Structures of Protein−Protein Complexes Are Docked Using Only NMR Restraints from Residual Dipolar Coupling and Chemical Shift Perturbations

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Abstract
NMR structures of protein−protein and protein−ligand complexes rely heavily on intermolecular NOEs. Recent work has shown that if no significant conformational changes occur upon complex formation residual dipolar coupling can replace most of the NOE restraints in protein−protein complexes, while restraints derived from chemical shift perturbations can largely replace intermolecular NOEs in protein−ligand structures. By combining restraints from chemical shift perturbations with orientation restraints derived from measurements of residual dipolar couplings, we show that the structure of the EIN−HPr complex can be calculated without NOE restraints. The final structure, built from the crystal structures of EIN and HPr in their uncomplexed form and docked only with NMR restraints, places HPr within 2.5 Å of the position determined from the mean NMR structure of the complex.