data_26029 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 26029 _Entry.Title ; Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2016-04-10 _Entry.Accession_date 2016-04-14 _Entry.Last_release_date 2016-10-14 _Entry.Original_release_date 2016-10-14 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _Entry.Original_NMR_STAR_version 3.1.1.99 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _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 Matthias Wittwer . . . . 26029 2 Sonja Dames . A. . . 26029 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'Technical University of Munich, Department of Chemistry, Biomolecular NMR' . 26029 2 'not applicable' 'Institute of Structural Biology, Helmholtz Zentrum Munich' . 26029 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 26029 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 154 26029 '15N chemical shifts' 44 26029 '1H chemical shifts' 44 26029 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 . . 2016-10-14 . original BMRB . 26029 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 26027 ; Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG) ; 26029 BMRB 26028 ; Chemical shift assignment of residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain ; 26029 BMRB 26030 ; Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) ; 26029 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 26029 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 27632081 _Citation.Full_citation . _Citation.Title ; Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biomol. NMR Assign.' _Citation.Journal_name_full . _Citation.Journal_volume 10 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _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 401 _Citation.Page_last 406 _Citation.Year 2016 _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 Matthias Wittwer . . . . 26029 1 2 Sonja Dames . A. . . 26029 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Mycobacterium tuberculosis' 26029 1 'natively disordered protein' 26029 1 'protein kinase G' 26029 1 'redox-sensitive metal binding motif' 26029 1 rubredoxin 26029 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 26029 _Assembly.ID 1 _Assembly.Name 'Protein kinase G (PknG) 74-147 rubredoxin domain oxidized, metal free form' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number 2.7.11.1 _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 'Rubredoxin domain (RD)' 1 $PknG_74-147 A . yes native no no . 'Regulatory metal binding site of a ser/thr kinase' . 26029 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 2PZI . . X-ray 2.7 . 'Crystal structure of PknG 73-750 in complex with the inhibitor AX20017' 26029 1 yes PDB 4Y0X . . X-ray 1.74 . 'Crystal structure of PknG 64-405 in complex with ADP' 26029 1 yes PDB 4Y12 . . X-ray 1.9 . 'Crystal structure of PknG 64-405 in complex with AGS' 26029 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID ; The eukaryotic like serine /threonine protein kinase G promotes cellular survival of pathogenic mycobacteria by inhibiting phagosome-lysosome fusion within host macophages. ; 26029 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PknG_74-147 _Entity.Sf_category entity _Entity.Sf_framecode PknG_74-147 _Entity.Entry_ID 26029 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name PknG_74-147 _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 ; LGGGLVEIPRAPDIDPLEAL MTNPVVPESKRFCWNCGRPV GRSDSETKGASEGWCPYCGS PYSFLPQLNPGDIV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states yes _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 74 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment ; PknG 74-147 (metal free state) ; _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 7949.01 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details 'PknG 74-147 contains the rubredoxin like metal binding site of mycobacterial protein kinase G' _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'metal coordination' 26029 1 stop_ 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 74 LEU . 