All MM-MD simulations were performed with GROMACS 2019.4 32 using the CHARMM36 force field. Most of the following MD settings were used as suggested by CHARMM-GUI. First, an energy minimization was performed using the steepest descent algorithm with a maximum force tolerance of 1000 kJ•mol -1 •nm -1 and a maximum of 5000 steps. The short-range van der Waals and Coulomb cut-off distances were both set to 1.2 nm. The system was simulated using periodic boundary conditions. Particle mesh Ewald 34 was used to calculate long-range electrostatic interactions. Rigid holonomic constraints were activated on covalent bonds involving hydrogen atoms using the LINCS algorithm while SETTLE constraints in rigid TIP3P water were applied. Several potentials were used for imposing restraints on the motion of the POPC bilayer: i) a position restraint on the phosphor atoms of the phosphate groups was applied in the z direction with a force constant of k P z = 1000 kJ•mol -1 •nm -2 to keep the thickness of the bilayer, ii) the dihedral angle C1-C3-C2-O21 corresponding to the glycerol (GL) head is restrained to a reference angle θ GL 0 = 120 • , ∆θ GL = 2.5 • with a force constant of k GL dihr = 1000 kJ mol -1 nm -2 to keep the stereoisomer, and iii) the dihedral angle C18-C19-C110-C111 corresponding to the oleoyl chain (OL) was restrained to θ OL 0 = ∆θ OL = 0 • with a force constant of k OL dihr = 1000 kJ mol -1 nm -2 to keep the cis-isomer. Similarly, several position restraints were activated in both chains of the protein: a position restraint in the backbone atoms (BB) was applied with a force constant of k BB = k x = k y = k z = 4000 mol -1 nm -2 and for the side-chain (SC) atoms with a force constant of