2eza | pdb_00002eza

AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

spinqualitylabelsall models 2eza, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2eza is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2ezb, 2ezc Activity: Phosphoenolpyruvate--protein phosphotransferase, with EC number 2.7.3.9 Resources: FirstGlance, OCA, RCSB, PDBsum 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 Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the form of short (< 5 A) interproton distances. In the case of modular or multidomain proteins and linear nucleic acids, the density of short interproton distance contacts between structural elements far apart in the sequence may be insufficient to define their relative orientations. In this paper we show how the dependence of heteronuclear longitudinal and transverse relaxation times on the rotational diffusion anisotropy of non-spherical molecules can be readily used to directly provide restraints for simulated annealing structure refinement that characterize long range order a priori. The method is demonstrated using the N-terminal domain of Enzyme I,a protein of 259 residues comprising two distinct domains with a diffusion anisotropy(Dparallel/Dperpendicular)of approximately 2. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.,Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM Nat Struct Biol. 1997 Jun;4(6):443-9. PMID:9187651 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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