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NMR processing:
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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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Refinement:
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Structure from chemical shifts:
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WeNMR CS-Rosetta
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Homology-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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PECAN
Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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UNIO Shiftinspector
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NMR model quality:
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iCing
RDCs:
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Pseudocontact shifts:
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SAVES2 or SAVES4
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NMR spectrum prediction:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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From sequence:
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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
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camGroEL
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Isotope labeling:
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Solid-state NMR:
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Default Solid-state NMR triple-resonance backbone assignments in a protein.

Solid-state NMR triple-resonance backbone assignments in a protein.

Related Articles Solid-state NMR triple-resonance backbone assignments in a protein.

J Biomol NMR. 1999 Apr;13(4):337-42

Authors: Tan WM, Gu Z, Zeri AC, Opella SJ

Triple-resonance solid-state NMR spectroscopy is demonstrated to sequentially assign the 13C' and 15N amide backbone resonances of adjacent residues in an oriented protein sample. The observed 13C' chemical shift frequency provides an orientational constraint complementary to those measured from the 1H and 15N amide resonances in double-resonance experiments.

PMID: 10353195 [PubMed - indexed for MEDLINE]



Source: PubMed
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