN CA . 51150 1 227 . 1 . 1 62 62 GLN CB C 13 30.473 0.011 . 1 . . . . . 63 GLN CB . 51150 1 228 . 1 . 1 62 62 GLN N N 15 121.144 0.054 . 1 . . . . . 63 GLN N . 51150 1 229 . 1 . 1 63 63 ASN H H 1 7.368 0.005 . 1 . . . . . 64 ASN H . 51150 1 230 . 1 . 1 63 63 ASN CA C 13 51.795 0.000 . 1 . . . . . 64 ASN CA . 51150 1 231 . 1 . 1 63 63 ASN CB C 13 41.025 0.000 . 1 . . . . . 64 ASN CB . 51150 1 232 . 1 . 1 63 63 ASN N N 15 116.254 0.048 . 1 . . . . . 64 ASN N . 51150 1 233 . 1 . 1 64 64 PRO CA C 13 63.811 0.015 . 1 . . . . . 65 PRO CA . 51150 1 234 . 1 . 1 64 64 PRO CB C 13 32.893 0.000 . 1 . . . . . 65 PRO CB . 51150 1 235 . 1 . 1 65 65 GLY H H 1 10.257 0.015 . 1 . . . . . 66 GLY H . 51150 1 236 . 1 . 1 65 65 GLY CA C 13 46.306 0.032 . 1 . . . . . 66 GLY CA . 51150 1 237 . 1 . 1 65 65 GLY N N 15 112.540 0.064 . 1 . . . . . 66 GLY N . 51150 1 238 . 1 . 1 66 66 THR H H 1 7.857 0.006 . 1 . . . . . 67 THR H . 51150 1 239 . 1 . 1 66 66 THR CA C 13 68.767 0.034 . 1 . . . . . 67 THR CA . 51150 1 240 . 1 . 1 66 66 THR N N 15 118.878 0.076 . 1 . . . . . 67 THR N . 51150 1 241 . 1 . 1 67 67 ALA H H 1 9.742 0.012 . 1 . . . . . 68 ALA H . 51150 1 242 . 1 . 1 67 67 ALA CA C 13 57.255 0.000 . 1 . . . . . 68 ALA CA . 51150 1 243 . 1 . 1 67 67 ALA CB C 13 15.130 0.000 . 1 . . . . . 68 ALA CB . 51150 1 244 . 1 . 1 67 67 ALA N N 15 124.092 0.056 . 1 . . . . . 68 ALA N . 51150 1 245 . 1 . 1 68 68 PRO CA C 13 65.628 0.030 . 1 . . . . . 69 PRO CA . 51150 1 246 . 1 . 1 68 68 PRO CB C 13 31.000 0.054 . 1 . . . . . 69 PRO CB . 51150 1 247 . 1 . 1 69 69 LYS H H 1 7.358 0.007 . 1 . . . . . 70 LYS H . 51150 1 248 . 1 . 1 69 69 LYS CA C 13 58.855 0.036 . 1 . . . . . 70 LYS CA . 51150 1 249 . 1 . 1 69 69 LYS CB C 13 32.007 0.052 . 1 . . . . . 70 LYS CB . 51150 1 250 . 1 . 1 69 69 LYS N N 15 117.110 0.054 . 1 . . . . . 70 LYS N . 51150 1 251 . 1 . 1 70 70 TYR H H 1 7.297 0.004 . 1 . . . . . 71 TYR H . 51150 1 252 . 1 . 1 70 70 TYR CA C 13 58.384 0.045 . 1 . . . . . 71 TYR CA . 51150 1 253 . 1 . 1 70 70 TYR CB C 13 39.564 0.057 . 1 . . . . . 71 TYR CB . 51150 1 254 . 1 . 1 70 70 TYR N N 15 114.748 0.057 . 1 . . . . . 71 TYR N . 51150 1 255 . 1 . 1 71 71 GLY H H 1 7.497 0.006 . 1 . . . . . 72 GLY H . 51150 1 256 . 1 . 1 71 71 GLY CA C 13 46.696 0.008 . 1 . . . . . 72 GLY CA . 51150 1 257 . 1 . 1 71 71 GLY N N 15 107.999 0.045 . 1 . . . . . 72 GLY N . 51150 1 258 . 1 . 1 72 72 ILE H H 1 7.137 0.013 . 1 . . . . . 73 ILE H . 51150 1 259 . 1 . 1 72 72 ILE CA C 13 61.342 0.048 . 1 . . . . . 73 ILE CA . 51150 1 260 . 1 . 1 72 72 ILE CB C 13 36.533 0.005 . 1 . . . . . 73 ILE CB . 51150 1 261 . 1 . 1 72 72 ILE N N 15 119.343 0.057 . 1 . . . . . 73 ILE N . 51150 1 262 . 1 . 1 73 73 ARG H H 1 8.533 0.014 . 1 . . . . . 74 ARG H . 51150 1 263 . 1 . 1 73 73 ARG CA C 13 55.741 0.036 . 1 . . . . . 74 ARG CA . 51150 1 264 . 1 . 1 73 73 ARG CB C 13 31.324 0.000 . 1 . . . . . 74 ARG CB . 51150 1 265 . 1 . 1 73 73 ARG N N 15 128.272 0.056 . 1 . . . . . 74 ARG N . 51150 1 266 . 1 . 1 74 74 GLY H H 1 7.646 0.003 . 1 . . . . . 75 GLY H . 51150 1 267 . 1 . 1 74 74 GLY CA C 13 44.756 0.001 . 1 . . . . . 75 GLY CA . 51150 1 268 . 1 . 1 74 74 GLY N N 15 108.501 0.071 . 1 . . . . . 75 GLY N . 51150 1 269 . 1 . 1 75 75 ILE H H 1 8.227 0.026 . 1 . . . . . 76 ILE H . 51150 1 270 . 1 . 1 75 75 ILE CA C 13 58.223 0.000 . 1 . . . . . 76 ILE CA . 51150 1 271 . 1 . 1 75 75 ILE CB C 13 40.323 0.000 . 1 . . . . . 76 ILE CB . 51150 1 272 . 1 . 1 75 75 ILE N N 15 113.103 0.115 . 1 . . . . . 76 ILE N . 51150 1 273 . 1 . 1 77 77 THR CA C 13 64.492 0.045 . 1 . . . . . 78 THR CA . 51150 1 274 . 1 . 1 77 77 THR CB C 13 73.346 0.034 . 1 . . . . . 78 THR CB . 51150 1 275 . 1 . 1 78 78 LEU H H 1 9.166 0.017 . 1 . . . . . 79 LEU H . 51150 1 276 . 1 . 1 78 78 LEU CA C 13 53.047 0.046 . 1 . . . . . 79 LEU CA . 51150 1 277 . 1 . 1 78 78 LEU CB C 13 43.771 0.032 . 1 . . . . . 79 LEU CB . 51150 1 278 . 1 . 1 78 78 LEU N N 15 126.367 0.062 . 1 . . . . . 79 LEU N . 51150 1 279 . 1 . 1 79 79 LEU H H 1 9.031 0.017 . 1 . . . . . 80 LEU H . 51150 1 280 . 1 . 1 79 79 LEU CA C 13 53.413 0.001 . 1 . . . . . 80 LEU CA . 51150 1 281 . 1 . 1 79 79 LEU CB C 13 46.244 0.062 . 1 . . . . . 80 LEU CB . 51150 1 282 . 1 . 1 79 79 LEU N N 15 121.505 0.048 . 1 . . . . . 80 LEU N . 51150 1 283 . 1 . 1 80 80 LEU H H 1 8.823 0.006 . 1 . . . . . 81 LEU H . 51150 1 284 . 1 . 1 80 80 LEU CA C 13 53.264 0.085 . 1 . . . . . 81 LEU CA . 51150 1 285 . 1 . 1 80 80 LEU CB C 13 44.589 0.084 . 1 . . . . . 81 LEU CB . 51150 1 286 . 1 . 1 80 80 LEU N N 15 124.973 0.075 . 1 . . . . . 81 LEU N . 51150 1 287 . 1 . 1 81 81 PHE H H 1 9.966 0.004 . 1 . . . . . 82 PHE H . 51150 1 288 . 1 . 1 81 81 PHE CA C 13 57.337 0.018 . 1 . . . . . 82 PHE CA . 51150 1 289 . 1 . 1 81 81 PHE CB C 13 42.187 0.020 . 1 . . . . . 82 PHE CB . 51150 1 290 . 1 . 1 81 81 PHE N N 15 128.291 0.065 . 1 . . . . . 82 PHE N . 51150 1 291 . 1 . 1 82 82 LYS H H 1 8.746 0.006 . 1 . . . . . 83 LYS H . 51150 1 292 . 1 . 1 82 82 LYS CA C 13 56.361 0.015 . 1 . . . . . 83 LYS CA . 51150 1 293 . 1 . 1 82 82 LYS CB C 13 36.304 0.019 . 1 . . . . . 83 LYS CB . 51150 1 294 . 1 . 1 82 82 LYS N N 15 117.027 0.057 . 1 . . . . . 83 LYS N . 51150 1 295 . 1 . 1 83 83 ASN H H 1 9.390 0.006 . 1 . . . . . 84 ASN H . 51150 1 296 . 1 . 1 83 83 ASN CA C 13 54.438 0.031 . 1 . . . . . 84 ASN CA . 51150 1 297 . 1 . 1 83 83 ASN CB C 13 37.577 0.016 . 1 . . . . . 84 ASN CB . 51150 1 298 . 1 . 1 83 83 ASN N N 15 124.061 0.050 . 1 . . . . . 84 ASN N . 51150 1 299 . 1 . 1 84 84 GLY H H 1 9.591 0.005 . 1 . . . . . 85 GLY H . 51150 1 300 . 1 . 1 84 84 GLY CA C 13 46.463 0.032 . 1 . . . . . 85 GLY CA . 51150 1 301 . 1 . 1 84 84 GLY N N 15 104.476 0.050 . 1 . . . . . 85 GLY N . 51150 1 302 . 1 . 1 85 85 GLU H H 1 7.821 0.005 . 1 . . . . . 86 GLU H . 51150 1 303 . 1 . 1 85 85 GLU CA C 13 54.088 0.015 . 1 . . . . . 86 GLU CA . 51150 1 304 . 1 . 1 85 85 GLU CB C 13 33.484 0.003 . 1 . . . . . 86 GLU CB . 51150 1 305 . 1 . 1 85 85 GLU N N 15 118.684 0.063 . 1 . . . . . 86 GLU N . 51150 1 306 . 1 . 1 86 86 VAL H H 1 8.792 0.002 . 1 . . . . . 87 VAL H . 51150 1 307 . 1 . 1 86 86 VAL CA C 13 64.363 0.033 . 1 . . . . . 87 VAL CA . 51150 1 308 . 1 . 1 86 86 VAL CB C 13 31.562 0.076 . 1 . . . . . 87 VAL CB . 51150 1 309 . 1 . 1 86 86 VAL N N 15 122.804 0.053 . 1 . . . . . 87 VAL N . 51150 1 310 . 1 . 1 87 87 ALA H H 1 9.638 0.006 . 1 . . . . . 88 ALA H . 51150 1 311 . 1 . 1 87 87 ALA CA C 13 52.588 0.040 . 1 . . . . . 88 ALA CA . 51150 1 312 . 1 . 1 87 87 ALA CB C 13 20.308 0.063 . 1 . . . . . 88 ALA CB . 51150 1 313 . 1 . 1 87 87 ALA N N 15 133.364 0.079 . 1 . . . . . 88 ALA N . 51150 1 314 . 1 . 1 88 88 ALA H H 1 7.687 0.006 . 1 . . . . . 89 ALA H . 51150 1 315 . 1 . 1 88 88 ALA CA C 13 52.427 0.023 . 1 . . . . . 89 ALA CA . 51150 1 316 . 1 . 1 88 88 ALA CB C 13 22.506 0.038 . 1 . . . . . 89 ALA CB . 51150 1 317 . 1 . 1 88 88 ALA N N 15 117.375 0.049 . 1 . . . . . 89 ALA N . 51150 1 318 . 1 . 1 89 89 THR H H 1 8.498 0.004 . 1 . . . . . 90 THR H . 51150 1 319 . 1 . 1 89 89 THR CA C 13 61.766 0.025 . 1 . . . . . 90 THR CA . 51150 1 320 . 1 . 1 89 89 THR CB C 13 72.167 0.001 . 1 . . . . . 90 THR CB . 51150 1 321 . 1 . 1 89 89 THR N N 15 115.327 0.064 . 1 . . . . . 90 THR N . 51150 1 322 . 1 . 1 90 90 LYS H H 1 9.006 0.004 . 1 . . . . . 91 LYS H . 51150 1 323 . 1 . 1 90 90 LYS CA C 13 54.325 0.021 . 1 . . . . . 91 LYS CA . 51150 1 324 . 1 . 1 90 90 LYS CB C 13 34.475 0.090 . 1 . . . . . 91 LYS CB . 51150 1 325 . 1 . 1 90 90 LYS N N 15 126.236 0.091 . 1 . . . . . 91 LYS N . 51150 1 326 . 1 . 1 91 91 VAL H H 1 8.604 0.016 . 1 . . . . . 92 VAL H . 51150 1 327 . 1 . 1 91 91 VAL CA C 13 61.677 0.000 . 1 . . . . . 92 VAL CA . 51150 1 328 . 1 . 1 91 91 VAL CB C 13 33.963 0.032 . 1 . . . . . 92 VAL CB . 51150 1 329 . 1 . 1 91 91 VAL N N 15 125.751 0.092 . 1 . . . . . 92 VAL N . 51150 1 330 . 1 . 1 92 92 GLY H H 1 8.043 0.017 . 1 . . . . . 93 GLY H . 51150 1 331 . 1 . 1 92 92 GLY CA C 13 43.903 0.015 . 1 . . . . . 93 GLY CA . 51150 1 332 . 1 . 1 92 92 GLY N N 15 113.386 0.259 . 1 . . . . . 93 GLY N . 51150 1 333 . 1 . 1 93 93 ALA H H 1 8.164 0.004 . 1 . . . . . 94 ALA H . 51150 1 334 . 1 . 1 93 93 ALA CA C 13 52.787 0.021 . 1 . . . . . 94 ALA CA . 51150 1 335 . 1 . 1 93 93 ALA CB C 13 19.363 0.000 . 1 . . . . . 94 ALA CB . 51150 1 336 . 1 . 1 93 93 ALA N N 15 118.316 0.087 . 1 . . . . . 94 ALA N . 51150 1 337 . 1 . 1 94 94 LEU H H 1 6.776 0.025 . 1 . . . . . 95 LEU H . 51150 1 338 . 1 . 1 94 94 LEU CA C 13 54.433 0.025 . 1 . . . . . 95 LEU CA . 51150 1 339 . 1 . 1 94 94 LEU CB C 13 44.095 0.023 . 1 . . . . . 95 LEU CB . 51150 1 340 . 1 . 1 94 94 LEU N N 15 119.443 0.154 . 1 . . . . . 95 LEU N . 51150 1 341 . 1 . 1 95 95 SER H H 1 8.362 0.013 . 1 . . . . . 96 SER H . 51150 1 342 . 1 . 1 95 95 SER CA C 13 56.247 0.010 . 1 . . . . . 96 SER CA . 51150 1 343 . 1 . 1 95 95 SER CB C 13 66.083 0.032 . 1 . . . . . 96 SER CB . 51150 1 344 . 1 . 1 95 95 SER N N 15 114.626 0.060 . 1 . . . . . 96 SER N . 51150 1 345 . 1 . 1 96 96 LYS H H 1 9.314 0.003 . 1 . . . . . 97 LYS H . 51150 1 346 . 1 . 1 96 96 LYS CA C 13 60.922 0.005 . 1 . . . . . 97 LYS CA . 51150 1 347 . 1 . 1 96 96 LYS CB C 13 32.312 0.000 . 1 . . . . . 97 LYS CB . 51150 1 348 . 1 . 1 96 96 LYS N N 15 121.622 0.055 . 1 . . . . . 97 LYS N . 51150 1 349 . 1 . 1 97 97 GLY H H 1 8.799 0.003 . 1 . . . . . 98 GLY H . 51150 1 350 . 1 . 1 97 97 GLY CA C 13 47.158 0.018 . 1 . . . . . 98 GLY CA . 51150 1 351 . 1 . 1 97 97 GLY N N 15 105.581 0.040 . 1 . . . . . 98 GLY N . 51150 1 352 . 1 . 1 98 98 GLN H H 1 7.691 0.003 . 1 . . . . . 99 GLN H . 51150 1 353 . 1 . 1 98 98 GLN CA C 13 58.458 0.008 . 1 . . . . . 99 GLN CA . 51150 1 354 . 1 . 1 98 98 GLN CB C 13 29.499 0.004 . 1 . . . . . 99 GLN CB . 51150 1 355 . 1 . 1 98 98 GLN N N 15 120.846 0.037 . 1 . . . . . 99 GLN N . 51150 1 356 . 1 . 1 99 99 LEU H H 1 8.540 0.007 . 1 . . . . . 100 LEU H . 51150 1 357 . 1 . 1 99 99 LEU CA C 13 58.197 0.000 . 1 . . . . . 100 LEU CA . 51150 1 358 . 1 . 1 99 99 LEU CB C 13 41.093 0.000 . 1 . . . . . 100 LEU CB . 51150 1 359 . 1 . 1 99 99 LEU N N 15 123.533 0.043 . 1 . . . . . 100 LEU N . 51150 1 360 . 1 . 1 100 100 LYS H H 1 8.739 0.002 . 1 . . . . . 101 LYS H . 51150 1 361 . 1 . 1 100 100 LYS CA C 13 60.789 0.036 . 1 . . . . . 101 LYS CA . 51150 1 362 . 1 . 1 100 100 LYS CB C 13 31.352 0.033 . 1 . . . . . 101 LYS CB . 51150 1 363 . 1 . 