data_371 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 371 _Entry.Title ; Secondary Structure of a Leucine Zipper Determined by Nuclear Magnetic Resonance Spectroscopy ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _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 Terrence Oas . G. . 371 2 Lawrence McIntosh . P. . 371 3 Erin O'Shea . . . 371 4 Frederick Dahlquist . W. . 371 5 Peter Kim . S. . 371 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 371 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 125 371 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 5 . . 2010-06-11 . revision BMRB 'Complete natural source information' 371 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 371 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 371 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 371 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 371 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 371 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Oas, Terrence G., McIntosh, Lawrence P., O'Shea, Erin, Dahlquist, Frederick W., Kim, Peter S., "Secondary Structure of a Leucine Zipper Determined by Nuclear Magnetic Resonance Spectroscopy," Biochemistry 29, 2891-2894 (1990). ; _Citation.Title ; Secondary Structure of a Leucine Zipper Determined by Nuclear Magnetic Resonance Spectroscopy ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 29 _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 2891 _Citation.Page_last 2894 _Citation.Year 1990 _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 Terrence Oas . G. . 371 1 2 Lawrence McIntosh . P. . 371 1 3 Erin O'Shea . . . 371 1 4 Frederick Dahlquist . W. . 371 1 5 Peter Kim . S. . 371 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_transcriptional_regulator_GCN4 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_transcriptional_regulator_GCN4 _Assembly.Entry_ID 371 _Assembly.ID 1 _Assembly.Name 'transcriptional regulator GCN4' _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 . _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 'transcriptional regulator GCN4' 1 $transcriptional_regulator_GCN4 . . . . . . . . . 371 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'transcriptional regulator GCN4' system 371 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_transcriptional_regulator_GCN4 _Entity.Sf_category entity _Entity.Sf_framecode transcriptional_regulator_GCN4 _Entity.Entry_ID 371 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'transcriptional regulator GCN4' _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 ; XMKQLEDKVEELLSKNYHLE NEVARLKKLVGER ; _Entity.Polymer_seq_one_letter_code ; XMKQLEDKVEELLSKNYHLE NEVARLKKLVGER ; _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 33 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1396 . "transcriptional regulator GCN4" . . . . . 96.97 61 100.00 100.00 6.77e-12 . . . . 371 1 2 no BMRB 1397 . "transcriptional regulator GCN4" . . . . . 96.97 61 100.00 100.00 6.77e-12 . . . . 371 1 3 no BMRB 1398 . "transcriptional regulator GCN4" . . . . . 96.97 61 100.00 100.00 6.77e-12 . . . . 371 1 4 no BMRB 1399 . "transcriptional regulator GCN4" . . . . . 96.97 61 100.00 100.00 6.77e-12 . . . . 371 1 5 no BMRB 1451 . "transcriptional regulator GCN4" . . . . . 96.97 61 100.00 100.00 6.77e-12 . . . . 371 1 6 no BMRB 1452 . "transcriptional regulator GCN4" . . . . . 96.97 61 100.00 100.00 6.77e-12 . . . . 371 1 7 no BMRB 1453 . "transcriptional regulator GCN4" . . . . . 96.97 61 100.00 100.00 6.77e-12 . . . . 371 1 8 no BMRB 1454 . "transcriptional regulator GCN4" . . . . . 96.97 61 100.00 100.00 6.77e-12 . . . . 371 1 9 no BMRB 15316 . GCN4p-wt . . . . . 93.94 33 100.00 100.00 1.29e-10 . . . . 371 1 10 no BMRB 17511 . LZ-GCN4 . . . . . 96.97 36 100.00 100.00 2.30e-11 . . . . 371 1 11 no BMRB 2062 . "transcriptional regulator GCN4-p2N" . . . . . 96.97 37 100.00 100.00 2.26e-11 . . . . 371 1 12 no PDB 1DGC . "The X-Ray Structure Of The Gcn4-Bzip Bound To AtfCREB SITE Dna Shows The Complex Depends On Dna Flexibility" . . . . . 96.97 62 100.00 100.00 6.68e-12 . . . . 371 1 13 no PDB 1LD4 . "Placement Of The Structural Proteins In Sindbis Virus" . . . . . 96.97 57 100.00 100.00 7.20e-12 . . . . 371 1 14 no PDB 1LLM . "Crystal Structure Of A Zif23-Gcn4 Chimera Bound To Dna" . . . . . 87.88 88 100.00 100.00 2.69e-09 . . . . 371 1 15 no PDB 1NKN . "Visualizing An Unstable Coiled Coil: The Crystal Structure Of An N-Terminal Segment Of The Scallop Myosin Rod" . . . . . 96.97 89 100.00 100.00 2.64e-11 . . . . 371 1 16 no PDB 1YSA . "The Gcn4 Basic Region Leucine Zipper Binds Dna As A Dimer Of Uninterrupted Alpha Helices: Crystal Structure Of The Protein-Dna " . . . . . 96.97 58 100.00 100.00 8.71e-12 . . . . 371 1 17 no PDB 1ZTA . "The Solution Structure Of A Leucine-Zipper Motif Peptide" . . . . . 96.97 35 100.00 100.00 2.13e-11 . . . . 371 1 18 no PDB 2DGC . "Gcn4 Basic Domain, Leucine Zipper Complexed With AtfCREB Site Dna" . . . . . 96.97 63 100.00 100.00 6.96e-12 . . . . 371 1 19 no PDB 2EFR . "Crystal Structure Of The C-Terminal Tropomyosin Fragment With N- And C-Terminal Extensions Of The Leucine Zipper At 1.8 Angstro" . . . . . 84.85 155 100.00 100.00 4.21e-08 . . . . 371 1 20 no PDB 2EFS . "Crystal Structure Of The C-Terminal Tropomyosin Fragment With N- And C-Terminal Extensions Of The Leucine Zipper At 2.0 Angstro" . . . . . 84.85 155 100.00 100.00 4.21e-08 . . . . 