data_5910 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5910 _Entry.Title ; Backbone 1HN and 15N Chemical Shift Assignments for Sso7d I30V ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2003-08-20 _Entry.Accession_date 2003-08-20 _Entry.Last_release_date 2005-05-03 _Entry.Original_release_date 2005-05-03 _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 Andrew Clark . T. . 5910 2 Bradford McCrary . S. . 5910 3 Stephen Edmondson . P. . 5910 4 John Shriver . W. . 5910 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5910 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 62 5910 '1H chemical shifts' 62 5910 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 . . 2005-05-03 2003-08-20 original author . 5910 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4570 'Sso7d-F31A mutant' 5910 BMRB 5905 'Sac7d monomer' 5910 BMRB 5908 'Sac7d monomer mutant' 5910 BMRB 5909 'Sso7d monomer' 5910 PDB 1BBX 'BMRB Entry Tracking System' 5910 PDB 1BF4 'BMRB Entry Tracking System' 5910 PDB 1BNZ 'BMRB Entry Tracking System' 5910 PDB 1C8C 'BMRB Entry Tracking System' 5910 PDB 1CA5 'BMRB Entry Tracking System' 5910 PDB 1CA6 'BMRB Entry Tracking System' 5910 PDB 1JIC 'BMRB Entry Tracking System' 5910 PDB 1SSO 'BMRB Entry Tracking System' 5910 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5910 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 15005619 _Citation.Full_citation . _Citation.Title ; Thermodynamics of core hydrophobicity and packing in the hyperthermophile proteins Sac7d and Sso7d. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 43 _Citation.Journal_issue 10 _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 2840 _Citation.Page_last 2853 _Citation.Year 2004 _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 Andrew Clark . T. . 5910 1 2 Bradford McCrary . S. . 5910 1 3 Stephen Edmondson . P. . 5910 1 4 John Shriver . W. . 5910 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID calorimetry 5910 1 hyperthermophile 5910 1 'nuclear magnetic resonance' 5910 1 Sulfolobus 5910 1 stop_ save_ save_references_1 _Citation.Sf_category citations _Citation.Sf_framecode references_1 _Citation.Entry_ID 5910 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11398456 _Citation.Full_citation ; Edmondson SP, Shriver JW. Methods Enzymol. 2001;334:129-45. ; _Citation.Title 'DNA binding proteins Sac7d and Sso7d from Sulfolobus.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Meth. Enzymol.' _Citation.Journal_name_full 'Methods in enzymology' _Citation.Journal_volume 334 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN 0076-6879 _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 129 _Citation.Page_last 145 _Citation.Year 2001 _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 S.P. Edmondson S. P. . 5910 2 2 J.W. Shriver J. W. . 5910 2 stop_ save_ save_references_2 _Citation.Sf_category citations _Citation.Sf_framecode references_2 _Citation.Entry_ID 5910 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11031116 _Citation.Full_citation ; Su S, Gao YG, Robinson H, Liaw YC, Edmondson SP, Shriver JW, Wang AH. J Mol Biol. 2000 Oct 27;303(3):395-403. ; _Citation.Title 'Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 303 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 395 _Citation.Page_last 403 _Citation.Year 2000 _Citation.Details ; Sso7d and Sac7d are two small chromatin proteins from the hyperthermophilic archaeabacterium Sulfolobus solfataricus and Sulfolobus acidocaldarius, respectively. The crystal structures of Sso7d-GTGATCGC, Sac7d-GTGATCGC and Sac7d-GTGATCAC have been determined and refined at 1.45 A, 2.2 A and 2.2 A, respectively, to investigate the DNA binding property of Sso7d/Sac7d in the presence of a T-G mismatch base-pair. Detailed structural analysis revealed that the intercalation site includes the T-G mismatch base-pair and Sso7d/Sac7d bind to that mismatch base-pair in a manner similar to regular DNA. In the Sso7d-GTGATCGC complex, a new inter-strand hydrogen bond between T2O4 and C14N4 is formed and well-order bridging water molecules are found. The results suggest that the less stable DNA stacking site involving a T-G mismatch may be a preferred site for protein side-chain intercalation. ; 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 S. Su S. . . 