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. 2020 Apr 3;117(16):8890–8899. doi: 10.1073/pnas.1910670117

Fig. 4.

Fig. 4.

Chemically equivalent residues in the axial and peripheral HS binding sites. (A) Sequence alignment of E2 of different EEEV strains (FL91-4679, TX95, MA38, MS83, TX91, FL96, LA50, GA91, LA47, and NJ60) of the E2 glycoproteins. (B) Sequence alignment of E2 of the different alphaviruses (VEEV, EEEV, WEEV, CHIKV, SINV, and RRV) of the E2 glycoproteins. In A and B, residues in the axial (N80, H82, R84, H114, and R119) and peripheral (H5, H155, K156, and R157) sites are indicated below the extracted sequence regions. Residues highlighted in red are completely conserved, in blue are highly conserved, and in white are not conserved. (C) Structural alignment of residues in the axial (labeled black) and peripheral (labeled orange) sites. The Cα atoms of residues in the axial and peripheral sites are shown as gray spheres. The “best” structural alignment is shown with the lowest RMSD between the axial and peripheral sites as listed in Table 2.