Figure 3

Comparison of dynamically important residues in kinesin predicted by various protocols. (a). key residues predicted by and δf _i are shown as red and green spheres, the common residues are colored in yellow, key components and sites in kinesin are also labeled; (b). key residues predicted by and δλ_{m, i}are shown as red and blue spheres, the common residues are colored in purple; (c). key residues predicted by GNM score and high connectivity are shown as green and blue spheres, the overlapping residues are colored in cyan. Shown in panel (d) is the observed conformational change from an ADP-bound KIF1A structure (PDB: 1I5S, colored in silver) to an ATP-analog-bound KIF1A structure (PDB: 1VFW, colored in cyan), including rotations and translations of α 4, α 5 helices (shown as arrows). For details of the predicted key residues, see Table S4 in Additional file 1.