5910 3 2 Y.G. Gao Y. G. . 5910 3 3 H. Robinson H. . . 5910 3 4 Y.C. Liaw Y. C. . 5910 3 5 S.P. Edmondson S. P. . 5910 3 6 J.W. Shriver J. W. . 5910 3 7 A.H. Wang A. H. . 5910 3 stop_ save_ save_references_3 _Citation.Sf_category citations _Citation.Sf_framecode references_3 _Citation.Entry_ID 5910 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9731772 _Citation.Full_citation ; Gao YG, Su SY, Robinson H, Padmanabhan S, Lim L, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nat Struct Biol. 1998 Sep;5(9):782-6. ; _Citation.Title 'The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full 'Nature structural biology' _Citation.Journal_volume 5 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1072-8368 _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 782 _Citation.Page_last 786 _Citation.Year 1998 _Citation.Details ; Sso7d and Sac7d are two small (approximately 7,000 Mr), but abundant, chromosomal proteins from the hyperthermophilic archaeabacteria Sulfolobus solfataricus and S. acidocaldarius respectively. These proteins have high thermal, acid and chemical stability. They bind DNA without marked sequence preference and increase the Tm of DNA by approximately 40 degrees C. Sso7d in complex with GTAATTAC and GCGT(iU)CGC + GCGAACGC was crystallized in different crystal lattices and the crystal structures were solved at high resolution. Sso7d binds in the minor groove of DNA and causes a single-step sharp kink in DNA (approximately 60 degrees) by the intercalation of the hydrophobic side chains of Val 26 and Met 29. The intercalation sites are different in the two complexes. Observations of this novel DNA binding mode in three independent crystal lattices indicate that it is not a function of crystal packing. ; 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 Y.G. Gao Y. G. . 5910 4 2 S.Y. Su S. Y. . 5910 4 3 H. Robinson H. . . 5910 4 4 S. Padmanabhan S. . . 5910 4 5 L. Lim L. . . 5910 4 6 B.S. McCrary B. S. . 5910 4 7 S.P. Edmondson S. P. . 5910 4 8 J.W. Shriver J. W. . 5910 4 9 A.H. Wang A. H. . 5910 4 stop_ save_ save_references_4 _Citation.Sf_category citations _Citation.Sf_framecode references_4 _Citation.Entry_ID 5910 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9515968 _Citation.Full_citation ; Robinson H, Gao YG, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nature. 1998 Mar 12;392(6672):202-5. ; _Citation.Title 'The hyperthermophile chromosomal protein Sac7d sharply kinks DNA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Nature _Citation.Journal_name_full Nature _Citation.Journal_volume 392 _Citation.Journal_issue 6672 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0028-0836 _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 202 _Citation.Page_last 205 _Citation.Year 1998 _Citation.Details ; The proteins Sac7d and Sso7d belong to a class of small chromosomal proteins from the hyperthermophilic archaeon Sulfolobus acidocaldarius and S. solfactaricus, respectively. These proteins are extremely stable to heat, acid and chemical agents. Sac7d binds to DNA without any particular sequence preference and thereby increases its melting temperature by approximately 40 degrees C. We have now solved and refined the crystal structure of Sac7d in complex with two DNA sequences to high resolution. The structures are examples of a nonspecific DNA-binding protein bound to DNA, and reveal that Sac7d binds in the minor groove, causing a sharp kinking of the DNA helix that is more marked than that induced by any sequence-specific DNA-binding proteins. The kink results from the intercalation of specific hydrophobic side chains of Sac7d into the DNA structure, but without causing any significant distortion of the protein structure relative to the uncomplexed protein in solution. ; 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. Robinson H. . . 