26029 1 2 75 GLY . 26029 1 3 76 GLY . 26029 1 4 77 GLY . 26029 1 5 78 LEU . 26029 1 6 79 VAL . 26029 1 7 80 GLU . 26029 1 8 81 ILE . 26029 1 9 82 PRO . 26029 1 10 83 ARG . 26029 1 11 84 ALA . 26029 1 12 85 PRO . 26029 1 13 86 ASP . 26029 1 14 87 ILE . 26029 1 15 88 ASP . 26029 1 16 89 PRO . 26029 1 17 90 LEU . 26029 1 18 91 GLU . 26029 1 19 92 ALA . 26029 1 20 93 LEU . 26029 1 21 94 MET . 26029 1 22 95 THR . 26029 1 23 96 ASN . 26029 1 24 97 PRO . 26029 1 25 98 VAL . 26029 1 26 99 VAL . 26029 1 27 100 PRO . 26029 1 28 101 GLU . 26029 1 29 102 SER . 26029 1 30 103 LYS . 26029 1 31 104 ARG . 26029 1 32 105 PHE . 26029 1 33 106 CYS . 26029 1 34 107 TRP . 26029 1 35 108 ASN . 26029 1 36 109 CYS . 26029 1 37 110 GLY . 26029 1 38 111 ARG . 26029 1 39 112 PRO . 26029 1 40 113 VAL . 26029 1 41 114 GLY . 26029 1 42 115 ARG . 26029 1 43 116 SER . 26029 1 44 117 ASP . 26029 1 45 118 SER . 26029 1 46 119 GLU . 26029 1 47 120 THR . 26029 1 48 121 LYS . 26029 1 49 122 GLY . 26029 1 50 123 ALA . 26029 1 51 124 SER . 26029 1 52 125 GLU . 26029 1 53 126 GLY . 26029 1 54 127 TRP . 26029 1 55 128 CYS . 26029 1 56 129 PRO . 26029 1 57 130 TYR . 26029 1 58 131 CYS . 26029 1 59 132 GLY . 26029 1 60 133 SER . 26029 1 61 134 PRO . 26029 1 62 135 TYR . 26029 1 63 136 SER . 26029 1 64 137 PHE . 26029 1 65 138 LEU . 26029 1 66 139 PRO . 26029 1 67 140 GLN . 26029 1 68 141 LEU . 26029 1 69 142 ASN . 26029 1 70 143 PRO . 26029 1 71 144 GLY . 26029 1 72 145 ASP . 26029 1 73 146 ILE . 26029 1 74 147 VAL . 26029 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 . LEU 1 1 26029 1 . GLY 2 2 26029 1 . GLY 3 3 26029 1 . GLY 4 4 26029 1 . LEU 5 5 26029 1 . VAL 6 6 26029 1 . GLU 7 7 26029 1 . ILE 8 8 26029 1 . PRO 9 9 26029 1 . ARG 10 10 26029 1 . ALA 11 11 26029 1 . PRO 12 12 26029 1 . ASP 13 13 26029 1 . ILE 14 14 26029 1 . ASP 15 15 26029 1 . PRO 16 16 26029 1 . LEU 17 17 26029 1 . GLU 18 18 26029 1 . ALA 19 19 26029 1 . LEU 20 20 26029 1 . MET 21 21 26029 1 . THR 22 22 26029 1 . ASN 23 23 26029 1 . PRO 24 24 26029 1 . VAL 25 25 26029 1 . VAL 26 26 26029 1 . PRO 27 27 26029 1 . GLU 28 28 26029 1 . SER 29 29 26029 1 . LYS 30 30 26029 1 . ARG 31 31 26029 1 . PHE 32 32 26029 1 . CYS 33 33 26029 1 . TRP 34 34 26029 1 . ASN 35 35 26029 1 . CYS 36 36 26029 1 . GLY 37 37 26029 1 . ARG 38 38 26029 1 . PRO 39 39 26029 1 . VAL 40 40 26029 1 . GLY 41 41 26029 1 . ARG 42 42 26029 1 . SER 43 43 26029 1 . ASP 44 44 26029 1 . SER 45 45 26029 1 . GLU 46 46 26029 1 . THR 47 47 26029 1 . LYS 48 48 26029 1 . GLY 49 49 26029 1 . ALA 50 50 26029 1 . SER 51 51 26029 1 . GLU 52 52 26029 1 . GLY 53 53 26029 1 . TRP 54 54 26029 1 . CYS 55 55 26029 1 . PRO 56 56 26029 1 . TYR 57 57 26029 1 . CYS 58 58 26029 1 . GLY 59 59 26029 1 . SER 60 60 26029 1 . PRO 61 61 26029 1 . TYR 62 62 26029 1 . SER 63 63 26029 1 . PHE 64 64 26029 1 . LEU 65 65 26029 1 . PRO 66 66 26029 1 . GLN 67 67 26029 1 . LEU 68 68 26029 1 . ASN 69 69 26029 1 . PRO 70 70 26029 1 . GLY 71 71 26029 1 . ASP 72 72 26029 1 . ILE 73 73 26029 1 . VAL 74 74 26029 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 26029 _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 $PknG_74-147 . 