Below are links to interactive visualizations of the SARS-CoV-2 RBD deep mutational scanning data (paper here and preprint here) mapped onto protein structures, enabled by dms-view.
Below are specific dms-view renderings of residues discussed in the indicated sections of the paper.
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Residues exhibiting binding-stability tradeoffs, e.g. G502 and Y449, L455, F486, Y505 (Figures 3, S5A,B [S6A,B in preprint])
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Residues exhibiting binding-specific mutational constraint (Figure 5C)
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Disulfide cysteines and N-linked glycans (Figure S5E [5F in preprint])
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Surface positions that could tolerate putative glycan knock-in (Figures S5G,H [S6E,F in preprint])
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ACE2 interface residues (Figure 5D [6A in preprint])
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ACE2 interface residues that differ between SARS-CoV-2 and SARS-CoV-1 (Figure 5F [6C in preprint])
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Antibody epitopes for B38, 80R, S230, F26G19, m396, CR3022, VHH-72, S309 (N343 glycan not shown), and our newly identified E465 patch (Figure 6A [7A in preprint])
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Sites of antibody escape mutations sampled by Baum et al. 2020 (Figures S6C,D [S7C,D in preprint])