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TitleMurine norovirus protein NS1/2 aspartate to glutamate mutation, sufficient for persistence, reorients side chain of surface exposed tryptophan within a novel structured domain.
Journal, issue, pagesProteins, Vol. 82, Page 1200-1209, Year 2014
Publish dateAug 18, 2013 (structure data deposition date)
AuthorsBorin, B.N. / Tang, W. / Nice, T.J. / McCune, B.T. / Virgin, H.W. / Krezel, A.M.
External linksProteins / PubMed:24273131
MethodsNMR (solution)
Structure data

PDB-2mcd:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus NS1/2 D94E mutant
Method: SOLUTION NMR

PDB-2mch:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus NS1/2 CW3 WT
Method: SOLUTION NMR

PDB-2mck:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus CR6 NS1/2 protein
Method: SOLUTION NMR

Source
  • murine norovirus 1
  • murine norovirus gv/cr6/2005/usa
KeywordsHYDROLASE / Norovirus / NS1/2

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