data_50313 ####################### # Entry information # ####################### save_entry_information_1 _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information_1 _Entry.ID 50313 _Entry.Title ; 13C and 15N Chemical Shift Assignments for human M129V variant Y145Stop Prion Protein Amyloid Fibrils ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2020-06-10 _Entry.Accession_date 2020-06-10 _Entry.Last_release_date 2020-06-10 _Entry.Original_release_date 2020-06-10 _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 solid-state _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 . _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 Hanh Dao . H. . . 50313 2 May Hlaing . Z. . . 50313 3 Yixuan Ma . . . . 50313 4 Krystyna Surewicz . . . . 50313 5 Witold Surewicz . K. . . 50313 6 Christopher Jaroniec . P. . . 50313 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 50313 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 62 50313 '15N chemical shifts' 18 50313 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 . . 2021-07-27 . original BMRB . 50313 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 50312 'huPrP23-144 A117V' 50313 stop_ save_ ############### # Citations # ############### save_citations_1 _Citation.Sf_category citations _Citation.Sf_framecode citations_1 _Citation.Entry_ID 50313 _Citation.ID 1 _Citation.Name '13C and 15N chemical shift assignments of A117V and M129V human Y145Stop prion protein amyloid fibrils' _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 33123960 _Citation.DOI . _Citation.Full_citation . _Citation.Title ; 13C and 15N chemical shift assignments of A117V and M129V human Y145Stop prion protein amyloid fibrils ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biomol. NMR Assignments' _Citation.Journal_name_full . _Citation.Journal_volume 15 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1874-270X _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 45 _Citation.Page_last 51 _Citation.Year 2021 _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 Hanh Dao . H. . . 50313 1 2 May Hlaing . Z. . . 50313 1 3 Yixuan Ma . . . . 50313 1 4 Krystyna Surewicz . . . . 50313 1 5 Witold Surewicz . K. . . 50313 1 6 Christopher Jaroniec . P. . . 50313 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID amyloid 50313 1 'magic-angle spinning' 50313 1 'prion protein' 50313 1 'solid-state NMR' 50313 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly_1 _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly_1 _Assembly.Entry_ID 50313 _Assembly.ID 1 _Assembly.Name 'huPrP23-144 M129V' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _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 . _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 'huPrP23-144 M129V amyloid fibrils' 1 $entity_1 . . yes native no no . . . 50313 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 50313 _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 A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSDPKKRPKPGGWNTGGSRY PGQGSPGGNRYPPQGGGGWG QPHGGGWGQPHGGGWGQPHG GGWGQPHGGGWGQGGGTHSQ WNKPSKPKTNMKHMAGAAAA GAVVGGLGGYVLGSAMSRPI IHFGSD ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq '23 K; 24 K; 25 R ...... 