data_284 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Studies on the Solution Structure of Human Thioredoxin Using Heteronuclear 15N-1H Nuclear Magnetic Resonance Spectroscopy ; _BMRB_accession_number 284 _BMRB_flat_file_name bmr284.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 Forman-Kay Julie D. . 2 Gronenborn Angela M. . 3 Kay Lewis E. . 4 Wingfield Paul . . 5 Clore G. Marius . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "15N chemical shifts" 106 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-10 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Forman-Kay, Julie D., Gronenborn, Angela M., Kay, Lewis E., Wingfield, Paul, Clore, G. Marius, "Studies on the Solution Structure of Human Thioredoxin Using Heteronuclear 15N-1H Nuclear Magnetic Resonance Spectroscopy," Biochemistry 29 (6), 1566-1572 (1990). ; _Citation_title ; Studies on the Solution Structure of Human Thioredoxin Using Heteronuclear 15N-1H Nuclear Magnetic Resonance Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Forman-Kay Julie D. . 2 Gronenborn Angela M. . 3 Kay Lewis E. . 4 Wingfield Paul . . 5 Clore G. Marius . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1566 _Page_last 1572 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_thioredoxin _Saveframe_category molecular_system _Mol_system_name thioredoxin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label thioredoxin $thioredoxin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_thioredoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common thioredoxin _Name_variant 'N-val form' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; VKQIESKTAFQEALDAAGDK LVVVDFSATWCGPCKMIKPF FHSLSEKYSNVIFLEVDVDD CQDVASECEVKCTPTFQFFK KGQKVGEFSGANKEKLEATI NELV ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 LYS 3 GLN 4 ILE 5 GLU 6 SER 7 LYS 8 THR 9 ALA 10 PHE 11 GLN 12 GLU 13 ALA 14 LEU 15 ASP 16 ALA 17 ALA 18 GLY 19 ASP 20 LYS 21 LEU 22 VAL 23 VAL 24 VAL 25 ASP 26 PHE 27 SER 28 ALA 29 THR 30 TRP 31 CYS 32 GLY 33 PRO 34 CYS 35 LYS 36 MET 37 ILE 38 LYS 39 PRO 40 PHE 41 PHE 42 HIS 43 SER 44 LEU 45 SER 46 GLU 47 LYS 48 TYR 49 SER 50 ASN 51 VAL 52 ILE 53 PHE 54 LEU 55 GLU 56 VAL 57 ASP 58 VAL 59 ASP 60 ASP 61 CYS 62 GLN 63 ASP 64 VAL 65 ALA 66 SER 67 GLU 68 CYS 69 GLU 70 VAL 71 LYS 72 CYS 73 THR 74 PRO 75 THR 76 PHE 77 GLN 78 PHE 79 PHE 80 LYS 81 LYS 82 GLY 83 GLN 84 LYS 85 VAL 86 GLY 87 GLU 88 PHE 89 SER 90 GLY 91 ALA 92 ASN 93 LYS 94 GLU 95 LYS 96 LEU 97 GLU 98 ALA 99 THR 100 ILE 101 ASN 102 GLU 103 LEU 104 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-23 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 1400 thioredoxin 100.00 104 100.00 100.00 1.00e-67 BMRB 253 thioredoxin 100.00 105 100.00 100.00 9.06e-68 BMRB 254 thioredoxin 100.00 104 100.00 100.00 1.00e-67 BMRB 255 thioredoxin 100.00 104 100.00 100.00 1.00e-67 BMRB 256 thioredoxin 100.00 104 100.00 100.00 1.00e-67 BMRB 257 thioredoxin 100.00 105 100.00 100.00 9.06e-68 BMRB 283 thioredoxin 100.00 105 100.00 100.00 9.06e-68 BMRB 2958 thioredoxin 100.00 105 100.00 100.00 9.06e-68 BMRB 2959 thioredoxin 100.00 104 100.00 100.00 1.00e-67 PDB 1AIU "Human Thioredoxin (D60n Mutant, Reduced Form)" 100.00 105 98.08 99.04 1.72e-66 PDB 1AUC "Human Thioredoxin (Oxidized With Diamide)" 100.00 105 99.04 99.04 5.02e-67 PDB 1ERT "Human Thioredoxin (Reduced Form)" 100.00 105 99.04 99.04 5.02e-67 