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Title
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Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures.
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Authors
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K.D.Berndt,
P.Güntert,
L.P.Orbons,
K.Wüthrich.
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Ref.
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J Mol Biol, 1992,
227,
757-775.
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PubMed id
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Abstract
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A high-quality three-dimensional structure of the bovine pancreatic trypsin
inhibitor (BPTI) in aqueous solution was determined by 1H nuclear magnetic
resonance (n.m.r.) spectroscopy and compared to the three available
high-resolution X-ray crystal structures. A newly collected input of 642
distance constraints derived from nuclear Overhauser effects and 115 dihedral
angle constraints was used for the structure calculations with the program
DIANA, followed by restrained energy minimization with the program AMBER. The
BPTI solution structure is represented by a group of 20 conformers with an
average root-mean-square deviation (RMSD) relative to the mean solution
structure of 0.43 A for backbone atoms and 0.92 A for all heavy atoms of
residues 2 to 56. The pairwise RMSD values of the three crystal structures
relative to the mean solution structure are 0.76 to 0.85 A for the backbone
atoms and 1.24 to 1.33 A for all heavy atoms of residues 2 to 56. Small local
differences in backbone atom positions between the solution structure and the
X-ray structures near residues 9, 25 to 27, 46 to 48 and 52 to 58, and
conformational differences for individual amino acid side-chains were analyzed
for possible correlations with intermolecular protein-protein contacts in the
crystal lattices, using the pairwise RMSD values among the three crystal
structures as a reference.
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