Protein dynamics simulation data analyses and structural visualization were performed using CHARMM , VMD  and R (http://www.R-project.org) programs. Protein secondary structure was calculated with STRIDE . The solvent accessible surface area (ASA) was calculated by CHARMM with a water probe size of 1.4 Å. Relative ASA for each epitope was calculated using ASA of individual epitope normalized by the total MEFA protein ASA.