Correlations between binding affinity, thermal stability and local disorder in the opposable thumb region. Panel (A) shows the SPR binding affinity as a function of the thermal transition temperature (T*). Panel (B) correlates the binding affinity (left panel) and T* (right panel) with the average HD exchange fraction (after 1 hour) of the opposable thumb region. While p.Arg127Gln follows the trend in panel (A), it does not in panel (B). This observation demonstrates that p.Arg127Gln enhances the conformational dynamics of the opposable thumb indirectly through allostery while having little effect on the dynamics of local sequence environment near the mutation or the LRR domain.