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Biological Magnetic Resonance Data Bank


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BMRB Entry 17268

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17268
MolProbity Validation Chart

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Title: Solution Structures of Oxidized and Reduced Thioredoxin C from M. tb   PubMed: 23229911

Deposition date: 2010-10-28 Original release date: 2013-07-01

Authors: Olson, Andrew; Cai, Sheng; Sem, Daniel

Citation: Olson, Andrew; Neumann, Terrence; Cai, Sheng; Sem, Daniel. "Solution structures of Mycobacterium tuberculosis thioredoxin C and models of intact thioredoxin system suggest new approaches to inhibitor and drug design"  Proteins 81, 675-689 (2013).

Assembly members:
entity, polymer, 116 residues, 12557.545 Da.

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: MTDSEKSATIKVTDASFATD VLSSNKPVLVDFWATWCGPC KMVAPVLEEIATERATDLTV AKLDVDTNPETARNFQVVSI PTLILFKDGQPVKRIVGAKG KAALLRELSDVVPNLN

Data sets:
Data typeCount
13C chemical shifts302
15N chemical shifts104
1H chemical shifts739

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Thioredoxin C1

Entities:

Entity 1, Thioredoxin C 116 residues - 12557.545 Da.

1   METTHRASPSERGLULYSSERALATHRILE
2   LYSVALTHRASPALASERPHEALATHRASP
3   VALLEUSERSERASNLYSPROVALLEUVAL
4   ASPPHETRPALATHRTRPCYSGLYPROCYS
5   LYSMETVALALAPROVALLEUGLUGLUILE
6   ALATHRGLUARGALATHRASPLEUTHRVAL
7   ALALYSLEUASPVALASPTHRASNPROGLU
8   THRALAARGASNPHEGLNVALVALSERILE
9   PROTHRLEUILELEUPHELYSASPGLYGLN
10   PROVALLYSARGILEVALGLYALALYSGLY
11   LYSALAALALEULEUARGGLULEUSERASP
12   VALVALPROASNLEUASN

Samples:

Sample_1: potassium phosphate 50 mM; Thioredoxin_C, [U-13C; U-15N], 1.2 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: .05 M; pH: 6.3; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSample_1isotropicsample_conditions_1
3D C(CO)NHSample_1isotropicsample_conditions_1
3D HNCASample_1isotropicsample_conditions_1
3D HN(CO)CASample_1isotropicsample_conditions_1
3D HBHA(CO)NHSample_1isotropicsample_conditions_1
3D H(CCO)NHSample_1isotropicsample_conditions_1
3D HCCH-TOCSYSample_1isotropicsample_conditions_1
3D 1H-15N NOESYSample_1isotropicsample_conditions_1
3D 1H-13C NOESYSample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMRView, Johnson, One Moon Scientific - data analysis

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 17242
PDB
DBJ BAH28242 BAL68058 BAQ08156 GAA43797
EMBL CAA65071 CAL70004 CAL73962 CCC28997 CCC46265
GB AAK48398 ABQ75742 ABR08274 ACT27071 AEB06115
REF NP_218431 NP_857580 WP_003400164 WP_015288674 WP_031662639
SP P0A617 P9WG66 P9WG67

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts