The RGP method is the foundation of the generate-and-select hierarchical approach to the protein structure prediction problem. The RGP method is a highly efficient off-lattice residue buildup procedure that can quickly generate the complete set of topologies that satisfy a very small number of inter-residue distance restraints. For 3 restraints uniformly distributed in a 72-residue protein, we demonstrate that the size of this set is ~10^4. The RGP method can generate this set of structures in less than one hour using a Silicon Graphics R10000 single processor workstation. Following structure generation, a simple criterion that measures the burial of hydrophobic and hydrophilic residues can reliably select a reduced set of ~10^2 structures that contains the native topology. A minimization of the structures in the reduced set typically ranks the native topology in the five lowest energy folds. In the final hierarchical step, full atom models of the remaining candidate structures are created, allowing for further refinement and recognition of the final structure using full atom/full solvation molecular dynamics procedures. Thus, using this hierarchical approach, the de novo prediction of moderate resolution globular protein structure can be achieved in just a few hours on a single processor workstation. We have demonstrated the successful use of this hierarchy on two protein targets, 72-residue DNA-binding protein, and 146-residue Myoglobin. The results are in press in J. Phys. Chem. B.