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PDBsum entry 1bnr
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Microbial ribonuclease
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PDB id
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1bnr
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References listed in PDB file
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Key reference
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Title
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Determination of the three-Dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy.
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Authors
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M.Bycroft,
S.Ludvigsen,
A.R.Fersht,
F.M.Poulsen.
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Ref.
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Biochemistry, 1991,
30,
8697-8701.
[DOI no: ]
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PubMed id
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Abstract
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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].
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