83332 organism . 'Mycobacterium tuberculosis' 'Mycobacterium tuberculosis' . . Bacteria . Mycobacterium tuberculosis H37Rv . . . . . . . . . . 'pknG Rv0410c MTCY22G10.06c' . 26029 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 26029 _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 $PknG_74-147 . 'recombinant technology' 'Escherichia coli' . . 469008 Escherichia coli 'BL21 (DE3)' . . . . . pET15b . . . 26029 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 26029 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'PknG 74-147 in metal free state (oxidized)' _Sample.Aggregate_sample_number . _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 'PknG 74-147' '[U-13C; U-15N]' . . 1 $PknG_74-147 . protein . 0.4 0.8 mM . . . . 26029 1 2 TRIS-HCL 'natural abundance' . . . . . buffer 20 . . mM . . . . 26029 1 3 'sodium chloride' 'natural abundance' . . . . . salt 150 . . mM . . . . 26029 1 4 H2O 'natural abundance' . . . . . solvent 95 . . % . . . . 26029 1 5 D2O [U-2H] . . . . . solvent 5 . . % . . . . 26029 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 26029 _Sample_condition_list.ID 1 _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' 150 . mM 26029 1 pH 7.5 . pH 26029 1 pressure 1 . atm 26029 1 temperature 298 . K 26029 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 26029 _Software.ID 1 _Software.Name NMRView _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Johnson, One Moon Scientific' . . 26029 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 26029 1 'peak picking' 26029 1 stop_ save_ save_NMRDraw _Software.Sf_category software _Software.Sf_framecode NMRDraw _Software.Entry_ID 26029 _Software.ID 2 _Software.Name NMRDraw _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 26029 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 26029 2 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 26029 _Software.ID 3 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 26029 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 26029 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 26029 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 26029 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 26029 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 26029 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 500 . . . 26029 1 2 spectrometer_2 Bruker Avance . 600 . . . 26029 1 3 spectrometer_3 Bruker Avance . 900 . . . 26029 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 26029 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_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.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 3 $spectrometer_3 . . . . . . . . . . . . . . . . 26029 1 2 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 26029 1 3 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 26029 1 4 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 26029 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 26029 _Chem_shift_reference.ID 1 _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 water protons . . . . ppm 4.773 na indirect 0.251449530 . . . . . 26029 1 H 1 water protons . . . . ppm 4.773 internal direct 1.000000000 . . . . . 26029 1 N 15 water protons . . . . ppm 4.773 na indirect 0.101329118 . . . . . 