5910 5 2 Y.G. Gao Y. G. . 5910 5 3 B.S. McCrary B. S. . 5910 5 4 S.P. Edmondson S. P. . 5910 5 5 J.W. Shriver J. W. . 5910 5 6 A.H. Wang A. H. . 5910 5 stop_ save_ save_references_5 _Citation.Sf_category citations _Citation.Sf_framecode references_5 _Citation.Entry_ID 5910 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7577913 _Citation.Full_citation ; Edmondson SP, Qiu L, Shriver JW. Biochemistry. 1995 Oct 17;34(41):13289-304. ; _Citation.Title 'Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 34 _Citation.Journal_issue 41 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 13289 _Citation.Page_last 13304 _Citation.Year 1995 _Citation.Details ; The Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius are a heterogeneous mixture of small, thermostable, nonspecific DNA-binding proteins. One of these proteins, Sac7d, has been overexpressed in Escherichia coli to provide a homogeneous preparation for structure, stability, and function studies. We present here essentially complete sequence-specific 1H NMR assignments for Sac7d, a delineation of secondary structural elements, and the high-resolution solution structure obtained from a full relaxation matrix refinement. The final structure provides an excellent fit to the NMR data with an NOE R-factor of 0.27 for backbone NOEs. The structure has a compact globular fold with 82% of the sequence involved in regular secondary structure: an antiparallel two-stranded beta-ribbon with a tight turn, followed by a short 3(10) helix, an antiparallel three-stranded beta-sheet, another short 3(10) helix, and finally four turns of alpha-helix. The amphipathic alpha-helix packs across the hydrophobic face of the three-stranded beta-sheet in an open-faced sandwich arrangement with at least one turn of the helix exposed beyond the sheet. The hydrophobic face of the beta-ribbon packs against a corner of the twisted beta-sheet. The single tryptophan responsible for the 88% fluorescence quenching upon DNA binding is exposed on the surface of the three-stranded beta-sheet. Lysines 5 and 7, whose monomethylation may be associated with enhanced thermostability, are highly solvent exposed along the inner edge of the two-stranded ribbon. The structure of Sac7d differs in many respects from that reported for the homologous native Sso7d [Baumann et al. (1994) Nature Struct. Biol. 1, 808] with a backbone RMSD greater than 3.0 A, largely due to the packing and length of the C-terminal alpha-helix which may be important in Sac7d DNA binding. ; 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 S.P. Edmondson S. P. . 5910 6 2 L. Qiu L. . . 5910 6 3 J.W. Shriver J. W. . 5910 6 stop_ save_ save_references_6 _Citation.Sf_category citations _Citation.Sf_framecode references_6 _Citation.Entry_ID 5910 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7632679 _Citation.Full_citation ; McAfee JG, Edmondson SP, Datta PK, Shriver JW, Gupta R. Biochemistry. 1995 Aug 8;34(31):10063-77. ; _Citation.Title 'Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 34 _Citation.Journal_issue 31 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 10063 _Citation.Page_last 10077 _Citation.Year 1995 _Citation.Details ; The genes for two Sac7 DNA-binding proteins, Sac7d and Sac7e, from the extremely thermophilic archaeon Sulfolobus acidocaldarius have been cloned into Escherichia coli and sequenced. The sac7d and sac7e open reading frames encode 66 amino acid (7608 Da) and 65 amino acid (7469 Da) proteins, respectively. Southern blots indicate that these are the only two Sac7 protein genes in S. acidocaldarius, each present as a single copy. Sac7a, b, and c