data_5240 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5240 _Entry.Title ; 15N assignment of Alicyclobacillus acidocaldarius thermostable thioredoxin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-12-20 _Entry.Accession_date 2001-12-20 _Entry.Last_release_date 2004-09-10 _Entry.Original_release_date 2004-09-10 _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 Marilisa Leone . . . 5240 2 Paola 'Di Lello' . . . 5240 3 Emilia Pedone . Maria . 5240 4 Simonetta Bartolucci . . . 5240 5 Mose' Rossi . . . 5240 6 Benedetto 'Di Blasio' . . . 5240 7 Carlo Pedone . . . 5240 8 Michele Saviano . . . 5240 9 Carla Isernia . . . 5240 10 Roberto Fattorusso . . . 5240 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5240 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 111 5240 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 . . 2004-09-10 2001-12-20 original author . 5240 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5241 'Alicyclobacillus acidocaldarius thioredoxin (K18G/R82E mutant)' 5240 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5240 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 15147188 _Citation.Full_citation . _Citation.Title ; Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: a molecular analysis of its reduced thermal stability. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 43 _Citation.Journal_issue 20 _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 6043 _Citation.Page_last 6058 _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 Marilisa Leone . . . 5240 1 2 Paola 'Di Lello' . . . 5240 1 3 O. Ohlenschlager . . . 5240 1 4 Emilia Pedone . Maria . 5240 1 5 Simonetta Bartolucci . . . 5240 1 6 Mose' Rossi . . . 5240 1 7 Benedetto 'Di Blasio' . . . 5240 1 8 Carlo Pedone . . . 5240 1 9 Michele Saviano . . . 5240 1 10 Carla Isernia . . . 5240 1 11 Roberto Fattorusso . . . 5240 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5240 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11391017 _Citation.Full_citation ; Pedone E, Saviano M, Rossi M, Bartolucci S. A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli. Protein Eng. 2001 Apr;14(4):255-60. ; _Citation.Title 'A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Eng.' _Citation.Journal_name_full 'Protein engineering' _Citation.Journal_volume 14 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0269-2139 _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 255 _Citation.Page_last 260 _Citation.Year 2001 _Citation.Details ; Glu85 in the Escherichia coli thioredoxin, which is localized in the loop between beta4 and beta5, was substituted with the Arg present in the corresponding position in Bacillus acidocaldarius thioredoxin. This suggested that it could play an important role in the structure and thermostability of this protein owing to its involvement in numerous interactions. The effects of the mutation on the biophysical properties were analysed by circular dichroism, spectrofluorimetry and limited proteolysis, supported by molecular dynamics data. As modelling predicted, an increase in stability for E85R due to additional H-bonds between the beta5 and alpha4 regions was observed. ; 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 E Pedone E. . . 5240 2 2 M Saviano M. . . 5240 2 3 M Rossi M. . . 5240 2 4 S Bartolucci S. . . 5240 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5240 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10632710 _Citation.Full_citation ; Nicastro G, De Chiara C, Pedone E, Tato M, Rossi M, Bartolucci S. NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability. Eur J Biochem. 