Additional examples of the successful integration of NMR and virtual screening as applied to protein targets are also found in the literature, further demonstrating the practicality and complementarity of virtual screening and NMR [329,335,336,337]. For example, Li et al. [338] used virtual screening filtered by NMR to identify and characterize non-metal chelating metallo-β-lactamase (MBL) inhibitors, and in particular, Verona integron-encoded MBL (VIM)-2, when previously there were no clinically significant inhibitors of MBL, since MBL enzymes hydrolyse many, if not all, β-lactam antibacterials compounds specifically designed to inhibit their activity [339]. Furthermore, Shan et al. [340] and Bertini et al. [337] both used virtual screening and NMR, in their respective studies. Through the combined use of NMR and virtual screening, Shan et al. was able to identify, design, and synthesize novel PDZ domain inhibitors, which are proteins implicated in tumorigenesis [340]. Bertini et al. was able to combine NMR to study the interaction of ligands with metalloproteinases, using known inhibitors of metalloproteinases as a starting point [337]. While HSQC NOESY NMR data provided structural and spatial constraints for the proposed 3D models, virtual screening was used to refine the models, and to probe the ligand-protein interaction. In each case (i.e., ligand-protein interaction), Bertini et al. was able to obtain a well-defined ligand conformation in the protein binding site, thus offering a viable alternative to other approaches described in the literature [337]. Clearly, combining virtual screening with NMR-based methods is advantageous in studying how ligands (drugs) bind and interact with targets (proteins) of interest.