371 1 21 no PDB 2OVN . "Nmr Structure Of The Gcn4 Trigger Peptide" . . . . . 51.52 17 100.00 100.00 2.08e-01 . . . . 371 1 22 no PDB 2ZTA . "X-Ray Structure Of The Gcn4 Leucine Zipper, A Two-Stranded, Parallel Coiled Coil" . . . . . 96.97 34 100.00 100.00 2.25e-11 . . . . 371 1 23 no PDB 3BAS . "Crystal Structure Of The N-Terminal Region Of The Scallop Myosin Rod, Monoclinic (C2) Form" . . . . . 96.97 89 100.00 100.00 2.64e-11 . . . . 371 1 24 no PDB 3BAT . "Crystal Structure Of The N-Terminal Region Of The Scallop Myosin Rod, Monoclinic (P21) Form" . . . . . 96.97 89 100.00 100.00 2.64e-11 . . . . 371 1 25 no PDB 3I5C . "Crystal Structure Of A Fusion Protein Containing The Leucine Zipper Of Gcn4 And The Ggdef Domain Of Wspr From Pseudomonas Aerug" . . . . . 87.88 206 100.00 100.00 5.39e-09 . . . . 371 1 26 no PDB 3P8M . "Human Dynein Light Chain (Dynll2) In Complex With An In Vitro Evolved Peptide Dimerized By Leucine Zipper" . . . . . 96.97 46 100.00 100.00 7.71e-12 . . . . 371 1 27 no PDB 4DMD . "Gcn4 Leucine Zipper Domain In A Dimeric Oligomerization State" . . . . . 96.97 34 100.00 100.00 2.25e-11 . . . . 371 1 28 no PDB 4DME . "Gcn4 Leucine Zipper Domain In A Trimeric Oligomerization State" . . . . . 96.97 35 100.00 100.00 2.27e-11 . . . . 371 1 29 no DBJ GAA22815 . "K7_Gcn4p [Saccharomyces cerevisiae Kyokai no. 7]" . . . . . 96.97 281 100.00 100.00 1.29e-11 . . . . 371 1 30 no EMBL CAE52206 . "Gcn4p [Saccharomyces cerevisiae]" . . . . . 96.97 281 100.00 100.00 2.05e-09 . . . . 371 1 31 no EMBL CAE52207 . "Gcn4p [Saccharomyces cerevisiae]" . . . . . 96.97 281 100.00 100.00 2.05e-09 . . . . 371 1 32 no EMBL CAE52208 . "Gcn4p [Saccharomyces cerevisiae]" . . . . . 96.97 281 100.00 100.00 1.66e-09 . . . . 371 1 33 no EMBL CAE52209 . "Gcn4p [Saccharomyces cerevisiae]" . . . . . 96.97 281 100.00 100.00 2.05e-09 . . . . 371 1 34 no EMBL CAE52210 . "Gcn4p [Saccharomyces cerevisiae]" . . . . . 96.97 281 100.00 100.00 1.29e-11 . . . . 371 1 35 no GB AAA34640 . "GCN4 protein [Saccharomyces cerevisiae]" . . . . . 96.97 281 100.00 100.00 2.16e-09 . . . . 371 1 36 no GB AAB64486 . "Transcriptional activator of amino acid biosynthetic genes [Saccharomyces cerevisiae]" . . . . . 96.97 281 100.00 100.00 2.16e-09 . . . . 371 1 37 no GB AAC33186 . "hinge-region and leucine-zipper with N-terminal PelB-leader and C-terminal hexahistidine tag [synthetic construct]" . . . . . 96.97 84 100.00 100.00 5.22e-12 . . . . 371 1 38 no GB AAD37724 . "PelB-IgG kappa light chain fusion protein [Cloning vector pCLZip]" . . . . . 96.97 192 100.00 100.00 1.43e-11 . . . . 371 1 39 no GB AAK07887 . "cI-GCN4 repressor fusion protein [Cloning vector pJH370]" . . . . . 96.97 166 100.00 100.00 3.40e-11 . . . . 371 1 40 no REF NP_010907 . "amino acid starvation-responsive transcription factor GCN4 [Saccharomyces cerevisiae S288c]" . . . . . 96.97 281 100.00 100.00 2.16e-09 . . . . 371 1 41 no SP P03069 . "RecName: Full=General control protein GCN4; AltName: Full=Amino acid biosynthesis regulatory protein" . . . . . 96.97 281 100.00 100.00 2.16e-09 . . . . 371 1 42 no TPG DAA07643 . "TPA: amino acid starvation-responsive transcription factor GCN4 [Saccharomyces cerevisiae S288c]" . . . . . 96.97 281 100.00 100.00 2.16e-09 . . . . 371 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'residues 239-271' variant 371 1 'transcriptional regulator GCN4' common 371 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 . X . 371 1 2 . MET . 371 1 3 . LYS . 371 1 4 . GLN . 371 1 5 . LEU . 371 1 6 . GLU . 371 1 7 . ASP . 371 1 8 . LYS . 371 1 9 . VAL . 371 1 10 . GLU . 371 1 11 . GLU . 371 1 12 . LEU . 371 1 13 . LEU . 371 1 14 . SER . 371 1 15 . LYS . 371 1 16 . ASN . 371 1 17 . TYR . 371 1 18 . HIS . 371 1 19 . LEU . 371 1 20 . GLU . 371 1 21 . ASN . 371 1 22 . GLU . 371 1 23 . VAL . 371 1 24 . ALA . 371 1 25 . ARG . 371 1 26 . LEU . 371 1 27 . LYS . 371 1 28 . LYS . 371 1 29 . LEU . 371 1 30 . VAL . 371 1 31 . GLY . 371 1 32 . GLU . 371 1 33 . ARG . 371 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 . X 1 1 371 1 . MET 2 2 371 1 . LYS 3 3 371 1 . GLN 4 4 371 1 . LEU 5 5 371 1 . GLU 6 6 371 1 . ASP 7 7 371 1 . LYS 8 8 371 1 . VAL 9 9 371 1 . GLU 10 10 371 1 . GLU 11 11 371 1 . LEU 12 12 371 1 . LEU 13 13 371 1 . SER 14 14 371 1 . LYS 15 15 371 1 . ASN 16 16 371 1 . TYR 17 17 371 1 . HIS 18 18 371 1 . LEU 19 19 371 1 . GLU 20 20 371 1 . ASN 21 21 371 1 . GLU 22 22 371 1 . VAL 23 23 371 1 . ALA 24 24 371 1 . ARG 25 25 371 1 . LEU 26 26 371 1 . LYS 27 27 371 1 . LYS 28 28 371 1 . LEU 29 29 371 1 . VAL 30 30 371 1 . GLY 31 31 371 1 . GLU 32 32 371 1 . ARG 33 33 371 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 371 _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 $transcriptional_regulator_GCN4 . 4932 organism . 'Saccharomyces cerevisiae' yeast . . Eukaryota Fungi Saccharomyces cerevisiae KY803 . . . . . . . . . . . . . . . . . . . . 371 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 371 _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 $transcriptional_regulator_GCN4 . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 371 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 371 _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 . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 371 _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 . na 371 1 temperature 293 . K 371 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 371 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 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 371 _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 unknown unknown . 0 'spectrometer information not available' . . 371 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 371 _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 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 371 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 371 _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 . TSP . . . . . ppm -.01 . . . . . . 1 $entry_citation . . 1 $entry_citation 371 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_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 371 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_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 . 371 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 MET H H 1 8.61 . . 1 . . . . . . . . 371 1 2 . 1 1 2 2 MET HA H 1 4.07 . . 1 . . . . . . . . 371 1 3 . 1 1 2 2 MET HB2 H 1 2.08 . . 1 . . . . . . . . 371 1 4 . 1 1 2 2 MET HB3 H 1 2.08 . . 1 . . . . . . . . 371 1 5 . 1 1 3 3 LYS H H 1 7.83 . . 1 . . . . . . . . 371 1 6 . 1 1 3 3 LYS HA H 1 4.14 . . 1 . . . . . . . . 371 1 7 . 1 1 3 3 LYS HB2 H 1 1.84 . . 1 . . . . . . . . 371 1 8 . 1 1 3 3 LYS HB3 H 1 1.84 . . 1 . . . . . . . . 371 1 9 . 1 1 4 4 GLN H H 1 7.78 . . 1 . . . . . . . . 371 1 10 . 1 1 4 4 GLN HA H 1 4.13 . . 1 . . . . . . . . 371 1 11 . 1 1 4 4 GLN HB2 H 1 2.22 . . 1 . . . . . . . . 371 1 12 . 1 1 4 4 GLN HB3 H 1 2.22 . . 1 . . . . . . . . 371 1 13 . 1 1 5 5 LEU H H 1 8.23 . . 1 . . . . . . . . 371 1 14 . 1 1 5 5 LEU HA H 1 4.08 . . 1 . . . . . . . . 371 1 15 . 1 1 5 5 LEU HB2 H 1 2.13 . . 2 . . . . . . . . 371 1 16 . 1 1 5 5 LEU HB3 H 1 1.34 . . 2 . . . . . . . . 371 1 17 . 1 1 6 6 GLU H H 1 8.56 . . 1 . . . . . . . . 371 1 18 . 1 1 6 6 GLU HA H 1 3.86 . . 1 . . . . . . . . 371 1 19 . 1 1 6 6 GLU HB2 H 1 2.28 . . 1 . . . . . . . . 371 1 20 . 1 1 6 6 GLU HB3 H 1 2.28 . . 1 . . . . . . . . 371 1 21 . 1 1 7 7 ASP H H 1 8.73 . . 1 . . . . . . . . 371 1 22 . 1 1 7 7 ASP HA H 1 4.39 . . 1 . . . . . . . . 371 1 23 . 1 1 7 7 ASP HB2 H 1 2.85 . . 2 . . . . . . . . 371 1 24 . 1 1 7 7 ASP HB3 H 1 2.68 . . 2 . . . . . . . . 371 1 25 . 1 1 8 8 LYS H H 1 8.03 . . 1 . . . . . . . . 371 1 26 . 1 1 8 8 LYS HA H 1 4.23 . . 1 . . . . . . . . 371 1 27 . 1 1 8 8 LYS HB2 H 1 2.13 . . 2 . . . . . . . . 371 1 28 . 1 1 8 8 LYS HB3 H 1 2.03 . . 2 . . . . . . . . 371 1 29 . 1 1 9 9 VAL H H 1 8.51 . . 1 . . . . . . . . 371 1 30 . 1 1 9 9 VAL HA H 1 3.42 . . 1 . . . . . . . . 371 1 31 . 1 1 9 9 VAL HB H 1 2.27 . . 1 . . . . . . . . 371 1 32 . 1 1 10 10 GLU H H 1 7.75 . . 1 . . . . . . . . 371 1 33 . 1 1 10 10 GLU HA H 1 4 . . 1 . . . . . . . . 371 1 34 . 1 1 10 10 GLU HB2 H 1 2.18 . . 1 . . . . . . . . 371 1 35 . 1 1 10 10 GLU HB3 H 1 2.18 . . 1 . . . . . . . . 371 1 36 . 1 1 11 11 GLU H H 1 8.24 . . 1 . . . . . . . . 371 1 37 . 1 1 11 11 GLU HA H 1 4.11 . . 1 . . . . . . . . 371 1 38 . 1 1 11 11 GLU HB2 H 1 2.3 . . 2 . . . . . . . . 371 1 39 . 1 1 11 11 GLU HB3 H 1 2.28 . . 2 . . . . . . . . 371 1 40 . 1 1 12 12 LEU H H 1 8.74 . . 1 . . . . . . . . 371 1 41 . 1 1 12 12 LEU HA H 1 4.01 . . 1 . . . . . . . . 371 1 42 . 1 1 12 12 LEU HB2 H 1 2.09 . . 2 . . . . . . . . 371 1 43 . 1 1 12 12 LEU HB3 H 1 1.27 . . 2 . . . . . . . . 371 1 44 . 1 1 13 13 LEU H H 1 9.05 . . 1 . . . . . . . . 371 1 45 . 1 1 13 13 LEU HA H 1 4.06 . . 1 . . . . . . . . 371 1 46 . 1 1 13 13 LEU HB2 H 1 1.96 . . 2 . . . . . . . . 371 1 47 . 1 1 13 13 LEU HB3 H 1 1.46 . . 2 . . . . . . . . 371 1 48 . 1 1 14 14 SER H H 1 7.78 . . 1 . . . . . . . . 371 1 49 . 1 1 14 14 SER HA H 1 4.36 . . 1 . . . . . . . . 371 1 50 . 1 1 14 14 SER HB2 H 1 4.09 . . 1 . . . . . . . . 371 1 51 . 1 1 14 14 SER HB3 H 1 4.09 . . 1 . . . . . . . . 371 1 52 . 1 1 15 15 LYS H H 1 8.33 . . 1 . . . . . . . . 371 1 53 . 1 1 15 15 LYS HA H 1 4.21 . . 1 . . . . . . . . 371 1 54 . 1 1 15 15 LYS HB2 H 1 1.94 . . 1 . . . . . . . . 371 1 55 . 1 1 15 15 LYS HB3 H 1 1.94 . . 1 . . . . . . . . 371 1 56 . 1 1 16 16 ASN H H 1 8.87 . . 1 . . . . . . . . 371 1 57 . 1 1 16 16 ASN HA H 1 4.39 . . 1 . . . . . . . . 371 1 58 . 1 1 16 16 ASN HB2 H 1 3.28 . . 2 . . . . . . . . 371 1 59 . 1 1 16 16 ASN HB3 H 1 2.75 . . 2 . . . . . . . . 371 1 60 . 1 1 17 17 TYR H H 1 8.26 . . 1 . . . . . . . . 371 1 61 . 1 1 17 17 TYR HA H 1 4.39 . . 1 . . . . . . . . 371 1 62 . 1 1 17 17 TYR HB2 H 1 3.28 . . 2 . . . . . . . . 371 1 63 . 1 1 17 17 TYR HB3 H 1 3.15 . . 2 . . . . . . . . 371 1 64 . 1 1 18 18 HIS H H 1 7.93 . . 1 . . . . . . . . 371 1 65 . 1 1 18 18 HIS HA H 1 4.38 . . 1 . . . . . . . . 371 1 66 . 1 1 18 18 HIS HB2 H 1 3.44 . . 1 . . . . . . . . 371 1 67 . 1 1 18 18 HIS HB3 H 1 3.44 . . 1 . . . . . . . . 371 1 68 . 1 1 19 19 LEU H H 1 8.66 . . 1 . . . . . . . . 371 1 69 . 1 1 19 19 LEU HA H 1 3.98 . . 1 . . . . . . . . 371 1 70 . 1 1 19 19 LEU HB2 H 1 2.16 . . 2 . . . . . . . . 371 1 71 . 1 1 19 19 LEU HB3 H 1 1.33 . . 2 . . . . . . . . 371 1 72 . 1 1 20 20 GLU H H 1 8.88 . . 1 . . . . . . . . 371 1 73 . 1 1 20 20 GLU HA H 1 3.94 . . 1 . . . . . . . . 371 1 74 . 1 1 20 20 GLU HB2 H 1 2.19 . . 2 . . . . . . . . 371 1 75 . 1 1 20 20 GLU HB3 H 1 2.01 . . 2 . . . . . . . . 371 1 76 . 1 1 21 21 ASN H H 1 7.77 . . 1 . . . . . . . . 371 1 77 . 1 1 21 21 ASN HA H 1 4.44 . . 1 . . . . . . . . 371 1 78 . 1 1 21 21 ASN HB2 H 1 2.84 . . 2 . . . . . . . . 371 1 79 . 1 1 21 21 ASN HB3 H 1 2.76 . . 2 . . . . . . . . 371 1 80 . 1 1 22 22 GLU H H 1 8.04 . . 