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Side-chains:
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NOEs:
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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Flexibility from structure:
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Methyl S2
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
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ArShift- Aromatic
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Proshift
PPM
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From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
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Isotope labeling:
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Solid-state NMR:
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Default NMR Structure of the SARS Coronavirus Nonstructural Protein 7 in Solution at pH 6.5.

NMR Structure of the SARS Coronavirus Nonstructural Protein 7 in Solution at pH 6.5.

Related Articles NMR Structure of the SARS Coronavirus Nonstructural Protein 7 in Solution at pH 6.5.

J Mol Biol. 2010 Aug 12;

Authors: Johnson MA, Jaudzems K, Wüthrich K

The NMR structure of the severe acute respiratory syndrome coronavirus (SARS-CoV) non-structural protein 7 (nsp7) in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provides further insights into the polymorphisms implicated by comparison of the presently available three nsp7 structures.

PMID: 20709084 [PubMed - as supplied by publisher]



Source: PubMed
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