26029 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_PknG74-147_metal_free _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode PknG74-147_metal_free _Assigned_chem_shift_list.Entry_ID 26029 _Assigned_chem_shift_list.ID 1 _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 $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.02 _Assigned_chem_shift_list.Chem_shift_13C_err 0.15 _Assigned_chem_shift_list.Chem_shift_15N_err 0.1 _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' 1 $sample_1 isotropic 26029 1 2 '3D HNCA' 1 $sample_1 isotropic 26029 1 3 '3D HNCACB' 1 $sample_1 isotropic 26029 1 4 '3D C(CO)NH' 1 $sample_1 isotropic 26029 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 1 $NMRView . . 26029 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_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.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 4 4 GLY H H 1 8.325 0.02 . 1 . . . . 77 GLY HN . 26029 1 2 . 1 1 4 4 GLY CA C 13 45.183 0.15 . 1 . . . . 77 GLY CA . 26029 1 3 . 1 1 4 4 GLY N N 15 108.642 0.1 . 1 . . . . 77 GLY N . 26029 1 4 . 1 1 5 5 LEU H H 1 8.106 0.02 . 1 . . . . 78 LEU HN . 26029 1 5 . 1 1 5 5 LEU CA C 13 55.277 0.15 . 1 . . . . 78 LEU CA . 26029 1 6 . 1 1 5 5 LEU CB C 13 42.444 0.15 . 1 . . . . 78 LEU CB . 26029 1 7 . 1 1 5 5 LEU CD1 C 13 24.919 0.15 . 2 . . . . 78 LEU CD1 . 26029 1 8 . 1 1 5 5 LEU CD2 C 13 23.639 0.15 . 2 . . . . 78 LEU CD2 . 26029 1 9 . 1 1 5 5 LEU CG C 13 27.059 0.15 . 1 . . . . 78 LEU CG . 26029 1 10 . 1 1 5 5 LEU N N 15 121.655 0.1 . 1 . . . . 78 LEU N . 26029 1 11 . 1 1 6 6 VAL H H 1 8.091 0.02 . 1 . . . . 79 VAL HN . 26029 1 12 . 1 1 6 6 VAL CA C 13 62.143 0.15 . 1 . . . . 79 VAL CA . 26029 1 13 . 1 1 6 6 VAL CB C 13 32.901 0.15 . 1 . . . . 79 VAL CB . 26029 1 14 . 1 1 6 6 VAL CG1 C 13 20.908 0.15 . 2 . . . . 79 VAL CG1 . 26029 1 15 . 1 1 6 6 VAL N N 15 121.114 0.1 . 1 . . . . 79 VAL N . 26029 1 16 . 1 1 7 7 GLU H H 1 8.397 0.02 . 1 . . . . 80 GLU HN . 26029 1 17 . 1 1 7 7 GLU CA C 13 56.162 0.15 . 1 . . . . 80 GLU CA . 26029 1 18 . 1 1 7 7 GLU CB C 13 30.649 0.15 . 1 . . . . 80 GLU CB . 26029 1 19 . 1 1 7 7 GLU CG C 13 36.302 0.15 . 1 . . . . 80 GLU CG . 26029 1 20 . 1 1 7 7 GLU N N 15 125.112 0.1 . 1 . . . . 80 GLU N . 26029 1 21 . 1 1 8 8 ILE H H 1 8.252 0.02 . 1 . . . . 81 ILE HN . 26029 1 22 . 1 1 8 8 ILE CA C 13 58.595 0.15 . 1 . . . . 81 ILE CA . 26029 1 23 . 1 1 8 8 ILE CB C 13 38.631 0.15 . 1 . . . . 81 ILE CB . 26029 1 24 . 1 1 8 8 ILE N N 15 124.510 0.1 . 1 . . . . 81 ILE N . 26029 1 25 . 1 1 9 9 PRO CA C 13 63.155 0.15 . 1 . . . . 82 PRO CA . 26029 1 26 . 1 1 9 9 PRO CB C 13 32.182 0.15 . 1 . . . . 82 PRO CB . 26029 1 27 . 1 1 9 9 PRO CD C 13 51.168 0.15 . 1 . . . . 82 PRO CD . 26029 1 28 . 1 1 9 9 PRO CG C 13 27.399 0.15 . 1 . . . . 82 PRO CG . 26029 1 29 . 1 1 10 10 ARG H H 1 8.348 0.02 . 1 . . . . 83 ARG HN . 26029 1 30 . 1 1 10 10 ARG CA C 13 55.710 0.15 . 1 . . . . 83 ARG CA . 26029 1 31 . 1 1 10 10 ARG CB C 13 31.235 0.15 . 1 . . . . 83 ARG CB . 26029 1 32 . 1 1 10 10 ARG CD C 13 43.468 0.15 . 1 . . . . 83 ARG CD . 26029 1 33 . 1 1 10 10 ARG CG C 13 27.070 0.15 . 1 . . . . 83 ARG CG . 26029 1 34 . 1 1 10 10 ARG N N 15 121.793 0.1 . 1 . . . . 83 ARG N . 26029 1 35 . 1 1 11 11 ALA H H 1 8.409 0.02 . 1 . . . . 84 ALA HN . 26029 1 36 . 1 1 11 11 ALA CA C 13 50.609 0.15 . 1 . . . . 84 ALA CA . 26029 1 37 . 1 1 11 11 ALA CB C 13 18.127 0.15 . 1 . . . . 84 ALA CB . 26029 1 38 . 1 1 11 11 ALA N N 15 127.421 0.1 . 1 . . . . 84 ALA N . 26029 1 39 . 1 1 12 12 PRO CA C 13 63.152 0.15 . 1 . . . . 85 PRO CA . 26029 1 40 . 1 1 12 12 PRO CB C 13 32.061 0.15 . 1 . . . . 85 PRO CB . 26029 1 41 . 1 1 12 12 PRO CD C 13 50.551 0.15 . 1 . . . . 85 PRO CD . 26029 1 42 . 1 1 12 12 PRO CG C 13 27.337 0.15 . 1 . . . . 85 PRO CG . 26029 1 43 . 1 1 13 13 ASP H H 1 8.354 0.02 . 1 . . . . 