proteins appear to be carboxy-terminal modified Sac7d species. The transcription initiation and termination regions of the sac7d and sac7e genes have been identified along with the promoter elements. Potential ribosome binding sites have been identified downstream of the initiator codons. The sac7d gene has been expressed in E. coli, and various physical properties of the recombinant protein have been compared with those of native Sac7. The UV absorbance spectra and extinction coefficients, the fluorescence excitation and emission spectra, the circular dichroism, and the two-dimensional double-quantum filtered 1H NMR spectra of the native and recombinant species are essentially identical, indicating essentially identical local and global folds. The recombinant and native proteins bind and stabilize double-stranded DNA with a site size of 3.5 base pairs and an intrinsic binding constant of 2 x 10(7) M-1 for poly[dGdC].poly[dGdC] in 0.01 M KH2PO4 at pH 7.0. The availability of the recombinant protein permits a direct comparison of the thermal stabilities of the methylated and unmethylated forms of the protein. Differential scanning calorimetry demonstrates that the native protein is extremely thermostable and unfolds reversibly at pH 6.0 with a Tm of approximately 100 degrees C, while the recombinant protein unfolds at 92.7 degrees C. ; 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 J.G. McAfee J. G. . 5910 7 2 S.P. Edmondson S. P. . 5910 7 3 P.K. Datta P. K. . 5910 7 4 J.W. Shriver J. W. . 5910 7 5 R. Gupta R. . . 5910 7 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Sso7d _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Sso7d _Assembly.Entry_ID 5910 _Assembly.ID 1 _Assembly.Name 'Sso7d monomer' _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 . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5910 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 'Sso7d monomer' 1 $Sso7d . . . native . . . . . 5910 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 yes PDB 1B40 . . . . . . 5910 1 yes PDB 1BBX . . . . . . 5910 1 yes PDB 1BF4 . . . . . . 5910 1 yes PDB 1BNZ . . . . . . 5910 1 yes PDB 1C8C . . . . . . 5910 1 yes PDB 1CA5 . . . . . . 5910 1 yes PDB 1CA6 . . . . . . 5910 1 yes PDB 1JIC . . . . . . 5910 1 yes PDB 1SSO . . . . . . 5910 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID Sso7d abbreviation 5910 1 'Sso7d monomer' system 5910 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'DNA-binding chromosomal protein' 5910 1 'function unknown' 5910 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Sso7d _Entity.Sf_category entity _Entity.Sf_framecode Sso7d _Entity.Entry_ID 5910 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Sso7d _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 ; MATVKFKYKGEEKQVDISKI KKVWRVGKMVSFTYDEGGGK TGRGAVSEKDAPKELLQMLE KQKK ; _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 64 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 7265 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 5909 . Sso7d . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 2 no PDB 1BBX . "Non-Specific Protein-Dna Interactions In The Sso7d-Dna Complex, Nmr, 1 Structure" . . . . . 98.44 63 98.41 100.00 1.47e-34 . . . . 5910 1 3 no PDB 1JIC . "Solution Nmr Structure Of Recombinant Sso7d With Rnase Activity, Minimized Average Structure" . . . . . 96.88 62 98.39 100.00 4.20e-34 . . . . 5910 1 4 no PDB 1SSO . "Solution Structure And Dna-Binding Properties Of A Thermostable Protein From The Archaeon Sulfolobus Solfataricus" . . . . . 96.88 62 98.39 100.00 4.20e-34 . . . . 5910 1 5 no DBJ BAA28274 . "Ssh7a [Sulfolobus shibatae]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 6 no GB AAB25172 . "ribonuclease p2 [Sulfolobus solfataricus, MT-4, ATCC 49155, Peptide, 62 aa]" . . . . . 96.88 62 98.39 100.00 4.20e-34 . . . . 