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NMR processing:
MDD
NMR assignment:
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MARS
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Side-chains:
UNIO ATNOS-Ascan
NOEs:
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Structure from NMR restraints:
Ab initio:
GeNMR
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Fragment-based:
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GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
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TALOS
MICS caps, β-turns
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PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
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Chemical shifts:
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iCing
RDCs:
DC
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Pseudocontact shifts:
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Protein geomtery:
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What-If
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PSVS
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SAVES2 or SAVES4
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Ramachandran Plot
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ERRAT
Verify_3D
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
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
Zyggregator
Isotope labeling:
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Solid-state NMR:
sedNMR


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Default The impact of direct refinement against proton chemical shifts on protein structure d

The impact of direct refinement against proton chemical shifts on protein structure determination by NMR.

Related Articles The impact of direct refinement against proton chemical shifts on protein structure determination by NMR.

J Magn Reson B. 1995 Jun;107(3):293-7

Authors: Kuszewski J, Gronenborn AM, Clore GM



PMID: 7788102 [PubMed - indexed for MEDLINE]



Source: PubMed
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