86 ASP HN . 26029 1 44 . 1 1 13 13 ASP CA C 13 54.463 0.15 . 1 . . . . 86 ASP CA . 26029 1 45 . 1 1 13 13 ASP CB C 13 41.065 0.15 . 1 . . . . 86 ASP CB . 26029 1 46 . 1 1 13 13 ASP N N 15 119.921 0.1 . 1 . . . . 86 ASP N . 26029 1 47 . 1 1 14 14 ILE H H 1 7.912 0.02 . 1 . . . . 87 ILE HN . 26029 1 48 . 1 1 14 14 ILE CA C 13 60.552 0.15 . 1 . . . . 87 ILE CA . 26029 1 49 . 1 1 14 14 ILE CB C 13 39.297 0.15 . 1 . . . . 87 ILE CB . 26029 1 50 . 1 1 14 14 ILE CD1 C 13 12.947 0.15 . 1 . . . . 87 ILE CD1 . 26029 1 51 . 1 1 14 14 ILE CG1 C 13 27.188 0.15 . 1 . . . . 87 ILE CG1 . 26029 1 52 . 1 1 14 14 ILE CG2 C 13 17.404 0.15 . 1 . . . . 87 ILE CG2 . 26029 1 53 . 1 1 14 14 ILE N N 15 120.082 0.1 . 1 . . . . 87 ILE N . 26029 1 54 . 1 1 15 15 ASP H H 1 8.524 0.02 . 1 . . . . 88 ASP HN . 26029 1 55 . 1 1 15 15 ASP CA C 13 52.142 0.15 . 1 . . . . 88 ASP CA . 26029 1 56 . 1 1 15 15 ASP CB C 13 41.677 0.15 . 1 . . . . 88 ASP CB . 26029 1 57 . 1 1 15 15 ASP N N 15 126.809 0.1 . 1 . . . . 88 ASP N . 26029 1 58 . 1 1 16 16 PRO CA C 13 63.984 0.15 . 1 . . . . 89 PRO CA . 26029 1 59 . 1 1 16 16 PRO CB C 13 32.227 0.15 . 1 . . . . 89 PRO CB . 26029 1 60 . 1 1 16 16 PRO CD C 13 51.042 0.15 . 1 . . . . 89 PRO CD . 26029 1 61 . 1 1 16 16 PRO CG C 13 27.324 0.15 . 1 . . . . 89 PRO CG . 26029 1 62 . 1 1 17 17 LEU H H 1 8.335 0.02 . 1 . . . . 90 LEU HN . 26029 1 63 . 1 1 17 17 LEU CA C 13 56.014 0.15 . 1 . . . . 90 LEU CA . 26029 1 64 . 1 1 17 17 LEU CB C 13 41.541 0.15 . 1 . . . . 90 LEU CB . 26029 1 65 . 1 1 17 17 LEU CD1 C 13 24.976 0.15 . 2 . . . . 90 LEU CD1 . 26029 1 66 . 1 1 17 17 LEU CD2 C 13 23.286 0.15 . 2 . . . . 90 LEU CD2 . 26029 1 67 . 1 1 17 17 LEU CG C 13 27.180 0.15 . 1 . . . . 90 LEU CG . 26029 1 68 . 1 1 17 17 LEU N N 15 119.601 0.1 . 1 . . . . 90 LEU N . 26029 1 69 . 1 1 18 18 GLU H H 1 7.959 0.02 . 1 . . . . 91 GLU HN . 26029 1 70 . 1 1 18 18 GLU CA C 13 55.353 0.15 . 1 . . . . 91 GLU CA . 26029 1 71 . 1 1 18 18 GLU CB C 13 29.933 0.15 . 1 . . . . 91 GLU CB . 26029 1 72 . 1 1 18 18 GLU CG C 13 36.396 0.15 . 1 . . . . 91 GLU CG . 26029 1 73 . 1 1 18 18 GLU N N 15 120.363 0.1 . 1 . . . . 91 GLU N . 26029 1 74 . 1 1 19 19 ALA H H 1 8.044 0.02 . 1 . . . . 92 ALA HN . 26029 1 75 . 1 1 19 19 ALA CA C 13 53.129 0.15 . 1 . . . . 92 ALA CA . 26029 1 76 . 1 1 19 19 ALA CB C 13 18.862 0.15 . 1 . . . . 92 ALA CB . 26029 1 77 . 1 1 19 19 ALA N N 15 123.053 0.1 . 1 . . . . 92 ALA N . 26029 1 78 . 1 1 20 20 LEU H H 1 7.860 0.02 . 1 . . . . 93 LEU HN . 26029 1 79 . 1 1 20 20 LEU CA C 13 55.638 0.15 . 1 . . . . 93 LEU CA . 26029 1 80 . 1 1 20 20 LEU CB C 13 42.299 0.15 . 1 . . . . 93 LEU CB . 26029 1 81 . 1 1 20 20 LEU CD1 C 13 25.020 0.15 . 2 . . . . 93 LEU CD1 . 26029 1 82 . 1 1 20 20 LEU CD2 C 13 23.539 0.15 . 2 . . . . 93 LEU CD2 . 26029 1 83 . 1 1 20 20 LEU CG C 13 26.964 0.15 . 1 . . . . 93 LEU CG . 26029 1 84 . 1 1 20 20 LEU N N 15 119.359 0.1 . 1 . . . . 93 LEU N . 26029 1 85 . 1 1 21 21 MET H H 1 8.094 0.02 . 1 . . . . 94 MET HN . 26029 1 86 . 1 1 21 21 MET CA C 13 55.744 0.15 . 1 . . . . 94 MET CA . 26029 1 87 . 1 1 21 21 MET CB C 13 32.734 0.15 . 1 . . . . 94 MET CB . 26029 1 88 . 1 1 21 21 MET CG C 13 32.169 0.15 . 1 . . . . 94 MET CG . 26029 1 89 . 1 1 21 21 MET N N 15 119.462 0.1 . 1 . . . . 94 MET N . 26029 1 90 . 1 1 22 22 THR H H 1 7.956 0.02 . 1 . . . . 95 THR HN . 26029 1 91 . 1 1 22 22 THR CA C 13 61.983 0.15 . 1 . . . . 95 THR CA . 26029 1 92 . 1 1 22 22 THR CB C 13 69.877 0.15 . 1 . . . . 95 THR CB . 26029 1 93 . 1 1 22 22 THR N N 15 113.911 0.1 . 1 . . . . 95 THR N . 26029 1 94 . 1 1 24 24 PRO CA C 13 63.115 0.15 . 