The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamics
Open Access
- 1 January 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 1 (4) , 305-311
- https://doi.org/10.1093/protein/1.4.305
Abstract
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 ø 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 Å 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 β-sheet flanked by a 13 residue α helix on one side and the reactive site loop on the other.This publication has 16 references indexed in Scilit:
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