2000 Jan;267(2):403-13. ; _Citation.Title 'NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 267 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-2956 _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 403 _Citation.Page_last 413 _Citation.Year 2000 _Citation.Details ; The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx), an eubacterium growing optimally at 333 K, is the first Trx described to date from a moderate thermophilic source. To understand the molecular basis of its thermostability, the three-dimensional structure in the oxidized form was determined by NMR methods. A total of 2276 1H-NMR derived distance constraints along with 23 hydrogen-bonds, 72 phi and 27 chi1 torsion angle restraints, were used in a protocol employing simulated annealing followed by restrained molecular dynamics and restrained energy minimization. BacTrx consists of a well-defined core region of five strands of beta-sheet, surrounded by four exposed alpha-helices, features shared by other members of the thioredoxin family. The BacTrx 3D structure was compared with the Escherichia coli Trx (EcTrx) determined by X-ray crystallographic diffraction, and a number of structural differences were observed that may contribute to its thermostabilty. The results of structural analysis indicated that protein stability is due to cumulative effects, the main factor being an increased number of ionic interactions cross-linking different secondary structural elements and clamping the C-terminal alpha-helix to the core of the protein. ; 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 G Nicastro G. . . 5240 3 2 C 'De Chiara' C. . . 5240 3 3 E Pedone E. . . 5240 3 4 M Tato M. . . 5240 3 5 M Rossi M. . . 5240 3 6 S Bartolucci S. . . 5240 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5240 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9359865 _Citation.Full_citation ; Bartolucci S, Guagliardi A, Pedone E, De Pascale D, Cannio R, Camardella L, Rossi M, Nicastro G, de Chiara C, Facci P, Mascetti G, Nicolini C. Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling. Biochem J. 1997 Nov 15;328 ( Pt 1):277-85. ; _Citation.Title 'Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochem. J.' _Citation.Journal_name_full 'The Biochemical journal' _Citation.Journal_volume '328 ( Pt 1)' _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN 0264-6021 _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 277 _Citation.Page_last 285 _Citation.Year 1997 _Citation.Details ; The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx) was purified to homogeneity by anion-exchange chromatography and gel-filtration chromatography, based on its ability to catalyse the dithiothreitol-dependent reduction of bovine insulin disulphides. The protein has a molecular mass of 11577 Da, determined by electrospray mass spectrometry, a pI of 4.2, and its primary structure was obtained by automated Edman degradation after cleavage with trypsin and cyanogen bromide. The sequences of known bacterial Trxs were aligned at the active site: BacTrx has an identity ranging from 45 to 53% with all sequences except that of the unusual Anabaena strain 7120 Trx (37% identity). The gene coding for BacTrx was isolated by a strategy based on PCR gene amplification and cloned in a plasmid downstream of a lac-derived promoter sequence; the recombinant clone was used as the expression vector for Escherichia coli. The expression was optimized by varying both the time of cell growth and the time of exposure to the inducer isopropyl beta-d-thiogalactoside; expressed BacTrx represents approx. 5% of the total cytosolic protein. CD spectra and differential scanning calorimetry measurements demonstrated that BacTrx is endowed with a higher conformational heat stability than the Trx from E. coli. Nanogravimetry experiments showed a lower content of bound water in BacTrx than in E. coli Trx, and a transition temperature approx. 10 degrees C higher for BacTrx. The three-dimensional model of the oxidized form of BacTrx was constructed by a comparative molecular modelling technique, using E. coli Trx and Anabaena strain 7120 Trx as reference proteins. Increased networks of ion-pairs and shorter loops emerged as major features of the BacTrx structure compared with those of the template proteins. The findings are discussed in the light of the current knowledge about molecular determinants of protein stability. ; 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 Bartolucci S. . . 5240 4 2 A Guagliardi A. . . 5240 4 3 E Pedone E. . . 5240 4 4 D 'De Pascale' D. . . 5240 4 5 R Cannio R. . . 5240 4 6 L Camardella L. . . 5240 4 7 M Rossi M. . . 5240 4 8 G Nicastro G. . . 5240 4 9 C 'de Chiara' C. . . 5240 4 10 P Facci P. . . 5240 4 11 G Mascetti G. . . 5240 4 12 C Nicolini C. . . 5240 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Trx _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Trx _Assembly.Entry_ID 5240 _Assembly.ID 1 _Assembly.Name Thioredoxin _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 'all disulfide bound' _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 5240 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 'BacTrx wt' 1 $Trx_wt . . . native . . . . . 5240 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 29 29 SG . 1 . 1 CYS 32 32 SG . . . . . . . . . . 5240 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 1QUW . . . . . . 5240 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID Thioredoxin system 5240 1 Trx abbreviation 5240 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'disulfide oxidoreductase' 5240 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Trx_wt _Entity.Sf_category entity _Entity.Sf_framecode Trx_wt _Entity.Entry_ID 5240 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Alicyclobacillus acidocaldarius thioredoxin' _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 ; ATMTLTDANFQQAIQGDKPV LVDFWAAWCGPCRMMAPVLE EFAEAHADKVTVAKLNVDEN PETTSQFGIMSIPTLILFKG GRPVKQLIGYQPKEQLEAQL ADVLQ ; _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 105 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 11573.2 _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 4446 . Bactrx . . . . . 100.00 105 100.00 100.00 2.01e-70 . . . . 5240 1 2 no BMRB 5241 . Trx_mut . . . . . 100.00 105 98.10 98.10 1.78e-68 . . . . 5240 1 3 no PDB 1NSW . "The Crystal Structure Of The K18g Mutant Of The Thioredoxin From Alicyclobacillus Acidocaldarius" . . . . . 100.00 105 99.05 99.05 2.13e-69 . . . . 5240 1 4 no PDB 1NW2 . "The Crystal Structure Of The Mutant R82e Of Thioredoxin From Alicyclobacillus Acidocaldarius" . . . . . 100.00 105 99.05 99.05 1.83e-69 . . . . 5240 1 5 no PDB 1QUW . "Solution Structure Of The Thioredoxin From Bacillus Acidocaldarius" . . . . . 100.00 105 100.00 100.00 2.01e-70 . . . . 5240 1 6 no PDB 1RQM . "Solution Structure Of The K18gR82E ALICYCLOBACILLUS Acidocaldarius Thioredoxin Mutant" . . . . . 