data_195 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 195 _Entry.Title ; Stereospecific Nuclear Magnetic Resonance Assignments of the Methyl Groups of Valine and Leucine in the DNA-Binding Domain of the 434 Repressor by Biosynthetically Directed Fractional 13C Labeling ; _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 Dario Neri . . . 195 2 Thomas Szyperski . . . 195 3 Gottfried Otting . . . 195 4 Hans Senn . . . 195 5 Kurt Wuthrich . . . 195 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 195 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 28 195 '1H chemical shifts' 84 195 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 . . 2010-06-10 . revision BMRB 'Complete natural source information' 195 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 195 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 195 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 195 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 195 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 195 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Neri, Dario, Szyperski, Thomas, Otting, Gottfried, Senn, Hans, Wuthrich, Kurt, "Stereospecific Nuclear Magnetic Resonance Assignments of the Methyl Groups of Valine and Leucine in the DNA-Binding Domain of the 434 Repressor by Biosynthetically Directed Fractional 13C Labeling," Biochemistry 28, 7510-7516 (1989). ; _Citation.Title ; Stereospecific Nuclear Magnetic Resonance Assignments of the Methyl Groups of Valine and Leucine in the DNA-Binding Domain of the 434 Repressor by Biosynthetically Directed Fractional 13C Labeling ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 28 _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 7510 _Citation.Page_last 7516 _Citation.Year 1989 _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 Dario Neri . . . 195 1 2 Thomas Szyperski . . . 195 1 3 Gottfried Otting . . . 195 1 4 Hans Senn . . . 195 1 5 Kurt Wuthrich . . . 195 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_434_repressor _Assembly.Sf_category assembly _Assembly.Sf_framecode system_434_repressor _Assembly.Entry_ID 195 _Assembly.ID 1 _Assembly.Name '434 repressor' _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 '434 repressor' 1 $434_repressor . . . . . . . . . 195 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID '434 repressor' system 195 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_434_repressor _Entity.Sf_category entity _Entity.Sf_framecode 434_repressor _Entity.Entry_ID 195 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name '434 repressor' _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 ; SISSRVKSKRIQLGLNQAEL AQKVGTTQQSIEQLENGKTK RPRFLPELASALGVSVDWLL NGTSDSNVR ; _Entity.Polymer_seq_one_letter_code ; SISSRVKSKRIQLGLNQAEL AQKVGTTQQSIEQLENGKTK RPRFLPELASALGVSVDWLL NGTSDSNVR ; _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 69 _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 2539 . "434 repressor" . . . . . 