Unbiased 200-ns simulations used for equilibration of the experimentally mapped lipid-binding site on PI(4,5)P2-rich bilayers for the moesin FERM domain. The simulations correspond to one of the three independent replicas that were used to generate the data shown in Figs. 3 and 4 and Fig. S5. At the beginning of the simulations, both proteins were placed slightly above the bilayer (<0.5 nm) with the known binding surface facing the lipids. Equilibration was reached in ∼50–60 ns, as quantified by saturation of the number of hydrogen bonds between the protein and the lipids. Phosphoinositide-interacting residues mapped in previous mutagenesis experiments are shown in blue licorice representation. PI(4,5)P2 and POPS lipids are shown in red and cyan, respectively. POPC and POPE lipids are shown in white.