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NMR processing:
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Side-chains:
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NOEs:
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UNIO Candid
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
CSI (via RCI server)
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
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NMR model quality:
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Chemical shifts:
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RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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NMR spectrum prediction:
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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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CH3shift- Methyl
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Proshift
PPM
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From sequence:
Shifty
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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
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Old 08-22-2010, 03:33 AM
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Default The impact of direct refinement against three-bond HN-C alpha H coupling constants on

The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR.

Related Articles The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR.

J Magn Reson B. 1994 May;104(1):99-103

Authors: Garrett DS, Kuszewski J, Hancock TJ, Lodi PJ, Vuister GW, Gronenborn AM, Clore GM



PMID: 8025816 [PubMed - indexed for MEDLINE]



Source: PubMed
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