The structural characterization of denatured state is essential to understand the mechanism of protein folding.Since the denatured state is composed of an ensemble of many possible conformations, the statistical description of the structure is required.The molecular weight dependence of the molecular sizes obeyed power law of 0.6 led the conclusion that the denatured state is described well with the random coil, while NMR studies on the denatured states of some proteins suggested the existence of residual structures.The former gives the statistical description over various protein, and the latter gives a local structure information of an individual protein.We aimed to obtain a statistical image of the denatured state of an individual protein.