PDB 1ERU "Human Thioredoxin (Oxidized Form)" 100.00 105 99.04 99.04 5.02e-67 PDB 1ERV "Human Thioredoxin Mutant With Cys 73 Replaced By Ser (Reduced Form)" 100.00 105 98.08 98.08 6.10e-66 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 5.01e-65 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 2.81e-65 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 2.81e-65 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 2.81e-65 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 2.81e-65 PDB 2HSH "Crystal Structure Of C73s Mutant Of Human Thioredoxin-1 Oxidized With H2o2" 100.00 105 98.08 98.08 6.10e-66 PDB 2HXK "Crystal Structure Of S-Nitroso Thioredoxin" 100.00 105 97.12 97.12 1.40e-64 PDB 2IFQ "Crystal Structure Of S-Nitroso Thioredoxin" 100.00 105 99.04 99.04 5.02e-67 PDB 2IIY "Crystal Structure Of S-Nitroso Thioredoxin" 100.00 105 97.12 97.12 1.40e-64 PDB 3E3E "Human Thioredoxin Double Mutant C35s,C73r" 100.00 105 97.12 97.12 9.12e-65 PDB 3M9J "Crystal Structure Of Human Thioredoxin C6973S DOUBLE MUTANT, REDUCED Form" 100.00 105 97.12 97.12 5.01e-65 PDB 3M9K "Crystal Structure Of Human Thioredoxin C6973S DOUBLE-Mutant, Oxidized Form" 100.00 105 97.12 97.12 5.01e-65 PDB 3QFA "Crystal Structure Of The Human Thioredoxin Reductase-Thioredoxin Complex" 100.00 116 97.12 97.12 1.92e-65 PDB 3QFB "Crystal Structure Of The Human Thioredoxin Reductase-Thioredoxin Complex" 100.00 116 97.12 97.12 1.92e-65 PDB 3TRX "High-Resolution Three-Dimensional Structure Of Reduced Recombinant Human Thioredoxin In Solution" 100.00 105 100.00 100.00 9.06e-68 PDB 4LL1 "The Structure Of The Trx And Txnip Complex" 100.00 105 98.08 98.08 4.96e-66 PDB 4LL4 "The Structure Of The Trx And Txnip Complex" 100.00 105 98.08 98.08 4.96e-66 PDB 4PUF "Complex Between The Salmonella T3ss Effector Slrp And Its Human Target Thioredoxin-1" 100.00 117 99.04 99.04 2.15e-67 PDB 4TRX "High-Resolution Three-Dimensional Structure Of Reduced Recombinant Human Thioredoxin In Solution" 100.00 105 100.00 100.00 9.06e-68 DBJ BAF82197 "unnamed protein product [Homo sapiens]" 100.00 105 99.04 99.04 5.02e-67 EMBL CAA38410 "thioredoxin [Homo sapiens]" 100.00 105 99.04 99.04 5.02e-67 EMBL CAA54687 "ATL-derived factor/thioredoxin [Homo sapiens]" 100.00 105 99.04 99.04 5.02e-67 EMBL CAG28593 "TXN [Homo sapiens]" 100.00 105 99.04 99.04 5.02e-67 EMBL CAH91537 "hypothetical protein [Pongo abelii]" 100.96 106 98.10 98.10 3.85e-65 EMBL CEK46668 "Thioredoxin-1 [synthetic construct]" 100.00 125 99.04 99.04 1.49e-67 GB AAA74596 "thioredoxin [Homo sapiens]" 100.00 105 99.04 99.04 3.82e-67 GB AAF86466 "thioredoxin 1 [Homo sapiens]" 100.00 105 99.04 99.04 3.82e-67 GB AAF87085 "thioredoxin [Homo sapiens]" 100.00 105 99.04 99.04 5.02e-67 GB AAG34699 "thioredoxin [Homo sapiens]" 100.00 105 99.04 99.04 5.02e-67 GB AAH03377 "Thioredoxin [Homo sapiens]" 100.00 105 99.04 99.04 5.02e-67 REF NP_001125903 "thioredoxin [Pongo abelii]" 100.00 105 99.04 99.04 5.02e-67 REF NP_003320 "thioredoxin isoform 1 [Homo sapiens]" 100.00 105 99.04 99.04 5.02e-67 REF WP_052431332 "hypothetical protein, partial [Acinetobacter sp. MII]" 97.12 101 99.01 99.01 4.48e-65 REF XP_001142154 "PREDICTED: thioredoxin [Pan troglodytes]" 100.00 105 99.04 99.04 5.02e-67 REF XP_003257823 "PREDICTED: thioredoxin [Nomascus leucogenys]" 100.00 105 99.04 99.04 5.02e-67 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 