Protein Science
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NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family
Protein Sci LIU et al. 7: 132

Data Supplement

There are files for each of 2 figures and 4 tables. They are probably Word Perfect files. The two figures show assigned 1H-15N HSQC maps of rCMTI-III and rCMTI-III*. The four tables contain experimental R1, R2, and NOE data and computed model-free parameters (S^2, Tau_e, and R_ex) of rCMTI-III and rCMTI-III*.

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This Article
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