100.00 105 98.10 98.10 1.78e-68 . . . . 5240 1 7 no GB ACV57898 . "thioredoxin [Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446]" . . . . . 100.00 106 100.00 100.00 1.58e-70 . . . . 5240 1 8 no GB AEJ42820 . "thioredoxin [Alicyclobacillus acidocaldarius subsp. acidocaldarius Tc-4-1]" . . . . . 98.10 103 99.03 100.00 1.42e-68 . . . . 5240 1 9 no GB EED08563 . "thioredoxin [Alicyclobacillus acidocaldarius LAA1]" . . . . . 100.00 106 98.10 98.10 1.24e-68 . . . . 5240 1 10 no REF WP_008336730 . "thioredoxin [Alicyclobacillus acidocaldarius]" . . . . . 100.00 106 98.10 98.10 1.24e-68 . . . . 5240 1 11 no REF WP_012810252 . "thioredoxin [Alicyclobacillus acidocaldarius]" . . . . . 100.00 106 100.00 100.00 1.58e-70 . . . . 5240 1 12 no REF WP_014463721 . "thioredoxin [Alicyclobacillus acidocaldarius]" . . . . . 98.10 103 99.03 100.00 1.42e-68 . . . . 5240 1 13 no REF YP_003184287 . "thioredoxin [Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446]" . . . . . 100.00 106 100.00 100.00 1.58e-70 . . . . 5240 1 14 no REF YP_005517339 . "thioredoxin [Alicyclobacillus acidocaldarius subsp. acidocaldarius Tc-4-1]" . . . . . 98.10 103 99.03 100.00 1.42e-68 . . . . 5240 1 15 no SP P80579 . "RecName: Full=Thioredoxin; Short=Trx [Alicyclobacillus acidocaldarius subsp. acidocaldarius]" . . . . . 100.00 105 100.00 100.00 2.01e-70 . . . . 5240 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Alicyclobacillus acidocaldarius thioredoxin' common 5240 1 'BacTrx wt' abbreviation 5240 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 . ALA . 5240 1 2 . THR . 5240 1 3 . MET . 5240 1 4 . THR . 5240 1 5 . LEU . 5240 1 6 . THR . 5240 1 7 . ASP . 5240 1 8 . ALA . 5240 1 9 . ASN . 5240 1 10 . PHE . 5240 1 11 . GLN . 5240 1 12 . GLN . 5240 1 13 . ALA . 5240 1 14 . ILE . 5240 1 15 . GLN . 5240 1 16 . GLY . 5240 1 17 . ASP . 5240 1 18 . LYS . 5240 1 19 . PRO . 5240 1 20 . VAL . 5240 1 21 . LEU . 5240 1 22 . VAL . 5240 1 23 . ASP . 5240 1 24 . PHE . 5240 1 25 . TRP . 5240 1 26 . ALA . 5240 1 27 . ALA . 5240 1 28 . TRP . 5240 1 29 . CYS . 5240 1 30 . GLY . 5240 1 31 . PRO . 5240 1 32 . CYS . 5240 1 33 . ARG . 5240 1 34 . MET . 5240 1 35 . MET . 5240 1 36 . ALA . 5240 1 37 . PRO . 5240 1 38 . VAL . 5240 1 39 . LEU . 5240 1 40 . GLU . 5240 1 41 . GLU . 5240 1 42 . PHE . 5240 1 43 . ALA . 5240 1 44 . GLU . 5240 1 45 . ALA . 5240 1 46 . HIS . 5240 1 47 . ALA . 5240 1 48 . ASP . 5240 1 49 . LYS . 5240 1 50 . VAL . 5240 1 51 . THR . 5240 1 52 . VAL . 5240 1 53 . ALA . 5240 1 54 . LYS . 5240 1 55 . LEU . 5240 1 56 . ASN . 5240 1 57 . VAL . 5240 1 58 . ASP . 5240 1 59 . GLU . 5240 1 60 . ASN . 5240 1 61 . PRO . 5240 1 62 . GLU . 5240 1 63 . THR . 5240 1 64 . THR . 5240 1 65 . SER . 5240 1 66 . GLN . 5240 1 67 . PHE . 5240 1 68 . GLY . 5240 1 69 . ILE . 5240 1 70 . MET . 5240 1 71 . SER . 5240 1 72 . ILE . 5240 1 73 . PRO . 5240 1 74 . THR . 5240 1 75 . LEU . 5240 1 76 . ILE . 5240 1 77 . LEU . 5240 1 78 . PHE . 5240 1 79 . LYS . 5240 1 80 . GLY . 5240 1 81 . GLY . 5240 1 82 . ARG . 5240 1 83 . PRO . 5240 1 84 . VAL . 5240 1 85 . LYS . 5240 1 86 . GLN . 5240 1 87 . LEU . 5240 1 88 . ILE . 5240 1 89 . GLY . 5240 1 90 . TYR . 5240 1 91 . GLN . 5240 1 92 . PRO . 5240 1 93 . LYS . 5240 1 94 . GLU . 5240 1 95 . GLN . 5240 1 96 . LEU . 5240 1 97 . GLU . 5240 1 98 . ALA . 5240 1 99 . GLN . 5240 1 100 . LEU . 5240 1 101 . ALA . 5240 1 102 . ASP . 5240 1 103 . VAL . 5240 1 104 . LEU . 5240 1 105 . GLN . 