Figure 7
Varied electrostatic contributions of colicin/pyocin residues to interactions with the Im α3 region. Colicin residues that substantially contribute electrostatically to interactions with the Im α3 helix are shown as sticks, colored according to their energy contributions, as in Fig. 3. Colicin residues that contributed similarly to interactions across multiple members are marked with diamonds, colored as follows (the corresponding E7 position number, as in Fig. 3B, is also noted): orange (E7#514), gray (E7#515), purple (E7#517), green (E7#528), yellow (E7#530), blue (E7#531), red (E7#534), and cyan (E7#539). The α4 helices are colored cyan and the α4–β2 loops are colored green. Residues that contributed to interactions with the cognate immunity protein only in one complex are marked with black triangles. Colicin/pyocin structures are rotated 70° about the Y-axis relative to Fig. 5.
