NMR assignments of the sylvatic dengue 1 virus envelope protein domain III.
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.
Volk
David E
DE
Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX 77555-1157, USA. devolk@utmb.edu
Anderson
Kurtis M
KM
Gandham
Sai H A
SH
May
Fiona J
FJ
Li
Li
L
Beasley
David W C
DW
Barrett
Alan D T
AD
Gorenstein
David G
DG
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*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D014759:Viral Envelope Proteins