142 G; 143 S; 144 D.' _Entity.Polymer_author_seq_details ; The four N-terminal residues (GSDP) correspond to non-native thrombin cleavage sites used for protein purification. This is a truncated version of the human prion protein. This Y145Stop human prion protein includes residues 23 to 144, starting at 23K, 24K, 25R, and ending at 142G, 143S, 144D. ; _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 126 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _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 1 GLY . 50313 1 2 2 SER . 50313 1 3 3 ASP . 50313 1 4 4 PRO . 50313 1 5 23 LYS . 50313 1 6 24 LYS . 50313 1 7 25 ARG . 50313 1 8 26 PRO . 50313 1 9 27 LYS . 50313 1 10 28 PRO . 50313 1 11 29 GLY . 50313 1 12 30 GLY . 50313 1 13 31 TRP . 50313 1 14 32 ASN . 50313 1 15 33 THR . 50313 1 16 34 GLY . 50313 1 17 35 GLY . 50313 1 18 36 SER . 50313 1 19 37 ARG . 50313 1 20 38 TYR . 50313 1 21 39 PRO . 50313 1 22 40 GLY . 50313 1 23 41 GLN . 50313 1 24 42 GLY . 50313 1 25 43 SER . 50313 1 26 44 PRO . 50313 1 27 45 GLY . 50313 1 28 46 GLY . 50313 1 29 47 ASN . 50313 1 30 48 ARG . 50313 1 31 49 TYR . 50313 1 32 50 PRO . 50313 1 33 51 PRO . 50313 1 34 52 GLN . 50313 1 35 53 GLY . 50313 1 36 54 GLY . 50313 1 37 55 GLY . 50313 1 38 56 GLY . 50313 1 39 57 TRP . 50313 1 40 58 GLY . 50313 1 41 59 GLN . 50313 1 42 60 PRO . 50313 1 43 61 HIS . 50313 1 44 62 GLY . 50313 1 45 63 GLY . 50313 1 46 64 GLY . 50313 1 47 65 TRP . 50313 1 48 66 GLY . 50313 1 49 67 GLN . 50313 1 50 68 PRO . 50313 1 51 69 HIS . 50313 1 52 70 GLY . 50313 1 53 71 GLY . 50313 1 54 72 GLY . 50313 1 55 73 TRP . 50313 1 56 74 GLY . 50313 1 57 75 GLN . 50313 1 58 76 PRO . 50313 1 59 77 HIS . 50313 1 60 78 GLY . 50313 1 61 79 GLY . 50313 1 62 80 GLY . 50313 1 63 81 TRP . 50313 1 64 82 GLY . 50313 1 65 83 GLN . 50313 1 66 84 PRO . 50313 1 67 85 HIS . 50313 1 68 86 GLY . 50313 1 69 87 GLY . 50313 1 70 88 GLY . 50313 1 71 89 TRP . 50313 1 72 90 GLY . 50313 1 73 91 GLN . 50313 1 74 92 GLY . 50313 1 75 93 GLY . 50313 1 76 94 GLY . 50313 1 77 95 THR . 50313 1 78 96 HIS . 50313 1 79 97 SER . 50313 1 80 98 GLN . 50313 1 81 99 TRP . 50313 1 82 100 ASN . 50313 1 83 101 LYS . 50313 1 84 102 PRO . 50313 1 85 103 SER . 50313 1 86 104 LYS . 50313 1 87 105 PRO . 50313 1 88 106 LYS . 50313 1 89 107 THR . 50313 1 90 108 ASN . 50313 1 91 109 MET . 50313 1 92 110 LYS . 50313 1 93 111 HIS . 50313 1 94 112 MET . 50313 1 95 113 ALA . 50313 1 96 114 GLY . 50313 1 97 115 ALA . 50313 1 98 116 ALA . 50313 1 99 117 ALA . 50313 1 100 118 ALA . 50313 1 101 119 GLY . 50313 1 102 120 ALA . 50313 1 103 121 VAL . 50313 1 104 122 VAL . 50313 1 105 123 GLY . 50313 1 106 124 GLY . 50313 1 107 125 LEU . 50313 1 108 126 GLY . 50313 1 109 127 GLY . 50313 1 110 128 TYR . 50313 1 111 129 VAL . 50313 1 112 130 LEU . 50313 1 113 131 GLY . 50313 1 114 132 SER . 50313 1 115 133 ALA . 50313 1 116 134 MET . 50313 1 117 135 SER . 50313 1 118 136 ARG . 50313 1 119 137 PRO . 50313 1 120 138 ILE . 50313 1 121 139 ILE . 50313 1 122 140 HIS . 50313 1 123 141 PHE . 50313 1 124 142 GLY . 50313 1 125 143 SER . 50313 1 126 144 ASP . 