The typical SII-P residues, such as Glu62, Asp69 and Tyr96, were identified to form key interactions with these two studied compounds, closely following observations from the analogous structures . The major discrepancy in direct interactions of these two inhibitors occurred with Lys16, Glu63 and His95. Discrepancy in interactions to Glu63 and His95 can be readily explained with the structural characteristics of the inhibitors (Figures and). However, interactions between LY3537982 and Lys16 were observed with relatively low frequency, when compared to what has been observed in comparable simulations earlier with other KRAS SII-P inhibitors 7,49 .