REMD simulation of ligand exiting from the cavity of IFABP and LFABP.

The time interval (Δt) of REMD was kept constant at 0.25 ps for all trajectories.
#Random force was applied on OLA129 only, while OLA128 was present in the low affinity binding site.
†The number of trajectories in which the ligand successfully egressed using the individual portals.
‡The number of trajectories in which the ligand failed to exit from the cavity in 200 ps.
**For IFABP, portal I refers to the helical portal.
*In this single trajectory, OLA129 partially protruded outside from portal II initially, then tried to slide over βE/βF loop, and eventually dissociated from the gap between the βE/βF loop and α-helix cap.
§Trajectories were used for the analysis of residues constituting individual portals of LFABP (Table 2).
§§Trajectories of successful dissociations were used for the analysis of residues constituting the portal of IFABP (Table 2).