data_254 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 254 _Entry.Title ; A Proton Nuclear Magnetic Resonance Assignment and Secondary Structure Determination of Recombinant Human Thioredoxin ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Julie Forman-Kay . D. . 254 2 G. Clore . Marius . 254 3 Paul Driscoll . C. . 254 4 Paul Wingfield . . . 254 5 Frederic Richards . M. . 254 6 Angela Gronenborn . M. . 254 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 254 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 2 254 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 5 . . 2010-06-10 . revision BMRB 'Complete natural source information' 254 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 254 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 254 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 254 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 254 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 254 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Forman-Kay, Julie D., Clore, G. Marius, Driscoll, Paul C., Wingfield, Paul, Richards, Frederic M., Gronenborn, Angela M., "A Proton Nuclear Magnetic Resonance Assignment and Secondary Structure Determination of Recombinant Human Thioredoxin," Biochemistry 28, 7088-7097 (1989). ; _Citation.Title ; A Proton Nuclear Magnetic Resonance Assignment and Secondary Structure Determination of Recombinant Human Thioredoxin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 28 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 7088 _Citation.Page_last 7097 _Citation.Year 1989 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Julie Forman-Kay . D. . 254 1 2 G. Clore . Marius . 254 1 3 Paul Driscoll . C. . 254 1 4 Paul Wingfield . . . 254 1 5 Frederic Richards . M. . 254 1 6 Angela Gronenborn . M. . 254 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_thioredoxin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_thioredoxin _Assembly.Entry_ID 254 _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 . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 thioredoxin 1 $thioredoxin . . . . . . . . . 254 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 1AIU . 'Human Thioredoxin (D60n Mutant, Reduced Form)' . . . . 256 1 yes PDB 1AUC . 'Human Thioredoxin (Oxidized With Diamide)' . . . . 256 1 yes PDB 1ERT . 'Human Thioredoxin (Reduced Form)' . . . . 256 1 yes PDB 1ERU . 'Human Thioredoxin (Oxidized Form)' . . . . 256 1 yes PDB 1ERV . 'Human Thioredoxin Mutant With Cys 73 Replaced By Ser (Reduced Form)' . . . . 256 1 yes PDB 3TRX . 'Thioredoxin (Reduced Form)' . . . . 256 1 yes PDB 4TRX . 'Thioredoxin (Reduced Form)' . . . . 256 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID thioredoxin system 254 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_thioredoxin _Entity.Sf_category entity _Entity.Sf_framecode thioredoxin _Entity.Entry_ID 254 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 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 ; VKQIESKTAFQEALDAAGDK LVVVDFSATWCGPCKMIKPF FHSLSEKYSNVIFLEVDVDD CQDVASECEVKCTPTFQFFK KGQKVGEFSGANKEKLEATI NELV ; _Entity.Polymer_seq_one_letter_code ; VKQIESKTAFQEALDAAGDK LVVVDFSATWCGPCKMIKPF FHSLSEKYSNVIFLEVDVDD CQDVASECEVKCTPTFQFFK KGQKVGEFSGANKEKLEATI NELV ; _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 104 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1400 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 254 1 2 no BMRB 253 . thioredoxin . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 254 1 3 no BMRB 255 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 254 1 4 no BMRB 256 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 254 1 5 no BMRB 257 . thioredoxin . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 254 1 6 no BMRB 283 . thioredoxin . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 254 1 7 no BMRB 284 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 254 1 8 no BMRB 2958 . thioredoxin . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 254 1 9 no BMRB 2959 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 254 1 10 no PDB 1AIU . "Human Thioredoxin (D60n Mutant, Reduced Form)" . . . . . 100.00 105 98.08 99.04 1.83e-66 . . . . 254 1 11 no PDB 1AUC . "Human Thioredoxin (Oxidized With Diamide)" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 12 no PDB 1ERT . "Human Thioredoxin (Reduced Form)" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 13 no PDB 1ERU . "Human Thioredoxin (Oxidized Form)" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 14 no PDB 1ERV . "Human Thioredoxin Mutant With Cys 73 Replaced By Ser (Reduced Form)" . . . . . 100.00 105 98.08 98.08 6.49e-66 . . . . 254 1 15 no PDB 1ERW . "Human Thioredoxin Double Mutant With Cys 32 Replaced By Ser And Cys 35 Replaced By Ser" . . . . . 100.00 105 97.12 97.12 5.32e-65 . . . . 254 1 16 no PDB 1TRS . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.12 97.12 2.99e-65 . . . . 254 1 17 no PDB 1TRU . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.12 97.12 2.99e-65 . . . . 254 1 18 no PDB 1TRV . "The High-resolution Three-dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.12 97.12 2.99e-65 . . . . 254 1 19 no PDB 1TRW . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.12 97.12 2.99e-65 . . . . 254 1 20 no PDB 2HSH . "Crystal Structure Of C73s Mutant Of Human Thioredoxin-1 Oxidized With H2o2" . . . . . 100.00 105 98.08 98.08 6.49e-66 . . . . 254 1 21 no PDB 2HXK . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 97.12 97.12 1.48e-64 . . . . 254 1 22 no PDB 2IFQ . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 23 no PDB 2IIY . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 97.12 97.12 1.48e-64 . . . . 254 1 24 no PDB 3E3E . "Human Thioredoxin Double Mutant C35s,C73r" . . . . . 100.00 105 97.12 97.12 9.70e-65 . . . . 254 1 25 no PDB 3M9J . "Crystal Structure Of Human Thioredoxin C6973S DOUBLE MUTANT, REDUCED Form" . . . . . 100.00 105 97.12 97.12 5.32e-65 . . . . 254 1 26 no PDB 3M9K . "Crystal Structure Of Human Thioredoxin C6973S DOUBLE-Mutant, Oxidized Form" . . . . . 100.00 105 97.12 97.12 5.32e-65 . . . . 254 1 27 no PDB 3QFA . "Crystal Structure Of The Human Thioredoxin Reductase-Thioredoxin Complex" . . . . . 100.00 116 97.12 97.12 2.05e-65 . . . . 254 1 28 no PDB 3QFB . "Crystal Structure Of The Human Thioredoxin Reductase-Thioredoxin Complex" . . . . . 100.00 116 97.12 97.12 2.05e-65 . . . . 254 1 29 no PDB 3TRX . "High-Resolution Three-Dimensional Structure Of Reduced Recombinant Human Thioredoxin In Solution" . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 254 1 30 no PDB 4LL1 . "The Structure Of The Trx And Txnip Complex" . . . . . 100.00 105 98.08 98.08 5.27e-66 . . . . 254 1 31 no PDB 4LL4 . "The Structure Of The Trx And Txnip Complex" . . . . . 100.00 105 98.08 98.08 5.27e-66 . . . . 254 1 32 no PDB 4PUF . "Complex Between The Salmonella T3ss Effector Slrp And Its Human Target Thioredoxin-1" . . . . . 100.00 117 99.04 99.04 2.29e-67 . . . . 254 1 33 no PDB 4TRX . "High-Resolution Three-Dimensional Structure Of Reduced Recombinant Human Thioredoxin In Solution" . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 254 1 34 no DBJ BAF82197 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 35 no EMBL CAA38410 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 36 no EMBL CAA54687 . "ATL-derived factor/thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 37 no EMBL CAG28593 . "TXN [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 38 no EMBL CAH91537 . "hypothetical protein [Pongo abelii]" . . . . . 100.96 106 98.10 98.10 4.09e-65 . . . . 254 1 39 no EMBL CEK46668 . "Thioredoxin-1 [synthetic construct]" . . . . . 100.00 125 99.04 99.04 1.58e-67 . . . . 254 1 40 no GB AAA74596 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 4.07e-67 . . . . 254 1 41 no GB AAF86466 . "thioredoxin 1 [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 4.07e-67 . . . . 254 1 42 no GB AAF87085 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 43 no GB AAG34699 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 44 no GB AAH03377 . "Thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 45 no REF NP_001125903 . "thioredoxin [Pongo abelii]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 46 no REF NP_003320 . "thioredoxin isoform 1 [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 47 no REF WP_052431332 . "hypothetical protein, partial [Acinetobacter sp. MII]" . . . . . 97.12 101 99.01 99.01 4.76e-65 . . . . 254 1 48 no REF XP_001142154 . "PREDICTED: thioredoxin [Pan troglodytes]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 49 no REF XP_003257823 . "PREDICTED: thioredoxin [Nomascus leucogenys]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 50 no SP P10599 . "RecName: Full=Thioredoxin; Short=Trx; AltName: Full=ATL-derived factor; Short=ADF; AltName: Full=Surface-associated sulphydryl " . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 254 1 51 no SP Q5R9M3 . "RecName: Full=Thioredoxin; Short=Trx" . . . . . 100.96 106 98.10 98.10 4.09e-65 . . . . 254 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'N-val form' variant 254 1 thioredoxin common 254 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 . VAL . 254 1 2 . LYS . 254 1 3 . GLN . 254 1 4 . ILE . 254 1 5 . GLU . 254 1 6 . SER . 254 1 7 . LYS . 254 1 8 . THR . 254 1 9 . ALA . 254 1 10 . PHE . 254 1 11 . GLN . 254 1 12 . GLU . 254 1 13 . ALA . 254 1 14 . LEU . 254 1 15 . ASP . 254 1 16 . ALA . 254 1 17 . ALA . 254 1 18 . GLY . 254 1 19 . ASP . 254 1 20 . LYS . 254 1 21 . LEU . 254 1 22 . VAL . 254 1 23 . VAL . 254 1 24 . VAL . 254 1 25 . ASP . 254 1 26 . PHE . 254 1 27 . SER . 254 1 28 . ALA . 254 1 29 . THR . 254 1 30 . TRP . 254 1 31 . CYS . 254 1 32 . GLY . 254 1 33 . PRO . 254 1 34 . CYS . 254 1 35 . LYS . 254 1 36 . MET . 254 1 37 . ILE . 254 1 38 . LYS . 254 1 39 . PRO . 254 1 40 . PHE . 254 1 41 . PHE . 254 1 42 . HIS . 254 1 43 . SER . 254 1 44 . LEU . 254 1 45 . SER . 254 1 46 . GLU . 254 1 47 . LYS . 254 1 48 . TYR . 254 1 49 . SER . 254 1 50 . ASN . 254 1 51 . VAL . 254 1 52 . ILE . 254 1 53 . PHE . 254 1 54 . LEU . 254 1 55 . GLU . 254 1 56 . VAL . 254 1 57 . ASP . 254 1 58 . VAL . 254 1 59 . ASP . 254 1 60 . ASP . 254 1 61 . CYS . 254 1 62 . GLN . 254 1 63 . ASP . 254 1 64 . VAL . 254 1 65 . ALA . 254 1 66 . SER . 254 1 67 . GLU . 254 1 68 . CYS . 254 1 69 . GLU . 254 1 70 . VAL . 254 1 71 . LYS . 254 1 72 . CYS . 254 1 73 . THR . 254 1 74 . PRO . 254 1 75 . THR . 254 1 76 . PHE . 254 1 77 . GLN . 254 1 78 . PHE . 254 1 79 . PHE . 254 1 80 . LYS . 254 1 81 . LYS . 254 1 82 . GLY . 254 1 83 . GLN . 254 1 84 . LYS . 254 1 85 . VAL . 254 1 86 . GLY . 254 1 87 . GLU . 254 1 88 . PHE . 254 1 89 . SER . 254 1 90 . GLY . 254 1 91 . ALA . 254 1 92 . ASN . 