100.00 69 100.00 100.00 1.09e-39 . . . . 195 1 2 no PDB 1PER . "The Complex Between Phage 434 Repression Dna-Binding Domain And Operator Site Or3: Structural Differences Between Consensus And" . . . . . 100.00 69 100.00 100.00 1.09e-39 . . . . 195 1 3 no PDB 1PRA . "Determination Of The Nuclear Magnetic Resonance Solution Structure Of The Dna-Binding Domain (Residues 1 To 69) Of The 434 Repr" . . . . . 98.55 69 100.00 100.00 4.15e-39 . . . . 195 1 4 no PDB 1R63 . "Structural Role Of A Buried Salt Bridge In The 434 Repressor Dna-Binding Domain, Nmr, 20 Structures" . . . . . 91.30 63 100.00 100.00 3.25e-35 . . . . 195 1 5 no PDB 1R69 . "Structure Of The Amino-Terminal Domain Of Phage 434 Repressor At 2.0 Angstroms Resolution" . . . . . 100.00 69 100.00 100.00 1.09e-39 . . . . 195 1 6 no PDB 1RPE . "The Phage 434 Or2R1-69 Complex At 2.5 Angstroms Resolution" . . . . . 100.00 69 100.00 100.00 1.09e-39 . . . . 195 1 7 no PDB 2OR1 . "Recognition Of A Dna Operator By The Repressor Of Phage 434. A View At High Resolution" . . . . . 100.00 69 100.00 100.00 1.09e-39 . . . . 195 1 8 no PDB 2R63 . "Structural Role Of A Buried Salt Bridge In The 434 Repressor Dna-Binding Domain, Nmr, 20 Structures" . . . . . 91.30 63 98.41 98.41 2.47e-34 . . . . 195 1 9 no DBJ BAT39846 . "phage repressor protein CI [Escherichia albertii]" . . . . . 100.00 210 100.00 100.00 4.73e-38 . . . . 195 1 10 no EMBL CAA68301 . "unnamed protein product [Phage 434]" . . . . . 100.00 95 100.00 100.00 2.03e-39 . . . . 195 1 11 no EMBL CBG33631 . "putative prophage repressor [Escherichia coli 042]" . . . . . 100.00 210 100.00 100.00 4.73e-38 . . . . 195 1 12 no EMBL CSZ37563 . "prophage repressor CI [Shigella sonnei]" . . . . . 100.00 210 100.00 100.00 5.39e-38 . . . . 195 1 13 no EMBL CTR12671 . "putative prophage repressor [Escherichia coli]" . . . . . 100.00 210 100.00 100.00 5.33e-38 . . . . 195 1 14 no EMBL CTR54377 . "putative prophage repressor [Escherichia coli]" . . . . . 100.00 210 100.00 100.00 5.33e-38 . . . . 195 1 15 no GB AAA72530 . "cI repressor [unidentified cloning vector]" . . . . . 100.00 210 100.00 100.00 5.33e-38 . . . . 195 1 16 no GB AAD50896 . "434-GCN4-linker [Cloning vector pLS3]" . . . . . 100.00 138 100.00 100.00 3.65e-39 . . . . 195 1 17 no GB ABF02546 . "putative prophage repressor CI [Shigella flexneri 5 str. 8401]" . . . . . 100.00 210 100.00 100.00 4.73e-38 . . . . 195 1 18 no GB ADD54938 . "SOS-response transcriptional repressor [Escherichia coli O55:H7 str. CB9615]" . . . . . 100.00 210 100.00 100.00 4.73e-38 . . . . 195 1 19 no GB AEZ38914 . "SOS-response transcriptional repressor [Escherichia coli O55:H7 str. RM12579]" . . . . . 100.00 210 100.00 100.00 4.73e-38 . . . . 195 1 20 no PIR S32822 . "repressor protein cI - phage 434" . . . . . 100.00 210 100.00 100.00 5.33e-38 . . . . 