Fig. 4.

Conformational free energy landscapes. (A) The order parameter (ξ₁, ξ₂) used to describe large-scale conformational transitions in the ML032222a LBD. ξ₁ and ξ₂ each represent the distance (dashed line) between the upper and lower lobes of the protein at the centers of mass of the highlighted atoms. Disulfide bonds are shown in red. (B) Free energy landscapes for the WT apo state (Top) and glycine complex (Bottom) plotted as 2D PMFs (Left) and 1D PMFs (Right). Contour lines correspond to a difference of 1 kcal/mol, with cooler colors being lower in free energy (see the color bar). Fig. S3 shows the SDs for the 2D PMFs, as determined by block averaging. For the 1D PMFs, the red-shaded region indicates the SD of the free energy. The locations of crystal structures are indicated by yellow dots. (C) Free energy landscapes for the R703K LBD. (D) Free energy landscapes for the E423S LBD.