50313 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 . GLY 1 1 50313 1 . SER 2 2 50313 1 . ASP 3 3 50313 1 . PRO 4 4 50313 1 . LYS 5 5 50313 1 . LYS 6 6 50313 1 . ARG 7 7 50313 1 . PRO 8 8 50313 1 . LYS 9 9 50313 1 . PRO 10 10 50313 1 . GLY 11 11 50313 1 . GLY 12 12 50313 1 . TRP 13 13 50313 1 . ASN 14 14 50313 1 . THR 15 15 50313 1 . GLY 16 16 50313 1 . GLY 17 17 50313 1 . SER 18 18 50313 1 . ARG 19 19 50313 1 . TYR 20 20 50313 1 . PRO 21 21 50313 1 . GLY 22 22 50313 1 . GLN 23 23 50313 1 . GLY 24 24 50313 1 . SER 25 25 50313 1 . PRO 26 26 50313 1 . GLY 27 27 50313 1 . GLY 28 28 50313 1 . ASN 29 29 50313 1 . ARG 30 30 50313 1 . TYR 31 31 50313 1 . PRO 32 32 50313 1 . PRO 33 33 50313 1 . GLN 34 34 50313 1 . GLY 35 35 50313 1 . GLY 36 36 50313 1 . GLY 37 37 50313 1 . GLY 38 38 50313 1 . TRP 39 39 50313 1 . GLY 40 40 50313 1 . GLN 41 41 50313 1 . PRO 42 42 50313 1 . HIS 43 43 50313 1 . GLY 44 44 50313 1 . GLY 45 45 50313 1 . GLY 46 46 50313 1 . TRP 47 47 50313 1 . GLY 48 48 50313 1 . GLN 49 49 50313 1 . PRO 50 50 50313 1 . HIS 51 51 50313 1 . GLY 52 52 50313 1 . GLY 53 53 50313 1 . GLY 54 54 50313 1 . TRP 55 55 50313 1 . GLY 56 56 50313 1 . GLN 57 57 50313 1 . PRO 58 58 50313 1 . HIS 59 59 50313 1 . GLY 60 60 50313 1 . GLY 61 61 50313 1 . GLY 62 62 50313 1 . TRP 63 63 50313 1 . GLY 64 64 50313 1 . GLN 65 65 50313 1 . PRO 66 66 50313 1 . HIS 67 67 50313 1 . GLY 68 68 50313 1 . GLY 69 69 50313 1 . GLY 70 70 50313 1 . TRP 71 71 50313 1 . GLY 72 72 50313 1 . GLN 73 73 50313 1 . GLY 74 74 50313 1 . GLY 75 75 50313 1 . GLY 76 76 50313 1 . THR 77 77 50313 1 . HIS 78 78 50313 1 . SER 79 79 50313 1 . GLN 80 80 50313 1 . TRP 81 81 50313 1 . ASN 82 82 50313 1 . LYS 83 83 50313 1 . PRO 84 84 50313 1 . SER 85 85 50313 1 . LYS 86 86 50313 1 . PRO 87 87 50313 1 . LYS 88 88 50313 1 . THR 89 89 50313 1 . ASN 90 90 50313 1 . MET 91 91 50313 1 . LYS 92 92 50313 1 . HIS 93 93 50313 1 . MET 94 94 50313 1 . ALA 95 95 50313 1 . GLY 96 96 50313 1 . ALA 97 97 50313 1 . ALA 98 98 50313 1 . ALA 99 99 50313 1 . ALA 100 100 50313 1 . GLY 101 101 50313 1 . ALA 102 102 50313 1 . VAL 103 103 50313 1 . VAL 104 104 50313 1 . GLY 105 105 50313 1 . GLY 106 106 50313 1 . LEU 107 107 50313 1 . GLY 108 108 50313 1 . GLY 109 109 50313 1 . TYR 110 110 50313 1 . VAL 111 111 50313 1 . LEU 112 112 50313 1 . GLY 113 113 50313 1 . SER 114 114 50313 1 . ALA 115 115 50313 1 . MET 116 116 50313 1 . SER 117 117 50313 1 . ARG 118 118 50313 1 . PRO 119 119 50313 1 . ILE 120 120 50313 1 . ILE 121 121 50313 1 . HIS 122 122 50313 1 . PHE 123 123 50313 1 . GLY 124 124 50313 1 . SER 125 125 50313 1 . ASP 126 126 50313 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 50313 _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 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 50313 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 50313 _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 . . pRSETB . . . 50313 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 50313 _Sample.ID 1 _Sample.Name 'huPrP23-144 M129V' _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Amyloid fibril formation was performed at 25C under quiescent conditions (i.e. in absence of continuous agitation).' _Sample.Aggregate_sample_number 1 _Sample.Solvent_system none _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 'huPrP23-144 M129V' '[U-100% 13C; U-100% 15N]' . . 