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. 2019 Nov 26;116(51):25446–25455. doi: 10.1073/pnas.1915948116

Fig. 4.

Fig. 4.

β-sheet topology of wt* and Δ10 (Top), and Δ10/I24N and Δ30 (Bottom) ngMinE constructs derived from the CS-ROSETTA structures. The complete sheet for one subunit is shown in blue, and only the strand of the second subunit located at the dimer interface is shown in red. The registers of the β-sheets, including those at the dimer interface, for both the 6-stranded (wt* and Δ10) and 4-stranded (Δ10/I24N and Δ30) forms of ngMinE, are fully consistent with the corresponding previously published structures [NMR structure of full-length ngMinE, 2KXO (9); NMR structure of Δ30-ecMinE, 1EVO (14); 4.3-Å resolution X-ray structure of I24N ecMinE complexed to MinD, 3R9J (10); these structures were not present in the high-resolution 3D protein coordinate database used in the CS-ROSETTA calculations].