Data set for "Structural diversity in de novo cyclic peptide ligands from genetically encoded library technologies"

The related publication reviews the cyclic peptides identified through these techniques reported in the period 2015 to 2019, with a particular focus on the three-dimensional structures that peptides adopt when binding to their targets. It also highlights examples where co-crystal structures have informed the key interactions that promote high affinity and selectivity of cyclic peptides against their targets, identified novel inhibitor binding sites, and provided new insights into the biology of their targets.This dataset comprises contents of tables 1 and 2 with additional data as used in figures 1 and 2.Table 1: Overview of recent CPs identified through genetically encoded library techniques against protein targets.Table 2: X-ray crystal structures of CPs in complex with their targets.The figures referenced are briefly described below:Figure 1: Calculated physicochemical properties of cyclic peptides identified through selection technologies.Figure 2: Properties of cyclic peptides co-crystallised with their target.