Fig. 3: Exchange behaviour in βPGMWT.
From: Allomorphy as a mechanism of post-translational control of enzyme activity

Crystal structure of βPGMWT (PDB 2WHE29) showing residues of βPGMWT undergoing conformational exchange on different timescales. Residues that populate two conformations in slow exchange are coloured in shades of blue according to chemical shift differences between conformer A and conformer B, with the intensity of colour and thickness of the backbone corresponding to larger values. Residues in conformer A and conformer B with missing backbone amide peaks in the 1H15N-TROSY spectrum of βPGMWT are coloured black, whereas missing backbone amide peaks in conformer B only are coloured purple. The amide 1H15N coherences are likely broadened beyond detection owing to intermediate exchange on the millisecond timescale. The catalytic Mg2+ ion is indicated as a green sphere.