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-Structure paper
| Title | Solution nmr structure of the ob-fold domain of heme chaperone ccme from desulfovibrio vulgaris. northeast structural genomics target dvr115g. |
|---|---|
| Journal, issue, pages | To be Published |
| Publish date | Dec 29, 2008 (structure data deposition date) |
Authors | Aramini, J.M. / Rossi, P. / Lee, H. / Lemak, A. / Wang, H. / Foote, E.L. / Jiang, M. / Xiao, R. / Nair, R. / Swapna, G.V.T. ...Aramini, J.M. / Rossi, P. / Lee, H. / Lemak, A. / Wang, H. / Foote, E.L. / Jiang, M. / Xiao, R. / Nair, R. / Swapna, G.V.T. / Acton, T.B. / Rost, B. / Everett, J.K. / Montelione, G.T. |
External links | Search PubMed |
| Methods | NMR (solution) |
| Structure data | ![]() PDB-2kct: |
| Source |
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Keywords | CHAPERONE / solution NMR structure / heme chaperone / cytochrome c biogenesis / OB-fold domain / NESG / PSI-2 / Structural Genomics / Protein Structure Initiative / Northeast Structural Genomics Consortium / BIOSYNTHETIC PROTEIN |
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desulfovibrio vulgaris str. hildenborough (bacteria)
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