195 1 21 no PRF 1011238A . "cI gene" . . . . . 100.00 210 100.00 100.00 5.33e-38 . . . . 195 1 22 no REF WP_000028392 . "MULTISPECIES: repressor [Enterobacteriaceae]" . . . . . 100.00 210 100.00 100.00 4.73e-38 . . . . 195 1 23 no REF WP_000028393 . "MULTISPECIES: cI repressor protein [Enterobacteriaceae]" . . . . . 100.00 210 100.00 100.00 5.50e-38 . . . . 195 1 24 no REF WP_000028394 . "repressor [Escherichia coli]" . . . . . 100.00 210 100.00 100.00 5.33e-38 . . . . 195 1 25 no REF WP_000028395 . "repressor [Escherichia coli]" . . . . . 100.00 210 98.55 100.00 1.45e-37 . . . . 195 1 26 no REF WP_001592290 . "hypothetical protein [Escherichia coli]" . . . . . 100.00 210 100.00 100.00 4.73e-38 . . . . 195 1 27 no SP P16117 . "RecName: Full=Repressor protein CI" . . . . . 100.00 95 100.00 100.00 2.03e-39 . . . . 195 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID '434 repressor' common 195 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 . SER . 195 1 2 . ILE . 195 1 3 . SER . 195 1 4 . SER . 195 1 5 . ARG . 195 1 6 . VAL . 195 1 7 . LYS . 195 1 8 . SER . 195 1 9 . LYS . 195 1 10 . ARG . 195 1 11 . ILE . 195 1 12 . GLN . 195 1 13 . LEU . 195 1 14 . GLY . 195 1 15 . LEU . 195 1 16 . ASN . 195 1 17 . GLN . 195 1 18 . ALA . 195 1 19 . GLU . 195 1 20 . LEU . 195 1 21 . ALA . 195 1 22 . GLN . 195 1 23 . LYS . 195 1 24 . VAL . 195 1 25 . GLY . 195 1 26 . THR . 195 1 27 . THR . 195 1 28 . GLN . 195 1 29 . GLN . 195 1 30 . SER . 195 1 31 . ILE . 195 1 32 . GLU . 195 1 33 . GLN . 195 1 34 . LEU . 195 1 35 . GLU . 195 1 36 . ASN . 195 1 37 . GLY . 195 1 38 . LYS . 195 1 39 . THR . 195 1 40 . LYS . 195 1 41 . ARG . 195 1 42 . PRO . 195 1 43 . ARG . 195 1 44 . PHE . 195 1 45 . LEU . 195 1 46 . PRO . 195 1 47 . GLU . 195 1 48 . LEU . 195 1 49 . ALA . 195 1 50 . SER . 195 1 51 . ALA . 195 1 52 . LEU . 195 1 53 . GLY . 195 1 54 . VAL . 195 1 55 . SER . 195 1 56 . VAL . 195 1 57 . ASP . 195 1 58 . TRP . 195 1 59 . LEU . 195 1 60 . LEU . 195 1 61 . ASN . 195 1 62 . GLY . 195 1 63 . THR . 195 1 64 . SER . 195 1 65 . ASP . 195 1 66 . SER . 195 1 67 . ASN . 195 1 68 . VAL . 195 1 69 . ARG . 195 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 . SER 1 1 195 1 . ILE 2 2 195 1 . SER 3 3 195 1 . SER 4 4 195 1 . ARG 5 5 195 1 . VAL 6 6 195 1 . LYS 7 7 195 1 . SER 8 8 195 1 . LYS 9 9 195 1 . ARG 10 10 195 1 . ILE 11 11 195 1 . GLN 12 12 195 1 . LEU 13 13 195 1 . GLY 14 14 195 1 . LEU 15 15 195 1 . ASN 16 16 195 1 . GLN 17 17 195 1 . ALA 18 18 195 1 . GLU 19 19 195 1 . LEU 20 20 195 1 . ALA 21 21 195 1 . GLN 22 22 195 1 . LYS 23 23 195 1 . VAL 24 24 195 1 . GLY 25 25 195 1 . THR 26 26 195 1 . THR 27 27 195 1 . GLN 28 28 195 1 . GLN 29 29 195 1 . SER 30 30 195 1 . ILE 31 31 195 1 . GLU 32 32 195 1 . GLN 33 33 195 1 . LEU 34 34 195 1 . GLU 35 35 195 1 . ASN 36 36 195 1 . GLY 37 37 195 1 . LYS 38 38 195 1 . THR 39 39 195 1 . LYS 40 40 195 1 . ARG 41 41 195 1 . PRO 42 42 195 1 . ARG 43 