5910 1 7 no GB AAK42090 . "7 KD DNA-binding protein (SSO7D) (SSH7A) (ssh7A /Sso7d-2) [Sulfolobus solfataricus P2]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 8 no GB AAK42212 . "7 KD DNA-binding protein (SSO7D) (SSH7A) (ssh7A /Sso7d-3) [Sulfolobus solfataricus P2]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 9 no GB ACP37540 . "DNA-binding 7 kDa protein [Sulfolobus islandicus M.14.25]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 10 no GB ACP45250 . "DNA-binding 7 kDa protein [Sulfolobus islandicus Y.G.57.14]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 11 no PRF 1908252A . ribonuclease . . . . . 96.88 62 98.39 100.00 4.20e-34 . . . . 5910 1 12 no REF NP_343300 . "DNA-binding protein [Sulfolobus solfataricus P2]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 13 no REF NP_343422 . "DNA-binding protein [Sulfolobus solfataricus P2]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 14 no REF WP_009992021 . "MULTISPECIES: DNA-binding protein [Sulfolobus]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 15 no REF YP_002828838 . "DNA-binding 7 kDa protein [Sulfolobus islandicus M.14.25]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 16 no REF YP_002837172 . "DNA-binding 7 kDa protein [Sulfolobus islandicus Y.G.57.14]" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 17 no SP P61990 . "RecName: Full=DNA-binding protein 7a; AltName: Full=7 kDa DNA-binding protein a; AltName: Full=Endoribonuclease P2; AltName: Fu" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 18 no SP P61991 . "RecName: Full=DNA-binding protein 7a; AltName: Full=7 kDa DNA-binding protein a; AltName: Full=Endoribonuclease P2; AltName: Fu" . . . . . 100.00 64 98.44 100.00 1.83e-35 . . . . 5910 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Sso7d abbreviation 5910 1 Sso7d common 5910 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 . MET . 5910 1 2 . ALA . 5910 1 3 . THR . 5910 1 4 . VAL . 5910 1 5 . LYS . 5910 1 6 . PHE . 5910 1 7 . LYS . 5910 1 8 . TYR . 5910 1 9 . LYS . 5910 1 10 . GLY . 5910 1 11 . GLU . 5910 1 12 . GLU . 5910 1 13 . LYS . 5910 1 14 . GLN . 5910 1 15 . VAL . 5910 1 16 . ASP . 5910 1 17 . ILE . 5910 1 18 . SER . 5910 1 19 . LYS . 5910 1 20 . ILE . 5910 1 21 . LYS . 5910 1 22 . LYS . 5910 1 23 . VAL . 5910 1 24 . TRP . 5910 1 25 . ARG . 5910 1 26 . VAL . 5910 1 27 . GLY . 5910 1 28 . LYS . 5910 1 29 . MET . 5910 1 30 . VAL . 5910 1 31 . SER . 5910 1 32 . PHE . 5910 1 33 . THR . 5910 1 34 . TYR . 5910 1 35 . ASP . 5910 1 36 . GLU . 5910 1 37 . GLY . 5910 1 38 . GLY . 5910 1 39 . GLY . 5910 1 40 . LYS . 5910 1 41 . THR . 5910 1 42 . GLY . 5910 1 43 . ARG . 5910 1 44 . GLY . 5910 1 45 . ALA . 5910 1 46 . VAL . 5910 1 47 . SER . 5910 1 48 . GLU . 5910 1 49 . LYS . 5910 1 50 . ASP . 5910 1 51 . ALA . 5910 1 52 . PRO . 5910 1 53 . LYS . 5910 1 54 . GLU . 5910 1 55 . LEU . 5910 1 56 . LEU . 5910 1 57 . GLN . 5910 1 58 . MET . 5910 1 59 . LEU . 5910 1 60 . GLU . 5910 1 61 . LYS . 5910 1 62 . GLN . 5910 1 63 . LYS . 5910 1 64 . LYS . 5910 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 . MET 1 1 5910 1 . ALA 2 2 5910 1 . THR 3 3 5910 1 . VAL 4 4 5910 1 . LYS 5 5 5910 1 . PHE 6 6 5910 1 . LYS 7 7 5910 1 . TYR 8 8 5910 1 . LYS 9 9 5910 1 . GLY 10 10 5910 1 . GLU 11 11 5910 1 . GLU 12 12 5910 1 . LYS 13 13 5910 1 . GLN 14 14 5910 1 . VAL 15 15 5910 1 . ASP 16 16 5910 1 . ILE 17 17 5910 1 . SER 18 18 5910 1 . LYS 19 19 5910 1 . ILE 20 20 5910 1 . LYS 21 21 5910 1 . LYS 22 22 5910 1 . VAL 23 23 5910 1 . TRP 24 24 5910 1 . ARG 25 25 5910 1 . VAL 26 26 5910 1 . GLY 27 27 5910 1 . LYS 28 28 5910 1 . MET 29 29 5910 1 . VAL 30 30 5910 1 . SER 31 31 5910 1 . PHE 32 32 5910 1 . THR 33 33 5910 1 . TYR 34 34 5910 1 . ASP 35 35 5910 1 . GLU 36 36 5910 1 . GLY 37 37 5910 1 . GLY 38 38 5910 1 . GLY 39 39 5910 1 . LYS 40 40 5910 1 . THR 41 41 5910 1 . GLY 42 42 5910 1 . ARG 43 43 5910 1 . GLY 44 44 5910 1 . ALA 45 45 5910 1 . VAL 46 46 5910 1 . SER 47 47 5910 1 . GLU 48 48 5910 1 . LYS 49 49 5910 1 . ASP 50 50 5910 1 . ALA 51 51 5910 1 . PRO 52 52 5910 1 . LYS 53 53 5910 1 . GLU 54 54 5910 1 . LEU 55 55 5910 1 . LEU 56 56 5910 1 . GLN 57 57 5910 1 . MET 58 58 5910 1 . LEU 59 59 5910 1 . GLU 60 60 5910 1 . LYS 61 61 5910 1 . GLN 62 62 5910 1 . LYS 63 63 5910 1 . LYS 64 64 5910 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 5910 _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 $Sso7d . 