Exposed surface area (SA) and radius of gyration (Rg) of arginine and lysine residues in the pentasaccharide binding site of antithrombin and exosite II of thrombin.*

*Exposed Surface Area was calculated using the Connolly surface area analysis, while Rg was calculated from the variation in the position of terminal group of Lys and Arg, as described in Methods.†Represents the number of crystal structures used in calculations. This number is different for different residues because the number of completely resolved side chains varies among crystal structures.‡Calculated using fully exposed SAs for lysine and arginine in a tripeptide, which were found to be 127 and 145 Å2, respectively.