title: NMR assignments of the yellow fever virus envelope protein domain III.
abstract: Nearly complete backbone and sidechain resonance assignments have been obtained for the third domain, residues S288-K398, of the envelope protein from the Asibi strain of yellow fever virus using double- and triple-resonance spectroscopy.
authors.affiliation: Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX 77555-1157, USA.
authors.forename: David E
authors.initials: DE
authors.lastname: Volk
authors.forename: Sai H A
authors.initials: SH
authors.lastname: Gandham
authors.forename: Fiona J
authors.initials: FJ
authors.lastname: May
authors.forename: Anjenique
authors.initials: A
authors.lastname: Anderson
authors.forename: Alan D T
authors.initials: AD
authors.lastname: Barrett
authors.forename: David G
authors.initials: DG
authors.lastname: Gorenstein
mesh_terms: D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics; D015005:Yellow fever virus / Q000737:chemistry* / Q000235:genetics
chemical_list: D010446:Peptide Fragments; D011994:Recombinant Proteins; D014759:Viral Envelope Proteins; C078400:yellow fever virus envelope protein E