1bnr
From Proteopedia
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| - | [[Image:1bnr.gif|left|200px]] | + | [[Image:1bnr.gif|left|200px]] |
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| - | '''BARNASE''' | + | {{Structure |
| + | |PDB= 1bnr |SIZE=350|CAPTION= <scene name='initialview01'>1bnr</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= BARNASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 Bacillus amyloliquefaciens]) | ||
| + | }} | ||
| + | |||
| + | '''BARNASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BNR is a [ | + | 1BNR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BNR OCA]. |
==Reference== | ==Reference== | ||
| - | Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy., Bycroft M, Ludvigsen S, Fersht AR, Poulsen FM, Biochemistry. 1991 Sep 3;30(35):8697-701. PMID:[http:// | + | Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy., Bycroft M, Ludvigsen S, Fersht AR, Poulsen FM, Biochemistry. 1991 Sep 3;30(35):8697-701. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1888730 1888730] |
[[Category: Bacillus amyloliquefaciens]] | [[Category: Bacillus amyloliquefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: microbial ribonuclease]] | [[Category: microbial ribonuclease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:13:27 2008'' |
Revision as of 08:13, 20 March 2008
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| Gene: | BARNASE (Bacillus amyloliquefaciens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BARNASE
Overview
The solution conformation of the ribonuclease barnase has been determined by using 1H nuclear magnetic resonance (NMR) spectroscopy. The 20 structures were calculated by using 853 interproton distance restraints obtained from analyses of two-dimensional nuclear Overhauser spectra, 72 phi and 53 chi 1 torsion angle restraints, and 17 hydrogen-bond distance restraints. The calculated structures contain two alpha-helices (residues 6-18 and 26-34) and a five-stranded antiparallel beta-sheet (residues 50-55, 70-75, 85-91, 94-101, and 105-108). The core of the protein is formed by the packing of one of the alpha-helices (residues 6-18) onto the beta-sheet. The average RMS deviation between the calculated structures and the mean structure is 1.11 A for the backbone atoms and 1.75 A for all atoms. The protein is least well-defined in the N-terminal region and in three large loops. When these regions are excluded, the average RMS deviation between the calculated structures and the mean structure for residues 5-34, 50-56, 71-76, 85-109 is 0.62 A for the backbone atoms and 1.0 A for all atoms. The NMR-derived structure has been compared with the crystal structure of barnase [Mauguen et al. (1982) Nature (London) 297, 162-164].
About this Structure
1BNR is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.
Reference
Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy., Bycroft M, Ludvigsen S, Fersht AR, Poulsen FM, Biochemistry. 1991 Sep 3;30(35):8697-701. PMID:1888730
Page seeded by OCA on Thu Mar 20 10:13:27 2008
