data_5488 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5488 _Entry.Title ; Backbone and 1H assignments for Tachyplesin I, phenylalanine mutant ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-08-02 _Entry.Accession_date 2002-08-02 _Entry.Last_release_date 2002-11-04 _Entry.Original_release_date 2002-11-04 _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 Alain Laederach . . . 5488 2 Amy Andreotti . H . 5488 3 Donald Fulton . B . 5488 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5488 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 72 5488 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 . . 2002-11-04 2002-08-02 original author . 5488 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5486 'Tachyplesin I, Wild type' 5488 BMRB 5487 'Tachyplesin I, tyrosine mutant' 5488 BMRB 5489 'Tachyplesin I, alanine mutant' 5488 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5488 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 41 _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 12359 _Citation.Page_last 12368 _Citation.Year 2002 _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 Alain Laederach . . . 5488 1 2 Amy Andreotti . H . 5488 1 3 Donald Fulton . B . 5488 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Tachyplesin I' 5488 1 'beta hairpin' 5488 1 'antimicrobial peptide' 5488 1 dodecylphosphocholine 5488 1 NMR 5488 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5488 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9882437 _Citation.Full_citation ; Rao AG. Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch Biochem Biophys. 1999 Jan 1;361(1):127-34. ; _Citation.Title 'Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Arch. Biochem. Biophys.' _Citation.Journal_name_full 'Archives of biochemistry and biophysics' _Citation.Journal_volume 361 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0003-9861 _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 127 _Citation.Page_last 134 _Citation.Year 1999 _Citation.Details ; Tachyplesin is a potent antimicrobial peptide isolated from the hemocytes of the horseshoe crab, Tachypleus tridentatus. Previous studies have shown that the 17-residue peptide has an intrinsic amphipathic structure conferred by two antiparallel beta-sheets held rigidly by two disulfide bonds. Taking its short length into account and the potential of such a small polypeptide to take on multiple conformational states, one may assume that the disulfide bonds are relevant determinants of function. However, in order to gain a global perspective on the tolerance of cysteine residues in tachyplesin to amino acid substitutions, a series of linear peptides have been synthesized and their physicochemical properties analyzed. In these linear peptides, the cysteines have been replaced with amino acids possessing different side-chain properties, i.e., aliphatic hydrophobic (Ala, Leu, Ile, Val, and Met), aromatic hydrophobic (Phe and Tyr), and acidic (Asp). Activity assays using natural and synthetic membranes, and conformational measurements, highlight the subtle influence and variability of the amino acid side-chain properties on peptide structure. While an unequivocal interpretation of the results will have to await more refined structural measurements, our results indicate that a rigidly held disulfide-bonded beta-pleated sheet structure may not be absolutely essential for antimicrobial activity. Furthermore, the results challenge the accepted dogma of structure-activity relationships among antimicrobial peptides and suggest that the maintenance of peptide hydrophobic-hydrophilic balance may be a critical parameter, in addition to structure, in the design of peptides with pharmaceutical relevance. ; 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 'A G' Rao A. G. . 