Fig. 4: Structural characterization of five-helix, six-helix and eight-helix targets.
From: Rationally seeded computational protein design of ɑ-helical barrels
a–d, Top, X-ray crystal structures of sc-apCC-8 at a 2.0-Å resolution (PDB ID, 8QAF) (a), sc-CC-5 at a 1.9-Å resolution (PDB ID, 8QKD) (b), sc-CC-6-95 at a 2.8-Å resolution (PDB ID, 8QAG) (c) and sc-CC-8-58 at a 2.35-Å resolution (PDB ID, 8QAH) (d). Coiled-coil regions identified by Socket2 (ref. 72) (packing cutoff, 7.5 Å for sc-apCC-8, sc-CC-5-24, sc-CC-6-95 and sc-CC-8-58 at 7.0 Å) are colored as chainbows from N termini (blue) to C termini (red). Bottom, overlays for the middle helical turns of each crystal structure (cyan) and the corresponding AlphaFold2 (refs. 55,56) model (magenta); RMSDbb = 0.413 Å (a), RMSDbb = 0.371 Å (b), RMSDbb = 0.300 Å (c) and RMSDbb = 0.530 Å (d).
