data_5910 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1HN and 15N Chemical Shift Assignments for Sso7d I30V ; _BMRB_accession_number 5910 _BMRB_flat_file_name bmr5910.str _Entry_type original _Submission_date 2003-08-20 _Accession_date 2003-08-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Clark Andrew T. . 2 McCrary Bradford S. . 3 Edmondson Stephen P. . 4 Shriver John W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 62 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-03 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4570 'Sso7d-F31A mutant' 5905 'Sac7d monomer' 5908 'Sac7d monomer mutant' 5909 'Sso7d monomer' stop_ _Original_release_date 2005-05-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Thermodynamics of core hydrophobicity and packing in the hyperthermophile proteins Sac7d and Sso7d. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15005619 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Clark Andrew T. . 2 McCrary Bradford S. . 3 Edmondson Stephen P. . 4 Shriver John W. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2840 _Page_last 2853 _Year 2004 _Details . loop_ _Keyword calorimetry hyperthermophile 'nuclear magnetic resonance' Sulfolobus stop_ save_ ####################################### # Cited references within the entry # ####################################### save_references_1 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11398456 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Edmondson S.P. P. . 2 Shriver J.W. W. . stop_ _Journal_abbreviation 'Meth. Enzymol.' _Journal_name_full 'Methods in enzymology' _Journal_volume 334 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 129 _Page_last 145 _Year 2001 _Details . save_ save_references_2 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11031116 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Su S. . . 2 Gao Y.G. G. . 3 Robinson H. . . 4 Liaw Y.C. C. . 5 Edmondson S.P. P. . 6 Shriver J.W. W. . 7 Wang A.H. H. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 303 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 395 _Page_last 403 _Year 2000 _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. ; save_ save_references_3 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9731772 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gao Y.G. G. . 2 Su S.Y. Y. . 3 Robinson H. . . 4 Padmanabhan S. . . 5 Lim L. . . 6 McCrary B.S. S. . 7 Edmondson S.P. P. . 8 Shriver J.W. W. . 9 Wang A.H. H. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature structural biology' _Journal_volume 5 _Journal_issue 9 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 782 _Page_last 786 _Year 1998 _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. ; save_ save_references_4 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9515968 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Robinson H. . . 2 Gao Y.G. G. . 3 McCrary B.S. S. . 4 Edmondson S.P. P. . 5 Shriver J.W. W. . 6 Wang A.H. H. . stop_ _Journal_abbreviation Nature _Journal_name_full Nature _Journal_volume 392 _Journal_issue 6672 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 202 _Page_last 205 _Year 1998 _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. ; save_ save_references_5 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7577913 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Edmondson S.P. P. . 2 Qiu L. . . 3 Shriver J.W. W. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 34 _Journal_issue 41 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 13289 _Page_last 13304 _Year 1995 _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. ; save_ save_references_6 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7632679 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McAfee J.G. G. . 2 Edmondson S.P. P. . 3 Datta P.K. K. . 4 Shriver J.W. W. . 5 Gupta R. . