data_25212 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25212 _Entry.Title ; High-resolution NMR structure of the protegrin-2 docked to DPC Micelles ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-09-10 _Entry.Accession_date 2014-09-10 _Entry.Last_release_date 2016-09-23 _Entry.Original_release_date 2016-09-23 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 Andrey Filippov . V. . . 25212 2 Sergey Efimov . V. . . 25212 3 Vladimir Klochkov . V. . . 25212 4 Oleg Antzutkin . N. . . 25212 5 Konstantin Usachev . S. . . 25212 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 25212 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'Antimicrobial peptide' . 25212 Protegrin . 25212 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25212 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 107 25212 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 2 . . 2016-09-23 2014-09-10 update BMRB 'update entry citation' 25212 1 . . 2014-12-08 2014-09-10 original author 'original release' 25212 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2MUH 'BMRB Entry Tracking System' 25212 stop_ save_ ############### # Citations # ############### save_High-resolution_NMR_structure_of_the_antimicrobial_peptide_protegrin-2_docked_to_DPC_Micelles _Citation.Sf_category citations _Citation.Sf_framecode High-resolution_NMR_structure_of_the_antimicrobial_peptide_protegrin-2_docked_to_DPC_Micelles _Citation.Entry_ID 25212 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 25430060 _Citation.Full_citation . _Citation.Title ; High-resolution NMR structure of the antimicrobial peptide protegrin-2 docked to DPC Micelles ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 61 _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 227 _Citation.Page_last 234 _Citation.Year 2015 _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 Konstantin Usachev . S. . . 25212 1 2 Sergey Efimov . V. . . 25212 1 3 A. Kolosova . A. . . 25212 1 4 Andrey Filippov . V. . . 25212 1 5 Vladimir Klochkov . V. . . 25212 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25212 _Assembly.ID 1 _Assembly.Name 'protegrin-2 docked to DPC Micelles' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _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 PG-2 1 $PG-2 A . yes native no no . . . 25212 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PG-2 _Entity.Sf_category entity _Entity.Sf_framecode PG-2 _Entity.Entry_ID 25212 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name PG-2 _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 ; RGGRLCYCRRRFCVCV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 16 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 1952.423 _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 ARG . 25212 1 2 2 GLY . 25212 1 3 3 GLY . 25212 1 4 4 ARG . 25212 1 5 5 LEU . 25212 1 6 6 CYS . 25212 1 7 7 TYR . 25212 1 8 8 CYS . 25212 1 9 9 ARG . 25212 1 10 10 ARG . 25212 1 11 11 ARG . 