1 $entity_1 . . 16.5 15 18 mg . . . . 50313 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 50313 _Sample_condition_list.ID 1 _Sample_condition_list.Name 'Sample Condition for huPrP23-144 M129V' _Sample_condition_list.Details 'The temperature control setting is 273 K.' 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 pH 6.4 . pH 50313 1 pressure 1 . atm 50313 1 temperature 275 2 K 50313 1 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 50313 _Software.ID 1 _Software.Type . _Software.Name TOPSPIN _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 50313 1 stop_ loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID collection . 50313 1 stop_ save_ save_software_2 _Software.Sf_category software _Software.Sf_framecode software_2 _Software.Entry_ID 50313 _Software.ID 2 _Software.Type . _Software.Name NMRPipe _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 50313 2 stop_ loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID processing . 50313 2 stop_ save_ save_software_3 _Software.Sf_category software _Software.Sf_framecode software_3 _Software.Entry_ID 50313 _Software.ID 3 _Software.Type . _Software.Name SPARKY _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 50313 3 stop_ loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' . 50313 3 stop_ save_ save_software_4 _Software.Sf_category software _Software.Sf_framecode software_4 _Software.Entry_ID 50313 _Software.ID 4 _Software.Type . _Software.Name TALOS _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Cornilescu, Delaglio and Bax' . . 50313 4 stop_ loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID 'data analysis' . 50313 4 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 50313 _NMR_spectrometer.ID 1 _NMR_spectrometer.Name 'Bruker Avance III HD Ascend 800 MHz' _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 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 50313 _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 NCA' no . . . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50313 1 2 '2D NCACX' no . . . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50313 1 3 '2D NCOCX' no . . . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50313 1 4 '3D NCACX' no . . . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50313 1 5 '3D NCOCX' no . . . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50313 1 6 '3D CANCOCX' no . . . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50313 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 50313 _Chem_shift_reference.ID 1 _Chem_shift_reference.Name DSS _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 DSS 'methyl protons' . . . . ppm 0 na indirect 0.251449530 . . . . . 50313 1 N 15 DSS 'methyl protons' . . . . ppm 0 na indirect 0.101329118 . . . . . 50313 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 50313 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Name 'huPrP23-144 M129V' _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 NCA' . . . 