BMRB Entry 5680
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5680
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Title: Letter to the Editor: Sequence-specific assignment and secondary structure determination of the 195-residue complex formed by the Mycobacterium tuberculosis proteins CFP-10 and ESAT-6. Towards an understanding of their role in tuberculosis pathogenesis
Deposition date: 2003-01-31 Original release date: 2004-11-29
Authors: Renshaw, Philip; Veverka, Vaclav; Kelly, Geoff; Frenkiel, Thomas; Williamson, Richard; Gordon, Stephen; Hewinson, R.; Carr, Mark
Citation: Renshaw, Philip; Veverka, Vaclav; Kelly, Geoff; Frenkiel, Thomas; Williamson, Richard; Gordon, Stephen; Hewinson, R.; Carr, Mark. "Letter to the Editor: Sequence-specific assignment and secondary structure determination of the 195-residue complex formed by the Mycobacterium tuberculosis proteins CFP-10 and ESAT-6. " J. Biomol. NMR 30, 225-226 (2004).
Assembly members:
Culture Filtrate Protein of 10 kDa, polymer, 100 residues, 10662 Da.
ESAT-6, polymer, 95 residues, Formula weight is not available
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Eubacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis and bovis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Culture Filtrate Protein of 10 kDa: MAEMKTDAATLAQEAGNFER
ISGDLKTQIDQVESTAGSLQ
GQWRGAAGTAAQAAVVRFQE
AANKQKQELDEISTNIRQAG
VQYSRADEEQQQALSSQMGF
ESAT-6: MTEQQWNFAGIEAAASAIQG
NVTSIHSLLDEGKQSLTKLA
AAWGGSGSEAYQGVQQKWDA
TATELNNALQNLARTISEAG
QAMASTEGNVTGMFA
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 1141 |
13C chemical shifts | 533 |
15N chemical shifts | 194 |
Additional metadata:
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