1 . . . . 97 PRO CA . 26029 1 95 . 1 1 24 24 PRO CB C 13 32.146 0.15 . 1 . . . . 97 PRO CB . 26029 1 96 . 1 1 24 24 PRO CD C 13 50.692 0.15 . 1 . . . . 97 PRO CD . 26029 1 97 . 1 1 24 24 PRO CG C 13 27.280 0.15 . 1 . . . . 97 PRO CG . 26029 1 98 . 1 1 25 25 VAL H H 1 8.154 0.02 . 1 . . . . 98 VAL HN . 26029 1 99 . 1 1 25 25 VAL CA C 13 62.525 0.15 . 1 . . . . 98 VAL CA . 26029 1 100 . 1 1 25 25 VAL CB C 13 32.366 0.15 . 1 . . . . 98 VAL CB . 26029 1 101 . 1 1 25 25 VAL CG2 C 13 21.052 0.15 . 2 . . . . 98 VAL CG2 . 26029 1 102 . 1 1 25 25 VAL N N 15 120.305 0.1 . 1 . . . . 98 VAL N . 26029 1 103 . 1 1 26 26 VAL H H 1 8.163 0.02 . 1 . . . . 99 VAL HN . 26029 1 104 . 1 1 26 26 VAL CA C 13 59.731 0.15 . 1 . . . . 99 VAL CA . 26029 1 105 . 1 1 26 26 VAL CB C 13 32.621 0.15 . 1 . . . . 99 VAL CB . 26029 1 106 . 1 1 26 26 VAL N N 15 125.600 0.1 . 1 . . . . 99 VAL N . 26029 1 107 . 1 1 27 27 PRO CA C 13 63.324 0.15 . 1 . . . . 100 PRO CA . 26029 1 108 . 1 1 27 27 PRO CB C 13 32.178 0.15 . 1 . . . . 100 PRO CB . 26029 1 109 . 1 1 27 27 PRO CD C 13 51.137 0.15 . 1 . . . . 100 PRO CD . 26029 1 110 . 1 1 27 27 PRO CG C 13 27.428 0.15 . 1 . . . . 100 PRO CG . 26029 1 111 . 1 1 28 28 GLU H H 1 8.606 0.02 . 1 . . . . 101 GLU HN . 26029 1 112 . 1 1 28 28 GLU CA C 13 57.629 0.15 . 1 . . . . 101 GLU CA . 26029 1 113 . 1 1 28 28 GLU CB C 13 29.961 0.15 . 1 . . . . 101 GLU CB . 26029 1 114 . 1 1 28 28 GLU CG C 13 36.441 0.15 . 1 . . . . 101 GLU CG . 26029 1 115 . 1 1 28 28 GLU N N 15 121.166 0.1 . 1 . . . . 101 GLU N . 26029 1 116 . 1 1 29 29 SER H H 1 8.273 0.02 . 1 . . . . 102 SER HN . 26029 1 117 . 1 1 29 29 SER CA C 13 59.027 0.15 . 1 . . . . 102 SER CA . 26029 1 118 . 1 1 29 29 SER CB C 13 63.687 0.15 . 1 . . . . 102 SER CB . 26029 1 119 . 1 1 29 29 SER N N 15 115.618 0.1 . 1 . . . . 102 SER N . 26029 1 120 . 1 1 40 40 VAL CA C 13 62.472 0.15 . 1 . . . . 113 VAL CA . 26029 1 121 . 1 1 40 40 VAL CB C 13 32.949 0.15 . 1 . . . . 113 VAL CB . 26029 1 122 . 1 1 40 40 VAL CG1 C 13 20.769 0.15 . 2 . . . . 113 VAL CG1 . 26029 1 123 . 1 1 41 41 GLY H H 1 8.429 0.02 . 1 . . . . 114 GLY HN . 26029 1 124 . 1 1 41 41 GLY CA C 13 45.325 0.15 . 1 . . . . 114 GLY CA . 26029 1 125 . 1 1 41 41 GLY N N 15 112.178 0.1 . 1 . . . . 114 GLY N . 26029 1 126 . 1 1 42 42 ARG H H 1 7.794 0.02 . 1 . . . . 115 ARG HN . 26029 1 127 . 1 1 42 42 ARG CA C 13 57.172 0.15 . 1 . . . . 115 ARG CA . 26029 1 128 . 1 1 42 42 ARG CB C 13 31.551 0.15 . 1 . . . . 115 ARG CB . 26029 1 129 . 1 1 42 42 ARG N N 15 125.464 0.1 . 1 . . . . 115 ARG N . 26029 1 130 . 1 1 45 45 SER CA C 13 58.662 0.15 . 1 . . . . 118 SER CA . 26029 1 131 . 1 1 45 45 SER CB C 13 63.876 0.15 . 1 . . . . 118 SER CB . 26029 1 132 . 1 1 46 46 GLU H H 1 8.324 0.02 . 1 . . . . 119 GLU HN . 26029 1 133 . 1 1 46 46 GLU CA C 13 57.021 0.15 . 1 . . . . 119 GLU CA . 26029 1 134 . 1 1 46 46 GLU CB C 13 30.244 0.15 . 1 . . . . 119 GLU CB . 26029 1 135 . 1 1 46 46 GLU CG C 13 36.517 0.15 . 1 . . . . 119 GLU CG . 26029 1 136 . 1 1 46 46 GLU N N 15 122.107 0.1 . 1 . . . . 119 GLU N . 26029 1 137 . 1 1 47 47 THR H H 1 8.100 0.02 . 1 . . . . 120 THR HN . 26029 1 138 . 1 1 47 47 THR CA C 13 62.262 0.15 . 1 . . . . 120 THR CA . 26029 1 139 . 1 1 47 47 THR CB C 13 69.731 0.15 . 1 . . . . 120 THR CB . 26029 1 140 . 1 1 47 47 THR CG2 C 13 21.735 0.15 . 1 . . . . 120 THR CG2 . 26029 1 141 . 1 1 47 47 THR N N 15 114.728 0.1 . 1 . . . . 120 THR N . 26029 1 142 . 1 1 48 48 LYS H H 1 8.281 0.02 . 1 . . . . 121 LYS HN . 26029 1 143 . 1 1 48 48 LYS CA C 13 56.703 0.15 . 1 . . . . 121 LYS CA . 26029 1 144 . 