BMRB Entry 17242

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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/BMR17242
MolProbity Validation Chart

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Title:
Solution Structures of Oxidized and Reduced Thioredoxin C from M. tb
Deposition date:
2010-10-07
Original release date:
2013-07-01
Authors:
Olson, Andrew; Cai, Sheng; Sem, Dan
Citation:

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).
PubMed: 23229911

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-23b

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts104
1H chemical shifts759

Time Domain Data

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:

H2O_sample: Thioredoxin C, [U-13C; U-15N], 1.2 mM; potassium phosphate 50 mM

D2O_sample: Thioredoxin C, [U-13C; U-15N], 1.2 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.3; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCH2O_sampleisotropicsample_conditions_1
3D CBCA(CO)NHH2O_sampleisotropicsample_conditions_1
3D C(CO)NHH2O_sampleisotropicsample_conditions_1
3D HNCOH2O_sampleisotropicsample_conditions_1
3D HNCAH2O_sampleisotropicsample_conditions_1
3D HNCACBH2O_sampleisotropicsample_conditions_1
3D HBHA(CO)NHH2O_sampleisotropicsample_conditions_1
3D HN(CO)CAH2O_sampleisotropicsample_conditions_1
3D H(CCO)NHH2O_sampleisotropicsample_conditions_1
3D HCCH-TOCSYD2O_sampleisotropicsample_conditions_1
3D 1H-15N NOESYH2O_sampleisotropicsample_conditions_1
3D 1H-13C NOESYD2O_sampleisotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

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

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 17268
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
AlphaFold P0A617 P9WG66 P9WG67

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks