Figure 2

Comparison of dynamically important residues in myosin 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 myosin 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; (d). hinge residues identified by DynDom are shown as red spheres. Also shown in panel (d) is the observed conformational change from a pre-powerstroke myosin structure (PDB: 1VOM, colored in silver) to a post-powerstroke myosin structure (PDB: 2AKA, colored in cyan) superimposed along the N-terminal subdomain (residues 80–186), including rotations of U50, L50 and converter subdomains (shown as arrows). For details of the predicted key residues, see Table S3 in Additional file 1.