We built a dataset of CH-p interactions formed by b-D-galactose (galactose) and aromatic amino acids in protein-carbohydrate binding pockets, to assess their orientational dependence and energetics. We used the advanced search tool in the Protein Data Bank (PDB) 62 on 11.19.2021 to identify protein structures containing a galactose lacking any covalent bond to the protein. We required that the protein structure determined by X-ray crystallography has an R factor of at least 20% and an overall resolution of no worse than 2 Å. We first identified close contacts between galactose and three aromatic amino acids: tryptophan, tyrosine, and phenylalanine by selecting all amino acid-galactose pairs in which the centroids of the two species were within 7 Å of one another. Histidine was excluded from this dataset because it is believed to primarily form hydrogen bonding interactions, not CH-p interactions. We obtained the electron density score for individual atoms (EDIA) and its combination for molecular fragments (EDIAm) for each relevant protein residue and carbohydrate monomer. We retained close contacts for those species that had EDIAm scores of at least 0.8, the previously suggested cutoff , to ensure that all heavy atoms are well resolved. Finally, because we included structures with monomeric galactose or with galactose as a component of a larger polysaccharide ligand, the anomeric oxygen substituent (O1) atoms often participated in glycosidic linkages and were assigned to another carbohydrate monomer. Thus, we omitted any attached O1 atoms when processing the PDB structures and reinserted them by adding an oxygen atom bound to C1 by a 1.43 Å sp 3 bond along the PyMOL v. 2.5.2 -inserted equatorial C-H bond vector (Supporting Information Figure ). In total, this screen identified 351 tryptophan, 154 tyrosine, and 45 phenylalanine side chains with close contacts to galactose (Supporting Information Table ).