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.

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