Fig. 2: X-ray crystal structure of CC-Type2-(LaIdGe)4.
From: Structural resolution of switchable states of a de novo peptide assembly
a, b Orthogonal views of two states in the crystallographic unit cell (PDB entry 6ZT1). c, d Slices through the open (c) and collapsed (d) states showing side chains with the Gly residue at e sites highlighted green. The dashed lines highlight that both structures comprise similar three-helix sheets. e Overlay of the backbone structures of the two states. Two helical turns of each state for all chains are shown with the open C6-symmetric state in blue and the closed C2-symmetric state in red. The backbone root-mean-square deviation (RMSD) for the pair of helices labelled ‘1’ is 0.265 Å. f As in d with knobs-into-holes interactions highlighted with ‘cyclic’ knob residues coloured red and ‘non-cyclic’ and ‘inter-sheet’ knob residues coloured blue.
