Biomolecular and cellular probing of the interaction between the bitter peptide VAPFPEVF and TAS2R16 reveals a distinct binding studied by an integrated AFM and modeling approach

Topology and initial coordinates files of the Molecular Dynamics (MD) simulations of TAS2R16 models in the complex with VAPFPEVF peptide. We used OpenMM (v8.0) as a molecular engine, CHARMM36 as force field. Three replicas of 1 µs (dcd files: filtered1.dcd, filtered2.dcd, filtered3.dcd) for each binding modes are reported. Water molecules, ions, and membrane atoms (POPC: phosphatidylcholine) atoms were removed from the original trajectories and topologies before the upload.