Supplementary Figure 4: Residue-wise conformational flexibility of the sorLA Vps10p domain.

(a) Structural changes that accompany propeptide binding. The residue number is plotted against distance between mainchain Cα atoms in the ligand-free (at pH 4.5) and the propeptide-bound (at pH 6.5) forms of the sorLA Vps10p domain after structural superposition. Regions disordered in either structure are indicated by horizontal light blue bars. Note that the largest structural differences are found in L1 and the 10CC-b segments. (b) RMSF values for each residue during the MD simulation of the propeptide-bound form of sorLA Vps10p domain (see the legend to Figure 5d) are plotted similarly to the (a).