Figure 3.

(A) Superimposed structures of K‐Ras ⋅ Mg²⁺ ⋅ GDP (MD derived structure ^[36] ) (grey) and the nucleotide free H‐Ras ⋅ Sos compex (PDB: 1BKD, magenta). Regions displaying C^α positional differences larger than 2 Å between the two complexes are highlighted in yellow. Residues exhibiting a contribution to transverse relaxation of R _ex >2 Hz in K‐Ras ⋅ Mg²⁺ ⋅ GDP are depicted in blue. (B) C^α positional differences between K‐Ras ⋅ Mg²⁺ ⋅ GDP and H‐Ras ⋅ Sos along the amino acid sequence. (C) Values of ¹⁵ N R _ex (at 800 MHz for ¹H) of ¹⁵N‐labeled wild‐type K‐Ras ⋅ Mg²⁺ ⋅ GDP (T=25 °C, pH 7.4) as a function of amino acid sequence. R _ex is estimated from the difference in R _2,eff at the lowest and highest ν_CPMG values. Secondary structural elements are indicated at the top. Regions displaying d _CA>2 Å in (B) are shown in a yellow background.