Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2

Protein Eng. Aug-Sep 1987;1(4):313-8. doi: 10.1093/protein/1.4.313.


A comparison of the solution n.m.r. structures of barley serine protease inhibitor 2 (BSPI-2) with the X-ray structures of both subtilisin complexed and native BSPI-2 is presented. It is shown that the n.m.r. and X-ray structures are very similar in terms of overall shape, size, polypeptide fold and secondary structure. The average atomic rms difference between the 11 restrained dynamics structures on the one hand and the two X-ray structures on the other is 1.9 +/- 0.2 A for the backbone atoms and 3.0 +/- 0.3 A for all atoms. The corresponding values for the restrained energy minimized mean dynamics structure are 1.5 and 2.4 A, respectively.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography
  • Edible Grain / enzymology*
  • Hordeum / enzymology*
  • Magnetic Resonance Spectroscopy
  • Serine Proteinase Inhibitors*
  • Solutions


  • Serine Proteinase Inhibitors
  • Solutions