50313 1 2 '2D NCACX' . . . 50313 1 3 '2D NCOCX' . . . 50313 1 4 '3D NCACX' . . . 50313 1 5 '3D NCOCX' . . . 50313 1 6 '3D CANCOCX' . . . 50313 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 . 1 102 102 ALA C C 13 177.344 0.088 . 1 . . . . . 120 A CO . 50313 1 2 . 1 . 1 103 103 VAL C C 13 176.149 0.144 . 1 . . . . . 121 V CO . 50313 1 3 . 1 . 1 103 103 VAL CA C 13 62.359 0.106 . 1 . . . . . 121 V CA . 50313 1 4 . 1 . 1 103 103 VAL CB C 13 40.471 0.079 . 1 . . . . . 121 V CB . 50313 1 5 . 1 . 1 103 103 VAL CG1 C 13 23.915 0.015 . 2 . . . . . 121 V CG1 . 50313 1 6 . 1 . 1 103 103 VAL CG2 C 13 21.355 0.021 . 2 . . . . . 121 V CG2 . 50313 1 7 . 1 . 1 103 103 VAL N N 15 121.576 0.185 . 1 . . . . . 121 V N . 50313 1 8 . 1 . 1 104 104 VAL C C 13 176.305 0.084 . 1 . . . . . 122 V CO . 50313 1 9 . 1 . 1 104 104 VAL CA C 13 61.684 0.096 . 1 . . . . . 122 V CA . 50313 1 10 . 1 . 1 104 104 VAL CB C 13 36.191 0.086 . 1 . . . . . 122 V CB . 50313 1 11 . 1 . 1 104 104 VAL CG1 C 13 21.934 0.065 . 2 . . . . . 122 V CG1 . 50313 1 12 . 1 . 1 104 104 VAL CG2 C 13 21.376 0.013 . 2 . . . . . 122 V CG2 . 50313 1 13 . 1 . 1 104 104 VAL N N 15 125.242 0.102 . 1 . . . . . 122 V N . 50313 1 14 . 1 . 1 105 105 GLY C C 13 172.588 0.202 . 1 . . . . . 123 G CO . 50313 1 15 . 1 . 1 105 105 GLY CA C 13 46.349 0.031 . 1 . . . . . 123 G CA . 50313 1 16 . 1 . 1 105 105 GLY N N 15 112.403 0.130 . 1 . . . . . 123 G N . 50313 1 17 . 1 . 1 106 106 GLY C C 13 172.411 0.165 . 1 . . . . . 124 G CO . 50313 1 18 . 1 . 1 106 106 GLY CA C 13 45.451 0.044 . 1 . . . . . 124 G CA . 50313 1 19 . 1 . 1 106 106 GLY N N 15 109.860 0.083 . 1 . . . . . 124 G N . 50313 1 20 . 1 . 1 107 107 LEU C C 13 178.503 0.083 . 1 . . . . . 125 L CO . 50313 1 21 . 1 . 1 107 107 LEU CA C 13 53.224 0.091 . 1 . . . . . 125 L CA . 50313 1 22 . 1 . 1 107 107 LEU CB C 13 45.424 0.000 . 1 . . . . . 125 L CB . 50313 1 23 . 1 . 1 107 107 LEU N N 15 126.797 0.134 . 1 . . . . . 125 L N . 50313 1 24 . 1 . 1 108 108 GLY C C 13 174.119 0.061 . 1 . . . . . 126 G CO . 50313 1 25 . 1 . 1 108 108 GLY CA C 13 49.271 0.044 . 1 . . . . . 126 G CA . 50313 1 26 . 1 . 1 108 108 GLY N N 15 114.812 0.144 . 1 . . . . . 126 G N . 50313 1 27 . 1 . 1 109 109 GLY C C 13 173.089 0.206 . 1 . . . . . 127 G CO . 50313 1 28 . 1 . 1 109 109 GLY CA C 13 46.098 0.048 . 1 . . . . . 127 G CA . 50313 1 29 . 1 . 1 109 109 GLY N N 15 97.968 0.112 . 1 . . . . . 127 G N . 50313 1 30 . 1 . 1 110 110 TYR C C 13 175.758 0.173 . 1 . . . . . 128 Y CO . 50313 1 31 . 1 . 1 110 110 TYR CA C 13 62.981 0.053 . 1 . . . . . 128 Y CA . 50313 1 32 . 1 . 1 110 110 TYR CB C 13 39.949 0.008 . 1 . . . . . 128 Y CB . 50313 1 33 . 1 . 1 110 110 TYR N N 15 116.862 0.070 . 1 . . . . . 128 Y N . 50313 1 34 . 1 . 1 111 111 VAL C C 13 174.790 0.143 . 1 . . . . . 129 V CO . 50313 1 35 . 1 . 1 111 111 VAL CA C 13 62.314 0.124 . 1 . . . . . 129 V CA . 50313 1 36 . 1 . 1 111 111 VAL CB C 13 33.867 0.039 . 1 . . . . . 129 V CB . 50313 1 37 . 1 . 1 111 111 VAL CG1 C 13 22.724 0.060 . 2 . . . . . 129 V CG1 . 50313 1 38 . 1 . 1 111 111 VAL CG2 C 13 21.002 0.014 . 2 . . . . . 129 V CG2 . 50313 1 39 . 1 . 1 111 111 VAL N N 15 119.017 0.056 . 1 . . . . . 129 V N . 