NMR Structure of Ribonuclease HI from Escherichia coli
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概要
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The solution structure of ribonuclease HI (RNase HI) from Escherichia coli (E. coli), a protein of 155 residues, was determined. Three-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain 1424 distance constraints between individually assigned polypeptide chain hydrogen atoms. Supplemental geometric constraints of 90φ angles and 12_<χ1> angles, and the distance constraints of 66 hydrogen bonds were experimentally derived. Using the DADAS90 program that calculates structures in dihedral angle space, 15 structures satisfying almost all constraints were obtained. The average root mean square deviation (RMSD) from the mean structure was 0.75Å for backbone atoms. The RMSD for backbone atoms between the representative NMR structure with the smallest constraint violation and crystal structures was within 1.2Å. Although the NMR and crystal structures thus resemble one another, a significant discrepancy was observed in a region termed 'basic protrusion.' The discrepancy observed in NMR experiments is explained by fluctuation in this region.
- 公益社団法人日本薬学会の論文
- 2000-10-01
著者
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Fujiwara Masako
Analytical Engineering Department Jeol Datum Ltd.
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Yamazaki Toshio
Protein Research Institute Osaka University
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KATO Toshiyo
Analytical Engineering Department, JEOL DATUM Ltd.,
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YAMASAKI Kazuhiko
Protein Engineering Research Institute
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NAGAYAMA Kuniaki
Graduate School of Arts and Sciences, The University of Tokyo
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Kato Toshiyo
Analytical Engineering Department Jeol Datum Ltd.
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Nagayama Kuniaki
Graduate School Of Arts And Sciences The University Of Tokyo:(present Address)national Institute For
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Yamasaki K
Okayama Univ. Okayama Jpn
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Yamazaki T
Protein Research Institute Osaka University
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