In order to create a Gō-like model based on hydrogen bond networks, we searched the literature for ab initio calculations of hydrogen bond energies and use the data to create a hydrogen bond donor/acceptor energy matrix (Table ). The collected energy values lie in the range of 3.5-8.0 kcal/mol. This is in line with other ab initio calculations and literature reviews reporting hydrogen bond energies in the range of 5-6 kcal/mol in the gas phase, representative of the protein interior (dielectric constant of ≈3), though the bond energy can be as low as 1.5-2.0 kcal/mol in a water environment. By using an energy matrix for the construction of a hydrogen bond network between different hydrogen bond donor/acceptor moieties, OLIVES increases the chemical specificity of the Gō-like bonds, which in turn is more representative of the local protein environment, compared to uniform energy across all bias potentials as currently used in elastic bond networks and the GoMARTINI Gō-like model. We classify the hydrogen bonding beads in the Martini 3 protein model according to Figure . As we were not able to find a complete matrix for all possible combinations of hydrogen bond partners in proteins, we have to simplify a few interactions, consequently, we set the hydroxyl and carboxylic acids acceptor energy to be equivalent to a ketone acceptor. Likewise, we did not find specific values for the lysine primary amine and arginine guanidino groups, which we instead set to equal the energy of imidazole partners. We include π-acceptor energies 13 in the model, although because of the coarse-grained granularity of aromatic rings in Martini 3, we split the interaction energy in two between the outermost beads in aromatic groups (Figure , PHE, TYR, TRP). Table : Hydrogen bond energy matrix collected from ab initio calculations in the literature in units of kcal/mol. (HYD) hydroxyl donor, (AMD) amide donor, (IMD) imidazole donor, (IND) indole donor, (KEA) ketone donor, (AMA) amide acceptor, (IMA) imidazole acceptor, (PIA) π acceptor. Note that the majority of the results were obtained by DFT calculations, which have a typical error of 2 kcal/mol. The OLIVES algorithm identifies native contacts with hydrogen bond capabilities in coarse-grained proteins. The algorithm is outlined in Figure ,A. In the initial step, OLIVES calculates all pairwise distances between beads within a 0.55 nm cutoff in the input coarsegrained structure and uses the classification scheme outlined in Figure to group the bead pairs into hydrogen bond donor/acceptor pairs. These are further divided into two networks which we denote the secondary network and the tertiary network. The secondary network exclusively contains pairs between backbone beads while the tertiary network consists of pairs from side chain beads to backbone beads and side chain beads to side chain beads.