NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3
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Sequence-specific NMR assignments of an internal domain of the protein nsp3, nsp3(513–651), which is a part of the SARS coronavirus (SARS-CoV) replicase polyprotein, have been determined, using triple-resonance NMR experiments with the uniformly [13C,15N]-labeled protein. The complete assignments (>99%) provide the basis for the ongoing three-dimensional structure determination.
KeywordsSARS-CoV Nonstructural protein nsp3 nsp3c SARS-unique domain
We thank Jeremiah Joseph, Vanitha Subramanian, Benjamin W. Neuman, Michael J. Buchmeier, Raymond C. Stevens and Peter Kuhn of the Consortium for Functional and Structural Proteomics of the SARS-CoV for providing us with the nsp3(451-651) and nsp3(466-651) constructs for the initial NMR screening. This study was supported by the NIAID/NIH contract #HHSN266200400058C “Functional and Structural Proteomics of the SARS-CoV” to P. Kuhn and M. J. Buchmeier, and by the Joint Center for Structural Genomics through the NIH/NIGMS grant #U54-GM074898. Additional support was obtained for M. A. J., P. S. and B. P. through fellowships from the Canadian Institutes of Health Research, the Spanish Ministry of Science and Education, and the Swiss National Science Foundation (PA00A-109047/1), respectively, and by the Skaggs Institute for Chemical Biology. Kurt Wüthrich is the Cecil H. and Ida M. Green Professor of Structural Biology at TSRI.
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