1 1 48 48 LYS CB C 13 32.766 0.15 . 1 . . . . 121 LYS CB . 26029 1 145 . 1 1 48 48 LYS CD C 13 29.081 0.15 . 1 . . . . 121 LYS CD . 26029 1 146 . 1 1 48 48 LYS CE C 13 42.235 0.15 . 1 . . . . 121 LYS CE . 26029 1 147 . 1 1 48 48 LYS CG C 13 24.786 0.15 . 1 . . . . 121 LYS CG . 26029 1 148 . 1 1 48 48 LYS N N 15 123.763 0.1 . 1 . . . . 121 LYS N . 26029 1 149 . 1 1 49 49 GLY H H 1 8.356 0.02 . 1 . . . . 122 GLY HN . 26029 1 150 . 1 1 49 49 GLY CA C 13 45.305 0.15 . 1 . . . . 122 GLY CA . 26029 1 151 . 1 1 49 49 GLY N N 15 109.803 0.1 . 1 . . . . 122 GLY N . 26029 1 152 . 1 1 50 50 ALA H H 1 8.139 0.02 . 1 . . . . 123 ALA HN . 26029 1 153 . 1 1 50 50 ALA CA C 13 52.871 0.15 . 1 . . . . 123 ALA CA . 26029 1 154 . 1 1 50 50 ALA CB C 13 19.268 0.15 . 1 . . . . 123 ALA CB . 26029 1 155 . 1 1 50 50 ALA N N 15 123.652 0.1 . 1 . . . . 123 ALA N . 26029 1 156 . 1 1 51 51 SER H H 1 8.269 0.02 . 1 . . . . 124 SER HN . 26029 1 157 . 1 1 51 51 SER CA C 13 58.620 0.15 . 1 . . . . 124 SER CA . 26029 1 158 . 1 1 51 51 SER CB C 13 63.790 0.15 . 1 . . . . 124 SER CB . 26029 1 159 . 1 1 51 51 SER N N 15 114.606 0.1 . 1 . . . . 124 SER N . 26029 1 160 . 1 1 52 52 GLU CA C 13 56.946 0.15 . 1 . . . . 125 GLU CA . 26029 1 161 . 1 1 52 52 GLU CB C 13 30.189 0.15 . 1 . . . . 125 GLU CB . 26029 1 162 . 1 1 52 52 GLU CG C 13 36.397 0.15 . 1 . . . . 125 GLU CG . 26029 1 163 . 1 1 53 53 GLY H H 1 8.315 0.02 . 1 . . . . 126 GLY HN . 26029 1 164 . 1 1 53 53 GLY CA C 13 45.311 0.15 . 1 . . . . 126 GLY CA . 26029 1 165 . 1 1 53 53 GLY N N 15 109.248 0.1 . 1 . . . . 126 GLY N . 26029 1 166 . 1 1 54 54 TRP H H 1 8.178 0.02 . 1 . . . . 127 TRP HN . 26029 1 167 . 1 1 54 54 TRP CA C 13 57.618 0.15 . 1 . . . . 127 TRP CA . 26029 1 168 . 1 1 54 54 TRP CB C 13 29.572 0.15 . 1 . . . . 127 TRP CB . 26029 1 169 . 1 1 54 54 TRP N N 15 120.303 0.1 . 1 . . . . 127 TRP N . 26029 1 170 . 1 1 55 55 CYS H H 1 7.883 0.02 . 1 . . . . 128 CYS HN . 26029 1 171 . 1 1 55 55 CYS CA C 13 56.055 0.15 . 1 . . . . 128 CYS CA . 26029 1 172 . 1 1 55 55 CYS CB C 13 28.667 0.15 . 1 . . . . 128 CYS CB . 26029 1 173 . 1 1 55 55 CYS N N 15 124.744 0.1 . 1 . . . . 128 CYS N . 26029 1 174 . 1 1 56 56 PRO CA C 13 63.551 0.15 . 1 . . . . 129 PRO CA . 26029 1 175 . 1 1 57 57 TYR H H 1 7.914 0.02 . 1 . . . . 130 TYR HN . 26029 1 176 . 1 1 57 57 TYR CA C 13 57.766 0.15 . 1 . . . . 130 TYR CA . 26029 1 177 . 1 1 57 57 TYR N N 15 118.933 0.1 . 1 . . . . 130 TYR N . 26029 1 178 . 1 1 59 59 GLY CA C 13 45.386 0.15 . 1 . . . . 132 GLY CA . 26029 1 179 . 1 1 60 60 SER H H 1 8.035 0.02 . 1 . . . . 133 SER HN . 26029 1 180 . 1 1 60 60 SER N N 15 116.203 0.1 . 1 . . . . 133 SER N . 26029 1 181 . 1 1 61 61 PRO CA C 13 63.577 0.15 . 1 . . . . 134 PRO CA . 26029 1 182 . 1 1 61 61 PRO CB C 13 31.722 0.15 . 1 . . . . 134 PRO CB . 26029 1 183 . 1 1 61 61 PRO CD C 13 50.771 0.15 . 1 . . . . 134 PRO CD . 26029 1 184 . 1 1 61 61 PRO CG C 13 27.070 0.15 . 1 . . . . 134 PRO CG . 26029 1 185 . 1 1 62 62 TYR H H 1 7.883 0.02 . 1 . . . . 135 TYR HN . 26029 1 186 . 1 1 62 62 TYR CA C 13 57.680 0.15 . 1 . . . . 135 TYR CA . 26029 1 187 . 1 1 62 62 TYR CB C 13 38.876 0.15 . 1 . . . . 135 TYR CB . 26029 1 188 . 1 1 62 62 TYR N N 15 118.743 0.1 . 1 . . . . 135 TYR N . 26029 1 189 . 1 1 63 63 SER H H 1 7.901 0.02 . 1 . . . . 136 SER HN . 26029 1 190 . 1 1 63 63 SER CA C 13 58.322 0.15 . 1 . . . . 136 SER CA . 26029 1 191 . 1 1 63 63 SER CB C 13 64.120 0.15 . 1 . . . . 136 SER CB . 26029 1 192 . 1 1 63 63 SER N N 15 116.214 0.1 . 1 . . . . 136 SER N . 26029 1 193 . 1 1 64 64 PHE H H 1 7.938 0.02 . 1 . . . . 