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pubmed-article:10423386pubmed:abstractTextA method for accurately measuring H(N)-H(alpha) residual dipolar couplings is described. Using this technique, both the sign and magnitude of the coupling can be determined easily. Residual dipolar coupling between H(N)(i)-H(alpha)(i) and H(N)(i)-H(alpha)(i-1) were measured for the FK506 binding protein complexed to FK506. The experimental values were in excellent agreement with predictions based on an X-ray crystal structure of the protein/ligand complex, suggesting that these residual dipolar couplings will provide accurate structural constraints for the refinement of protein structures determined by NMR.lld:pubmed
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pubmed-article:10423386pubmed:authorpubmed-author:WangHHlld:pubmed
pubmed-article:10423386pubmed:authorpubmed-author:FesikS WSWlld:pubmed
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pubmed-article:10423386pubmed:copyrightInfoCopyright 1999 Academic Press.lld:pubmed
pubmed-article:10423386pubmed:issnTypePrintlld:pubmed
pubmed-article:10423386pubmed:volume139lld:pubmed
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pubmed-article:10423386pubmed:pagination451-3lld:pubmed
pubmed-article:10423386pubmed:dateRevised2000-12-18lld:pubmed
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pubmed-article:10423386pubmed:articleTitleAccurate measurement of H(N)-H(alpha) residual dipolar couplings in proteins.lld:pubmed
pubmed-article:10423386pubmed:affiliationPharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064, USA.lld:pubmed
pubmed-article:10423386pubmed:publicationTypeJournal Articlelld:pubmed
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