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pubmed-article:12834346pubmed:abstractText13C[(15)N] and (13)C[(19)F] rotational-echo double-resonance NMR have been used to characterize the enzyme-bound structure of ZK-816042, an amidine-imidazoline inhibitor of human factor Xa (FXa). The NMR experiments were performed on a lyophilized FXa-inhibitor complex. The complex was formed in solution in the presence of stabilizing excipients and frozen after gradual supercooling prior to lyophilization. The results indicate that the inhibitor binds with a distribution of orientations of the imidazoline ring.lld:pubmed
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pubmed-article:12834346pubmed:articleTitleConformation of a bound inhibitor of blood coagulant factor Xa.lld:pubmed
pubmed-article:12834346pubmed:affiliationDepartment of Chemistry, Washington University, St. Louis, Missouri 63130, USA.lld:pubmed
pubmed-article:12834346pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12834346pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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