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Dynamically-Driven Inactivation of the Catalytic Machinery of the SARS 3C-Like Protease by the N214A Mutation on the Extra Domain

Figure 9

Dynamic behavior of the mutation site.

Ramachandran plots of the residues Asn214 for WT (a–c); R298A (d–f) and Ala214 of N214A (g–i) in the 30 ns simulations. Time-trajectories of the Phi dihedral angle of Asn214 of WT (j–l); R298A (m–o), and Ala214 for N214A (p–r). Time-trajectories of the Psi dihedral angle of Asn214 of WT (s–u); R298A (v–x), and Ala214 for N214A (y–aa).

Figure 9

doi: https://doi.org/10.1371/journal.pcbi.1001084.g009