5240 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 . ALA 1 1 5240 1 . THR 2 2 5240 1 . MET 3 3 5240 1 . THR 4 4 5240 1 . LEU 5 5 5240 1 . THR 6 6 5240 1 . ASP 7 7 5240 1 . ALA 8 8 5240 1 . ASN 9 9 5240 1 . PHE 10 10 5240 1 . GLN 11 11 5240 1 . GLN 12 12 5240 1 . ALA 13 13 5240 1 . ILE 14 14 5240 1 . GLN 15 15 5240 1 . GLY 16 16 5240 1 . ASP 17 17 5240 1 . LYS 18 18 5240 1 . PRO 19 19 5240 1 . VAL 20 20 5240 1 . LEU 21 21 5240 1 . VAL 22 22 5240 1 . ASP 23 23 5240 1 . PHE 24 24 5240 1 . TRP 25 25 5240 1 . ALA 26 26 5240 1 . ALA 27 27 5240 1 . TRP 28 28 5240 1 . CYS 29 29 5240 1 . GLY 30 30 5240 1 . PRO 31 31 5240 1 . CYS 32 32 5240 1 . ARG 33 33 5240 1 . MET 34 34 5240 1 . MET 35 35 5240 1 . ALA 36 36 5240 1 . PRO 37 37 5240 1 . VAL 38 38 5240 1 . LEU 39 39 5240 1 . GLU 40 40 5240 1 . GLU 41 41 5240 1 . PHE 42 42 5240 1 . ALA 43 43 5240 1 . GLU 44 44 5240 1 . ALA 45 45 5240 1 . HIS 46 46 5240 1 . ALA 47 47 5240 1 . ASP 48 48 5240 1 . LYS 49 49 5240 1 . VAL 50 50 5240 1 . THR 51 51 5240 1 . VAL 52 52 5240 1 . ALA 53 53 5240 1 . LYS 54 54 5240 1 . LEU 55 55 5240 1 . ASN 56 56 5240 1 . VAL 57 57 5240 1 . ASP 58 58 5240 1 . GLU 59 59 5240 1 . ASN 60 60 5240 1 . PRO 61 61 5240 1 . GLU 62 62 5240 1 . THR 63 63 5240 1 . THR 64 64 5240 1 . SER 65 65 5240 1 . GLN 66 66 5240 1 . PHE 67 67 5240 1 . GLY 68 68 5240 1 . ILE 69 69 5240 1 . MET 70 70 5240 1 . SER 71 71 5240 1 . ILE 72 72 5240 1 . PRO 73 73 5240 1 . THR 74 74 5240 1 . LEU 75 75 5240 1 . ILE 76 76 5240 1 . LEU 77 77 5240 1 . PHE 78 78 5240 1 . LYS 79 79 5240 1 . GLY 80 80 5240 1 . GLY 81 81 5240 1 . ARG 82 82 5240 1 . PRO 83 83 5240 1 . VAL 84 84 5240 1 . LYS 85 85 5240 1 . GLN 86 86 5240 1 . LEU 87 87 5240 1 . ILE 88 88 5240 1 . GLY 89 89 5240 1 . TYR 90 90 5240 1 . GLN 91 91 5240 1 . PRO 92 92 5240 1 . LYS 93 93 5240 1 . GLU 94 94 5240 1 . GLN 95 95 5240 1 . LEU 96 96 5240 1 . GLU 97 97 5240 1 . ALA 98 98 5240 1 . GLN 99 99 5240 1 . LEU 100 100 5240 1 . ALA 101 101 5240 1 . ASP 102 102 5240 1 . VAL 103 103 5240 1 . LEU 104 104 5240 1 . GLN 105 105 5240 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 5240 _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 $Trx_wt . 1388 . . 'Alicyclobacillus acidocaldarius' 'Alicyclobacillus acidocaldarius (Bacillus acidocaldarius)' . . Eubacteria . Alicyclobacillus acidocaldarius . . . . . . . . . . . . . . . . . . . . . 5240 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 5240 _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 $Trx_wt . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli Rb791 . . . . . . . . . . . . plasmid . . pTrc99A . . . . . . 5240 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5240 _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 'Alicyclobacillus acidocaldarius thioredoxin' [U-15N] . . 1 $Trx_wt . . 1.0 . . mM . . . . 5240 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_BacTrx _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_BacTrx _Sample_condition_list.Entry_ID 5240 _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 6.0 0.1 na 5240 1 temperature 298.0 0.1 K 5240 1 stop_ save_ ############################ # Computer software used # ############################ save_Vnmr _Software.Sf_category software _Software.Sf_framecode Vnmr _Software.Entry_ID 5240 _Software.ID 1 _Software.Name VNMR _Software.Version 6.1B _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectra processing' 5240 1 stop_ save_ save_PROSA _Software.Sf_category software _Software.Sf_framecode PROSA _Software.Entry_ID 5240 _Software.ID 2 _Software.Name PROSA _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectra processing' 5240 2 stop_ save_ save_xeasy _Software.Sf_category software _Software.Sf_framecode xeasy _Software.Entry_ID 5240 _Software.ID 3 _Software.Name XEASY _Software.Version 1.3.13 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5240 3 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 5240 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5240 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITY_INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5240 _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 INOVA . 750 . . . 5240 1 2 NMR_spectrometer_2 Varian UNITY_INOVA . 600 . . . 5240 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 5240 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-1H DQCOSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5240 1 2 '2D 1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5240 1 3 '2D 1H-1H TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5240 1 4 '2D 1H-15N HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5240 1 5 '3D 1H-1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5240 1 6 '3D 1H-1H-15N TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5240 1 7 '3D HNHA' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5240 1 8 '3D HNHB' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5240 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 5240 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '2D 1H-1H DQCOSY' _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 5240 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '2D 1H-1H NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5240 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '2D 1H-1H TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5240 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '2D 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_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5240 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '3D 1H-1H-15N NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5240 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '3D 1H-1H-15N 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_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5240 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name '3D HNHA' _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_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 5240 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name '3D HNHB' _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 5240 _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 water protons . . . . ppm 4.75 internal direct 1.0 internal spherical parallel . . . . . . 5240 1 N 15 'ammonium chloride' nitrogen . . . . ppm 119.33647 external direct 1.0 external spherical parallel . . . . . . 5240 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_shifts_BacTrx_wt _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shifts_BacTrx_wt _Assigned_chem_shift_list.Entry_ID 5240 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_BacTrx _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 '2D 1H-1H DQCOSY' 1 $sample_1 . 5240 1 2 '2D 1H-1H NOESY' 1 $sample_1 . 5240 1 3 '2D 1H-1H TOCSY' 1 $sample_1 . 5240 1 4 '2D 1H-15N HSQC' 1 $sample_1 . 5240 1 5 '3D 1H-1H-15N NOESY' 1 $sample_1 . 5240 1 6 '3D 1H-1H-15N TOCSY' 1 $sample_1 . 5240 1 7 '3D HNHA' 1 $sample_1 . 5240 1 8 '3D HNHB' 1 $sample_1 . 5240 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 THR N N 15 121.9 0.1 . 