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== Publication Abstract from PubMed ==

Targeting of proteins for structure determination in structural genomic programs often includes the use of threading and fold recognition methods to exclude proteins belonging to well-populated fold families, but such methods can still fail to recognize preexisting folds. The authors illustrate here a method in which limited amounts of structural data are used to improve an initial homology search and the data are subsequently used to produce a structure by data-constrained refinement of an identified structural template. The data used are primarily NMR-based residual dipolar couplings, but they also include additional chemical shift and backbone-nuclear Overhauser effect data. Using this methodology, a backbone structure was efficiently produced for a 10 kDa protein (PF1455) from Pyrococcus furiosus. Its relationship to existing structures and its probable function are discussed.

Structure determination of a new protein from backbone-centered NMR data and NMR-assisted structure prediction.,Mayer KL, Qu Y, Bansal S, LeBlond PD, Jenney FE Jr, Brereton PS, Adams MW, Xu Y, Prestegard JH Proteins. 2006 Nov 1;65(2):480-9. PMID:16927360<ref>PMID:16927360</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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