data_18104 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18104 _Entry.Title ; MARCKS MH2 Domain free and mAb 3C3 bounded ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-11-28 _Entry.Accession_date 2011-11-28 _Entry.Last_release_date 2014-03-14 _Entry.Original_release_date 2014-03-14 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details ; The S25p and S25up (1.2 mM) NMR samples were prepared in 10 mM phosphate buffer saline (PBS) pH 7.2 and pH 5.0 with 10% of D2O. For the peptide-antibody interaction studies, mAb 3C3 was added directly on the NMR samples for a final concentration of 3.6 M (300:1 molar ratio peptide-antibody). NMR experiments were carried out on Varian Inova 600 MHz or on Bruker Avance DRX 600 MHz at 5 oC or 25 oC. ; _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.Entry_ID 1 Luzineide Tinoco . W. . 18104 2 Jully Fraga . L. . 18104 3 Cristiane AnoBom . D. . 18104 4 Flavio Zolessi . . . 18104 5 Gonzalo Obal . . . 18104 6 Andrea Toledo . . . 18104 7 Otto Pritsch . . . 18104 8 Cristina Arruti . . . 18104 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'Federal University of Rio de Janeiro' . 18104 2 . 'Multiusers NMR Laboratory - LAMAR' . 18104 3 . 'Universidad de la Rep blica' . 18104 4 . 'Institut Pasteur de Montevideo' . 18104 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18104 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 93 18104 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 . . 2014-03-14 2011-11-28 original author . 18104 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 18105 'S25p (phosphorylated)' 18104 BMRB 18106 'S25p complex with 3C3' 18104 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 18104 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 24590112 _Citation.Full_citation . _Citation.Title 'Structural characterization of a neuroblast-specific phosphorylated region of MARCKS' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochim. Biophys. Acta' _Citation.Journal_name_full 'Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics' _Citation.Journal_volume 1844 _Citation.Journal_issue 4 _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 837 _Citation.Page_last 849 _Citation.Year 2014 _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.Entry_ID _Citation_author.Citation_ID 1 Luzineide Tinoco . W. . 18104 1 2 Jully Fraga . L. . 18104 1 3 Cristiane AnoBom . D. . 18104 1 4 Flavio Zolessi . . . 18104 1 5 Gonzalo Obal . . . 18104 1 6 Andrea Toledo . . . 18104 1 7 Otto Pritsch . . . 18104 1 8 Cristina Arruti . . . 18104 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'MH2 domain' 18104 1 neuroblast 18104 1 peptide-antibody 18104 1 phophorylation 18104 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18104 _Assembly.ID 1 _Assembly.Name S25up _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 172000 _Assembly.Enzyme_commission_number . _Assembly.Details 'S25p (phosphorylated MARCKS peptide) interacting wiht the monoclonal antibody 3C3' _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 S25up 1 $MARCKS_peptides A . yes native no no . . . 