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. 2015 Dec 30;113(2):E137–E145. doi: 10.1073/pnas.1517288113

Fig. S3.

Fig. S3.

Rotameric state of binding site residues as determined from cryoEM experiments. Shown is the experimentally determined electron density (gray shading, arbitrary isovalue) superimposed to the structure of the protein (atomic coordinates as deposited in the protein databank, gray sticks) and to our docking pose of capsaicin (orange sticks). Purple color highlights the side-chains of residues Y511, L515, F522, F543, T550, F591, I661, and A665, whose conformation is highly restrained by the density, whereas cyan indicates those (M547 and L669) for which the experimental information is less abundant.