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Structure of hen lysozyme in solution.

Abstract:

The structure of the 129-residue protein hen lysozyme has been determined in solution by two-dimensional 1H nuclear magnetic resonance methods. 1158 NOE distance restraints, and 68 phi and 24 chi 1 dihedral angle restraints were employed in conjunction with distance geometry and simulated annealing procedures. The overall C alpha root-mean-square deviation from the average for 16 calculated structures is 1.8(+/- 0.2) A, but excluding 14 residues in exposed disordered regions, this value reduc...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.1993.1097

Authors


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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry
Role:
Author
Journal:
Journal of molecular biology
Volume:
229
Issue:
4
Pages:
930-944
Publication date:
1993-02-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:f702050b-bb7f-467d-bca5-5d6e93521b94
Source identifiers:
35863
Local pid:
pubs:35863

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