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Title
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The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamics.
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Authors
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G.M.Clore,
A.M.Gronenborn,
M.Kjaer,
F.M.Poulsen.
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Ref.
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Protein Eng, 1987,
1,
305-311.
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PubMed id
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Abstract
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The solution structure of the 64 residue structured domain (residues 20-83) of
barley serine proteinase inhibitor 2 (BSPI-2) is determined on the basis of 403
interproton distance, 34 phi backbone torsion angle and 26 hydrogen bonding
restraints derived from n.m.r. measurements. A total of 11 converged structures
were computed using a metric matrix distance geometry algorithm and refined by
restrained molecular dynamics. The average rms difference between the final 11
structures and the mean structure obtained by averaging their coordinates is 1.4
+/- 0.2 A for the backbone atoms and 2.1 +/- 0.1 A for all atoms. The overall
structure, which is almost identical to that found by X-ray crystallography, is
disc shaped and consists of a central four component mixed parallel and
antiparallel beta-sheet flanked by a 13 residue alpha-helix on one side and the
reactive site loop on the other.
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