Molecular Dynamic simulation.

<p>A) The evolution of the RMSD (Root Mean Square Deviation) of WT-g14-3-3 (in red) and Pho-g14-3-3 (in black) during the simulation. In order to allow the system to equilibrate, the first 20 ns of simulation were discarded from the analyses (region shaded in grey). B) The per residue RMSF (Root Mean Square Fluctuation). Helices H and I are enclosed in dashed boxes. The position of Thr214 is indicated with an arrow. The bottom plot (grey) shows the per residue RMSF difference between WT-g14-3-3 and Pho-g14-3-3. A schematic secondary structure diagram of the g14-3-3 is reported on the top. C) Eigenvectors cumulative weight on total motion for WT-g14-3-3 (in red) and Pho-g14-3-3 (in black). Projection of motion along the first eigenvector for Pho-g14-3-3 D) and the WT-g14-3-3 E) protein structures. The amplitude of motion follows the color scale from red to blue. The phosphorylated residue is represented in grey and indicated with an arrow.