1tec
From Proteopedia
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CRYSTALLOGRAPHIC REFINEMENT BY INCORPORATION OF MOLECULAR DYNAMICS. THE THERMOSTABLE SERINE PROTEASE THERMITASE COMPLEXED WITH EGLIN-C
Overview
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.
About this Structure
1TEC is a Protein complex structure of sequences from Hirudo medicinalis and Thermoactinomyces vulgaris with and as ligands. Active as Thermitase, with EC number 3.4.21.66 Full crystallographic information is available from OCA.
Reference
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
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