2285 organism . 'Sulfolobus acidocaldarius' 'Sulfolobus acidocaldarius Brock et al' . . Archaea . Sulfolobus acidocaldarius . . . . . . . . . . . . . . . . . . . . . 5910 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 5910 _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 $Sso7d . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5910 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_I30V_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode I30V_sample_1 _Sample.Entry_ID 5910 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Sso7d '[U-98% 15N]' . . 1 $Sso7d . . 1.28 1 1.5 mM . . . . 5910 1 2 H2O . . . . . . . 90 . . % . . . . 5910 1 3 D2O . . . . . . . 10 . . % . . . . 5910 1 4 DSS . . . . . . . 100 . . uM . . . . 5910 1 stop_ save_ ####################### # Sample conditions # ####################### save_pH5_0salt _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode pH5_0salt _Sample_condition_list.Entry_ID 5910 _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 5.07 0.1 na 5910 1 temperature 303 1 K 5910 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Software.Sf_category software _Software.Sf_framecode NMRpipe _Software.Entry_ID 5910 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5910 1 referencing 5910 1 transformation 5910 1 stop_ save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 5910 _Software.ID 2 _Software.Name NMRView _Software.Version 5 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'sequential assignments' 5910 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5910 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VXR-S _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5910 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5910 _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_1 Varian VXR-S . 500 . . . 5910 1 2 NMR_spectrometer_2 Varian INOVA . 800 . . . 5910 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 5910 _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 '1H,15N HSQC' . . . . . . . . . . . 1 $I30V_sample_1 . . . 1 $pH5_0salt . . . . . . . . . . . . . . . . . . . . . 5910 1 2 '3D HSQC-TOCSY' . . . . . . . . . . . 1 $I30V_sample_1 . . . 1 $pH5_0salt . . . . . . . . . . . . . . . . . . . . . 5910 1 3 '3D HSQC-NOESY' . . . . . . . . . . . 1 $I30V_sample_1 . . . 1 $pH5_0salt . . . . . . . . . . . . . . . . . . . . . 5910 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 5910 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H,15N HSQC' _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 5910 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '3D HSQC-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 5910 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '3D HSQC-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_ #################### # 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 5910 _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 1.000000000 . . . . . . . . . 5910 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5910 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_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5910 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $pH5_0salt _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 '1H,15N HSQC' 1 $I30V_sample_1 . 5910 1 2 '3D HSQC-TOCSY' 1 $I30V_sample_1 . 5910 1 3 '3D HSQC-NOESY' 1 $I30V_sample_1 . 5910 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 3 3 THR H H 1 8.552 0.01 . 1 . . . . . . . . 5910 1 2 . 1 1 3 3 THR N N 15 113.473 0.05 . 1 . . . . . . . . 5910 1 3 . 