It was unexpected. I believe finetuning may be in order and EvoDiff is not really intended to generate binders out-of-the-box anyway. Still though, the changes in tertiary structure for the generated protein are puzzling and interesting. How does an alpha-helix with an some higher pLDDT scores (middle picture of the unbound generated binder) turn into beta-sheets with low pLDDT scores in the presence of the target protein (picture on the right)? I find that strange and interesting. Is this a more extreme example of sampling multiple conformations of proteins that are fold-switching? (see https://www.biorxiv.org/content/10.1101/2023.12.16.571997v1)