Figure 2.

(a) RBD one letter sequence with contacting residues shown in red for the different hNAbs studied in this work. Amino acid residues in the WT sequence that were mutated are shown with an underline and larger font size. (b) Location of the amino acid residues in the RBD that interact with the different hNAbs. The location of the simulated mutations is also shown in the RBD geometry shown as a surface. (c) Binding energy values between the RBD (WT and mutated) and Class I hNAbs. These mutations include MT1: N501Y, MT2: E484K/N501Y, and MT3: K417N/E484K/N501Y. The values inside the bars are the compute binding energy. (d) Binding energy between the RBD (WT and mutated) and Class II hNAbs. (e) Binding energy map between RBD, ACE2, and several hNAbs. The color map indicates the difference in binding taking as a reference the WT RBD and the ACE2 receptor. The number in each cell is the actual binding energy in kJ mol${}^{-1}$. The ‘x’ symbol indicates that the binding energy was not computed for that combination since the mutation did not affect the binding residues.