Fig. 1.

Comparison between experimental and MD-derived PISEMA resonances of the M2 TMD. For the apo form, the experimental data are taken from ref. 15. Values for Ser-31, Gly-34, and His-37 were not available. For the amantadine-bound form, the experimental data are taken from ref. 9. Values for Ser-31 and His-37 were not available. Typical differences between experimental and MD resonances amount to <5° errors in peptide-plane orientations. The helix tilt angle obtained from the MD results as a whole agrees with the experimental counterpart to within ≈2°; the helix rotation angle agrees to within ≈10°.