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Protein structure provides insight into the evolutionary origins, functions, and mechanisms of proteins. We are pursuing a minimalist approach to protein fold identification that characterizes possible folds in terms of consistency of their geometric features with restraints derived from relatively cheap, highthroughput experiments. One such experiment is residue-specific cross-linking analyzed by mass spectrometry. This paper presents a suite of novel lower-and upper-bounding algorithms fordoi:10.1142/9789812704856_0042 fatcat:s7puzvflsja7be6ou275yfotq4