137 PHE HN . 26029 1 194 . 1 1 64 64 PHE CA C 13 57.492 0.15 . 1 . . . . 137 PHE CA . 26029 1 195 . 1 1 64 64 PHE CB C 13 39.653 0.15 . 1 . . . . 137 PHE CB . 26029 1 196 . 1 1 64 64 PHE N N 15 121.341 0.1 . 1 . . . . 137 PHE N . 26029 1 197 . 1 1 65 65 LEU H H 1 7.964 0.02 . 1 . . . . 138 LEU HN . 26029 1 198 . 1 1 65 65 LEU CA C 13 52.820 0.15 . 1 . . . . 138 LEU CA . 26029 1 199 . 1 1 65 65 LEU CB C 13 42.049 0.15 . 1 . . . . 138 LEU CB . 26029 1 200 . 1 1 65 65 LEU N N 15 124.629 0.1 . 1 . . . . 138 LEU N . 26029 1 201 . 1 1 66 66 PRO CA C 13 63.138 0.15 . 1 . . . . 139 PRO CA . 26029 1 202 . 1 1 66 66 PRO CB C 13 32.061 0.15 . 1 . . . . 139 PRO CB . 26029 1 203 . 1 1 66 66 PRO CD C 13 50.541 0.15 . 1 . . . . 139 PRO CD . 26029 1 204 . 1 1 66 66 PRO CG C 13 27.337 0.15 . 1 . . . . 139 PRO CG . 26029 1 205 . 1 1 67 67 GLN H H 1 8.389 0.02 . 1 . . . . 140 GLN HN . 26029 1 206 . 1 1 67 67 GLN CA C 13 55.576 0.15 . 1 . . . . 140 GLN CA . 26029 1 207 . 1 1 67 67 GLN CB C 13 29.466 0.15 . 1 . . . . 140 GLN CB . 26029 1 208 . 1 1 67 67 GLN CG C 13 33.880 0.15 . 1 . . . . 140 GLN CG . 26029 1 209 . 1 1 67 67 GLN N N 15 120.517 0.1 . 1 . . . . 140 GLN N . 26029 1 210 . 1 1 68 68 LEU H H 1 8.199 0.02 . 1 . . . . 141 LEU HN . 26029 1 211 . 1 1 68 68 LEU CA C 13 55.026 0.15 . 1 . . . . 141 LEU CA . 26029 1 212 . 1 1 68 68 LEU CB C 13 42.635 0.15 . 1 . . . . 141 LEU CB . 26029 1 213 . 1 1 68 68 LEU CD1 C 13 24.988 0.15 . 2 . . . . 141 LEU CD1 . 26029 1 214 . 1 1 68 68 LEU CD2 C 13 23.568 0.15 . 2 . . . . 141 LEU CD2 . 26029 1 215 . 1 1 68 68 LEU CG C 13 27.064 0.15 . 1 . . . . 141 LEU CG . 26029 1 216 . 1 1 68 68 LEU N N 15 123.542 0.1 . 1 . . . . 141 LEU N . 26029 1 217 . 1 1 69 69 ASN H H 1 8.572 0.02 . 1 . . . . 142 ASN HN . 26029 1 218 . 1 1 69 69 ASN CA C 13 51.208 0.15 . 1 . . . . 142 ASN CA . 26029 1 219 . 1 1 69 69 ASN CB C 13 38.937 0.15 . 1 . . . . 142 ASN CB . 26029 1 220 . 1 1 69 69 ASN N N 15 120.730 0.1 . 1 . . . . 142 ASN N . 26029 1 221 . 1 1 70 70 PRO CA C 13 64.086 0.15 . 1 . . . . 143 PRO CA . 26029 1 222 . 1 1 70 70 PRO CB C 13 31.909 0.15 . 1 . . . . 143 PRO CB . 26029 1 223 . 1 1 70 70 PRO CD C 13 50.758 0.15 . 1 . . . . 143 PRO CD . 26029 1 224 . 1 1 70 70 PRO CG C 13 27.345 0.15 . 1 . . . . 143 PRO CG . 26029 1 225 . 1 1 71 71 GLY H H 1 8.386 0.02 . 1 . . . . 144 GLY HN . 26029 1 226 . 1 1 71 71 GLY CA C 13 45.290 0.15 . 1 . . . . 144 GLY CA . 26029 1 227 . 1 1 71 71 GLY N N 15 108.124 0.1 . 1 . . . . 144 GLY N . 26029 1 228 . 1 1 72 72 ASP H H 1 8.029 0.02 . 1 . . . . 145 ASP HN . 26029 1 229 . 1 1 72 72 ASP CA C 13 54.599 0.15 . 1 . . . . 145 ASP CA . 26029 1 230 . 1 1 72 72 ASP CB C 13 41.337 0.15 . 1 . . . . 145 ASP CB . 26029 1 231 . 1 1 72 72 ASP N N 15 120.203 0.1 . 1 . . . . 145 ASP N . 26029 1 232 . 1 1 73 73 ILE H H 1 7.983 0.02 . 1 . . . . 146 ILE HN . 26029 1 233 . 1 1 73 73 ILE CA C 13 61.359 0.15 . 1 . . . . 146 ILE CA . 26029 1 234 . 1 1 73 73 ILE CB C 13 38.667 0.15 . 1 . . . . 146 ILE CB . 26029 1 235 . 1 1 73 73 ILE CD1 C 13 12.824 0.15 . 1 . . . . 146 ILE CD1 . 26029 1 236 . 1 1 73 73 ILE CG1 C 13 27.157 0.15 . 1 . . . . 146 ILE CG1 . 26029 1 237 . 1 1 73 73 ILE CG2 C 13 17.575 0.15 . 1 . . . . 146 ILE CG2 . 26029 1 238 . 1 1 73 73 ILE N N 15 120.713 0.1 . 1 . . . . 146 ILE N . 26029 1 239 . 1 1 74 74 VAL H H 1 7.689 0.02 . 1 . . . . 147 VAL HN . 26029 1 240 . 1 1 74 74 VAL CA C 13 63.708 0.15 . 1 . . . . 147 VAL CA . 26029 1 241 . 1 1 74 74 VAL CB C 13 33.323 0.15 . 1 . . . . 147 VAL CB . 26029 1 242 . 1 1 74 74 VAL N N 15 128.443 0.1 . 1 . . . . 147 VAL N . 26029 1 stop_ save_