Conformational changes mediate important protein functions, such as opening and closing of channel gates, activation and inactivation of enzymes, etc. The entire conformational repertoire of a given query protein may not be known; however, it may be possible to infer unknown conformations from other proteins. We developed the ConTemplate method to exploit the richness of the Protein Data Bank (PDB) for this purpose. ConTemplate uses a three-step process to suggest alternative conformations for a query protein with one known conformation . First, ConTemplate uses GESAMT to scan the PDB for proteins that share structural similarity with the query . Next, for each of the collected proteins, additional known conformations are detected using BLAST , and clustered into a predefined number of clusters . Finally, MODELLER  builds models of the query in various conformations, each representative of a cluster.