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We study the conformational freedom of a protein made by two rigid domainsconnected by a flexible linker. The conformational freedom is represented as anunknown probability distribution on the space of allowed states. A newalgorithm for the calculation of the Maximum Allowable Probability is proposed,which can be extended to any type of measurements. In this paper we use PseudoContact Shifts and Residual Dipolar Coupling. We reconstruct a single centraltendency in the distribution and discuss in depth the results.

Looking for central tendencies in the conformational freedom of proteins using NMR measurements