1omu | pdb_00001omu

SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (REFINED MODEL USING NETWORK EDITING ANALYSIS)

spinqualitylabelsall models 1omu Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1omu is a 1 chain structure with sequence from Meleagris gallopavo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 50 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function IOVO_MELGA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Network-editing experiments are variants of the basic NOESY experiment that allow more accurate direct measurement of interproton distances in macromolecules by defeating specific spin-diffusion pathways. Two network-editing approaches, block-decoupled NOESY and complementary-block-decoupled-NOESY, were applied as three-dimensional, heteronuclear-edited experiments to distance measurement in a small protein, turkey ovomucoid third domain (OMTKY3). Two-hundred and twelve of the original 655 distance constraints observed in this molecule (Krezel AM et al., 1994, J Mol Biol 242:203-214) were improved by their replacement by distances derived from network-edited spectra, and distance geometry/simulated annealing solution structure calculations were performed from both the unimproved and improved distance sets. The resulting two families of structures were found to differ significantly, the most important differences being the hinge angle of a beta-turn and an expansion of the sampled conformation space in the region of the reactive-site loop. The structures calculated from network-editing data are interpreted as a more accurate model of the solution conformation of OMTKY3. Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data.,Hoogstraten CG, Choe S, Westler WM, Markley JL Protein Sci. 1995 Nov;4(11):2289-99. PMID:8563625 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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