Figure 2.
Figure 2 C backbone
plot of the F protein in the closed procapsid (red). The
asymmetric unit triangle is shown, with the symmetry axes
marked. The F-protein structure from the virion (yellow) was
superimposed on the closed procapsid F protein by minimizing the
r.m.s. distance between corresponding C atoms
in the -helical
domain (residues 175-207, 305-319). The main difference in the F
protein between the virion and the closed procapsid is a hinge
movement between the -helical
domain and the -sandwich
domain. Residues involved in second-site suppression of
cold-sensitive D mutants21 are circled.
backbone
plot of the F protein in the closed procapsid (red). The
asymmetric unit triangle is shown, with the symmetry axes
marked. The F-protein structure from the virion (yellow) was
superimposed on the closed procapsid F protein by minimizing the
r.m.s. distance between corresponding C 
-sandwich
domain. Residues involved in second-site suppression of
cold-sensitive D mutants21 are circled.