CABS was able to explore large conformational changes of peptide-protein recognition via CABS-dock . The p53-MDM2 complex, a key target in anti-cancer drug design, where experimental data suggest significant rearrangements in the flexible N-terminal region of MDM2. Due to its large size and flexibility, atomistic models struggle with exhaustive binding dynamics studies for this complex. Using CABS-dock, simulations successfully generated near-native models without prior knowledge of the p53 peptide structure or binding site, aligning well with experimental data and the role of the N-terminal domain in binding . More recently, CABS-dock was employed within an integrative modelling to predict the self-assembled structures of protein fibrils such as 𝛽-amyloid by incorporating structural restraints that mimic experimental conditions. Although such protocol does not determine the overall structure of the assemble fibrils, and yet limits the whole exploration of the conformational space in proteins, it still yields an efficient method for protein structure determination. The CG potential can be accessed from the server .