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Many proteins and protein regions have been reported to be intrinsically disordered. Such disordered regions have been found to have conformational changes in various biological processes. Comprehensive studies on these disordered regions provide useful clues in understanding the mechanisms of a living cell. However, previous analyses only provided an overall number of disorder residues without definitely identifying the conformational changes. Besides, the variance of different binding types was averaged but not individually investigated. In this study, we have compiled a collection of structure pairs where the two members are identical except that one has an extra molecule than the other. This design, which enlarged the collection of analyzing targets with more various structures, is one of the most distinct features of this work to previous studies. By constructing the complete maps of every residue between two structures, this study performed more detailed and specific analyses than previous studies.