data_4180 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4180 _Entry.Title ; 1H Chemical Shift Assignments for the Peptide L1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1998-08-12 _Entry.Accession_date 1998-08-12 _Entry.Last_release_date 1999-12-23 _Entry.Original_release_date 1999-12-23 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method nmr _Entry.Experimental_method_subtype . _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.Entry_ID 1 Shari Spector . . . 4180 2 Michael Rosconi . . . 4180 3 Daniel Raleigh . P. . 4180 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4180 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 90 4180 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 . . 1999-12-23 1998-08-12 original author . 4180 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4179 'helix1 from the peripheral subunit-binding domain' 4180 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4180 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 99169414 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Conformational Analysis of Peptide Fragments Derived from the Peripheral Subunit-binding Domain from the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus stearothermophilus: Evidence for Non-random Structure in the Unfolded State ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biopolymers _Citation.Journal_name_full Biopolymers _Citation.Journal_volume 49 _Citation.Journal_issue . _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 29 _Citation.Page_last 40 _Citation.Year 1999 _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 Shari Spector . . . 4180 1 2 Michael Rosconi . . . 4180 1 3 Daniel Raleigh . P. . 4180 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_L1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_L1 _Assembly.Entry_ID 4180 _Assembly.ID 1 _Assembly.Name 'Loop1 from the peripheral subunit binding domain' _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 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details 'This peptide is N-terminally acetylated and C-terminally amidated.' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4180 1 stop_ 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 L1 1 $L1 . . . denatured . . . . . 4180 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 . PDB 2pdd . . . . . 'L1 corresponds to residues 12-23 of the peripheral subunit-binding domain.' 4180 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID L1 abbreviation 4180 1 'Loop1 from the peripheral subunit binding domain' system 4180 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_L1 _Entity.Sf_category entity _Entity.Sf_framecode L1 _Entity.Entry_ID 4180 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Loop1 from the peripheral subunit binding domain' _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 REKGVDIRLVQG _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 12 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID . _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 ; N-terminal Arginine is acetylated C-terminal Glycine is amidated ; _Entity.DB_query_date 2005-11-24 _Entity.DB_query_revised_last_date 2001-05-09 loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID L1 abbreviation 4180 1 'Loop1 from the peripheral subunit binding domain' common 4180 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 12 ARG . 4180 1 2 13 GLU . 4180 1 3 14 LYS . 4180 1 4 15 GLY . 4180 1 5 16 VAL . 4180 1 6 17 ASP . 4180 1 7 18 ILE . 4180 1 8 19 ARG . 4180 1 9 20 LEU . 4180 1 10 21 VAL . 4180 1 11 22 GLN . 4180 1 12 23 GLY . 4180 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 . ARG 1 1 4180 1 . GLU 2 2 4180 1 . LYS 3 3 4180 1 . GLY 4 4 4180 1 . VAL 5 5 4180 1 . ASP 6 6 4180 1 . ILE 7 7 4180 1 . ARG 8 8 4180 1 . LEU 9 9 4180 1 . VAL 10 10 4180 1 . GLN 11 11 4180 1 . GLY 12 12 4180 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 4180 _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 $L1 . 1422 . . 