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NMR processing:
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NMR assignment:
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PINE
Side-chains:
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NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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ASDP
UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
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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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
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NMR model quality:
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RDCs:
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Protein geomtery:
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iCing
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ERRAT
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
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Methyl S2
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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CH3shift- Methyl
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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:
UPLABEL
Solid-state NMR:
sedNMR


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Default Dynamic Nuclear PolarizationNMR Spectroscopy of MicrocrystallineSolids

Dynamic Nuclear PolarizationNMR Spectroscopy of MicrocrystallineSolids

Aaron J. Rossini, Alexandre Zagdoun, Franziska Hegner, Martin Schwarzwa?lder, David Gajan, Christophe Cope?ret, Anne Lesage and Lyndon Emsley



Journal of the American Chemical Society
DOI: 10.1021/ja308135r




Source: Journal of the American Chemical Society
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