25212 1 12 12 PHE . 25212 1 13 13 CYS . 25212 1 14 14 VAL . 25212 1 15 15 CYS . 25212 1 16 16 VAL . 25212 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 25212 1 . GLY 2 2 25212 1 . GLY 3 3 25212 1 . ARG 4 4 25212 1 . LEU 5 5 25212 1 . CYS 6 6 25212 1 . TYR 7 7 25212 1 . CYS 8 8 25212 1 . ARG 9 9 25212 1 . ARG 10 10 25212 1 . ARG 11 11 25212 1 . PHE 12 12 25212 1 . CYS 13 13 25212 1 . VAL 14 14 25212 1 . CYS 15 15 25212 1 . VAL 16 16 25212 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 25212 _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 $PG-2 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 25212 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 25212 _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 $PG-2 . 'chemical synthesis' . . . . . . . . . . . . . . . ; solid-phase peptide synthesis, using amino acids protected by the 9- uorenylmethoxycarbonyl group and with reaction mixture conductivity control. Fmoc-protected amino acids of peptide synthesis grade were purchased from Applied Biosystems, Foster City, CA, USA ; 25212 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_PG-2_sample _Sample.Sf_category sample _Sample.Sf_framecode PG-2_sample _Sample.Entry_ID 25212 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _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 PG-2 'natural abundance' . . 1 $PG-2 . . 4 . . mg . . . . 25212 1 2 H2O 'natural abundance' . . . . . . 90 . . % . . . . 25212 1 3 D2O '[U-99% 2H]' . . . . . . 10 . . % . . . . 25212 1 4 DPC '[U-99% 2H]' . . . . . . 20 . . mg . . . . 25212 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 25212 _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 temperature 293 . K 25212 1 stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 25212 _Software.ID 1 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 25212 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 25212 1 stop_ save_ save_X-PLOR_NIH _Software.Sf_category software _Software.Sf_framecode X-PLOR_NIH _Software.Entry_ID 25212 _Software.ID 2 _Software.Name X-PLOR_NIH _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Schwieters, Kuszewski, Tjandra and Clore' . . 25212 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 25212 2 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 25212 _Software.ID 3 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 25212 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 25212 3 stop_ save_ save_Molmol _Software.Sf_category software _Software.Sf_framecode Molmol _Software.Entry_ID 25212 _Software.ID 4 _Software.Name Molmol _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Koradi, Billeter and Wuthrich' . . 25212 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 25212 4 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 25212 _Software.ID 5 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 25212 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 25212 5 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 25212 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 25212 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 500 . . . 