There are two particular losses that were added to the hallucination. One was a secondary structure loss for the RBX1 protein. Here, we optimize for binders that create a intermolecular beta sheet with the N-terminal IDR of RBX1. If the target protein has a high secondary structure content (it is forming a beta sheet with the binder) we prefer that. The other loss was a contact loss to encourage as many contacts with RBX1 as possible. Since the vast majority of RBX1's residues have been shown to interact with other proteins, we try to make sure of the entire protein as much as possible as an epitope. Increasing the contacts should hopefully encourage tighter binding.

The other loss terms are standard loss terms we optimize for during hallucination (ipAE, ipTM, pLDDT, etc.)