  We present an algorithm for the exhaustive enumeration of all monomer
sequences and conformations of short lattice proteins as described by the
hydrophobic-polar (HP) model. The algorithm is used for an exact identification
of all designing sequences of HP proteins consisting of up to 19 monomers whose
conformations are represented by interacting self-avoiding walks on the simple
cubic lattice. Employing a parallelized implementation on a Linux cluster, we
generate the complete set of contact maps of such walks.