25212 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 25212 _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 NOESY' no . . . . . . . . . . 1 $PG-2_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25212 1 2 '2D 1H-1H TOCSY' no . . . . . . . . . . 1 $PG-2_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25212 1 3 '2D 1H-1H COSY' no . . . . . . . . . . 1 $PG-2_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25212 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_TSP-d4 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode TSP-d4 _Chem_shift_reference.Entry_ID 25212 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details '3-(trimethylsilyl)-propionic-2,2,3,3 2H4 acid' 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 H 1 TSP-d4 protons . . . . ppm 0 internal direct 1.0 . . . . . 25212 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_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 25212 _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 $TSP-d4 _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 2 '2D 1H-1H TOCSY' . . . 25212 1 3 '2D 1H-1H COSY' . . . 25212 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 HA H 1 4.075 0.002 . . . . . A 1 ARG HA . 25212 1 2 . 1 1 1 1 ARG HB2 H 1 1.924 0.004 . . . . . A 1 ARG HB2 . 25212 1 3 . 1 1 1 1 ARG HB3 H 1 1.924 0.004 . . . . . A 1 ARG HB3 . 25212 1 4 . 1 1 1 1 ARG HG2 H 1 1.669 0.004 . . . . . A 1 ARG HG2 . 25212 1 5 . 1 1 1 1 ARG HG3 H 1 1.669 0.004 . . . . . A 1 ARG HG3 . 25212 1 6 . 1 1 1 1 ARG HD2 H 1 3.196 0.004 . . . . . A 1 ARG HD2 . 25212 1 7 . 1 1 1 1 ARG HD3 H 1 3.196 0.004 . . . . . A 1 ARG HD3 . 25212 1 8 . 1 1 1 1 ARG HE H 1 7.403 0.007 . . . . . A 1 ARG HE . 25212 1 9 . 1 1 2 2 GLY H H 1 8.946 0.005 . . . . . A 2 GLY H . 25212 1 10 . 1 1 2 2 GLY HA2 H 1 3.995 0.005 . . . . . A 2 GLY HA2 . 25212 1 11 . 1 1 2 2 GLY HA3 H 1 3.995 0.005 . . . . . A 2 GLY HA3 . 25212 1 12 . 1 1 3 3 GLY H H 1 8.333 0.006 . . . . . A 3 GLY H . 25212 1 13 . 1 1 3 3 GLY HA2 H 1 3.861 0.004 . . . . . A 3 GLY HA2 . 25212 1 14 . 1 1 3 3 GLY HA3 H 1 3.861 0.004 . . . . . A 3 GLY HA3 . 25212 1 15 . 1 1 4 4 ARG H H 1 8.283 0.008 . . . . . A 4 ARG H . 25212 1 16 . 1 1 4 4 ARG HA H 1 4.380 0.010 . . . . . A 4 ARG HA . 25212 1 17 . 1 1 4 4 ARG HB2 H 1 1.738 0.004 . . . . . A 4 ARG HB2 . 25212 1 18 . 1 1 4 4 ARG HB3 H 1 1.738 0.004 . . . . . A 4 ARG HB3 . 25212 1 19 . 1 1 4 4 ARG HG2 H 1 1.596 0.007 . . . . . A 4 ARG HG2 . 25212 1 20 . 1 1 4 4 ARG HG3 H 1 1.596 0.007 . . . . . A 4 ARG HG3 . 25212 1 21 . 1 1 4 4 ARG HD2 H 1 3.105 0.008 . . . . . A 4 ARG HD2 . 25212 1 22 . 1 1 4 4 ARG HD3 H 1 3.105 0.008 . . . . . A 4 ARG HD3 . 25212 1 23 . 1 1 4 4 ARG HE H 1 7.266 0.006 . . . . . A 4 ARG HE . 25212 1 24 . 