Figure 3.

Dissociation of the CheYp–FliM_N complex at 0.1, 50, and 100 MPa, as simulated by PaCS-MD. (a) The inter-COM distance between CheYp and FliM_N, with d indicated as a function of the PaCS-MD cycle at 0.1 (top), 50 (center), and 100 (bottom) MPa. Five independent PaCS-MD simulations are shown in different colors. The broken lines indicate the borders between Phases 1–2 and 2–3. (b) COM positions of FliM_N obtained by PaCS-MD and all additional MD simulations at 100 MPa. Color differences denote different trials. (c) Examples of snapshots of FliM_N during a dissociation at 100 MPa. MD snapshots with four different d values are shown in different colors after superimposing CheYp. Molecular surfaces of the initial and last snapshots are shown in transparent colors. (d,e) Closeup view of the interface, (d) before the breakage of the key salt bridge (Lys119: CheY‒Asp12: FliM_N) at d = 18 Å, and (e) just after the detachment of the FliM_N helix at d = 27 Å at 100 MPa. Water molecules in the first hydration shell of each protein are shown with stick models and atomic-color basis.