43 195 1 . PHE 44 44 195 1 . LEU 45 45 195 1 . PRO 46 46 195 1 . GLU 47 47 195 1 . LEU 48 48 195 1 . ALA 49 49 195 1 . SER 50 50 195 1 . ALA 51 51 195 1 . LEU 52 52 195 1 . GLY 53 53 195 1 . VAL 54 54 195 1 . SER 55 55 195 1 . VAL 56 56 195 1 . ASP 57 57 195 1 . TRP 58 58 195 1 . LEU 59 59 195 1 . LEU 60 60 195 1 . ASN 61 61 195 1 . GLY 62 62 195 1 . THR 63 63 195 1 . SER 64 64 195 1 . ASP 65 65 195 1 . SER 66 66 195 1 . ASN 67 67 195 1 . VAL 68 68 195 1 . ARG 69 69 195 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 195 _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 $434_repressor . 562 organism . 'Escherichia coli' 'Escherichia coli bacteriophage' . . Eubacteria . Escherichia coli 'bacteriophage 434' . . . . . . . . . . . . . . . . . . . . 195 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 195 _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 $434_repressor . 'not available' 'Escherichia coli' . . . Escherichia coli NM522 . . . . . . . . . . . . . . . . . . . . . . 195 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 195 _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 195 _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 6 . na 195 1 temperature 301 . K 195 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 195 _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 195 _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' . . 195 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 195 _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 . . . . . . . . . . . . . . . . 195 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 195 _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 C . TSP . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 195 1 H . TSP . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 195 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 195 _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 . 195 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 6 6 VAL CG1 C 13 21.3 . . 1 . . . . . . . . 195 1 2 . 1 1 6 6 VAL CG2 C 13 25.9 . . 1 . . . . . . . . 195 1 3 . 1 1 6 6 VAL HG11 H 1 1.15 . . 1 . . . . . . . . 195 1 4 . 1 1 6 6 VAL HG12 H 1 1.15 . . 1 . . . . . . . . 195 1 5 . 1 1 6 6 VAL HG13 H 1 1.15 . . 1 . . . . . . . . 195 1 6 . 1 1 6 6 VAL HG21 H 1 1.16 . . 1 . . . . . . . . 195 1 7 . 1 1 6 6 VAL HG22 H 1 1.16 . . 1 . . . . . . . . 195 1 8 . 1 1 6 6 VAL HG23 H 1 1.16 . . 1 . . . . . . . . 195 1 9 . 1 1 13 13 LEU CD1 C 13 26.2 . . 1 . . . . . . . . 195 1 10 . 1 1 13 13 LEU CD2 C 13 22.9 . . 1 . . . . . . . . 195 1 11 . 1 1 13 13 LEU HD11 H 1 1.02 . . 1 . . . . . . . . 195 1 12 . 1 1 13 13 LEU HD12 H 1 1.02 . . 1 . . . . . . . . 195 1 13 . 1 1 13 13 LEU HD13 H 1 1.02 . . 1 . . . . . . . . 195 1 14 . 1 1 13 13 LEU HD21 H 1 .96 . . 1 . . . . . . . . 195 1 15 . 1 1 13 13 LEU HD22 H 1 .96 . . 1 . . . . . . . . 195 1 16 . 1 1 13 13 LEU HD23 H 1 .96 . . 1 . . . . . . . . 195 1 17 . 