5488 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5488 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8490053 _Citation.Full_citation ; Tamamura H, Kuroda M, Masuda M, Otaka A, Funakoshi S, Nakashima H, Yamamoto N, Waki M, Matsumoto A, Lancelin JM, et al. A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance. Biochim Biophys Acta. 1993 May 13;1163(2):209-16. ; _Citation.Title 'A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochim. Biophys. Acta' _Citation.Journal_name_full 'Biochimica et biophysica acta' _Citation.Journal_volume 1163 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-3002 _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 209 _Citation.Page_last 216 _Citation.Year 1993 _Citation.Details ; The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity. ; 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 H Tamamura H. . . 5488 3 2 M Kuroda M. . . 5488 3 3 M Masuda M. . . 5488 3 4 A Otaka A. . . 5488 3 5 S Funakoshi S. . . 5488 3 6 H Nakashima H. . . 5488 3 7 N Yamamoto N. . . 5488 3 8 M Waki M. . . 5488 3 9 A Matsumoto A. . . 5488 3 10 'J M' Lancelin J. M. . 5488 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_TP _Assembly.Sf_category assembly _Assembly.Sf_framecode system_TP _Assembly.Entry_ID 5488 _Assembly.ID 1 _Assembly.Name 'Tachyplesin I, phenylalanine mutant' _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 'Solution structures were not computed for TPF4 and TPA4.' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID Monomer 5488 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 'Tachyplesin I, phenylalanine mutant' 1 $TP . . . native . . . . . 5488 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 1MA2 . . . . . . 5488 1 . PDB 1MA4 . . . . . . 5488 1 . PDB 1MA5 . . . . . . 5488 1 . PDB 1MA6 . . . . . . 5488 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Tachyplesin I, phenylalanine mutant' system 5488 1 TP abbreviation 5488 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'antimicrobial peptide' 5488 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_TP _Entity.Sf_category entity _Entity.Sf_framecode TP _Entity.Entry_ID 5488 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Tachyplesin I, phenylalanine mutant' _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 KWFFRVFYRGIFYRRFR _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 17 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _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 ; Wild type, has two disulfide bridges (C3-C16, and C7-C12). Wild Type, TPY4 and TPF4 adopt beta-hairpins. TPY4, TPF4 and TPA4 are mutants in which the four Cyteine residues are uniformly mutated to tyrosine, phenylalanine, and alanine, respectively. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2005-12-09 loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Tachyplesin I, phenylalanine mutant' common 5488 1 TP abbreviation 5488 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 . LYS . 5488 1 2 . TRP . 5488 1 3 . PHE . 5488 1 4 . PHE . 5488 1 5 . ARG . 5488 1 6 . VAL . 5488 1 7 . PHE . 5488 1 8 . TYR . 5488 1 9 . ARG . 5488 1 10 . GLY . 5488 1 11 . ILE . 5488 1 12 . PHE . 5488 1 13 . TYR . 5488 1 14 . ARG . 5488 1 15 . ARG . 5488 1 16 . PHE . 5488 1 17 . ARG . 5488 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 . LYS 1 1 5488 1 . TRP 2 2 5488 1 . PHE 3 3 5488 1 . PHE 4 4 5488 1 . ARG 5 5 5488 1 . VAL 6 6 5488 1 . PHE 7 7 5488 1 . TYR 8 8 5488 1 . ARG 9 9 5488 1 . GLY 10 10 5488 1 . ILE 11 11 5488 1 . PHE 12 12 5488 1 . TYR 13 13 5488 1 . ARG 14 14 5488 1 . ARG 15 15 5488 1 . PHE 16 16 5488 1 . ARG 17 17 5488 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 5488 _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 $TP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 'The peptide was synthetically produced and is not natural.' . . 