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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:
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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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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
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NMR model quality:
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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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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
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From sequence:
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Camcoil
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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:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default NMR analysis of ERK2 [Biochemistry]

NMR analysis of ERK2 [Biochemistry]

Xiao, Y., Lee, T., Latham, M. P., Warner, L. R., Tanimoto, A., Pardi, A., Ahn, N. G....
Date: 2014-02-18

Protein motions control enzyme catalysis through mechanisms that are incompletely understood. Here NMR 13C relaxation dispersion experiments were used to monitor changes in side-chain motions that occur in response to activation by phosphorylation of the MAP kinase ERK2. NMR data for the methyl side chains on Ile, Leu, and Val... Read More


PNAS:
Number: 7
Volume: 111
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