1 1 15 15 LEU CD1 C 13 26.6 . . 1 . . . . . . . . 195 1 18 . 1 1 15 15 LEU CD2 C 13 23.3 . . 1 . . . . . . . . 195 1 19 . 1 1 15 15 LEU HD11 H 1 .85 . . 1 . . . . . . . . 195 1 20 . 1 1 15 15 LEU HD12 H 1 .85 . . 1 . . . . . . . . 195 1 21 . 1 1 15 15 LEU HD13 H 1 .85 . . 1 . . . . . . . . 195 1 22 . 1 1 15 15 LEU HD21 H 1 .83 . . 1 . . . . . . . . 195 1 23 . 1 1 15 15 LEU HD22 H 1 .83 . . 1 . . . . . . . . 195 1 24 . 1 1 15 15 LEU HD23 H 1 .83 . . 1 . . . . . . . . 195 1 25 . 1 1 20 20 LEU CD1 C 13 23.5 . . 1 . . . . . . . . 195 1 26 . 1 1 20 20 LEU CD2 C 13 26.9 . . 1 . . . . . . . . 195 1 27 . 1 1 20 20 LEU HD11 H 1 .89 . . 1 . . . . . . . . 195 1 28 . 1 1 20 20 LEU HD12 H 1 .89 . . 1 . . . . . . . . 195 1 29 . 1 1 20 20 LEU HD13 H 1 .89 . . 1 . . . . . . . . 195 1 30 . 1 1 20 20 LEU HD21 H 1 .95 . . 1 . . . . . . . . 195 1 31 . 1 1 20 20 LEU HD22 H 1 .95 . . 1 . . . . . . . . 195 1 32 . 1 1 20 20 LEU HD23 H 1 .95 . . 1 . . . . . . . . 195 1 33 . 1 1 24 24 VAL CG1 C 13 22.6 . . 1 . . . . . . . . 195 1 34 . 1 1 24 24 VAL CG2 C 13 24.1 . . 1 . . . . . . . . 195 1 35 . 1 1 24 24 VAL HG11 H 1 .75 . . 1 . . . . . . . . 195 1 36 . 1 1 24 24 VAL HG12 H 1 .75 . . 1 . . . . . . . . 195 1 37 . 1 1 24 24 VAL HG13 H 1 .75 . . 1 . . . . . . . . 195 1 38 . 1 1 24 24 VAL HG21 H 1 .88 . . 1 . . . . . . . . 195 1 39 . 1 1 24 24 VAL HG22 H 1 .88 . . 1 . . . . . . . . 195 1 40 . 1 1 24 24 VAL HG23 H 1 .88 . . 1 . . . . . . . . 195 1 41 . 1 1 34 34 LEU CD1 C 13 24.8 . . 1 . . . . . . . . 195 1 42 . 1 1 34 34 LEU CD2 C 13 28.3 . . 1 . . . . . . . . 195 1 43 . 1 1 34 34 LEU HD11 H 1 .94 . . 1 . . . . . . . . 195 1 44 . 1 1 34 34 LEU HD12 H 1 .94 . . 1 . . . . . . . . 195 1 45 . 1 1 34 34 LEU HD13 H 1 .94 . . 1 . . . . . . . . 195 1 46 . 1 1 34 34 LEU HD21 H 1 1.07 . . 1 . . . . . . . . 195 1 47 . 1 1 34 34 LEU HD22 H 1 1.07 . . 1 . . . . . . . . 195 1 48 . 1 1 34 34 LEU HD23 H 1 1.07 . . 1 . . . . . . . . 195 1 49 . 1 1 45 45 LEU CD1 C 13 25.7 . . 1 . . . . . . . . 195 1 50 . 1 1 45 45 LEU CD2 C 13 25.4 . . 1 . . . . . . . . 195 1 51 . 1 1 45 45 LEU HD11 H 1 .98 . . 1 . . . . . . . . 195 1 52 . 1 1 45 45 LEU HD12 H 1 .98 . . 1 . . . . . . . . 195 1 53 . 1 1 45 45 LEU HD13 H 1 .98 . . 1 . . . . . . . . 195 1 54 . 1 1 45 45 LEU HD21 H 1 .92 . . 1 . . . . . . . . 195 1 55 . 1 1 45 45 LEU HD22 H 1 .92 . . 1 . . . . . . . . 195 1 56 . 1 1 45 45 LEU HD23 H 1 .92 . . 1 . . . . . . . . 195 1 57 . 1 1 48 48 LEU CD1 C 13 25.1 . . 1 . . . . . . . . 195 1 58 . 1 1 48 48 LEU CD2 C 13 27.7 . . 1 . . . . . . . . 195 1 59 . 1 1 48 48 LEU HD11 H 1 1.05 . . 1 . . . . . . . . 195 1 60 . 1 1 48 48 LEU HD12 H 1 1.05 . . 1 . . . . . . . . 195 1 61 . 1 1 48 48 LEU HD13 H 1 1.05 . . 1 . . . . . . . . 195 1 62 . 1 1 48 48 LEU HD21 H 1 1.05 . . 1 . . . . . . . . 195 1 63 . 1 1 48 48 LEU HD22 H 1 1.05 . . 1 . . . . . . . . 195 1 64 . 1 1 48 48 LEU HD23 H 1 1.05 . . 1 . . . . . . . . 195 1 65 . 