1 1 4 4 VAL H H 1 8.877 0.01 . 1 . . . . . . . . 5910 1 4 . 1 1 4 4 VAL N N 15 120.826 0.05 . 1 . . . . . . . . 5910 1 5 . 1 1 5 5 LYS H H 1 8.493 0.01 . 1 . . . . . . . . 5910 1 6 . 1 1 5 5 LYS N N 15 127.728 0.05 . 1 . . . . . . . . 5910 1 7 . 1 1 6 6 PHE H H 1 8.599 0.01 . 1 . . . . . . . . 5910 1 8 . 1 1 6 6 PHE N N 15 119.763 0.05 . 1 . . . . . . . . 5910 1 9 . 1 1 7 7 LYS H H 1 8.768 0.01 . 1 . . . . . . . . 5910 1 10 . 1 1 7 7 LYS N N 15 119.186 0.05 . 1 . . . . . . . . 5910 1 11 . 1 1 8 8 TYR H H 1 9.020 0.01 . 1 . . . . . . . . 5910 1 12 . 1 1 8 8 TYR N N 15 124.902 0.05 . 1 . . . . . . . . 5910 1 13 . 1 1 9 9 LYS H H 1 9.143 0.01 . 1 . . . . . . . . 5910 1 14 . 1 1 9 9 LYS N N 15 127.732 0.05 . 1 . . . . . . . . 5910 1 15 . 1 1 10 10 GLY H H 1 8.453 0.01 . 1 . . . . . . . . 5910 1 16 . 1 1 10 10 GLY N N 15 103.618 0.05 . 1 . . . . . . . . 5910 1 17 . 1 1 11 11 GLU H H 1 7.866 0.01 . 1 . . . . . . . . 5910 1 18 . 1 1 11 11 GLU N N 15 120.461 0.05 . 1 . . . . . . . . 5910 1 19 . 1 1 12 12 GLU H H 1 8.736 0.01 . 1 . . . . . . . . 5910 1 20 . 1 1 12 12 GLU N N 15 123.661 0.05 . 1 . . . . . . . . 5910 1 21 . 1 1 13 13 LYS H H 1 8.816 0.01 . 1 . . . . . . . . 5910 1 22 . 1 1 13 13 LYS N N 15 126.261 0.05 . 1 . . . . . . . . 5910 1 23 . 1 1 14 14 GLN H H 1 8.035 0.01 . 1 . . . . . . . . 5910 1 24 . 1 1 14 14 GLN N N 15 117.608 0.05 . 1 . . . . . . . . 5910 1 25 . 1 1 15 15 VAL H H 1 8.622 0.01 . 1 . . . . . . . . 5910 1 26 . 1 1 15 15 VAL N N 15 121.683 0.05 . 1 . . . . . . . . 5910 1 27 . 1 1 16 16 ASP H H 1 8.658 0.01 . 1 . . . . . . . . 5910 1 28 . 1 1 16 16 ASP N N 15 127.357 0.05 . 1 . . . . . . . . 5910 1 29 . 1 1 17 17 ILE H H 1 8.357 0.01 . 1 . . . . . . . . 5910 1 30 . 1 1 17 17 ILE N N 15 125.757 0.05 . 1 . . . . . . . . 5910 1 31 . 1 1 18 18 SER H H 1 8.905 0.01 . 1 . . . . . . . . 5910 1 32 . 1 1 18 18 SER N N 15 116.137 0.05 . 1 . . . . . . . . 5910 1 33 . 1 1 19 19 LYS H H 1 8.041 0.01 . 1 . . . . . . . . 5910 1 34 . 1 1 19 19 LYS N N 15 119.350 0.05 . 1 . . . . . . . . 5910 1 35 . 1 1 20 20 ILE H H 1 7.496 0.01 . 1 . . . . . . . . 5910 1 36 . 1 1 20 20 ILE N N 15 121.081 0.05 . 1 . . . . . . . . 5910 1 37 . 1 1 21 21 LYS H H 1 8.827 0.01 . 1 . . . . . . . . 5910 1 38 . 1 1 21 21 LYS N N 15 127.280 0.05 . 1 . . . . . . . . 5910 1 39 . 1 1 22 22 LYS H H 1 7.502 0.01 . 1 . . . . . . . . 5910 1 40 . 1 1 22 22 LYS N N 15 120.099 0.05 . 1 . . . . . . . . 5910 1 41 . 1 1 23 23 VAL H H 1 8.375 0.01 . 1 . . . . . . . . 5910 1 42 . 1 1 23 23 VAL N N 15 119.827 0.05 . 1 . . . . . . . . 5910 1 43 . 1 1 24 24 TRP H H 1 9.325 0.01 . 1 . . . . . . . . 5910 1 44 . 1 1 24 24 TRP N N 15 126.012 0.05 . 1 . . . . . . . . 5910 1 45 . 1 1 24 24 TRP NE1 N 15 129.091 0.05 . 1 . . . . . . . . 5910 1 46 . 1 1 24 24 TRP HE1 H 1 10.057 0.01 . 2 . . . . . . . . 5910 1 47 . 1 1 25 25 ARG H H 1 8.796 0.01 . 1 . . . . . . . . 5910 1 48 . 1 1 25 25 ARG N N 15 120.393 0.05 . 1 . . . . . . . . 5910 1 49 . 1 1 26 26 VAL H H 1 8.523 0.01 . 1 . . . . . . . . 5910 1 50 . 1 1 26 26 VAL N N 15 125.016 0.05 . 1 . . . . . . . . 5910 1 51 . 1 1 27 27 GLY H H 1 9.145 0.01 . 1 . . . . . . . . 5910 1 52 . 1 1 27 27 GLY N N 15 118.443 0.05 . 1 . . . . . . . . 5910 1 53 . 1 1 28 28 LYS H H 1 8.880 0.01 . 1 . . . . . . . . 5910 1 54 . 1 1 28 28 LYS N N 15 126.137 0.05 . 1 . . . . . . . . 5910 1 55 . 1 1 29 29 MET H H 1 8.185 0.01 . 1 . . . . . . . . 5910 1 56 . 1 1 29 29 MET N N 15 118.109 0.05 . 1 . . . . . . . . 5910 1 57 . 1 1 30 30 VAL H H 1 9.316 0.01 . 1 . . . . . . . . 5910 1 58 . 1 1 30 30 VAL N N 15 124.296 0.05 . 1 . . . . . . . . 5910 1 59 . 1 1 31 31 SER H H 1 8.780 0.01 . 1 . . . . . . . . 5910 1 60 . 1 1 31 31 SER N N 15 122.737 0.05 . 1 . . . . . . . . 5910 1 61 . 1 1 32 32 PHE H H 1 7.557 0.01 . 1 . . . . . . . . 5910 1 62 . 1 1 32 32 PHE N N 15 114.872 0.05 . 1 . . . . . . . . 5910 1 63 . 1 1 33 33 THR H H 1 9.003 0.01 . 1 . . . . . . . . 5910 1 64 . 1 1 33 33 THR N N 15 109.228 0.05 . 