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. The metallo-β-lactamase IMP-1 features a flexible loop near the active site that assumes different conformations in single crystalstructures, which may assist in substrate binding and enzymatic activity. Toprobe the position of this loop, we labelled the tryptophan residues ofIMP-1 with 7-13C-indole and the protein with lanthanoid tags at threedifferent sites. The magnetic susceptibility anisotropy (Δχ)tensors were determined by measuring pseudocontact shifts (PCSs) of backbone amide protons. The Δχ tensors were subsequently used toidentify the atomic coordinates of the tryptophan side chains in theprotein. The PCSs were sufficient to determine the location of Trp28, whichis in the active site loop targeted by our experiments, with high accuracy. Its average atomic coordinates showed barely significant changes in response to the inhibitor captopril. It was found that localisation spaces could be defined with better accuracy by including only the PCSs of a single paramagnetic lanthanoid ion for each tag and tagging site. The effectwas attributed to the shallow angle with which PCS isosurfaces tend tointersect if generated by tags and tagging sites that are identical exceptfor the paramagnetic lanthanoid ion.

magnetic resonance

Localising individual atoms of tryptophan side chains in the metallo-&amp;lt;i&amp;gt;β&amp;lt;/i&amp;gt;-lactamase IMP-1 by pseudocontact shifts from paramagnetic lanthanoid tags at multiple sites