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. Author manuscript; available in PMC: 2021 Mar 14.
Published in final edited form as: Nature. 2020 Sep 14;588(7838):509–514. doi: 10.1038/s41586-020-2760-4

Extended Data Figure 1: Summary of ligand bound complexes of KSR1:MEK1 and KSR2:MEK1.

Extended Data Figure 1:

A. Resolution, number of reflections, and ligand omit maps for all described structures. Detailed data collection and refinement statistics are provided in Supplemental Data Table 1. Fo-Fc omit electron density maps are all contoured at 3.0 σ, with a 2.0 Å cutoff, around the ligands and shown as a blue mesh.

B. Trametinib bound to KSR2:MEK1:AMP-PNP.

C. Trametinib contacts include P878 in the pre-helix aG loop of KSR2. Direct contacts of trametinib with MEK1 also highlighted.

D. 2D schematic of the trametinib binding pocket in KSR2:MEK1.

E. 2D structures, formulas, and molecular weights of MEK inhibitors (MEKi) used in this study.