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. Author manuscript; available in PMC: 2021 Jun 11.
Published in final edited form as: Structure. 2019 Sep 5;27(11):1647–1659.e4. doi: 10.1016/j.str.2019.08.009

Figure 1. NMR CSPs and Mapping on the Structure.

Figure 1.

(A) NMR CSPs of residues by truncated KRas4B1-166 (red sticks) and by full-length KRas4B1-188 (light blue sticks) mapped onto the crystal structures of CaM with a stretched central linker (PDB: 1CLL) (left panel) and a collapsed linker (PDB: 1CDL) (right panel). The light green sticks denote the perturbed residues by both truncated and full-length KRas4B.

(B) NMR CSPs of residues in full-length KRas4B1-188 in the GTP-γ-S bound state by CaM (left panel), and mapping of the perturbed residues on the crystal structure (PDB: 3GFT) of the catalytic domain of KRas4B (right panel). In the structure, hydrophobic, hydrophilic, positively charged, and negatively charged residues are marked by black, green, blue, and red letters, respectively.