Fig. 3: NMR structure determination reveals strand swapping.
From: Role of backbone strain in de novo design of complex α/β protein structures
Design models (upper row), together with a representative conformer (middle row) and the ensemble of conformers (lower row) determined by NMR, for a P-loop fold: Pl2×3_BP_7 (PDB: 5GAJ), b Rossmann2×3 fold: R2×3_BP1_A5 (2L69) and R2×3_BP1_B9 (2LCI), and c Rossmann3×3 fold: R3×3_BP1_9 (2L82); topology diagrams are on the right. As is clear from the topology diagrams, in the NMR structures for the Rossmann2×3- and 3×3- folds, the positions of the green and blue β-strands are swapped compared to the order in the design models.