254 1 93 . LYS . 254 1 94 . GLU . 254 1 95 . LYS . 254 1 96 . LEU . 254 1 97 . GLU . 254 1 98 . ALA . 254 1 99 . THR . 254 1 100 . ILE . 254 1 101 . ASN . 254 1 102 . GLU . 254 1 103 . LEU . 254 1 104 . VAL . 254 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 . VAL 1 1 254 1 . LYS 2 2 254 1 . GLN 3 3 254 1 . ILE 4 4 254 1 . GLU 5 5 254 1 . SER 6 6 254 1 . LYS 7 7 254 1 . THR 8 8 254 1 . ALA 9 9 254 1 . PHE 10 10 254 1 . GLN 11 11 254 1 . GLU 12 12 254 1 . ALA 13 13 254 1 . LEU 14 14 254 1 . ASP 15 15 254 1 . ALA 16 16 254 1 . ALA 17 17 254 1 . GLY 18 18 254 1 . ASP 19 19 254 1 . LYS 20 20 254 1 . LEU 21 21 254 1 . VAL 22 22 254 1 . VAL 23 23 254 1 . VAL 24 24 254 1 . ASP 25 25 254 1 . PHE 26 26 254 1 . SER 27 27 254 1 . ALA 28 28 254 1 . THR 29 29 254 1 . TRP 30 30 254 1 . CYS 31 31 254 1 . GLY 32 32 254 1 . PRO 33 33 254 1 . CYS 34 34 254 1 . LYS 35 35 254 1 . MET 36 36 254 1 . ILE 37 37 254 1 . LYS 38 38 254 1 . PRO 39 39 254 1 . PHE 40 40 254 1 . PHE 41 41 254 1 . HIS 42 42 254 1 . SER 43 43 254 1 . LEU 44 44 254 1 . SER 45 45 254 1 . GLU 46 46 254 1 . LYS 47 47 254 1 . TYR 48 48 254 1 . SER 49 49 254 1 . ASN 50 50 254 1 . VAL 51 51 254 1 . ILE 52 52 254 1 . PHE 53 53 254 1 . LEU 54 54 254 1 . GLU 55 55 254 1 . VAL 56 56 254 1 . ASP 57 57 254 1 . VAL 58 58 254 1 . ASP 59 59 254 1 . ASP 60 60 254 1 . CYS 61 61 254 1 . GLN 62 62 254 1 . ASP 63 63 254 1 . VAL 64 64 254 1 . ALA 65 65 254 1 . SER 66 66 254 1 . GLU 67 67 254 1 . CYS 68 68 254 1 . GLU 69 69 254 1 . VAL 70 70 254 1 . LYS 71 71 254 1 . CYS 72 72 254 1 . THR 73 73 254 1 . PRO 74 74 254 1 . THR 75 75 254 1 . PHE 76 76 254 1 . GLN 77 77 254 1 . PHE 78 78 254 1 . PHE 79 79 254 1 . LYS 80 80 254 1 . LYS 81 81 254 1 . GLY 82 82 254 1 . GLN 83 83 254 1 . LYS 84 84 254 1 . VAL 85 85 254 1 . GLY 86 86 254 1 . GLU 87 87 254 1 . PHE 88 88 254 1 . SER 89 89 254 1 . GLY 90 90 254 1 . ALA 91 91 254 1 . ASN 92 92 254 1 . LYS 93 93 254 1 . GLU 94 94 254 1 . LYS 95 95 254 1 . LEU 96 96 254 1 . GLU 97 97 254 1 . ALA 98 98 254 1 . THR 99 99 254 1 . ILE 100 100 254 1 . ASN 101 101 254 1 . GLU 102 102 254 1 . LEU 103 103 254 1 . VAL 104 104 254 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 254 _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 $thioredoxin . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens EB-virus-immortalized-human-lymph . . . . . . . . . . . . . . . . . . . . 254 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 254 _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 $thioredoxin . 'not available' 'Escherichia coli' . . . Escherichia coli W3110cI . . . . . . . . . . . . . . . . . . . . . . 254 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 254 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 254 _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 5.5 . na 254 1 temperature 298 . K 254 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 254 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 254 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 254 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 254 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 254 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 254 _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 . DSS . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 254 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 254 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 254 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 57 57 ASP H H 1 9.04 . . 1 . . . . . . . . 254 1 2 . 1 1 57 57 ASP HA H 1 5.13 . . 1 . . . . . . . . 254 1 stop_ save_