NMR assignments of the sylvatic dengue 1 virus envelope protein domain III
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Nearly complete backbone and side chain resonance assignments have been obtained for the third domain, residues M289–K400, of the envelope protein from the sylvatic strain (P72–1244) of the dengue 1 virus, containing mutations N336S and E370K, using double- and triple-resonance spectroscopy.
KeywordsDengue Flavivirus Nuclear magnetic resonance assignments Envelope protein
This work was funded by the Pediatric Dengue Vaccine Initiative, the Centers for Disease Control (U90CCU618754), the National Institute for Allergic and Infectious Diseases (U01 AI054827), the Welch Foundation (H1296), and the State of Texas Advanced Technology Program (004952-0038-2003). We thank Sean Moran for assistance with the Rice University spectrometer whose carbon-enhanced HCN cold probe was obtained through the Strategic Partnership for Research in Nanotechnology Grant AFRL (AFOSR) FA9550-04-1-0328.