1 1 5 5 LEU H H 1 8.486 0.013 . . . . . A 5 LEU H . 25212 1 25 . 1 1 5 5 LEU HA H 1 4.550 0.004 . . . . . A 5 LEU HA . 25212 1 26 . 1 1 5 5 LEU HB2 H 1 1.738 0.005 . . . . . A 5 LEU HB2 . 25212 1 27 . 1 1 5 5 LEU HB3 H 1 1.738 0.005 . . . . . A 5 LEU HB3 . 25212 1 28 . 1 1 5 5 LEU HG H 1 1.579 0.007 . . . . . A 5 LEU HG . 25212 1 29 . 1 1 5 5 LEU HD11 H 1 0.897 0.027 . . . . . A 5 LEU HD11 . 25212 1 30 . 1 1 5 5 LEU HD12 H 1 0.897 0.027 . . . . . A 5 LEU HD12 . 25212 1 31 . 1 1 5 5 LEU HD13 H 1 0.897 0.027 . . . . . A 5 LEU HD13 . 25212 1 32 . 1 1 5 5 LEU HD21 H 1 0.897 0.027 . . . . . A 5 LEU HD21 . 25212 1 33 . 1 1 5 5 LEU HD22 H 1 0.897 0.027 . . . . . A 5 LEU HD22 . 25212 1 34 . 1 1 5 5 LEU HD23 H 1 0.897 0.027 . . . . . A 5 LEU HD23 . 25212 1 35 . 1 1 6 6 CYS H H 1 8.298 0.008 . . . . . A 6 CYS H . 25212 1 36 . 1 1 6 6 CYS HA H 1 5.694 0.017 . . . . . A 6 CYS HA . 25212 1 37 . 1 1 6 6 CYS HB2 H 1 2.853 0.012 . . . . . A 6 CYS HB2 . 25212 1 38 . 1 1 6 6 CYS HB3 H 1 2.661 0.006 . . . . . A 6 CYS HB3 . 25212 1 39 . 1 1 7 7 TYR H H 1 8.184 0.009 . . . . . A 7 TYR H . 25212 1 40 . 1 1 7 7 TYR HA H 1 4.675 0.005 . . . . . A 7 TYR HA . 25212 1 41 . 1 1 7 7 TYR HB2 H 1 2.837 0.010 . . . . . A 7 TYR HB2 . 25212 1 42 . 1 1 7 7 TYR HB3 H 1 2.837 0.010 . . . . . A 7 TYR HB3 . 25212 1 43 . 1 1 7 7 TYR HD1 H 1 7.001 0.004 . . . . . A 7 TYR HD1 . 25212 1 44 . 1 1 7 7 TYR HD2 H 1 7.001 0.004 . . . . . A 7 TYR HD2 . 25212 1 45 . 1 1 7 7 TYR HE1 H 1 6.695 0.005 . . . . . A 7 TYR HE1 . 25212 1 46 . 1 1 7 7 TYR HE2 H 1 6.695 0.005 . . . . . A 7 TYR HE2 . 25212 1 47 . 1 1 8 8 CYS H H 1 9.155 0.006 . . . . . A 8 CYS H . 25212 1 48 . 1 1 8 8 CYS HA H 1 5.695 0.012 . . . . . A 8 CYS HA . 25212 1 49 . 1 1 8 8 CYS HB2 H 1 2.858 0.007 . . . . . A 8 CYS HB2 . 25212 1 50 . 1 1 8 8 CYS HB3 H 1 2.661 0.005 . . . . . A 8 CYS HB3 . 25212 1 51 . 1 1 9 9 ARG H H 1 9.231 0.012 . . . . . A 9 ARG H . 25212 1 52 . 1 1 9 9 ARG HA H 1 4.347 0.006 . . . . . A 9 ARG HA . 25212 1 53 . 1 1 9 9 ARG HB2 H 1 1.845 0.006 . . . . . A 9 ARG HB2 . 25212 1 54 . 1 1 9 9 ARG HB3 H 1 1.845 0.006 . . . . . A 9 ARG HB3 . 25212 1 55 . 1 1 9 9 ARG HG2 H 1 1.609 0.008 . . . . . A 9 ARG HG2 . 25212 1 56 . 1 1 9 9 ARG HG3 H 1 1.609 0.008 . . . . . A 9 ARG HG3 . 25212 1 57 . 1 1 9 9 ARG HD2 H 1 3.300 0.006 . . . . . A 9 ARG HD2 . 25212 1 58 . 1 1 9 9 ARG HD3 H 1 3.300 0.006 . . . . . A 9 ARG HD3 . 25212 1 59 . 1 1 9 9 ARG HE H 1 7.754 0.006 . . . . . A 9 ARG HE . 25212 1 60 . 1 1 10 10 ARG H H 1 9.236 0.007 . . . . . A 10 ARG H . 25212 1 61 . 1 1 10 10 ARG HA H 1 3.774 0.007 . . . . . A 10 ARG HA . 25212 1 62 . 1 1 10 10 ARG HB2 H 1 2.044 0.007 . . . . . A 10 ARG HB2 . 25212 1 63 . 1 1 10 10 ARG HB3 H 1 2.044 0.007 . . . . . A 10 ARG HB3 . 25212 1 64 . 1 1 10 10 ARG HG2 H 1 1.655 0.008 . . . . . A 10 ARG HG2 . 25212 1 65 . 1 1 10 10 ARG HG3 H 1 1.655 0.008 . . . . . A 10 ARG HG3 . 25212 1 66 . 1 1 10 10 ARG HD2 H 1 3.273 0.008 . . . . . A 10 ARG HD2 . 25212 1 67 . 