The lysozyme from the T4 bacteriophage is a classical test case for estimating free energy of binding as well as its kinetics and has been experimentally characterized by Feher et al. This system is interesting in that it has been engineered with multiple mutants to study the protein stability but was observed to bind small organic moieties like benzene, which have been resolved by X-ray crystallography. The binding cavity appears inaccessible from the outside but the relatively modest residence times measured via NMR seem to suggest some degree of protein rearrangement is taking place while the ligands unbind from the cavity. Hence this system is interesting because it allows us to test the methodology on multiple protein mutants at the same time and to test the ability to implicitly recover modest protein rearrangements.