2prk
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(New page: 200px<br /><applet load="2prk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2prk, resolution 1.5Å" /> '''SYNCHROTRON X-RAY DAT...)
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Revision as of 11:30, 21 November 2007
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SYNCHROTRON X-RAY DATA COLLECTION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION
Overview
The structure of the serine endopeptidase proteinase K (279 amino acid, residues; 28,790 daltons) has been refined by restrained least-squares, methods to a conventional R value of 16.7% employing synchrotron film data, of 30,812 reflections greater than 3 sigma in the 5.0 to 1.5 A resolution, range. During refinement, the molecular structure was restrained to known, stereochemistry, with root-mean-square (r.m.s.) deviation of 0.015 A from, ideal bond lengths. The average atomic temperature factor, B, is 11.1 A2, for all atoms. The final model comprises 2020 protein atoms and 174, solvent molecules (which were given unit occupancies). Four corrections to, the amino acid sequence were made, which were confirmed later by sequence, analysis of the proteinase K gene: a deletion of one glycine in position, 80; a change of sequence in position 207-208 and insertions of the, dipeptide 210-211 and of residue 270. The r.m.s. deviation in the alpha-C, atomic positions between the final refined model and the initial model, built on the basis of a 3.3 A mini-map is 1.72 A for 227 out of 266, residues, which were originally traced in the mini-map without sequence, information. The positions of the remaining 39 residues deviate by more, than 8 A from the original ones and are located in regions where extensive, revision of the structural model was necessary.
About this Structure
2PRK is a Single protein structure of sequence from Engyodontium album with CA as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
Reference
Synchrotron X-ray data collection and restrained least-squares refinement of the crystal structure of proteinase K at 1.5 A resolution., Betzel C, Pal GP, Saenger W, Acta Crystallogr B. 1988 Apr 1;44 ( Pt 2):163-72. PMID:3271105
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