Thermodynamic analysis of protein-ligand binding using differential scanning calorimetry and two tables: Table 1: Ambiguous interaction restraints (AIR) and intermolecular NOE-derived distance restraints. Table 2: Apparent amide hydrogen-deuterium exchange rate constants and apparent Gibbs energies for the R21A Spc-SH3 domain at pH* 3.0 and 27.1°C, in its free form and in the presence of a 96% saturating concentration of the p41 peptide. description and equations used for analysis of DSC thermograms and list of AIR and SH3:P41 intermolecular NOEs and a list of amide hydrogen-deuterium exchange rate constants and apparent Gibbs energies.