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. Author manuscript; available in PMC: 2022 Nov 25.
Published in final edited form as: Nature. 2022 Jul 13;609(7926):408–415. doi: 10.1038/s41586-022-04928-2

Extended Data Figure 2. 200ns MD simulation of the SHOC2 complex, cryo-EM maps of SHOC2 T411 and proximal interactions with PP1C, SHOC2 N-term region degenerate RVxF motif and PP1C RVxF binding pocket, and AUC analysis of PP1C pair-wise interactions with complex members.

Extended Data Figure 2

a, An overview of the MD simulation system for the SHOC2 complex. b, Root-mean-square-deviation (RMSD) of the protein α-carbon throughout the simulation. c, Interaction fraction of contacting residue pairs between SHOC2 and PP1C. d, Interaction fraction of contacting residue pairs between SHOC2 and MRAS. e, Interaction fraction of contacting residue pairs between MRAS and PP1C. f, Local electron density map for T411 of SHOC2 (teal) and K147 of PP1CA (orange) and their neighboring residues (left) and SHOC2 N-terminal residues interacting with RVxF binding pocket of PP1c (right). The map (2Fo-Fc) is at 4.5 sigma. g, Sedimentation Velocity Analytical Ultracentrifugation (SV-AUC) analysis of PP1C binding to SHOC2 or MRAS-GppCp compared to PP1C alone, and with the presence of SHOC2 and MRAS-GppCp.