Figure 3. Mutational tolerance of Ras long and short constructs in the unregulated bacterial experiment.

(A) H-Ras^2-166, H-Ras^2-180, K-Ras^2-165, and K-Ras^2-173 in the unregulated experiment. The relative enrichment values (${\displaystyle \mathrm{\Delta }{E}_x^i}$) shown are the mean of three, four, two, and four biological replicates, respectively. Stop codons are labeled as ‘*’, and the bottom strip displays the functional effect of all amino acid substitutions at each position (${\displaystyle <\mathrm{\Delta }{E}_x^i{>}_x}$) – the average taken over each column. (B–C) Comparison of the mutational tolerance of residues in the hydrophobic core of K-Ras in the shorter and longer constructs. The enrichment scores for the hydrophobic core residues are shown for the two K-Ras constructs in B, and mapped onto K-Ras structure in C. PDB ID: 4OBE (Hunter et al., 2015).

Figure 3—figure supplement 1. ROC analysis between the mammalian Ba/F3 cell experiment and the unregulated bacterial H-Ras and K-Ras experiments.

Scores are lower than for the Ras+GAP experiments.