The simulation results reveal that, in general, the OLIVES and GoMARTINI RMSF are compatible with the atomistic reference (Figure ,B). In this test case, we can identify a slight difference between running OLIVES with and without DSSP restraints when inspecting residue RMSD from the initial structure (SI Figure ). In the first few helices, residues 20-80, both OLIVES and GoMARTINI have higher RMSD compared to the simulations with DSSP restraints (SI Figure ). However, since the native contacts are completely preserved for OLIVES without the DSSP restraints and the absolute errors in the RMSF profile are generally below 0.1 nm (Figure ,B), this should not be a major concern. However, one could consider applying the DSSP restraints if the study of interest does not require the ability to unfold or change the secondary structure. Inspecting the interface native contacts, we observe that a quaternary network is not required to stabilize the ClC dimer in line with the results for the OMPLA dimer. This is reassuring since Martini is extensively used for oligomerization studies of transmembrane proteins. to implement the Gō-like bonds. However, 1-4 LJ bonds are internally regarded as bonded interactions in GROMACS, which leads to errors if the bond length becomes more than half the length of a domain when using domain decomposition. This would happen if a protein complex dissociates while having a quaternary network defined, however, if OLIVES is used for a monomeric protein or very stable complexes like the 20S proteasome, there should be no issues using domain decomposition. One way to resolve the domain decomposition issue when using quaternary networks is to implement the Gō-like bonds as non-bonded LJ interactions at the force field level between virtual particles co-localized on top of the protein beads, as done in the current GoMARTINI implementation.