Despite the unresolvable intrinsic binding poses of weakly interacting proteins, it is possible to compare how the same protein pairs are stabilized when bound by different compounds assuming no ternary perturbation, i.e., ∆G s geo,ALB = 0 (Figure ). Figure shows four examples of well-aligned proteinprotein binding poses and four examples of different protein-protein binding poses. Surprisingly, despite distinctly different scaffolds between epibestatin and pyrrolidone1 (Tanimoto similarity = 0.11 with Morgan fingerprint with radius of 2) and different binding locations (ligand center-of-mass (COM) deviation = 0.99 nm), they reveal a very similar intermolecular geometry between proteins 14-3-3 and PMA2 (Figure ). Similarly, compounds BMS-8 and BMS-22 (Tanimoto similarity = 0.33) bind at different interfaces of the PDL1 homodimer (ligand COM deviation = 1.24 nm), yielding similar dimer configurations (Figure ). The same protein-protein binding poses are also observed when stabilized by compounds that bind at the same site such as (R)-CR8 and HQ461 (Tanimoto similarity = 0.13) binding to DDB1/CDK12 (ligand COM deviation = 0.15 nm) or two PROTACs with the same warheads and similar linker length binding to pVHL/SMARCA2 (Tanimoto similarity = 0.86) (Figure ).