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 34 _Journal_issue 31 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 10063 _Page_last 10077 _Year 1995 _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. ; save_ ################################## # Molecular system description # ################################## save_system_Sso7d _Saveframe_category molecular_system _Mol_system_name 'Sso7d monomer' _Abbreviation_common Sso7d _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Sso7d monomer' $Sso7d stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'DNA-binding chromosomal protein' 'function unknown' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Sso7d _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Sso7d _Abbreviation_common Sso7d _Molecular_mass 7265 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 64 _Mol_residue_sequence ; MATVKFKYKGEEKQVDISKI KKVWRVGKMVSFTYDEGGGK TGRGAVSEKDAPKELLQMLE KQKK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 THR 4 VAL 5 LYS 6 PHE 7 LYS 8 TYR 9 LYS 10 GLY 11 GLU 12 GLU 13 LYS 14 GLN 15 VAL 16 ASP 17 ILE 18 SER 19 LYS 20 ILE 21 LYS 22 LYS 23 VAL 24 TRP 25 ARG 26 VAL 27 GLY 28 LYS 29 MET 30 VAL 31 SER 32 PHE 33 THR 34 TYR 35 ASP 36 GLU 37 GLY 38 GLY 39 GLY 40 LYS 41 THR 42 GLY 43 ARG 44 GLY 45 ALA 46 VAL 47 SER 48 GLU 49 LYS 50 ASP 51 ALA 52 PRO 53 LYS 54 GLU 55 LEU 56 LEU 57 GLN 58 MET 59 LEU 60 GLU 61 LYS 62 GLN 63 LYS 64 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 5909 Sso7d 100.00 64 98.44 100.00 1.68e-35 PDB 1BBX "Non-Specific Protein-Dna Interactions In The Sso7d-Dna Complex, Nmr, 1 Structure" 98.44 63 98.41 100.00 1.35e-34 PDB 1JIC "Solution Nmr Structure Of Recombinant Sso7d With Rnase Activity, Minimized Average Structure" 96.88 62 98.39 100.00 3.85e-34 PDB 1SSO "Solution Structure And Dna-Binding Properties Of A Thermostable Protein From The Archaeon Sulfolobus Solfataricus" 96.88 62 98.39 100.00 3.85e-34 DBJ BAA28274 "Ssh7a [Sulfolobus shibatae]" 100.00 64 98.44 100.00 1.68e-35 GB AAB25172 "ribonuclease p2 [Sulfolobus solfataricus, MT-4, ATCC 49155, Peptide, 62 aa]" 96.88 62 98.39 100.00 3.85e-34 GB AAK42090 "7 KD DNA-binding protein (SSO7D) (SSH7A) (ssh7A /Sso7d-2) [Sulfolobus solfataricus P2]" 100.00 64 98.44 100.00 1.68e-35 GB AAK42212 "7 KD DNA-binding protein (SSO7D) (SSH7A) (ssh7A /Sso7d-3) [Sulfolobus solfataricus P2]" 100.00 64 98.44 100.00 1.68e-35 GB ACP37540 "DNA-binding 7 kDa protein [Sulfolobus islandicus M.14.25]" 100.00 64 98.44 100.00 1.68e-35 GB ACP45250 "DNA-binding 7 kDa protein [Sulfolobus islandicus Y.G.57.14]" 100.00 64 98.44 100.00 1.68e-35 PRF 1908252A ribonuclease 96.88 62 98.39 100.00 3.85e-34 REF NP_343300 "DNA-binding protein [Sulfolobus solfataricus P2]" 100.00 64 98.44 100.00 1.68e-35 REF NP_343422 "DNA-binding protein [Sulfolobus solfataricus P2]" 100.00 64 98.44 100.00 1.68e-35 REF WP_009992021 "MULTISPECIES: DNA-binding protein [Sulfolobus]" 100.00 64 98.44 100.00 1.68e-35 REF YP_002828838 "DNA-binding 7 kDa protein [Sulfolobus islandicus M.14.25]" 100.00 64 98.44 100.00 1.68e-35 REF YP_002837172 "DNA-binding 7 kDa protein [Sulfolobus islandicus Y.G.57.14]" 100.00 64 98.44 100.00 1.68e-35 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 1.68e-35 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 1.68e-35 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Sso7d 'Sulfolobus acidocaldarius Brock et al' 2285 Archaea . Sulfolobus acidocaldarius stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Sso7d 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_I30V_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sso7d 1.28 mM 1 1.5 '[U-98% 15N]' H2O 90 % . . . D2O 10 % . . . DSS 100 uM . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'data processing' referencing transformation stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5 loop_ _Task 'sequential assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VXR-S _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H,15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC' _Sample_label $I30V_sample_1 save_ save_3D_HSQC-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HSQC-TOCSY' _Sample_label $I30V_sample_1 save_ save_3D_HSQC-NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HSQC-NOESY' _Sample_label $I30V_sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HSQC-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HSQC-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_pH5_0salt _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.07 0.1 na temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H,15N HSQC' '3D HSQC-TOCSY' '3D HSQC-NOESY' stop_ loop_ _Sample_label $I30V_sample_1 stop_ _Sample_conditions_label $pH5_0salt _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Sso7d monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 3 THR H H 8.552 0.01 1 2 . 3 THR N N 113.473 0.05 1 3 . 4 VAL H H 8.877 0.01 1 4 . 4 VAL N N 120.826 0.05 1 5 . 5 LYS H H 8.493 0.01 1 6 . 5 LYS N N 127.728 0.05 1 7 . 6 PHE H H 8.599 0.01 1 8 . 6 PHE N N 119.763 0.05 1 9 . 7 LYS H H 8.768 0.01 1 10 . 7 LYS N N 119.186 0.05 1 11 . 8 TYR H H 9.020 0.01 1 12 . 8 TYR N N 124.902 0.05 1 13 . 9 LYS H H 9.143 0.01 1 14 . 9 LYS N N 127.732 0.05 1 15 . 10 GLY H H 8.453 0.01 1 16 . 10 GLY N N 103.618 0.05 1 17 . 11 GLU H H 7.866 0.01 1 18 . 11 GLU N N 120.461 0.05 1 19 . 12 GLU H H 8.736 0.01 1 20 . 12 GLU N N 123.661 0.05 1 21 . 13 LYS H H 8.816 0.01 1 22 . 13 LYS N N 126.261 0.05 1 23 . 14 GLN H H 8.035 0.01 1 24 . 14 GLN N N 117.608 0.05 1 25 . 15 VAL H H 8.622 0.01 1 26 . 15 VAL N N 121.683 0.05 1 27 . 16 ASP H H 8.658 0.01 1 28 . 16 ASP N N 127.357 0.05 1 29 . 17 ILE H H 8.357 0.01 1 30 . 17 ILE N N 125.757 0.05 1 31 . 18 SER H H 8.905 0.01 1 32 . 18 SER N N 116.137 0.05 1 33 . 19 LYS H H 8.041 0.01 1 34 . 19 LYS N N 119.350 0.05 1 35 . 20 ILE H H 7.496 0.01 1 36 . 20 ILE N N 121.081 0.05 1 37 . 21 LYS H H 8.827 0.01 1 38 . 21 LYS N N 127.280 0.05 1 39 . 22 LYS H H 7.502 0.01 1 40 . 22 LYS N N 120.099 0.05 1 41 . 23 VAL H H 8.375 0.01 1 42 . 23 VAL N N 119.827 0.05 1 43 . 24 TRP H H 9.325 0.01 1 44 . 24 TRP N N 126.012 0.05 1 45 . 24 TRP NE1 N 129.091 0.05 1 46 . 24 TRP HE1 H 10.057 0.01 2 47 . 25 ARG H H 8.796 0.01 1 48 . 25 ARG N N 120.393 0.05 1 49 . 26 VAL H H 8.523 0.01 1 50 . 26 VAL N N 125.016 0.05 1 51 . 27 GLY H H 9.145 0.01 1 52 . 27 GLY N N 118.443 0.05 1 53 . 28 LYS H H 8.880 0.01 1 54 . 28 LYS N N 126.137 0.05 1 55 . 29 MET H H 8.185 0.01 1 56 . 29 MET N N 118.109 0.05 1 57 . 30 VAL H H 9.316 0.01 1 58 . 30 VAL N N 124.296 0.05 1 59 . 31 SER H H 8.780 0.01 1 60 . 31 SER N N 122.737 0.05 1 61 . 32 PHE H H 7.557 0.01 1 62 . 32 PHE N N 114.872 0.05 1 63 . 33 THR H H 9.003 0.01 1 64 . 33 THR N N 109.228 0.05 1 65 . 34 TYR H H 8.551 0.01 1 66 . 34 TYR N N 115.868 0.05 1 67 . 35 ASP H H 8.798 0.01 1 68 . 35 ASP N N 119.843 0.05 1 69 . 36 GLU H H 8.463 0.01 1 70 . 36 GLU N N 126.498 0.05 1 71 . 37 GLY H H 8.514 0.01 1 72 . 37 GLY N N 109.719 0.05 1 73 . 38 GLY H H 8.839 0.01 1 74 . 38 GLY N N 110.086 0.05 1 75 . 39 GLY H H 8.999 0.01 1 76 . 39 GLY N N 107.377 0.05 1 77 . 40 LYS H H 7.514 0.01 1 78 . 40 LYS N N 121.313 0.05 1 79 . 41 THR H H 8.569 0.01 1 80 . 41 THR N N 119.356 0.05 1 81 . 42 GLY H H 8.567 0.01 1 82 . 42 GLY N N 114.376 0.05 1 83 . 43 ARG H H 7.766 0.01 1 84 . 43 ARG N N 117.217 0.05 1 85 . 44 GLY H H 7.744 0.01 1 86 . 44 GLY N N 107.450 0.05 1 87 . 45 ALA H H 6.755 0.01 1 88 . 45 ALA N N 117.263 0.05 1 89 . 46 VAL H H 9.026 0.01 1 90 . 46 VAL N N 115.685 0.05 1 91 . 47 SER H H 9.100 0.01 1 92 . 47 SER N N 120.925 0.05 1 93 . 48 GLU H H 8.791 0.01 1 94 . 48 GLU N N 124.363 0.05 1 95 . 49 LYS H H 8.040 0.01 1 96 . 49 LYS N N 116.126 0.05 1 97 . 50 ASP H H 7.555 0.01 1 98 . 50 ASP N N 116.765 0.05 1 99 . 51 ALA H H 7.469 0.01 1 100 . 51 ALA N N 124.526 0.05 1 101 . 53 LYS H H 9.107 0.01 1 102 . 53 LYS N N 124.892 0.05 1 103 . 54 GLU H H 9.891 0.01 1 104 . 54 GLU N N 117.027 0.05 1 105 . 55 LEU H H 7.334 0.01 1 106 . 55 LEU N N 117.417 0.05 1 107 . 56 LEU H H 7.334 0.01 1 108 . 56 LEU N N 117.417 0.05 1 109 . 57 GLN H H 8.298 0.01 1 110 . 57 GLN N N 117.983 0.05 1 111 . 58 MET H H 7.334 0.01 1 112 . 58 MET N N 117.417 0.05 1 113 . 59 LEU H H 7.475 0.01 1 114 . 59 LEU N N 118.616 0.05 1 115 . 60 GLU H H 7.796 0.01 1 116 . 60 GLU N N 118.322 0.05 1 117 . 61 LYS H H 7.931 0.01 1 118 . 61 LYS N N 119.376 0.05 1 119 . 62 GLN H H 8.010 0.01 1 120 . 62 GLN N N 119.372 0.05 1 121 . 63 LYS H H 8.112 0.01 1 122 . 63 LYS N N 122.676 0.05 1 123 . 64 LYS H H 7.965 0.01 1 124 . 64 LYS N N 127.977 0.05 1 stop_ save_