title: NMR assignments of the sylvatic dengue 1 virus envelope protein domain III.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX 77555-1157, USA. devolk@utmb.edu
authors.forename: David E
authors.initials: DE
authors.lastname: Volk
authors.forename: Kurtis M
authors.initials: KM
authors.lastname: Anderson
authors.forename: Sai H A
authors.initials: SH
authors.lastname: Gandham
authors.forename: Fiona J
authors.initials: FJ
authors.lastname: May
authors.forename: Li
authors.initials: L
authors.lastname: Li
authors.forename: David W C
authors.initials: DW
authors.lastname: Beasley
authors.forename: Alan D T
authors.initials: AD
authors.lastname: Barrett
authors.forename: David G
authors.initials: DG
authors.lastname: Gorenstein
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D003716:Dengue Virus / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons; D014759:Viral Envelope Proteins / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D014759:Viral Envelope Proteins