1 . . . . . . . . 5240 1 2 . 1 1 3 3 MET N N 15 124.2 0.1 . 1 . . . . . . . . 5240 1 3 . 1 1 4 4 THR N N 15 123.8 0.1 . 1 . . . . . . . . 5240 1 4 . 1 1 5 5 LEU N N 15 129.3 0.1 . 1 . . . . . . . . 5240 1 5 . 1 1 6 6 THR N N 15 111.8 0.1 . 1 . . . . . . . . 5240 1 6 . 1 1 7 7 ASP N N 15 121.1 0.1 . 1 . . . . . . . . 5240 1 7 . 1 1 8 8 ALA N N 15 121.0 0.1 . 1 . . . . . . . . 5240 1 8 . 1 1 9 9 ASN N N 15 116.5 0.1 . 1 . . . . . . . . 5240 1 9 . 1 1 9 9 ASN ND2 N 15 107.2 0.1 . 1 . . . . . . . . 5240 1 10 . 1 1 10 10 PHE N N 15 124.1 0.1 . 1 . . . . . . . . 5240 1 11 . 1 1 11 11 GLN N N 15 116.1 0.1 . 1 . . . . . . . . 5240 1 12 . 1 1 11 11 GLN NE2 N 15 113.0 0.1 . 1 . . . . . . . . 5240 1 13 . 1 1 12 12 GLN N N 15 117.5 0.1 . 1 . . . . . . . . 5240 1 14 . 1 1 12 12 GLN NE2 N 15 113.0 0.1 . 1 . . . . . . . . 5240 1 15 . 1 1 13 13 ALA N N 15 121.8 0.1 . 1 . . . . . . . . 5240 1 16 . 1 1 14 14 ILE N N 15 109.4 0.1 . 1 . . . . . . . . 5240 1 17 . 1 1 15 15 GLN N N 15 120.4 0.1 . 1 . . . . . . . . 5240 1 18 . 1 1 15 15 GLN NE2 N 15 113.5 0.1 . 1 . . . . . . . . 5240 1 19 . 1 1 16 16 GLY N N 15 109.2 0.1 . 1 . . . . . . . . 5240 1 20 . 1 1 17 17 ASP N N 15 119.0 0.1 . 1 . . . . . . . . 5240 1 21 . 1 1 18 18 LYS N N 15 122.7 0.1 . 1 . . . . . . . . 5240 1 22 . 1 1 20 20 VAL N N 15 126.1 0.1 . 1 . . . . . . . . 5240 1 23 . 1 1 21 21 LEU N N 15 132.6 0.1 . 1 . . . . . . . . 5240 1 24 . 1 1 22 22 VAL N N 15 128.2 0.1 . 1 . . . . . . . . 5240 1 25 . 1 1 23 23 ASP N N 15 126.7 0.1 . 1 . . . . . . . . 5240 1 26 . 1 1 24 24 PHE N N 15 130.6 0.1 . 1 . . . . . . . . 5240 1 27 . 1 1 25 25 TRP N N 15 122.0 0.1 . 1 . . . . . . . . 5240 1 28 . 1 1 25 25 TRP NE1 N 15 132.5 0.1 . 1 . . . . . . . . 5240 1 29 . 1 1 26 26 ALA N N 15 117.7 0.1 . 1 . . . . . . . . 5240 1 30 . 1 1 27 27 ALA N N 15 125.1 0.1 . 1 . . . . . . . . 5240 1 31 . 1 1 28 28 TRP N N 15 113.4 0.1 . 1 . . . . . . . . 5240 1 32 . 1 1 28 28 TRP NE1 N 15 138.3 0.1 . 1 . . . . . . . . 5240 1 33 . 1 1 29 29 CYS N N 15 122.7 0.1 . 1 . . . . . . . . 5240 1 34 . 1 1 30 30 GLY N N 15 123.6 0.1 . 1 . . . . . . . . 5240 1 35 . 1 1 32 32 CYS N N 15 112.7 0.1 . 1 . . . . . . . . 5240 1 36 . 1 1 33 33 ARG N N 15 123.5 0.1 . 1 . . . . . . . . 5240 1 37 . 1 1 34 34 MET N N 15 119.0 0.1 . 1 . . . . . . . . 5240 1 38 . 1 1 35 35 MET N N 15 117.2 0.1 . 1 . . . . . . . . 5240 1 39 . 1 1 36 36 ALA N N 15 124.3 0.1 . 1 . . . . . . . . 5240 1 40 . 1 1 38 38 VAL N N 15 121.3 0.1 . 1 . . . . . . . . 5240 1 41 . 1 1 39 39 LEU N N 15 121.3 0.1 . 1 . . . . . . . . 5240 1 42 . 1 1 40 40 GLU N N 15 119.0 0.1 . 1 . . . . . . . . 5240 1 43 . 1 1 41 41 GLU N N 15 121.0 0.1 . 1 . . . . . . . . 5240 1 44 . 1 1 42 42 PHE N N 15 122.9 0.1 . 1 . . . . . . . . 5240 1 45 . 1 1 43 43 ALA N N 15 121.9 0.1 . 1 . . . . . . . . 5240 1 46 . 1 1 44 44 GLU N N 15 117.7 0.1 . 1 . . . . . . . . 5240 1 47 . 1 1 45 45 ALA N N 15 121.3 0.1 . 1 . . . . . . . . 5240 1 48 . 1 1 46 46 HIS N N 15 113.5 0.1 . 1 . . . . . . . . 5240 1 49 . 1 1 47 47 ALA N N 15 125.4 0.1 . 1 . . . . . . . . 5240 1 50 . 1 1 48 48 ASP N N 15 115.0 0.1 . 1 . . . . . . . . 5240 1 51 . 1 1 49 49 LYS N N 15 119.3 0.1 . 1 . . . . . . . . 5240 1 52 . 1 1 50 50 VAL N N 15 116.7 0.1 . 1 . . . . . . . . 5240 1 53 . 1 1 51 51 THR N N 15 124.2 0.1 . 1 . . . . . . . . 5240 1 54 . 1 1 52 52 VAL N N 15 130.0 0.1 . 1 . . . . . . . . 5240 1 55 . 1 1 53 53 ALA N N 15 131.2 0.1 . 1 . . . . . . . . 5240 1 56 . 1 1 54 54 LYS N N 15 119.0 0.1 . 1 . . . . . . . . 5240 1 57 . 