1tec | pdb_00001tec

CRYSTALLOGRAPHIC REFINEMENT BY INCORPORATION OF MOLECULAR DYNAMICS. THE THERMOSTABLE SERINE PROTEASE THERMITASE COMPLEXED WITH EGLIN-C

spinqualitylabelsall models 1tec, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tec is a 2 chain structure with sequence from Atcc 43649 and Hirme. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, NA Activity: Thermitase, with EC number 3.4.21.66 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 In order to investigate the principles of protein thermostability, the crystal structure of thermitase from Thermoactinomyces vulgaris, a thermostable member of the subtilisin family of serine proteases, has been determined in a complex with eglin c. Eglin c is a serine protease inhibitor from the leech Hirudo medicinalis. After data collection with a television area-detector diffractometer and initial structure solution by molecular-replacement methods, crystallographic refinement proceeded with incorporation of molecular-dynamics techniques. It appeared that this refinement procedure has a large convergence radius with movements of more than 5 A for many atoms. Two procedures for the crystallographic molecular-dynamics refinement have been tested. They differed mainly in time span and weight on the X-ray 'energy'. The best results were obtained with a procedure which allowed the molecular-dynamics technique to search a large area in conformational space by having less weight on the X-ray restraints and allowing more time. The use of molecular-dynamics refinement considerably simplified the laborious and difficult task of fitting the model in its electron density during the refinement process. The final crystallographic R factor is 17.9% at 2.2 A resolution. Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c.,Gros P, Fujinaga M, Dijkstra BW, Kalk KH, Hol WG Acta Crystallogr B. 1989 Oct 1;45 ( Pt 5):488-99. PMID:2688688 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Eglin

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