5488 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 5488 _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 $TP . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5488 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_water_sample _Sample.Sf_category sample _Sample.Sf_framecode water_sample _Sample.Entry_ID 5488 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'All experiments in water were done in these conditions.' _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 'Tachyplesin I, phenylalanine mutant' . . . 1 $TP . . . 0.5 1.0 mM . . . . 5488 1 2 TFA . . . . . . . 0.15 . . % . . . . 5488 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_Water_25C _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_Water_25C _Sample_condition_list.Entry_ID 5488 _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 3.0 0.2 n/a 5488 1 temperature 298 1 K 5488 1 'ionic strength' 0.0015 0.0001 % 5488 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5488 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5488 _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 Bruker DRX . 500 . . . 5488 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 5488 _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' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5488 1 2 '2D 1H-1H TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5488 1 3 '2D 1H-1H ROESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5488 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 5488 _NMR_spec_expt.ID 1 _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 . 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 5488 _NMR_spec_expt.ID 2 _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 . 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 5488 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '2D 1H-1H 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_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5488 _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 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5488 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_Shift_phenylalanine_mutant_in_water _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode Shift_phenylalanine_mutant_in_water _Assigned_chem_shift_list.Entry_ID 5488 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_Water_25C _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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 $water_sample . 5488 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 LYS HA H 1 3.927 0.001 . 1 . . . . . . . . 5488 1 2 . 1 1 2 2 TRP H H 1 8.728 0.001 . 1 . . . . . . . . 5488 1 3 . 1 1 2 2 TRP HA H 1 4.636 0.001 . 1 . . . . . . . . 5488 1 4 . 1 1 2 2 TRP HB3 H 1 3.062 0.001 . 2 . . . . . . . . 5488 1 5 . 1 1 2 2 TRP HB2 H 1 3.143 0.001 . 2 . . . . . . . . 5488 1 6 . 1 1 3 3 PHE H H 1 8.035 0.001 . 1 . . . . . . . . 5488 1 7 . 1 1 3 3 PHE HA H 1 4.519 0.001 . 1 . . . . . . . . 5488 1 8 . 1 1 3 3 PHE HB3 H 1 2.737 0.001 . 2 . . . . . . . . 5488 1 9 . 1 1 3 3 PHE HB2 H 1 2.874 0.001 . 2 . . . . . . . . 5488 1 10 . 1 1 4 4 PHE H H 1 8.353 0.001 . 1 . . . . . . . . 5488 1 11 . 1 1 4 4 PHE HA H 1 4.423 0.001 . 1 . . . . . . . . 5488 1 12 . 1 1 4 4 PHE HB2 H 1 2.970 0.001 . 2 . . . . . . . . 5488 1 13 . 1 1 5 5 ARG H H 1 8.181 0.001 . 1 . . . . . . . . 5488 1 14 . 1 1 5 5 ARG HA H 1 4.333 0.001 . 1 . . . . . . . . 5488 1 15 . 1 1 5 5 ARG HB2 H 1 1.655 0.001 . 2 . . . . . . . . 5488 1 16 . 1 1 5 5 ARG HG3 H 1 1.467 0.001 . 2 . . . . . . . . 5488 1 17 . 1 1 5 5 ARG HG2 H 1 1.394 0.001 . 2 . . . . . . . . 5488 1 18 . 1 1 5 5 ARG HD2 H 1 3.019 0.001 . 2 . . . . . . . . 5488 1 19 . 