Orientations of Proteins in Membranes (OPM) database provides spatial positions of protein three-dimensional structures with respect to the lipid bilayer. The database was used in experimental and theoretical studies of membrane-associated proteins
Proteins structures are taken from the Protein Data Bank. Positions of the proteins in a hydrophobic slab are calculated using the implicit solvation model.
OPM provides structural classification of membrane-associated proteins into families and superfamilies (based on SCOP classification), membrane topology, and the type of a destination membrane for each protein. All protein coordinate files with calculated membrane boundaries are freely downloadable.
The site allows visualization of protein structures with membrane boundary planes through Jmol, MDL Chime and WebMol.
This is the only database that includes structures of peripheral membrane proteins. Calculated positions of proteins have been compared with relevant experimental data for 24 tranmembrane and 53 peripheral membrane proteins including site-directed spin labeling, chemical labeling, measurement of membrane binding affinities of protein mutants,fluorescence spectroscopy, solution or solid-state NMR spectroscopy,
ATR FTIR spectroscopy, and X-ray or neutron diffraction studies
The set of peripheral membrane proteins in OPM is incomplete. The database probably includes less than 50% of peripheral proteins from the Protein Data Bank, because membrane-anchoring elements of peripheral proteins (amphiphilicalpha helices, exposed nonpolar residues, or lipid anchors) are missing or disordered in the experimental protein structures, and therefore the mode of protein-membrane association can not be computationally predicted
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