50313 1 40 . 1 . 1 112 112 LEU C C 13 179.729 0.118 . 1 . . . . . 130 L CO . 50313 1 41 . 1 . 1 112 112 LEU CA C 13 54.259 0.052 . 1 . . . . . 130 L CA . 50313 1 42 . 1 . 1 112 112 LEU CB C 13 45.812 0.019 . 1 . . . . . 130 L CB . 50313 1 43 . 1 . 1 112 112 LEU CG C 13 29.599 0.025 . 1 . . . . . 130 L CG . 50313 1 44 . 1 . 1 112 112 LEU N N 15 126.699 0.130 . 1 . . . . . 130 L N . 50313 1 45 . 1 . 1 113 113 GLY C C 13 175.289 0.067 . 1 . . . . . 131 G CO . 50313 1 46 . 1 . 1 113 113 GLY CA C 13 48.917 0.039 . 1 . . . . . 131 G CA . 50313 1 47 . 1 . 1 113 113 GLY N N 15 114.345 0.107 . 1 . . . . . 131 G N . 50313 1 48 . 1 . 1 114 114 SER C C 13 171.487 0.097 . 1 . . . . . 132 S CO . 50313 1 49 . 1 . 1 114 114 SER CA C 13 59.092 0.081 . 1 . . . . . 132 S CA . 50313 1 50 . 1 . 1 114 114 SER CB C 13 68.765 0.055 . 1 . . . . . 132 S CB . 50313 1 51 . 1 . 1 114 114 SER N N 15 111.389 0.070 . 1 . . . . . 132 S N . 50313 1 52 . 1 . 1 115 115 ALA C C 13 177.386 0.116 . 1 . . . . . 133 A CO . 50313 1 53 . 1 . 1 115 115 ALA CA C 13 50.877 0.045 . 1 . . . . . 133 A CA . 50313 1 54 . 1 . 1 115 115 ALA CB C 13 25.437 0.031 . 1 . . . . . 133 A CB . 50313 1 55 . 1 . 1 115 115 ALA N N 15 124.933 0.100 . 1 . . . . . 133 A N . 50313 1 56 . 1 . 1 116 116 MET C C 13 175.214 0.143 . 1 . . . . . 134 M CO . 50313 1 57 . 1 . 1 116 116 MET CA C 13 54.317 0.047 . 1 . . . . . 134 M CA . 50313 1 58 . 1 . 1 116 116 MET CB C 13 38.322 0.062 . 1 . . . . . 134 M CB . 50313 1 59 . 1 . 1 116 116 MET CG C 13 35.358 0.040 . 1 . . . . . 134 M CG . 50313 1 60 . 1 . 1 116 116 MET N N 15 116.426 0.108 . 1 . . . . . 134 M N . 50313 1 61 . 1 . 1 117 117 SER C C 13 173.329 0.080 . 1 . . . . . 135 S CO . 50313 1 62 . 1 . 1 117 117 SER CA C 13 54.300 0.047 . 1 . . . . . 135 S CA . 50313 1 63 . 1 . 1 117 117 SER CB C 13 65.761 0.042 . 1 . . . . . 135 S CB . 50313 1 64 . 1 . 1 117 117 SER N N 15 117.787 0.117 . 1 . . . . . 135 S N . 50313 1 65 . 1 . 1 118 118 ARG C C 13 173.137 0.059 . 1 . . . . . 136 R CO . 50313 1 66 . 1 . 1 118 118 ARG CA C 13 56.500 0.044 . 1 . . . . . 136 R CA . 50313 1 67 . 1 . 1 118 118 ARG CB C 13 31.435 0.077 . 1 . . . . . 136 R CB . 50313 1 68 . 1 . 1 118 118 ARG N N 15 122.456 0.050 . 1 . . . . . 136 R N . 50313 1 69 . 1 . 1 119 119 PRO C C 13 176.298 0.000 . 1 . . . . . 137 P CO . 50313 1 70 . 1 . 1 119 119 PRO CA C 13 62.055 0.000 . 1 . . . . . 137 P CA . 50313 1 71 . 1 . 1 120 120 ILE C C 13 175.046 0.226 . 1 . . . . . 138 I CO . 50313 1 72 . 1 . 1 120 120 ILE CA C 13 60.256 0.079 . 1 . . . . . 138 I CA . 50313 1 73 . 1 . 1 120 120 ILE CB C 13 42.381 0.029 . 1 . . . . . 138 I CB . 50313 1 74 . 1 . 1 120 120 ILE CG1 C 13 27.887 0.031 . 1 . . . . . 138 I CG1 . 50313 1 75 . 1 . 1 120 120 ILE CG2 C 13 19.073 0.019 . 1 . . . . . 138 I CG2 . 50313 1 76 . 1 . 1 120 120 ILE CD1 C 13 14.422 0.007 . 1 . . . . . 138 I CD . 50313 1 77 . 1 . 1 120 120 ILE N N 15 123.444 0.107 . 1 . . . . . 138 I N . 50313 1 78 . 1 . 1 121 121 ILE C C 13 174.611 0.031 . 1 . . . . . 139 I CO . 50313 1 79 . 1 . 1 121 121 ILE CA C 13 55.303 0.036 . 1 . . . . . 139 I CA . 50313 1 80 . 1 . 1 121 121 ILE N N 15 126.277 0.089 . 1 . . . . . 139 I N . 50313 1 stop_ save_