1 . . . . . . . . 371 1 81 . 1 1 22 22 GLU HA H 1 4.39 . . 1 . . . . . . . . 371 1 82 . 1 1 22 22 GLU HB2 H 1 2.16 . . 2 . . . . . . . . 371 1 83 . 1 1 22 22 GLU HB3 H 1 2.02 . . 2 . . . . . . . . 371 1 84 . 1 1 23 23 VAL H H 1 8.68 . . 1 . . . . . . . . 371 1 85 . 1 1 23 23 VAL HA H 1 3.39 . . 1 . . . . . . . . 371 1 86 . 1 1 23 23 VAL HB H 1 2.12 . . 1 . . . . . . . . 371 1 87 . 1 1 24 24 ALA H H 1 7.78 . . 1 . . . . . . . . 371 1 88 . 1 1 24 24 ALA HA H 1 4.01 . . 1 . . . . . . . . 371 1 89 . 1 1 24 24 ALA HB1 H 1 1.49 . . 1 . . . . . . . . 371 1 90 . 1 1 24 24 ALA HB2 H 1 1.49 . . 1 . . . . . . . . 371 1 91 . 1 1 24 24 ALA HB3 H 1 1.49 . . 1 . . . . . . . . 371 1 92 . 1 1 25 25 ARG H H 1 7.94 . . 1 . . . . . . . . 371 1 93 . 1 1 25 25 ARG HA H 1 3.98 . . 1 . . . . . . . . 371 1 94 . 1 1 25 25 ARG HB2 H 1 2.13 . . 1 . . . . . . . . 371 1 95 . 1 1 25 25 ARG HB3 H 1 2.13 . . 1 . . . . . . . . 371 1 96 . 1 1 26 26 LEU H H 1 8.47 . . 1 . . . . . . . . 371 1 97 . 1 1 26 26 LEU HA H 1 3.98 . . 1 . . . . . . . . 371 1 98 . 1 1 26 26 LEU HB2 H 1 1.97 . . 2 . . . . . . . . 371 1 99 . 1 1 26 26 LEU HB3 H 1 1.32 . . 2 . . . . . . . . 371 1 100 . 1 1 27 27 LYS H H 1 9.01 . . 1 . . . . . . . . 371 1 101 . 1 1 27 27 LYS HA H 1 3.82 . . 1 . . . . . . . . 371 1 102 . 1 1 27 27 LYS HB2 H 1 1.83 . . 1 . . . . . . . . 371 1 103 . 1 1 27 27 LYS HB3 H 1 1.83 . . 1 . . . . . . . . 371 1 104 . 1 1 28 28 LYS H H 1 7.38 . . 1 . . . . . . . . 371 1 105 . 1 1 28 28 LYS HA H 1 4.13 . . 1 . . . . . . . . 371 1 106 . 1 1 28 28 LYS HB2 H 1 1.97 . . 2 . . . . . . . . 371 1 107 . 1 1 28 28 LYS HB3 H 1 1.9 . . 2 . . . . . . . . 371 1 108 . 1 1 29 29 LEU H H 1 7.49 . . 1 . . . . . . . . 371 1 109 . 1 1 29 29 LEU HA H 1 4.19 . . 1 . . . . . . . . 371 1 110 . 1 1 29 29 LEU HB2 H 1 2.05 . . 2 . . . . . . . . 371 1 111 . 1 1 29 29 LEU HB3 H 1 1.62 . . 2 . . . . . . . . 371 1 112 . 1 1 30 30 VAL H H 1 7.79 . . 1 . . . . . . . . 371 1 113 . 1 1 30 30 VAL HA H 1 4.08 . . 1 . . . . . . . . 371 1 114 . 1 1 30 30 VAL HB H 1 2.24 . . 1 . . . . . . . . 371 1 115 . 1 1 31 31 GLY H H 1 7.88 . . 1 . . . . . . . . 371 1 116 . 1 1 31 31 GLY HA2 H 1 3.9 . . 2 . . . . . . . . 371 1 117 . 1 1 31 31 GLY HA3 H 1 4.08 . . 2 . . . . . . . . 371 1 118 . 1 1 32 32 GLU H H 1 7.96 . . 1 . . . . . . . . 371 1 119 . 1 1 32 32 GLU HA H 1 4.38 . . 1 . . . . . . . . 371 1 120 . 1 1 32 32 GLU HB2 H 1 1.77 . . 1 . . . . . . . . 371 1 121 . 1 1 32 32 GLU HB3 H 1 1.77 . . 1 . . . . . . . . 371 1 122 . 1 1 33 33 ARG H H 1 7.99 . . 1 . . . . . . . . 371 1 123 . 1 1 33 33 ARG HA H 1 4.13 . . 1 . . . . . . . . 371 1 124 . 1 1 33 33 ARG HB2 H 1 1.83 . . 2 . . . . . . . . 371 1 125 . 1 1 33 33 ARG HB3 H 1 1.7 . . 2 . . . . . . . . 371 1 stop_ save_