1 1 6 6 VAL H H 1 8.361 0.001 . 1 . . . . . . . . 5488 1 20 . 1 1 6 6 VAL HA H 1 4.140 0.001 . 1 . . . . . . . . 5488 1 21 . 1 1 6 6 VAL HG21 H 1 0.809 0.001 . 4 . . . . . . . . 5488 1 22 . 1 1 6 6 VAL HG22 H 1 0.809 0.001 . 4 . . . . . . . . 5488 1 23 . 1 1 6 6 VAL HG23 H 1 0.809 0.001 . 4 . . . . . . . . 5488 1 24 . 1 1 6 6 VAL HG11 H 1 0.882 0.001 . 4 . . . . . . . . 5488 1 25 . 1 1 6 6 VAL HG12 H 1 0.882 0.001 . 4 . . . . . . . . 5488 1 26 . 1 1 6 6 VAL HG13 H 1 0.882 0.001 . 4 . . . . . . . . 5488 1 27 . 1 1 7 7 PHE H H 1 8.625 0.001 . 1 . . . . . . . . 5488 1 28 . 1 1 7 7 PHE HA H 1 4.731 0.001 . 1 . . . . . . . . 5488 1 29 . 1 1 7 7 PHE HB2 H 1 2.923 0.001 . 2 . . . . . . . . 5488 1 30 . 1 1 8 8 TYR H H 1 8.621 0.001 . 1 . . . . . . . . 5488 1 31 . 1 1 8 8 TYR HA H 1 4.512 0.001 . 1 . . . . . . . . 5488 1 32 . 1 1 8 8 TYR HB2 H 1 2.830 0.001 . 2 . . . . . . . . 5488 1 33 . 1 1 9 9 ARG H H 1 8.675 0.001 . 1 . . . . . . . . 5488 1 34 . 1 1 9 9 ARG HA H 1 3.936 0.001 . 1 . . . . . . . . 5488 1 35 . 1 1 9 9 ARG HB3 H 1 1.516 0.001 . 2 . . . . . . . . 5488 1 36 . 1 1 9 9 ARG HB2 H 1 1.760 0.001 . 2 . . . . . . . . 5488 1 37 . 1 1 9 9 ARG HG2 H 1 1.303 0.001 . 2 . . . . . . . . 5488 1 38 . 1 1 9 9 ARG HD2 H 1 2.827 0.001 . 2 . . . . . . . . 5488 1 39 . 1 1 10 10 GLY H H 1 7.587 0.001 . 1 . . . . . . . . 5488 1 40 . 1 1 10 10 GLY HA3 H 1 3.829 0.001 . 2 . . . . . . . . 5488 1 41 . 1 1 10 10 GLY HA2 H 1 3.972 0.001 . 2 . . . . . . . . 5488 1 42 . 1 1 11 11 ILE H H 1 7.807 0.001 . 1 . . . . . . . . 5488 1 43 . 1 1 11 11 ILE HA H 1 4.117 0.001 . 1 . . . . . . . . 5488 1 44 . 1 1 11 11 ILE HG12 H 1 1.284 0.001 . 4 . . . . . . . . 5488 1 45 . 1 1 11 11 ILE HG13 H 1 1.067 0.001 . 4 . . . . . . . . 5488 1 46 . 1 1 12 12 PHE H H 1 8.458 0.001 . 1 . . . . . . . . 5488 1 47 . 1 1 12 12 PHE HA H 1 4.705 0.001 . 1 . . . . . . . . 5488 1 48 . 1 1 12 12 PHE HB3 H 1 2.901 0.001 . 2 . . . . . . . . 5488 1 49 . 1 1 13 13 TYR H H 1 8.491 0.001 . 1 . . . . . . . . 5488 1 50 . 1 1 13 13 TYR HA H 1 4.473 0.001 . 1 . . . . . . . . 5488 1 51 . 1 1 13 13 TYR HB2 H 1 2.783 0.001 . 2 . . . . . . . . 5488 1 52 . 1 1 14 14 ARG H H 1 8.396 0.001 . 1 . . . . . . . . 5488 1 53 . 1 1 14 14 ARG HA H 1 4.214 0.001 . 1 . . . . . . . . 5488 1 54 . 1 1 14 14 ARG HB2 H 1 1.680 0.001 . 2 . . . . . . . . 5488 1 55 . 1 1 14 14 ARG HG2 H 1 1.541 0.001 . 2 . . . . . . . . 5488 1 56 . 1 1 14 14 ARG HD2 H 1 3.065 0.001 . 2 . . . . . . . . 5488 1 57 . 1 1 15 15 ARG H H 1 8.369 0.001 . 1 . . . . . . . . 5488 1 58 . 1 1 15 15 ARG HA H 1 4.332 0.001 . 1 . . . . . . . . 5488 1 59 . 1 1 15 15 ARG HB3 H 1 1.515 0.001 . 2 . . . . . . . . 5488 1 60 . 1 1 15 15 ARG HB2 H 1 1.635 0.001 . 2 . . . . . . . . 5488 1 61 . 1 1 15 15 ARG HG2 H 1 1.396 0.001 . 2 . . . . . . . . 5488 1 62 . 1 1 15 15 ARG HD2 H 1 3.039 0.001 . 2 . . . . . . . . 5488 1 63 . 1 1 16 16 PHE H H 1 8.528 0.001 . 1 . . . . . . . . 5488 1 64 . 1 1 16 16 PHE HA H 1 4.709 0.001 . 1 . . . . . . . . 5488 1 65 . 1 1 16 16 PHE HB3 H 1 2.899 0.001 . 2 . . . . . . . . 5488 1 66 . 1 1 16 16 PHE HB2 H 1 3.036 0.001 . 2 . . . . . . . . 5488 1 67 . 1 1 17 17 ARG H H 1 8.454 0.001 . 1 . . . . . . . . 5488 1 68 . 1 1 17 17 ARG HA H 1 4.240 0.001 . 1 . . . . . . . . 5488 1 69 . 1 1 17 17 ARG HB3 H 1 1.608 0.001 . 2 . . . . . . . . 5488 1 70 . 1 1 17 17 ARG HB2 H 1 1.773 0.001 . 2 . . . . . . . . 5488 1 71 . 1 1 17 17 ARG HG2 H 1 1.444 0.001 . 2 . . . . . . . . 5488 1 72 . 1 1 17 17 ARG HD2 H 1 3.001 0.001 . 2 . . . . . . . . 5488 1 stop_ loop_ _Ambiguous_atom_chem_shift.Ambiguous_shift_set_ID _Ambiguous_atom_chem_shift.Atom_chem_shift_ID _Ambiguous_atom_chem_shift.Entry_ID _Ambiguous_atom_chem_shift.Assigned_chem_shift_list_ID 1 26 5488 1 1 25 5488 1 1 24 5488 1 1 23 5488 1 1 22 5488 1 1 21 5488 1 2 45 5488 1 2 44 5488 1 stop_ save_