1 . . . . . . . . 5910 1 65 . 1 1 34 34 TYR H H 1 8.551 0.01 . 1 . . . . . . . . 5910 1 66 . 1 1 34 34 TYR N N 15 115.868 0.05 . 1 . . . . . . . . 5910 1 67 . 1 1 35 35 ASP H H 1 8.798 0.01 . 1 . . . . . . . . 5910 1 68 . 1 1 35 35 ASP N N 15 119.843 0.05 . 1 . . . . . . . . 5910 1 69 . 1 1 36 36 GLU H H 1 8.463 0.01 . 1 . . . . . . . . 5910 1 70 . 1 1 36 36 GLU N N 15 126.498 0.05 . 1 . . . . . . . . 5910 1 71 . 1 1 37 37 GLY H H 1 8.514 0.01 . 1 . . . . . . . . 5910 1 72 . 1 1 37 37 GLY N N 15 109.719 0.05 . 1 . . . . . . . . 5910 1 73 . 1 1 38 38 GLY H H 1 8.839 0.01 . 1 . . . . . . . . 5910 1 74 . 1 1 38 38 GLY N N 15 110.086 0.05 . 1 . . . . . . . . 5910 1 75 . 1 1 39 39 GLY H H 1 8.999 0.01 . 1 . . . . . . . . 5910 1 76 . 1 1 39 39 GLY N N 15 107.377 0.05 . 1 . . . . . . . . 5910 1 77 . 1 1 40 40 LYS H H 1 7.514 0.01 . 1 . . . . . . . . 5910 1 78 . 1 1 40 40 LYS N N 15 121.313 0.05 . 1 . . . . . . . . 5910 1 79 . 1 1 41 41 THR H H 1 8.569 0.01 . 1 . . . . . . . . 5910 1 80 . 1 1 41 41 THR N N 15 119.356 0.05 . 1 . . . . . . . . 5910 1 81 . 1 1 42 42 GLY H H 1 8.567 0.01 . 1 . . . . . . . . 5910 1 82 . 1 1 42 42 GLY N N 15 114.376 0.05 . 1 . . . . . . . . 5910 1 83 . 1 1 43 43 ARG H H 1 7.766 0.01 . 1 . . . . . . . . 5910 1 84 . 1 1 43 43 ARG N N 15 117.217 0.05 . 1 . . . . . . . . 5910 1 85 . 1 1 44 44 GLY H H 1 7.744 0.01 . 1 . . . . . . . . 5910 1 86 . 1 1 44 44 GLY N N 15 107.450 0.05 . 1 . . . . . . . . 5910 1 87 . 1 1 45 45 ALA H H 1 6.755 0.01 . 1 . . . . . . . . 5910 1 88 . 1 1 45 45 ALA N N 15 117.263 0.05 . 1 . . . . . . . . 5910 1 89 . 1 1 46 46 VAL H H 1 9.026 0.01 . 1 . . . . . . . . 5910 1 90 . 1 1 46 46 VAL N N 15 115.685 0.05 . 1 . . . . . . . . 5910 1 91 . 1 1 47 47 SER H H 1 9.100 0.01 . 1 . . . . . . . . 5910 1 92 . 1 1 47 47 SER N N 15 120.925 0.05 . 1 . . . . . . . . 5910 1 93 . 1 1 48 48 GLU H H 1 8.791 0.01 . 1 . . . . . . . . 5910 1 94 . 1 1 48 48 GLU N N 15 124.363 0.05 . 1 . . . . . . . . 5910 1 95 . 1 1 49 49 LYS H H 1 8.040 0.01 . 1 . . . . . . . . 5910 1 96 . 1 1 49 49 LYS N N 15 116.126 0.05 . 1 . . . . . . . . 5910 1 97 . 1 1 50 50 ASP H H 1 7.555 0.01 . 1 . . . . . . . . 5910 1 98 . 1 1 50 50 ASP N N 15 116.765 0.05 . 1 . . . . . . . . 5910 1 99 . 1 1 51 51 ALA H H 1 7.469 0.01 . 1 . . . . . . . . 5910 1 100 . 1 1 51 51 ALA N N 15 124.526 0.05 . 1 . . . . . . . . 5910 1 101 . 1 1 53 53 LYS H H 1 9.107 0.01 . 1 . . . . . . . . 5910 1 102 . 1 1 53 53 LYS N N 15 124.892 0.05 . 1 . . . . . . . . 5910 1 103 . 1 1 54 54 GLU H H 1 9.891 0.01 . 1 . . . . . . . . 5910 1 104 . 1 1 54 54 GLU N N 15 117.027 0.05 . 1 . . . . . . . . 5910 1 105 . 1 1 55 55 LEU H H 1 7.334 0.01 . 1 . . . . . . . . 5910 1 106 . 1 1 55 55 LEU N N 15 117.417 0.05 . 1 . . . . . . . . 5910 1 107 . 1 1 56 56 LEU H H 1 7.334 0.01 . 1 . . . . . . . . 5910 1 108 . 1 1 56 56 LEU N N 15 117.417 0.05 . 1 . . . . . . . . 5910 1 109 . 1 1 57 57 GLN H H 1 8.298 0.01 . 1 . . . . . . . . 5910 1 110 . 1 1 57 57 GLN N N 15 117.983 0.05 . 1 . . . . . . . . 5910 1 111 . 1 1 58 58 MET H H 1 7.334 0.01 . 1 . . . . . . . . 5910 1 112 . 1 1 58 58 MET N N 15 117.417 0.05 . 1 . . . . . . . . 5910 1 113 . 1 1 59 59 LEU H H 1 7.475 0.01 . 1 . . . . . . . . 5910 1 114 . 1 1 59 59 LEU N N 15 118.616 0.05 . 1 . . . . . . . . 5910 1 115 . 1 1 60 60 GLU H H 1 7.796 0.01 . 1 . . . . . . . . 5910 1 116 . 1 1 60 60 GLU N N 15 118.322 0.05 . 1 . . . . . . . . 5910 1 117 . 1 1 61 61 LYS H H 1 7.931 0.01 . 1 . . . . . . . . 5910 1 118 . 1 1 61 61 LYS N N 15 119.376 0.05 . 1 . . . . . . . . 5910 1 119 . 1 1 62 62 GLN H H 1 8.010 0.01 . 1 . . . . . . . . 5910 1 120 . 1 1 62 62 GLN N N 15 119.372 0.05 . 1 . . . . . . . . 5910 1 121 . 1 1 63 63 LYS H H 1 8.112 0.01 . 1 . . . . . . . . 5910 1 122 . 1 1 63 63 LYS N N 15 122.676 0.05 . 1 . . . . . . . . 5910 1 123 . 1 1 64 64 LYS H H 1 7.965 0.01 . 1 . . . . . . . . 5910 1 124 . 1 1 64 64 LYS N N 15 127.977 0.05 . 1 . . . . . . . . 5910 1 stop_ save_