Extended Data Fig. 1: The I358F mutation, selected by yeast surface display, increases protein stability and expression.
From: SARS-CoV-2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution
(A) The position of the I358F (bright yellow) mutation in the RBD structure (PDB ID 6M17) and the neighboring residues within 5 Å distance (pale yellow). (B) Shows the residues involved in the formation of the hydrophobic cavity around the I358F mutation predicted from the X-ray structure. Additional residues that are involved: K356, R357, S359, V395, Y396. (C) The spherical representation of the predicted position of the phenylalanine mutation inside the hydrophobic cavity (yellow) and wild-type residue (isoleucine, orange).
