The functional form of the standard biomolecular force field has five components. Covalent interactions between atoms are modelled using harmonic bond stretching and angle bending parameters, while rotations about a bond are described by anharmonic 4-body torsional terms. Non-bonded interactions are described by a sum of Coulombic interactions between (usually) atom-centered point charges and a physically-motivated Lennard-Jones interaction, which combines a short-range repulsive r -12 potential with a longer-range attractive r -6 interaction. We now provide an overview of how these various components are parameterized in the QUBE protein force field, and contrast the approaches to those used in standard transferable force fields. Since the methods used to parameterize the non-bonded, and bond and angle terms have been extensively described elsewhere, we focus here on the derivation of the torsional parameters.