18104 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_MARCKS_peptides _Entity.Sf_category entity _Entity.Sf_framecode MARCKS_peptides _Entity.Entry_ID 18104 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name MARCKS_peptides _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 ; EKPGEAVAASPSKANGQENG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'Residue 1-20 represents part (residues 16-35) of the MH2 Gallus gallus MARCKS domain' _Entity.Ambiguous_conformational_states yes _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality yes _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 20 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment 'MH2 Gallus gallus MARCKS domain' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 1941 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details P16527 _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no EMBL CAJ81538 . "myristoylated alanine-rich protein kinase C substrate [Xenopus (Silurana) tropicalis]" . . . . . 100.00 286 100.00 100.00 1.82e-02 . . . . 18104 1 2 no GB AAA48946 . "C kinase substrate [Gallus gallus]" . . . . . 100.00 281 100.00 100.00 1.99e-02 . . . . 18104 1 3 no GB AAH75394 . "marcks protein [Xenopus (Silurana) tropicalis]" . . . . . 100.00 286 100.00 100.00 1.90e-02 . . . . 18104 1 4 no GB EMP38065 . "Myristoylated alanine-rich C-kinase substrate [Chelonia mydas]" . . . . . 100.00 282 100.00 100.00 2.16e-02 . . . . 18104 1 5 no GB EOB08830 . "Myristoylated alanine-rich C-kinase substrate, partial [Anas platyrhynchos]" . . . . . 85.00 33 100.00 100.00 5.08e-01 . . . . 18104 1 6 no GB KQL91641 . "myristoylated alanine-rich protein kinase C substrate [Alligator mississippiensis]" . . . . . 100.00 197 100.00 100.00 1.56e-02 . . . . 18104 1 7 no REF NP_001006693 . "myristoylated alanine-rich C-kinase substrate [Xenopus (Silurana) tropicalis]" . . . . . 100.00 286 100.00 100.00 1.82e-02 . . . . 18104 1 8 no REF NP_990811 . "myristoylated alanine-rich C-kinase substrate [Gallus gallus]" . . . . . 100.00 281 100.00 100.00 1.99e-02 . . . . 18104 1 9 no REF XP_005287641 . "PREDICTED: LOW QUALITY PROTEIN: myristoylated alanine-rich C-kinase substrate [Chrysemys picta bellii]" . . . . . 100.00 280 100.00 100.00 2.24e-02 . . . . 18104 1 10 no REF XP_005518342 . "PREDICTED: myristoylated alanine-rich C-kinase substrate [Pseudopodoces humilis]" . . . . . 100.00 286 100.00 100.00 2.45e-02 . . . . 18104 1 11 no REF XP_005518343 . "PREDICTED: myristoylated alanine-rich C-kinase substrate [Pseudopodoces humilis]" . . . . . 100.00 286 100.00 100.00 2.45e-02 . . . . 18104 1 12 no SP P16527 . "RecName: Full=Myristoylated alanine-rich C-kinase substrate; Short=MARCKS [Gallus gallus]" . . . . . 100.00 281 100.00 100.00 1.99e-02 . . . . 18104 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'regions of MARCKS phosphorylated isoform specific for neuroblasts and some types of neurons' 18104 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 . GLU . 18104 1 2 . LYS . 18104 1 3 . PRO . 18104 1 4 . GLY . 18104 1 5 . GLU . 18104 1 6 . ALA . 18104 1 7 . VAL . 18104 1 8 . ALA . 18104 1 9 . ALA . 18104 1 10 . SER . 18104 1 11 . PRO . 18104 1 12 . SER . 18104 1 13 . LYS . 18104 1 14 . ALA . 18104 1 15 . ASN . 18104 1 16 . GLY . 18104 1 17 . GLN . 18104 1 18 . GLU . 18104 1 19 . ASN . 18104 1 20 . GLY . 18104 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 . GLU 1 1 18104 1 . LYS 2 2 18104 1 . PRO 3 3 18104 1 . GLY 4 4 18104 1 . GLU 5 5 18104 1 . ALA 6 6 18104 1 . VAL 7 7 18104 1 . ALA 8 8 18104 1 . ALA 9 9 18104 1 . SER 10 10 18104 1 . PRO 11 11 18104 1 . SER 12 12 18104 1 . LYS 13 13 18104 1 . ALA 14 14 18104 1 . ASN 15 15 18104 1 . GLY 16 16 18104 1 . GLN 17 17 18104 1 . GLU 18 18 18104 1 . ASN 19 19 18104 1 . GLY 20 20 18104 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 18104 _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.Subvariant _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.