1 1 10 10 ARG HD3 H 1 3.273 0.008 . . . . . A 10 ARG HD3 . 25212 1 68 . 1 1 10 10 ARG HE H 1 7.610 0.003 . . . . . A 10 ARG HE . 25212 1 69 . 1 1 11 11 ARG H H 1 8.125 0.008 . . . . . A 11 ARG H . 25212 1 70 . 1 1 11 11 ARG HA H 1 3.971 0.014 . . . . . A 11 ARG HA . 25212 1 71 . 1 1 11 11 ARG HB2 H 1 2.031 0.007 . . . . . A 11 ARG HB2 . 25212 1 72 . 1 1 11 11 ARG HB3 H 1 1.865 0.008 . . . . . A 11 ARG HB3 . 25212 1 73 . 1 1 11 11 ARG HG2 H 1 1.368 0.009 . . . . . A 11 ARG HG2 . 25212 1 74 . 1 1 11 11 ARG HG3 H 1 1.368 0.009 . . . . . A 11 ARG HG3 . 25212 1 75 . 1 1 11 11 ARG HD2 H 1 3.101 0.009 . . . . . A 11 ARG HD2 . 25212 1 76 . 1 1 11 11 ARG HD3 H 1 3.101 0.009 . . . . . A 11 ARG HD3 . 25212 1 77 . 1 1 11 11 ARG HE H 1 7.257 0.008 . . . . . A 11 ARG HE . 25212 1 78 . 1 1 12 12 PHE H H 1 8.478 0.007 . . . . . A 12 PHE H . 25212 1 79 . 1 1 12 12 PHE HA H 1 3.862 0.007 . . . . . A 12 PHE HA . 25212 1 80 . 1 1 12 12 PHE HB2 H 1 2.946 0.004 . . . . . A 12 PHE HB2 . 25212 1 81 . 1 1 12 12 PHE HB3 H 1 2.675 0.004 . . . . . A 12 PHE HB3 . 25212 1 82 . 1 1 13 13 CYS H H 1 8.807 0.004 . . . . . A 13 CYS H . 25212 1 83 . 1 1 13 13 CYS HA H 1 5.674 0.021 . . . . . A 13 CYS HA . 25212 1 84 . 1 1 13 13 CYS HB2 H 1 2.945 0.014 . . . . . A 13 CYS HB2 . 25212 1 85 . 1 1 13 13 CYS HB3 H 1 2.685 0.006 . . . . . A 13 CYS HB3 . 25212 1 86 . 1 1 14 14 VAL H H 1 8.945 0.006 . . . . . A 14 VAL H . 25212 1 87 . 1 1 14 14 VAL HA H 1 4.380 0.007 . . . . . A 14 VAL HA . 25212 1 88 . 1 1 14 14 VAL HB H 1 2.038 0.008 . . . . . A 14 VAL HB . 25212 1 89 . 1 1 14 14 VAL HG11 H 1 1.006 0.011 . . . . . A 14 VAL HG11 . 25212 1 90 . 1 1 14 14 VAL HG12 H 1 1.006 0.011 . . . . . A 14 VAL HG12 . 25212 1 91 . 1 1 14 14 VAL HG13 H 1 1.006 0.011 . . . . . A 14 VAL HG13 . 25212 1 92 . 1 1 14 14 VAL HG21 H 1 1.006 0.011 . . . . . A 14 VAL HG21 . 25212 1 93 . 1 1 14 14 VAL HG22 H 1 1.006 0.011 . . . . . A 14 VAL HG22 . 25212 1 94 . 1 1 14 14 VAL HG23 H 1 1.006 0.011 . . . . . A 14 VAL HG23 . 25212 1 95 . 1 1 15 15 CYS H H 1 8.858 0.005 . . . . . A 15 CYS H . 25212 1 96 . 1 1 15 15 CYS HA H 1 5.565 0.012 . . . . . A 15 CYS HA . 25212 1 97 . 1 1 15 15 CYS HB2 H 1 2.857 0.007 . . . . . A 15 CYS HB2 . 25212 1 98 . 1 1 15 15 CYS HB3 H 1 2.654 0.006 . . . . . A 15 CYS HB3 . 25212 1 99 . 1 1 16 16 VAL H H 1 8.813 0.009 . . . . . A 16 VAL H . 25212 1 100 . 1 1 16 16 VAL HA H 1 4.338 0.007 . . . . . A 16 VAL HA . 25212 1 101 . 1 1 16 16 VAL HB H 1 2.238 0.005 . . . . . A 16 VAL HB . 25212 1 102 . 1 1 16 16 VAL HG11 H 1 0.952 0.009 . . . . . A 16 VAL HG11 . 25212 1 103 . 1 1 16 16 VAL HG12 H 1 0.952 0.009 . . . . . A 16 VAL HG12 . 25212 1 104 . 1 1 16 16 VAL HG13 H 1 0.952 0.009 . . . . . A 16 VAL HG13 . 25212 1 105 . 1 1 16 16 VAL HG21 H 1 0.952 0.009 . . . . . A 16 VAL HG21 . 25212 1 106 . 1 1 16 16 VAL HG22 H 1 0.952 0.009 . . . . . A 16 VAL HG22 . 25212 1 107 . 1 1 16 16 VAL HG23 H 1 0.952 0.009 . . . . . A 16 VAL HG23 . 25212 1 stop_ save_