1 1 52 52 LEU CD1 C 13 27.3 . . 1 . . . . . . . . 195 1 66 . 1 1 52 52 LEU CD2 C 13 22.6 . . 1 . . . . . . . . 195 1 67 . 1 1 52 52 LEU HD11 H 1 1.05 . . 1 . . . . . . . . 195 1 68 . 1 1 52 52 LEU HD12 H 1 1.05 . . 1 . . . . . . . . 195 1 69 . 1 1 52 52 LEU HD13 H 1 1.05 . . 1 . . . . . . . . 195 1 70 . 1 1 52 52 LEU HD21 H 1 .85 . . 1 . . . . . . . . 195 1 71 . 1 1 52 52 LEU HD22 H 1 .85 . . 1 . . . . . . . . 195 1 72 . 1 1 52 52 LEU HD23 H 1 .85 . . 1 . . . . . . . . 195 1 73 . 1 1 54 54 VAL CG1 C 13 21.3 . . 1 . . . . . . . . 195 1 74 . 1 1 54 54 VAL CG2 C 13 21.2 . . 1 . . . . . . . . 195 1 75 . 1 1 54 54 VAL HG11 H 1 .46 . . 1 . . . . . . . . 195 1 76 . 1 1 54 54 VAL HG12 H 1 .46 . . 1 . . . . . . . . 195 1 77 . 1 1 54 54 VAL HG13 H 1 .46 . . 1 . . . . . . . . 195 1 78 . 1 1 54 54 VAL HG21 H 1 1.04 . . 1 . . . . . . . . 195 1 79 . 1 1 54 54 VAL HG22 H 1 1.04 . . 1 . . . . . . . . 195 1 80 . 1 1 54 54 VAL HG23 H 1 1.04 . . 1 . . . . . . . . 195 1 81 . 1 1 56 56 VAL CG1 C 13 22.1 . . 1 . . . . . . . . 195 1 82 . 1 1 56 56 VAL CG2 C 13 23.6 . . 1 . . . . . . . . 195 1 83 . 1 1 56 56 VAL HG11 H 1 1.02 . . 1 . . . . . . . . 195 1 84 . 1 1 56 56 VAL HG12 H 1 1.02 . . 1 . . . . . . . . 195 1 85 . 1 1 56 56 VAL HG13 H 1 1.02 . . 1 . . . . . . . . 195 1 86 . 1 1 56 56 VAL HG21 H 1 1.02 . . 1 . . . . . . . . 195 1 87 . 1 1 56 56 VAL HG22 H 1 1.02 . . 1 . . . . . . . . 195 1 88 . 1 1 56 56 VAL HG23 H 1 1.02 . . 1 . . . . . . . . 195 1 89 . 1 1 59 59 LEU CD1 C 13 26.4 . . 1 . . . . . . . . 195 1 90 . 1 1 59 59 LEU CD2 C 13 24.6 . . 1 . . . . . . . . 195 1 91 . 1 1 59 59 LEU HD11 H 1 .94 . . 1 . . . . . . . . 195 1 92 . 1 1 59 59 LEU HD12 H 1 .94 . . 1 . . . . . . . . 195 1 93 . 1 1 59 59 LEU HD13 H 1 .94 . . 1 . . . . . . . . 195 1 94 . 1 1 59 59 LEU HD21 H 1 1 . . 1 . . . . . . . . 195 1 95 . 1 1 59 59 LEU HD22 H 1 1 . . 1 . . . . . . . . 195 1 96 . 1 1 59 59 LEU HD23 H 1 1 . . 1 . . . . . . . . 195 1 97 . 1 1 60 60 LEU CD1 C 13 25.6 . . 1 . . . . . . . . 195 1 98 . 1 1 60 60 LEU CD2 C 13 23.3 . . 1 . . . . . . . . 195 1 99 . 1 1 60 60 LEU HD11 H 1 .89 . . 1 . . . . . . . . 195 1 100 . 1 1 60 60 LEU HD12 H 1 .89 . . 1 . . . . . . . . 195 1 101 . 1 1 60 60 LEU HD13 H 1 .89 . . 1 . . . . . . . . 195 1 102 . 1 1 60 60 LEU HD21 H 1 .87 . . 1 . . . . . . . . 195 1 103 . 1 1 60 60 LEU HD22 H 1 .87 . . 1 . . . . . . . . 195 1 104 . 1 1 60 60 LEU HD23 H 1 .87 . . 1 . . . . . . . . 195 1 105 . 1 1 68 68 VAL CG1 C 13 21.4 . . 1 . . . . . . . . 195 1 106 . 1 1 68 68 VAL CG2 C 13 21.7 . . 1 . . . . . . . . 195 1 107 . 1 1 68 68 VAL HG11 H 1 .97 . . 1 . . . . . . . . 195 1 108 . 1 1 68 68 VAL HG12 H 1 .97 . . 1 . . . . . . . . 195 1 109 . 1 1 68 68 VAL HG13 H 1 .97 . . 1 . . . . . . . . 195 1 110 . 1 1 68 68 VAL HG21 H 1 .97 . . 1 . . . . . . . . 195 1 111 . 1 1 68 68 VAL HG22 H 1 .97 . . 1 . . . . . . . . 195 1 112 . 1 1 68 68 VAL HG23 H 1 .97 . . 1 . . . . . . . . 195 1 stop_ save_