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $MARCKS_peptides . 9031 organism . 'Gallus gallus' chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 18104 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 18104 _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_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _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.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $MARCKS_peptides . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18104 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_S25up _Sample.Sf_category sample _Sample.Sf_framecode sample_S25up _Sample.Entry_ID 18104 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'MARCKS unphosphorylated peptide' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% 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 'MARCKS peptides' 'natural abundance' . . 1 $MARCKS_peptides . . 1.2 . . mM . . . . 18104 1 2 'sodium phosphate' 'natural abundance' . . . . . . 10 . . mM . . . . 18104 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 18104 _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' 13.7 . mM 18104 1 pH 7.2 . pH 18104 1 pressure 1 . atm 18104 1 temperature 298 . K 18104 1 stop_ save_ save_sample_conditions_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_2 _Sample_condition_list.Entry_ID 18104 _Sample_condition_list.ID 2 _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' 13.7 . mM 18104 2 pH 7.2 . pH 18104 2 pressure 1 . atm 18104 2 temperature 278 . K 18104 2 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 18104 _Software.ID 1 _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' . . 18104 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18104 1 stop_ save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 18104 _Software.ID 2 _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' . . 18104 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18104 2 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 18104 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 18104 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 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 18104 _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 DRX . 600 . . . 18104 1 2 spectrometer_2 Varian INOVA . 600 . . . 18104 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 18104 _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-1H TOCSY' no . . . . . . . . . . 1 $sample_S25up isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18104 1 2 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_S25up isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18104 1 stop_ save_ save_2D_1H-1H_TOCSY _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode 2D_1H-1H_TOCSY _NMR_spec_expt.Entry_ID 18104 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name 2D_1H-1H_TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details ; Water suppression was achieved using WATERGATE pulse sequence. TOCSY spectra were acquired using MLEV-17 for spin lock, using a mixing time of 70 ms and the spectra were collected with 256 data points in F1 and 2048 points in F2 with 32 transients/t1. ; save_ save_2D_1H-1H_NOESY _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode 2D_1H-1H_NOESY _NMR_spec_expt.Entry_ID 18104 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name 2D_1H-1H_NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details 'For NOESY spectra, an optimal mixing time of 300 ms was used, observed in a range of 150-500 ms.' 