Pattern recognition and self-correcting distance geometry calculations applied to myohemerythrin

A topological list, consisting of segments of regular secondary structures and a list of buried and solvent accessible residues, is automatically predicted from multiple aligned sequences in a protein family. This topological list is translated into geometric constraints for distance geometry calculation in torsion angle space. A new self-correcting distance geometry method detects and eliminates false distance constraints. In an application to the four-helix bundle protein, myohem-erythrin, the right-handed global fold was correctly reproduced with a root-mean-square deviation of 2.6 Å, when the topological list was derived from the X-ray structure. A predicted topological list, coupled with constraints from the residues in the active site of myohemerythrin, predicted the correct fold with a root-mean-square deviation of 4 Å for backbone atoms.