Biomolecules exhibit dynamic behavior and adopt a distribution of conformations influenced by factors including sequence, temperature, pressure, ligand binding, and solution conditions. Traditionally, structural biology has predominantly focused on single-conformation models. However, it is broadly appreciated that most biomolecules must move to function. One of the earliest experimental demonstrations of protein structure plasticity came from NMR studies of aromatic-ring flips of the small protein bovine pancreatic trypsin inhibitor, where it was observed that conformational fluctuations allow rapid rotations of aromatic rings buried in the hydrophobic core . Recent advances in experimental and computational methods illustrate the importance of multiple-conformation modeling for understanding biomolecule functions. In particular, as the machine learning (ML) methods of AlphaFold2 (AF2) ,