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A refined solution structure of hen lysozyme determined using residual dipolar coupling data.

Abstract:

A high resolution NMR structure of hen lysozyme has been determined using 209 residual 1H-15N dipolar coupling restraints from measurements made in two different dilute liquid crystalline phases (bicelles) in conjunction with a data set of 1632 NOE distance restraints, 110 torsion angle restraints, and 60 hydrogen bond restraints. The ensemble of 50 low-energy calculated structures has an average backbone RMSD of 0.50+/-0.13A to the mean structure and of 1.49+/-0.10A to the crystal structure ...

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Publication status:
Published

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Publisher copy:
10.1110/ps.43301

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Journal:
Protein science : a publication of the Protein Society
Volume:
10
Issue:
4
Pages:
677-688
Publication date:
2001-04-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:1d34ffbe-e754-443a-8515-93ff324a6994
Source identifiers:
31853
Local pid:
pubs:31853

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