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. Author manuscript; available in PMC: 2022 Oct 14.
Published in final edited form as: Proteins. 2021 Oct 10;89(12):1647–1672. doi: 10.1002/prot.26247

FIGURE 12.

FIGURE 12

Single chain of the Tuna (T1087) crystal structure (yellow) superimposed with exemplary predictions (red: AlphaFold2; cyan: FEIG-S, green: BAKER-ROBETTA). Tuna forms two coiled-coil interfaces, one intra-chain and one for homo-dimerization with another chain. Although only the monomer was a prediction target in CASP 14, several residues of the inter-chain interface were predicted in the correct rotamer by the top-ranking groups and servers. The N-terminal extension containing a polyproline-II helix is only shown for AlphaFold2, which predicted it most precisely in conformation and position.