3rn3
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SEGMENTED ANISOTROPIC REFINEMENT OF BOVINE RIBONUCLEASE A BY THE APPLICATION OF THE RIGID-BODY TLS MODEL
OverviewOverview
The anisotropic displacements of selected rigid groups in bovine, ribonuclease A have been refined from X-ray diffraction data by the, application of the rigid-body TLS model. The rigid groups chosen were the, side chains of tyrosine, histidine and phenylalanine and the planar side, chains of aspartic acid, glutamic acid, glutamine, asparagine and, arginine. The method has also been applied to the co-crystallizing, active-site sulfate anion. This has enabled the description of the motion, of the above-mentioned side-chain atoms by anisotropic displacement, ellipsoids from a 1.45 A refinement. The hydrophobic side groups in the, protein core show mainly translational motion, with mean-square librations, of 20 deg2 which are similar to those found in some close-packed crystals, of small organic molecules. Librational displacements are much more, significant in the hydrophilic side groups where their magnitudes can be, correlated with solvent accessibility. Large librations of some solvent, exposed side chains correspond with the breakdown of a simple TLS model, and the existence of multiple orientations of the side groups. The TLS, model has also been applied to the whole protein molecule and shows that, the average motion is approximately isotropic with little librational, character.
About this StructureAbout this Structure
3RN3 is a Single protein structure of sequence from Bos taurus with SO4 as ligand. This structure superseeds the now removed PDB entry 1RN3. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.
ReferenceReference
Segmented anisotropic refinement of bovine ribonuclease A by the application of the rigid-body TLS model., Howlin B, Moss DS, Harris GW, Acta Crystallogr A. 1989 Dec 1;45 ( Pt 12):851-61. PMID:2619965
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