1 1 55 55 LEU N N 15 125.4 0.1 . 1 . . . . . . . . 5240 1 58 . 1 1 56 56 ASN N N 15 127.4 0.1 . 1 . . . . . . . . 5240 1 59 . 1 1 56 56 ASN ND2 N 15 111.3 0.1 . 1 . . . . . . . . 5240 1 60 . 1 1 57 57 VAL N N 15 124.6 0.1 . 1 . . . . . . . . 5240 1 61 . 1 1 58 58 ASP N N 15 122.7 0.1 . 1 . . . . . . . . 5240 1 62 . 1 1 59 59 GLU N N 15 117.0 0.1 . 1 . . . . . . . . 5240 1 63 . 1 1 60 60 ASN N N 15 117.2 0.1 . 1 . . . . . . . . 5240 1 64 . 1 1 60 60 ASN ND2 N 15 123.1 0.1 . 1 . . . . . . . . 5240 1 65 . 1 1 62 62 GLU N N 15 123.5 0.1 . 1 . . . . . . . . 5240 1 66 . 1 1 63 63 THR N N 15 122.3 0.1 . 1 . . . . . . . . 5240 1 67 . 1 1 64 64 THR N N 15 117.7 0.1 . 1 . . . . . . . . 5240 1 68 . 1 1 65 65 SER N N 15 115.5 0.1 . 1 . . . . . . . . 5240 1 69 . 1 1 66 66 GLN N N 15 124.9 0.1 . 1 . . . . . . . . 5240 1 70 . 1 1 66 66 GLN NE2 N 15 113.0 0.1 . 1 . . . . . . . . 5240 1 71 . 1 1 67 67 PHE N N 15 113.8 0.1 . 1 . . . . . . . . 5240 1 72 . 1 1 68 68 GLY N N 15 110.9 0.1 . 1 . . . . . . . . 5240 1 73 . 1 1 69 69 ILE N N 15 119.0 0.1 . 1 . . . . . . . . 5240 1 74 . 1 1 70 70 MET N N 15 128.9 0.1 . 1 . . . . . . . . 5240 1 75 . 1 1 71 71 SER N N 15 116.6 0.1 . 1 . . . . . . . . 5240 1 76 . 1 1 72 72 ILE N N 15 118.4 0.1 . 1 . . . . . . . . 5240 1 77 . 1 1 74 74 THR N N 15 121.1 0.1 . 1 . . . . . . . . 5240 1 78 . 1 1 75 75 LEU N N 15 128.7 0.1 . 1 . . . . . . . . 5240 1 79 . 1 1 76 76 ILE N N 15 121.7 0.1 . 1 . . . . . . . . 5240 1 80 . 1 1 77 77 LEU N N 15 130.0 0.1 . 1 . . . . . . . . 5240 1 81 . 1 1 78 78 PHE N N 15 129.3 0.1 . 1 . . . . . . . . 5240 1 82 . 1 1 79 79 LYS N N 15 120.3 0.1 . 1 . . . . . . . . 5240 1 83 . 1 1 80 80 GLY N N 15 120.1 0.1 . 1 . . . . . . . . 5240 1 84 . 1 1 81 81 GLY N N 15 106.2 0.1 . 1 . . . . . . . . 5240 1 85 . 1 1 82 82 ARG N N 15 119.7 0.1 . 1 . . . . . . . . 5240 1 86 . 1 1 84 84 VAL N N 15 122.4 0.1 . 1 . . . . . . . . 5240 1 87 . 1 1 85 85 LYS N N 15 120.0 0.1 . 1 . . . . . . . . 5240 1 88 . 1 1 86 86 GLN N N 15 124.9 0.1 . 1 . . . . . . . . 5240 1 89 . 1 1 86 86 GLN NE2 N 15 110.5 0.1 . 1 . . . . . . . . 5240 1 90 . 1 1 87 87 LEU N N 15 127.1 0.1 . 1 . . . . . . . . 5240 1 91 . 1 1 88 88 ILE N N 15 125.3 0.1 . 1 . . . . . . . . 5240 1 92 . 1 1 89 89 GLY N N 15 114.8 0.1 . 1 . . . . . . . . 5240 1 93 . 1 1 90 90 TYR N N 15 119.7 0.1 . 1 . . . . . . . . 5240 1 94 . 1 1 91 91 GLN N N 15 129.2 0.1 . 1 . . . . . . . . 5240 1 95 . 1 1 91 91 GLN NE2 N 15 111.5 0.1 . 1 . . . . . . . . 5240 1 96 . 1 1 93 93 LYS N N 15 124.4 0.1 . 1 . . . . . . . . 5240 1 97 . 1 1 94 94 GLU N N 15 116.6 0.1 . 1 . . . . . . . . 5240 1 98 . 1 1 95 95 GLN N N 15 120.8 0.1 . 1 . . . . . . . . 5240 1 99 . 1 1 95 95 GLN NE2 N 15 113.5 0.1 . 1 . . . . . . . . 5240 1 100 . 1 1 96 96 LEU N N 15 123.2 0.1 . 1 . . . . . . . . 5240 1 101 . 1 1 97 97 GLU N N 15 115.9 0.1 . 1 . . . . . . . . 5240 1 102 . 1 1 98 98 ALA N N 15 120.9 0.1 . 1 . . . . . . . . 5240 1 103 . 1 1 99 99 GLN N N 15 116.4 0.1 . 1 . . . . . . . . 5240 1 104 . 1 1 99 99 GLN NE2 N 15 112.0 0.1 . 1 . . . . . . . . 5240 1 105 . 1 1 100 100 LEU N N 15 117.8 0.1 . 1 . . . . . . . . 5240 1 106 . 1 1 101 101 ALA N N 15 123.8 0.1 . 1 . . . . . . . . 5240 1 107 . 1 1 102 102 ASP N N 15 115.0 0.1 . 1 . . . . . . . . 5240 1 108 . 1 1 103 103 VAL N N 15 114.9 0.1 . 1 . . . . . . . . 5240 1 109 . 1 1 104 104 LEU N N 15 120.8 0.1 . 1 . . . . . . . . 5240 1 110 . 1 1 105 105 GLN N N 15 124.7 0.1 . 1 . . . . . . . . 5240 1 111 . 1 1 105 105 GLN NE2 N 15 113.4 0.1 . 1 . . . . . . . . 5240 1 stop_ save_