Docking of 8400 peptides into an experimental structure of bacterial peptide transporter DtpB

<p>Di- and tripeptides composed of proteinogenic amino acids were docked into an experimental structure of DtpB using Rosetta FlexPepDock protocol. Additional experimental structures of DtpB were used to train a classifier to select top docking poses. Average Rosetta energy terms for top 10 hits were then combined with experimental affinity measurements to train a binary classifier that predicts binders to DtpB.</p> <p>This upload includes input and output data as well as code to run and analyse the full pipeline. Some intermediate results are available upon request.</p> <p>For more details, please see:<br> <strong>Plasticity of the binding pocket in peptide transporters underpins promiscuous substrate recognition</strong></p> <p>https://dx.doi.org/10.1016/j.celrep.2023.112831</p>