The ever-developing experimental methods and automation in the drug discovery industry have led to the popularity of high throughput screening for discovering molecules that bind to proteins of interest, a frequent consideration in the early stages of a drug discovery program. However, the chemical space of drug-like small molecules (Molecular Weight in the range 350-500 g.mol -1 ) is estimated to be around 10 20 -10 24 molecules , making it challenging to put together representative screening libraries of a reasonable size. Fragment based drug design (FBDD) is a more efficient strategy that relies on screening initially lower molecular weight compounds (under 300 g.mol -1 ). As the number of unique fragment-sized molecules is much smaller than that of drug-like small molecules, it is easier to routinely screen a greater fraction of fragment chemical space . Structure-enabled biophysical assay methods used to screen fragment libraries (MD mix, high-throughput X-ray crystallography) frequently identify numerous fragments that bind all over the surface of the protein of interest. Since fragments are usually weak binders, they only provide starting points for medicinal chemistry efforts to produce a lead molecule active in functional assays . This can be a slow and expensive process, with an uncertain outcome especially in cases where the fragment selected for elaboration binds to a site that is distinct from the active site. In this case it may be difficult to anticipate whether fragment elaboration will lead to a ligand that affects protein function through allosteric mechanisms .