'Bacillus stearothermophilus' 'Bacillus stearothermophilus' . . Eubacteria . Bacillus stearothermophilus . . . . . . . . . . . . . . . . . . . . . 4180 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 4180 _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 $L1 . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . 'L1 was prepared by solid phase peptide synthesis using standard Fmoc chemistry.' . . 4180 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4180 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 'Loop1 from the peripheral subunit binding domain' . . . 1 $L1 . . 8 . . mM . . . . 4180 1 2 D2O . . . . . . . 10 . . % . . . . 4180 1 3 H2O . . . . . . . 90 . . % . . . . 4180 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_one _Sample_condition_list.Entry_ID 4180 _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 pH 5.5 0.2 n/a 4180 1 temperature 298 1 K 4180 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_one _NMR_spectrometer.Entry_ID 4180 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4180 _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 NMR_spectrometer_one Varian INOVA . 600 . . . 4180 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 4180 _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 TOCSY . . . . . . . . . . . 1 $sample_one . . . . . . . . . . . . . . . . . . . . . . . . . . 4180 1 2 ROESY . . . . . . . . . . . 1 $sample_one . . . . . . . . . . . . . . . . . . . . . . . . . . 4180 1 3 DQF-COSY . . . . . . . . . . . 1 $sample_one . . . . . . . . . . . . . . . . . . . . . . . . . . 4180 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4180 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name 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 . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4180 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name ROESY _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 . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4180 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name DQF-COSY _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 . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_one _Chem_shift_reference.Entry_ID 4180 _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 TSP 'methyl protons' . . . . ppm 0.00 internal direct . . . . . . . . . . 4180 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_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_one _Assigned_chem_shift_list.Entry_ID 4180 _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_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_one _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 $sample_one . 4180 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 1 1 ARG H H 1 8.33 . . 1 . . . . . . . . 4180 1 2 . 1 1 1 1 ARG HA H 1 4.27 . . 1 . . . . . . . . 4180 1 3 . 1 1 1 1 ARG HB2 H 1 1.84 . . 2 . . . . . . . . 4180 1 4 . 1 1 1 1 ARG HB3 H 1 1.77 . . 2 . . . . . . . . 4180 1 5 . 1 1 1 1 ARG HG2 H 1 1.67 . . 1 . . . . . . . . 4180 1 6 . 1 1 1 1 ARG HG3 H 1 1.67 . . 1 . . . . . . . . 4180 1 7 . 1 1 1 1 ARG HD2 H 1 3.23 . . 1 . . . . . . . . 4180 1 8 . 1 1 1 1 ARG HD3 H 1 3.23 . . 1 . . . . . . . . 4180 1 9 . 1 1 1 1 ARG HE H 1 7.25 . . 1 . . . . . . . . 4180 1 10 . 1 1 2 2 GLU H H 1 8.65 . . 1 . . . . . . . . 4180 1 11 . 1 1 2 2 GLU HA H 1 4.30 . . 1 . . . . . . . . 4180 1 12 . 1 1 2 2 GLU HB2 H 1 2.06 . . 2 . . . . . . . . 4180 1 13 . 1 1 2 2 GLU HB3 H 1 1.97 . . 2 . . . . . . . . 4180 1 14 . 1 1 2 2 GLU HG2 H 1 2.28 . . 1 . . . . . . . . 4180 1 15 . 1 1 2 2 GLU HG3 H 1 2.28 . . 1 . . . . . . . . 4180 1 16 . 1 1 3 3 LYS H H 1 8.36 . . 1 . . . . . . . . 4180 1 17 . 1 1 3 3 LYS HA H 1 4.36 . . 1 . . . . . . . . 4180 1 18 . 1 1 3 3 LYS HB2 H 1 1.87 . . 2 . . . . . . . . 4180 1 19 . 1 1 3 3 LYS HB3 H 1 1.81 . . 2 . . . . . . . . 4180 1 20 . 1 1 3 3 LYS HG2 H 1 1.46 . . 1 . . . . . . . . 4180 1 21 . 1 1 3 3 LYS HG3 H 1 1.46 . . 1 . . . . . . . . 4180 1 22 . 1 1 3 3 LYS HD2 H 1 1.70 . . 1 . . . . . . . . 4180 1 23 . 1 1 3 3 LYS HD3 H 1 1.70 . . 