Fig. 4.
Secondary structure and flexibility analysis of RuV MD in (a) apo and (b) ADPr bound state. Comparison of secondary structure analysis from the crystal structures (upper; 8P0C and 8P0E, respectively) with secondary structure prediction based on NMR experimental data using the TALOS+ server (Shen et al. 2009) (middle) shows good agreement for both RuV MD forms. Red cartoon indicates α-helix and blue arrow β-strand. In the plot (lower), the α-helix and β-strand SS values predicted using the TALOS+ server for each residue are shown as positive and negative values, respectively. The negative SS values for β-strands propensities are given for illustration purposes. Values close to 1 or -1 indicate a high possibility for α-helix and β-strand, respectively. The flexibility of RuV MD is also depicted as Random Coil Index (RCI) derived S2 (RCI-S2) values predicted by the TALOS+ server (Shen et al. 2009) and shown with blue dots. The reported amino acids for RuV MD are numbered in accordance with the native sequence of the multi-domain p150 protein.