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 18104 _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.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 water protons . . . . ppm 4.7 internal direct 1.0 . . . . . . . . . 18104 1 stop_ save_ save_chemical_shift_reference_2 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_2 _Chem_shift_reference.Entry_ID 18104 _Chem_shift_reference.ID 2 _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.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 water protons . . . . ppm 4.96 internal direct 1.0 . . . . . . . . . 18104 2 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_S25up-25 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode S25up-25 _Assigned_chem_shift_list.Entry_ID 18104 _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 . _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-1H TOCSY' . . . 18104 1 2 '2D 1H-1H NOESY' . . . 18104 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 2 2 LYS HA H 1 4.565 . . 1 . . . . 2 K HA . 18104 1 2 . 1 1 2 2 LYS HB3 H 1 1.745 . . 2 . . . . 2 K HB3 . 18104 1 3 . 1 1 2 2 LYS HG2 H 1 1.376 . . 2 . . . . 2 K HG2 . 18104 1 4 . 1 1 2 2 LYS HD2 H 1 1.605 . . 2 . . . . 2 K HD2 . 18104 1 5 . 1 1 2 2 LYS HE2 H 1 2.905 . . 2 . . . . 2 K HE2 . 18104 1 6 . 1 1 3 3 PRO HA H 1 4.346 . . 1 . . . . 3 P HA . 18104 1 7 . 1 1 3 3 PRO HB2 H 1 2.361 . . 2 . . . . 3 P HB2 . 18104 1 8 . 1 1 3 3 PRO HB3 H 1 2.234 . . 2 . . . . 3 P HB3 . 18104 1 9 . 1 1 3 3 PRO HG2 H 1 1.929 . . 2 . . . . 3 P HG2 . 18104 1 10 . 1 1 3 3 PRO HG3 H 1 1.975 . . 2 . . . . 3 P HG3 . 18104 1 11 . 1 1 3 3 PRO HD2 H 1 3.889 . . 2 . . . . 3 P HD2 . 18104 1 12 . 1 1 3 3 PRO HD3 H 1 3.575 . . 2 . . . . 3 P HD3 . 18104 1 13 . 1 1 5 5 GLU H H 1 8.519 . . 1 . . . . 5 E HN . 18104 1 14 . 1 1 5 5 GLU HA H 1 4.166 . . 1 . . . . 5 E HA . 18104 1 15 . 1 1 5 5 GLU HB2 H 1 1.854 . . 2 . . . . 5 E HB2 . 18104 1 16 . 1 1 5 5 GLU HB3 H 1 1.941 . . 2 . . . . 5 E HB3 . 18104 1 17 . 1 1 5 5 GLU HG2 H 1 2.167 . . 2 . . . . 5 E HG2 . 18104 1 18 . 1 1 6 6 ALA H H 1 8.258 . . 1 . . . . 6 A HN . 18104 1 19 . 1 1 6 6 ALA HA H 1 4.208 . . 1 . . . . 6 A HA . 18104 1 20 . 1 1 6 6 ALA HB1 H 1 1.291 . . 1 . . . . 6 A HB3 . 18104 1 21 . 1 1 6 6 ALA HB2 H 1 1.273 . . 1 . . . . 6 A HB2 . 18104 1 22 . 1 1 6 6 ALA HB3 H 1 1.291 . . 1 . . . . 6 A HB3 . 18104 1 23 . 1 1 7 7 VAL H H 1 7.986 . . 1 . . . . 7 V HN . 18104 1 24 . 1 1 7 7 VAL HA H 1 3.971 . . 1 . . . . 7 V HA . 18104 1 25 . 1 1 7 7 VAL HB H 1 1.951 . . 1 . . . . 7 V HB . 18104 1 26 . 1 1 7 7 VAL HG11 H 1 0.838 . . 2 . . . . 7 V HG11 . 18104 1 27 . 1 1 7 7 VAL HG12 H 1 0.877 . . 2 . . . . 7 V HG12 . 18104 1 28 . 1 1 7 7 VAL HG13 H 1 0.877 . . 2 . . . . 7 V HG13 . 18104 1 29 . 1 1 7 7 VAL HG21 H 1 0.838 . . 2 . . . . 7 V HG21 . 18104 1 30 . 1 1 7 7 VAL HG22 H 1 0.877 . . 2 . . . . 7 V HG22 . 18104 1 31 . 1 1 7 7 VAL HG23 H 1 0.877 . . 2 . . . . 7 V HG23 . 18104 1 32 . 1 1 8 8 ALA H H 1 8.256 . . 1 . . . . 8 A HN . 18104 1 33 . 1 1 8 8 ALA HA H 1 4.229 . . 1 . . . . 8 A HA . 18104 1 34 . 1 1 8 8 ALA HB1 H 1 1.293 . . 1 . . . . 8 A HB3 . 18104 1 35 . 1 1 8 8 ALA HB2 H 1 1.266 . . 1 . . . . 8 A HB2 . 18104 1 36 . 1 1 8 8 ALA HB3 H 1 1.293 . . 1 . . . . 8 A HB3 . 18104 1 37 . 1 1 9 9 ALA H H 1 8.163 . . 1 . . . . 9 A HN . 18104 1 38 . 1 1 9 9 ALA HB1 H 1 1.298 . . 1 . . . . 9 A HB3 . 18104 1 39 . 1 1 9 9 ALA HB2 H 1 1.266 . . 1 . . . . 9 A HB2 . 18104 1 40 . 1 1 9 9 ALA HB3 H 1 1.298 . . 1 . . . . 9 A HB3 . 18104 1 41 . 1 1 10 10 SER H H 1 8.477 . . 9 . . . . 10 S HN . 18104 1 42 . 1 1 10 10 SER HA H 1 4.595 . . 1 . . . . 10 S HA . 18104 1 43 . 1 1 10 10 SER HB3 H 1 3.850 . . 2 . . . . 10 S HB3 . 18104 1 44 . 1 1 11 11 PRO HA H 1 4.370 . . 1 . . . . 11 P HA . 18104 1 45 . 1 1 11 11 PRO HB2 H 1 2.210 . . 2 . . . . 11 P HB2 . 18104 1 46 . 1 1 11 11 PRO HB3 H 1 2.231 . . 2 . . . . 11 P HB3 . 18104 1 47 . 1 1 11 11 PRO HG2 H 1 1.930 . . 2 . . . . 11 P HG2 . 18104 1 48 . 1 1 11 11 PRO HG3 H 1 1.850 . . 2 . . . . 11 P HG3 . 18104 1 49 . 1 1 11 11 PRO HD2 H 1 3.641 . . 2 . . . . 11 P HD2 . 18104 1 50 . 1 1 11 11 PRO HD3 H 1 3.729 . . 2 . . . . 11 P HD3 . 18104 1 51 . 1 1 12 12 SER H H 1 8.282 . . 1 . . . . 12 S HN . 18104 1 52 . 1 1 12 12 SER HA H 1 4.660 . . 1 . . . . 12 S HA . 18104 1 53 . 1 1 12 12 SER HB2 H 1 3.789 . . 2 . . . . 12 S HB2 . 18104 1 54 . 1 1 12 12 SER HB3 H 1 3.874 . . 2 . . . . 12 S HB3 . 18104 1 55 . 1 1 13 13 LYS H H 1 8.216 . . 1 . . . . 13 K HN . 18104 1 56 . 1 1 13 13 LYS HA H 1 4.235 . . 1 . . . . 13 K HA . 18104 1 57 . 1 1 13 13 LYS HB3 H 1 1.754 . . 2 . . . . 13 K HB3 . 18104 1 58 . 1 1 13 13 LYS HG2 H 1 1.356 . . 2 . . . . 13 K HG2 . 18104 1 59 . 1 1 13 13 LYS HG3 H 1 1.337 . . 2 . . . . 13 K HG3 . 18104 1 60 . 1 1 13 13 LYS HD2 H 1 1.584 . . 2 . . . . 13 K HD2 . 18104 1 61 . 1 1 13 13 LYS HD3 H 1 1.650 . . 2 . . . . 13 K HD3 . 18104 1 62 . 1 1 13 13 LYS HE2 H 1 2.899 . . 2 . . . . 13 K HE2 . 18104 1 63 . 1 1 14 14 ALA H H 1 8.162 . . 1 . . . . 14 A HN . 18104 1 64 . 1 1 14 14 ALA HA H 1 4.219 . . 1 . . . . 14 A HA . 18104 1 65 . 1 1 14 14 ALA HB1 H 1 1.310 . . 1 . . . . 14 A HB3 . 18104 1 66 . 1 1 14 14 ALA HB2 H 1 1.270 . . 1 . . . . 14 A HB2 . 18104 1 67 . 1 1 14 14 ALA HB3 H 1 1.310 . . 1 . . . . 14 A HB3 . 18104 1 68 . 1 1 15 15 ASN H H 1 8.326 . . 1 . . . . 15 N HN . 18104 1 69 . 1 1 15 15 ASN HA H 1 4.657 . . 1 . . . . 15 N HA . 18104 1 70 . 1 1 15 15 ASN HB2 H 1 2.752 . . 2 . . . . 15 N HB2 . 18104 1 71 . 1 1 15 15 ASN HB3 H 1 2.705 . . 2 . . . . 15 N HB3 . 18104 1 72 . 1 1 15 15 ASN HD21 H 1 7.342 . . 2 . . . . 15 N HD21 . 18104 1 73 . 1 1 15 15 ASN HD22 H 1 7.433 . . 2 . . . . 15 N HD22 . 18104 1 74 . 1 1 16 16 GLY H H 1 8.278 . . 1 . . . . 16 G HN . 18104 1 75 . 1 1 16 16 GLY HA2 H 1 3.829 . . 2 . . . . 16 G HA1 . 18104 1 76 . 1 1 17 17 GLN H H 1 8.124 . . 1 . . . . 17 Q HN . 18104 1 77 . 1 1 17 17 GLN HA H 1 4.250 . . 1 . . . . 17 Q HA . 18104 1 78 . 1 1 17 17 GLN HB2 H 1 1.871 . . 1 . . . . 17 Q HB2 . 18104 1 79 . 1 1 17 17 GLN HB3 H 1 2.034 . . 2 . . . . 17 Q HB3 . 18104 1 80 . 1 1 17 17 GLN HG2 H 1 2.241 . . 1 . . . . 17 Q HG2 . 18104 1 81 . 1 1 17 17 GLN HG3 H 1 2.311 . . 2 . . . . 17 Q HG3 . 18104 1 82 . 1 1 18 18 GLU H H 1 7.967 . . 1 . . . . 18 E HN . 18104 1 83 . 1 1 18 18 GLU HA H 1 4.187 . . 1 . . . . 18 E HA . 18104 1 84 . 1 1 18 18 GLU HB2 H 1 1.851 . . 2 . . . . 18 E HB2 . 18104 1 85 . 1 1 18 18 GLU HB3 H 1 1.959 . . 2 . . . . 18 E HB3 . 18104 1 86 . 1 1 18 18 GLU HG2 H 1 2.146 . . 2 . . . . 18 E HG2 . 18104 1 87 . 1 1 18 18 GLU HG3 H 1 2.214 . . 2 . . . . 18 E HG3 . 18104 1 88 . 1 1 19 19 ASN H H 1 8.473 . . 1 . . . . 19 N HN . 18104 1 89 . 1 1 19 19 ASN HA H 1 4.598 . . 1 . . . . 19 N HA . 18104 1 90 . 1 1 19 19 ASN HB2 H 1 2.776 . . 2 . . . . 19 N HB2 . 18104 1 91 . 1 1 19 19 ASN HB3 H 1 2.695 . . 2 . . . . 19 N HB3 . 18104 1 92 . 1 1 20 20 GLY H H 1 8.474 . . 1 . . . . 20 G HN . 18104 1 93 . 1 1 20 20 GLY HA2 H 1 4.150 . . 2 . . . . 20 G HA2 . 18104 1 stop_ save_