Extended Data Fig. 8: Illustration of the potential van der Waals interactions between 9 residues of mScarlet3 near the surface of one head of the β-barrel.
From: mScarlet3: a brilliant and fast-maturing red fluorescent protein
Residues belong to the central α-helix traversing the β-barrel (Thr74), to the α-helix capping one head of the β-barrel (Trp84), to the loop linking the latter helices (His76), to the 7th strand (Leu151), to the 8th strand (Leu158), to the loop bridging the 9th and 10th strands (Pro191), to the 10th strand (Phe194, Ile196), to the 11th strand (Ala220). Potential van der Waals interactions (dashed black lines) are highlighted by inter-carbon atom distances below 4.0 Å. a. View from the side of the β-barrel. The set of vdW interactions forms a crown-like structure.b. 90° view (from the barrel head) showing residues organized in three layers: the main one is formed of residues Thr74, Trp84, Leu158, Phe194 and Ala220, with residues His76 and Pro191 ahead of this layer, and residues Leu151 and Ile196 behind it.