5.02e-67 SP Q5R9M3 "RecName: Full=Thioredoxin; Short=Trx" 100.96 106 98.10 98.10 3.85e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $thioredoxin Human 9606 Eukaryota Metazoa Homo sapiens 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 $thioredoxin 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . na temperature 313 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label 'liquid NH3' N . . ppm 0 . . . . . $entry_citation $entry_citation 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name thioredoxin _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 . 2 LYS N N 128.9 . 1 2 . 3 GLN N N 126.5 . 1 3 . 4 ILE N N 127.3 . 1 4 . 5 GLU N N 123.4 . 1 5 . 6 SER N N 111.4 . 1 6 . 7 LYS N N 122.3 . 1 7 . 8 THR N N 115.3 . 1 8 . 9 ALA N N 123.7 . 1 9 . 10 PHE N N 120.5 . 1 10 . 11 GLN NE2 N 113.4 . 1 11 . 11 GLN N N 117.3 . 1 12 . 12 GLU N N 117.6 . 1 13 . 13 ALA N N 121.7 . 1 14 . 14 LEU N N 117.2 . 1 15 . 15 ASP N N 119.7 . 1 16 . 16 ALA N N 121.3 . 1 17 . 17 ALA N N 119 . 1 18 . 18 GLY N N 105.8 . 1 19 . 19 ASP N N 128.5 . 1 20 . 20 LYS N N 119.3 . 1 21 . 21 LEU N N 122.8 . 1 22 . 22 VAL N N 126 . 1 23 . 23 VAL N N 126.9 . 1 24 . 24 VAL N N 126.8 . 1 25 . 25 ASP N N 123.5 . 1 26 . 26 PHE N N 125.4 . 1 27 . 27 SER N N 117.7 . 1 28 . 28 ALA N N 121.7 . 1 29 . 29 THR N N 116.2 . 1 30 . 31 CYS N N 122.6 . 1 31 . 33 PRO N N 128.8 . 1 32 . 34 CYS N N 113.8 . 1 33 . 35 LYS N N 120.7 . 1 34 . 36 MET N N 116.2 . 1 35 . 37 ILE N N 115.8 . 1 36 . 38 LYS N N 125.3 . 1 37 . 39 PRO N N 129.1 . 1 38 . 40 PHE N N 119.5 . 1 39 . 41 PHE N N 121.9 . 1 40 . 42 HIS N N 114.6 . 1 41 . 43 SER N N 118.4 . 1 42 . 44 LEU N N 122.7 . 1 43 . 45 SER N N 114.2 . 1 44 . 46 GLU N N 118.5 . 1 45 . 47 LYS N N 119.2 . 1 46 . 48 TYR N N 118.7 . 1 47 . 49 SER N N 115.4 . 1 48 . 50 ASN ND2 N 112.2 . 1 49 . 50 ASN N N 118.3 . 1 50 . 51 VAL N N 120.7 . 1 51 . 52 ILE N N 127.7 . 1 52 . 53 PHE N N 125.9 . 1 53 . 54 LEU N N 122.6 . 1 54 . 55 GLU N N 121.5 . 1 55 . 56 VAL N N 125 . 1 56 . 57 ASP N N 128.8 . 1 57 . 58 VAL N N 119.6 . 1 58 . 59 ASP N N 119.4 . 1 59 . 60 ASP N N 120.8 . 1 60 . 61 CYS N N 120.3 . 1 61 . 62 GLN NE2 N 111.4 . 1 62 . 62 GLN N N 122.3 . 1 63 . 63 ASP N N 118.2 . 1 64 . 64 VAL N N 121.9 . 1 65 . 65 ALA N N 120.2 . 1 66 . 66 SER N N 111.5 . 1 67 . 67 GLU N N 123.8 . 1 68 . 68 CYS N N 114.5 . 1 69 . 69 GLU N N 116.9 . 1 70 . 70 VAL N N 119.6 . 1 71 . 71 LYS N N 126.9 . 1 72 . 72 CYS N N 114.3 . 1 73 . 73 THR N N 112.2 . 1 74 . 75 THR N N 119 . 1 75 . 76 PHE N N 125.6 . 1 76 . 77 GLN NE2 N 105.8 . 1 77 . 77 GLN N N 118.8 . 1 78 . 78 PHE N N 119.7 . 1 79 . 79 PHE N N 122.5 . 1 80 . 80 LYS N N 118.7 . 1 81 . 81 LYS N N 128.3 . 1 82 . 82 GLY N N 104.2 . 1 83 . 83 GLN NE2 N 112.1 . 1 84 . 83 GLN N N 118.7 . 1 85 . 84 LYS N N 125.9 . 1 86 . 85 VAL N N 120.3 . 1 87 . 86 GLY N N 107.6 . 1 88 . 87 GLU N N 117.7 . 1 89 . 88 PHE N N 117.8 . 1 90 . 89 SER N N 116.1 . 1 91 . 90 GLY N N 107.8 . 1 92 . 91 ALA N N 122.9 . 1 93 . 92 ASN ND2 N 112.6 . 1 94 . 92 ASN N N 121.8 . 1 95 . 93 LYS N N 125.1 . 1 96 . 94 GLU N N 119.2 . 1 97 . 95 LYS N N 120.7 . 1 98 . 96 LEU N N 122.8 . 1 99 . 97 GLU N N 117.3 . 1 100 . 98 ALA N N 120.3 . 1 101 . 99 THR N N 115 . 1 102 . 100 ILE N N 120.2 . 1 103 . 101 ASN N N 113.3 . 1 104 . 102 GLU N N 117.9 . 1 105 . 103 LEU N N 117.8 . 1 106 . 104 VAL N N 123.4 . 1 stop_ save_