We analyzed the protein-lipid interaction between the β 2 -adrenergic receptor and cholesterol using the PyLipID package. Similar to the original paper, we used 0.475 and 0.80 nm for the dual cutoffs that deal with the "rattling effect" in lipid binding. The binding sites were required to consist of at least four residues. We computed the per-residue and perbinding-site lipid count, occupancy, duration, residence time, and unbinding rate k off for each combination of lincs order and time step, as in simulations of membranes without proteins. Additionally, we calculated the SASA and binding pose RMSD for the binding sites. The per-residue and per-binding-site observables computed by PyLipID were averaged over the 50 highest scoring residues and the top 3 scoring binding sites, respectively. See the original PyLipID paper for more details about the quantities. Here and in the following, the internal doubling by Gromacs is not taken into account. The reason behind the high eigenvalues is closely related to the unequal masses and coupled, far-from-equilateral triangles involved in the constraints. While the use of equal masses and equilateral triangles would completely distort the topology of cholesterol, it would result in λ max ≈ 0.50 and lincs order = 5. The excessively large lincs order of the original Martini 2 cholesterol is not only infeasible in simulations, but would also be applied to all constraints in the system, not just the coupled ones with convergence issues.