1egl

THE SOLUTION STRUCTURE OF EGLIN C BASED ON MEASUREMENTS OF MANY NOES AND COUPLING CONSTANTS AND ITS COMPARISON WITH X-RAY STRUCTURESTHE SOLUTION STRUCTURE OF EGLIN C BASED ON MEASUREMENTS OF MANY NOES AND COUPLING CONSTANTS AND ITS COMPARISON WITH X-RAY STRUCTURES

Structural highlights 1egl is a 1 chain structure with sequence from Hirudo medicinalis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: SYNTHETIC GENE (Hirudo medicinalis) Resources: FirstGlance, OCA, RCSB, PDBsum Function [ICIC_HIRME] Inhibits both elastase and cathepsin G. 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 A high-precision solution structure of the elastase inhibitor eglin c was determined by NMR and distance geometry calculations. A large set of 947 nuclear Overhauser (NOE) distance constraints was identified, 417 of which were quantified from two-dimensional NOE spectra at short mixing times. In addition, a large number of homonuclear 1H-1H and heteronuclear 1H-15N vicinal coupling constants were used, and constraints on 42 chi 1 and 38 phi angles were obtained. Structure calculations were carried out using the distance geometry program DG-II. These calculations had a high convergence rate, in that 66 out of 75 calculations converged with maximum residual NOE violations ranging from 0.17 A to 0.47 A. The spread of the structures was characterized with average root mean square deviations (<rmsd>) between the structures and a mean structure. To calculate the <rmsd> unbiased toward any single structure, a new procedure was used for structure alignment. A canonical structure was calculated from the mean distances, and all structures were aligned relative to that. Furthermore, an angular order parameter S was defined and used to characterize the spread of structures in torsion angle space. To obtain an accurate estimate of the precision of the structure, the number of calculations was increased until the <rmsd> and the angular order parameters stabilized. This was achieved after approximately 40 calculations. The structure consists of a well-defined core whose backbone deviates from the canonical structure ca. 0.4 A, a disordered N-terminal heptapeptide whose backbone deviates by 0.8-12 A, and a proteinase-binding loop whose backbone deviates up to 3.0 A. Analysis of the angular order parameters and inspection of the structures indicates that a hinge-bending motion of the binding loop may occur in solution. Secondary structures were analyzed by comparison of dihedral angle patterns. The high precision of the structure allows one to identify subtle differences with four crystal structures of eglin c determined in complexes with proteinases. The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures.,Hyberts SG, Goldberg MS, Havel TF, Wagner G Protein Sci. 1992 Jun;1(6):736-51. PMID:1304915 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Eglin

spinqualitylabelsall models 1egl, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image