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Title
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Automated combined assignment of NOESY spectra and three-dimensional protein structure determination.
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Authors
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C.Mumenthaler,
P.Güntert,
W.Braun,
K.Wüthrich.
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Ref.
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J Biomol Nmr, 1997,
10,
351-362.
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PubMed id
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Abstract
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A procedure for automated protein structure determination is presented that is
based on an iterative procedure during which the NOESY peak list assignment and
the structure calculation are performed simultaneously. The input consists of a
list of NOESY peak positions and a list of chemical shifts as obtained from
sequence-specific resonance assignment. For the present applications of this
approach the previously introduced NOAH routine was implemented in the distance
geometry program DIANA. As an illustration, experimental 2D and 3D NOESY
cross-peak lists of six proteins have been analyzed, for which complete
sequence-specific 1H assignments are available for the polypeptide backbone and
the amino acid side chains. The automated method assigned 70-90% of all NOESY
cross peaks, which is on average 10% less than with the interactive approach,
and only between 0.8% and 2.4% of the automatically assigned peaks had a
different assignment than in the corresponding manually assigned peak lists. The
structures obtained with NOAH/DIANA are in close agreement with those from
manually assigned peak lists, and with both approaches the residual constraint
violations correspond to high-quality NMR structure determinations. Systematic
comparisons of the bundles of conformers that represent corresponding
automatically and interactively determined structures document the absence of
significant bias in either approach, indicating that an important step has been
made towards automation of structure determination from NMR spectra.
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