1 100 100 LYS N N 15 119.655 0.052 . 1 . . . . . 101 LYS N . 51150 1 364 . 1 . 1 101 101 GLU H H 1 7.824 0.004 . 1 . . . . . 102 GLU H . 51150 1 365 . 1 . 1 101 101 GLU CA C 13 59.925 0.000 . 1 . . . . . 102 GLU CA . 51150 1 366 . 1 . 1 101 101 GLU CB C 13 29.899 0.021 . 1 . . . . . 102 GLU CB . 51150 1 367 . 1 . 1 101 101 GLU N N 15 117.888 0.042 . 1 . . . . . 102 GLU N . 51150 1 368 . 1 . 1 102 102 PHE H H 1 7.639 0.009 . 1 . . . . . 103 PHE H . 51150 1 369 . 1 . 1 102 102 PHE CA C 13 60.066 0.019 . 1 . . . . . 103 PHE CA . 51150 1 370 . 1 . 1 102 102 PHE CB C 13 39.021 0.036 . 1 . . . . . 103 PHE CB . 51150 1 371 . 1 . 1 102 102 PHE N N 15 120.204 0.060 . 1 . . . . . 103 PHE N . 51150 1 372 . 1 . 1 103 103 LEU H H 1 8.601 0.004 . 1 . . . . . 104 LEU H . 51150 1 373 . 1 . 1 103 103 LEU CA C 13 57.821 0.000 . 1 . . . . . 104 LEU CA . 51150 1 374 . 1 . 1 103 103 LEU CB C 13 41.154 0.019 . 1 . . . . . 104 LEU CB . 51150 1 375 . 1 . 1 103 103 LEU N N 15 121.246 0.039 . 1 . . . . . 104 LEU N . 51150 1 376 . 1 . 1 104 104 ASP H H 1 9.216 0.004 . 1 . . . . . 105 ASP H . 51150 1 377 . 1 . 1 104 104 ASP CA C 13 57.697 0.014 . 1 . . . . . 105 ASP CA . 51150 1 378 . 1 . 1 104 104 ASP CB C 13 39.406 0.018 . 1 . . . . . 105 ASP CB . 51150 1 379 . 1 . 1 104 104 ASP N N 15 120.335 0.055 . 1 . . . . . 105 ASP N . 51150 1 380 . 1 . 1 105 105 ALA H H 1 7.622 0.011 . 1 . . . . . 106 ALA H . 51150 1 381 . 1 . 1 105 105 ALA CA C 13 54.242 0.004 . 1 . . . . . 106 ALA CA . 51150 1 382 . 1 . 1 105 105 ALA CB C 13 18.902 0.009 . 1 . . . . . 106 ALA CB . 51150 1 383 . 1 . 1 105 105 ALA N N 15 118.775 0.051 . 1 . . . . . 106 ALA N . 51150 1 384 . 1 . 1 106 106 ASN H H 1 7.220 0.006 . 1 . . . . . 107 ASN H . 51150 1 385 . 1 . 1 106 106 ASN CA C 13 55.265 0.046 . 1 . . . . . 107 ASN CA . 51150 1 386 . 1 . 1 106 106 ASN CB C 13 41.618 0.032 . 1 . . . . . 107 ASN CB . 51150 1 387 . 1 . 1 106 106 ASN N N 15 113.126 0.051 . 1 . . . . . 107 ASN N . 51150 1 388 . 1 . 1 107 107 LEU H H 1 8.168 0.011 . 1 . . . . . 108 LEU H . 51150 1 389 . 1 . 1 107 107 LEU CA C 13 55.569 0.025 . 1 . . . . . 108 LEU CA . 51150 1 390 . 1 . 1 107 107 LEU CB C 13 42.125 0.077 . 1 . . . . . 108 LEU CB . 51150 1 391 . 1 . 1 107 107 LEU N N 15 120.305 0.042 . 1 . . . . . 108 LEU N . 51150 1 392 . 1 . 1 108 108 ALA H H 1 7.651 0.005 . 1 . . . . . 109 ALA H . 51150 1 393 . 1 . 1 108 108 ALA CA C 13 52.705 0.011 . 1 . . . . . 109 ALA CA . 51150 1 394 . 1 . 1 108 108 ALA CB C 13 18.635 0.012 . 1 . . . . . 109 ALA CB . 51150 1 395 . 1 . 1 108 108 ALA N N 15 121.999 0.056 . 1 . . . . . 109 ALA N . 51150 1 stop_ save_