FIG. 3.

Structure-based alignment of the amino acid sequences of E proteins from West Nile virus (wn) strain 2741 (2), Japanese encephalitis virus (je) strain JaOArS982, dengue virus type 2 (d2) strain S1, and tick-borne encephalitis virus (tbe) strain Neudörfl. Dots indicate amino acid identities; dashes show gaps. The domains are indicated by a colored bar as in Fig. 1. The sequences are truncated at the last residue (406) of the soluble fragment (sE) of West Nile virus E, which we crystallized. The conserved glycosylation site in domain I is indicated by a red asterisk and red lettering. Residues lining the hydrophobic pocket in sE are shaded in gray. Residues that are exposed on the viral surface and are conserved in West Nile virus strains but not in other flaviviruses are shaded in magenta. Residues that are exposed on the viral surface and are conserved in wn, je, d2, and tbe viruses are shaded in orange.