1 . . . . . . . . 4180 1 24 . 1 1 3 3 LYS HE2 H 1 3.03 . . 1 . . . . . . . . 4180 1 25 . 1 1 3 3 LYS HE3 H 1 3.03 . . 1 . . . . . . . . 4180 1 26 . 1 1 4 4 GLY H H 1 8.40 . . 1 . . . . . . . . 4180 1 27 . 1 1 4 4 GLY HA2 H 1 3.97 . . 1 . . . . . . . . 4180 1 28 . 1 1 4 4 GLY HA3 H 1 3.97 . . 1 . . . . . . . . 4180 1 29 . 1 1 5 5 VAL H H 1 7.92 . . 1 . . . . . . . . 4180 1 30 . 1 1 5 5 VAL HA H 1 4.13 . . 1 . . . . . . . . 4180 1 31 . 1 1 5 5 VAL HB H 1 2.07 . . 1 . . . . . . . . 4180 1 32 . 1 1 5 5 VAL HG11 H 1 0.97 . . 1 . . . . . . . . 4180 1 33 . 1 1 5 5 VAL HG12 H 1 0.97 . . 1 . . . . . . . . 4180 1 34 . 1 1 5 5 VAL HG13 H 1 0.97 . . 1 . . . . . . . . 4180 1 35 . 1 1 5 5 VAL HG21 H 1 0.97 . . 1 . . . . . . . . 4180 1 36 . 1 1 5 5 VAL HG22 H 1 0.97 . . 1 . . . . . . . . 4180 1 37 . 1 1 5 5 VAL HG23 H 1 0.97 . . 1 . . . . . . . . 4180 1 38 . 1 1 6 6 ASP H H 1 8.44 . . 1 . . . . . . . . 4180 1 39 . 1 1 6 6 ASP HA H 1 4.65 . . 1 . . . . . . . . 4180 1 40 . 1 1 6 6 ASP HB2 H 1 2.76 . . 2 . . . . . . . . 4180 1 41 . 1 1 6 6 ASP HB3 H 1 2.59 . . 2 . . . . . . . . 4180 1 42 . 1 1 7 7 ILE H H 1 8.14 . . 1 . . . . . . . . 4180 1 43 . 1 1 7 7 ILE HA H 1 4.14 . . 1 . . . . . . . . 4180 1 44 . 1 1 7 7 ILE HB H 1 1.82 . . 1 . . . . . . . . 4180 1 45 . 1 1 7 7 ILE HG12 H 1 1.44 . . 2 . . . . . . . . 4180 1 46 . 1 1 7 7 ILE HG13 H 1 1.24 . . 2 . . . . . . . . 4180 1 47 . 1 1 7 7 ILE HG21 H 1 0.93 . . 1 . . . . . . . . 4180 1 48 . 1 1 7 7 ILE HG22 H 1 0.93 . . 1 . . . . . . . . 4180 1 49 . 1 1 7 7 ILE HG23 H 1 0.93 . . 1 . . . . . . . . 4180 1 50 . 1 1 7 7 ILE HD11 H 1 0.93 . . 1 . . . . . . . . 4180 1 51 . 1 1 7 7 ILE HD12 H 1 0.93 . . 1 . . . . . . . . 4180 1 52 . 1 1 7 7 ILE HD13 H 1 0.93 . . 1 . . . . . . . . 4180 1 53 . 1 1 8 8 ARG H H 1 8.37 . . 1 . . . . . . . . 4180 1 54 . 1 1 8 8 ARG HA H 1 4.29 . . 1 . . . . . . . . 4180 1 55 . 1 1 8 8 ARG HB2 H 1 1.82 . . 1 . . . . . . . . 4180 1 56 . 1 1 8 8 ARG HB3 H 1 1.82 . . 1 . . . . . . . . 4180 1 57 . 1 1 8 8 ARG HG2 H 1 1.66 . . 1 . . . . . . . . 4180 1 58 . 1 1 8 8 ARG HG3 H 1 1.66 . . 1 . . . . . . . . 4180 1 59 . 1 1 8 8 ARG HD2 H 1 3.22 . . 1 . . . . . . . . 4180 1 60 . 1 1 8 8 ARG HD3 H 1 3.22 . . 1 . . . . . . . . 4180 1 61 . 1 1 8 8 ARG HE H 1 7.45 . . 1 . . . . . . . . 4180 1 62 . 1 1 9 9 LEU H H 1 8.11 . . 1 . . . . . . . . 4180 1 63 . 1 1 9 9 LEU HA H 1 4.37 . . 1 . . . . . . . . 4180 1 64 . 1 1 9 9 LEU HB2 H 1 1.69 . . 1 . . . . . . . . 4180 1 65 . 1 1 9 9 LEU HB3 H 1 1.69 . . 1 . . . . . . . . 4180 1 66 . 1 1 9 9 LEU HG H 1 1.60 . . 1 . . . . . . . . 4180 1 67 . 1 1 9 9 LEU HD11 H 1 0.94 . . 2 . . . . . . . . 4180 1 68 . 1 1 9 9 LEU HD12 H 1 0.94 . . 2 . . . . . . . . 4180 1 69 . 1 1 9 9 LEU HD13 H 1 0.94 . . 2 . . . . . . . . 4180 1 70 . 1 1 9 9 LEU HD21 H 1 0.88 . . 2 . . . . . . . . 4180 1 71 . 1 1 9 9 LEU HD22 H 1 0.88 . . 2 . . . . . . . . 4180 1 72 . 1 1 9 9 LEU HD23 H 1 0.88 . . 2 . . . . . . . . 4180 1 73 . 1 1 10 10 VAL H H 1 7.99 . . 1 . . . . . . . . 4180 1 74 . 1 1 10 10 VAL HA H 1 4.09 . . 1 . . . . . . . . 4180 1 75 . 1 1 10 10 VAL HB H 1 2.09 . . 1 . . . . . . . . 4180 1 76 . 1 1 10 10 VAL HG11 H 1 0.95 . . 1 . . . . . . . . 4180 1 77 . 1 1 10 10 VAL HG12 H 1 0.95 . . 1 . . . . . . . . 4180 1 78 . 1 1 10 10 VAL HG13 H 1 0.95 . . 1 . . . . . . . . 4180 1 79 . 1 1 10 10 VAL HG21 H 1 0.95 . . 1 . . . . . . . . 4180 1 80 . 1 1 10 10 VAL HG22 H 1 0.95 . . 1 . . . . . . . . 4180 1 81 . 1 1 10 10 VAL HG23 H 1 0.95 . . 1 . . . . . . . . 4180 1 82 . 1 1 11 11 GLN H H 1 8.49 . . 1 . . . . . . . . 4180 1 83 . 1 1 11 11 GLN HA H 1 4.35 . . 1 . . . . . . . . 4180 1 84 . 1 1 11 11 GLN HB2 H 1 2.14 . . 2 . . . . . . . . 4180 1 85 . 1 1 11 11 GLN HB3 H 1 2.02 . . 2 . . . . . . . . 4180 1 86 . 1 1 11 11 GLN HG2 H 1 2.28 . . 1 . . . . . . . . 4180 1 87 . 1 1 11 11 GLN HG3 H 1 2.28 . . 1 . . . . . . . . 4180 1 88 . 1 1 12 12 GLY H H 1 8.42 . . 1 . . . . . . . . 4180 1 89 . 1 1 12 12 GLY HA2 H 1 3.94 . . 1 . . . . . . . . 4180 1 90 . 1 1 12 12 GLY HA3 H 1 3.94 . . 1 . . . . . . . . 4180 1 stop_ save_