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PINE
Side-chains:
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NOEs:
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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UNIO ATNOS-Candid
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Fragment-based:
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Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
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MICS caps, β-turns
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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
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NMR model quality:
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iCing
RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
iCing
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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:
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CH3shift- Methyl
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From sequence:
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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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Old 03-08-2011, 04:02 AM
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Default Specific Binding of Adamantane Drugs and Direction of Their Polar Amines in the Pore of the Influenza M2 Transmembrane Domain in Lipid Bilayers and Dodecylphosphocholine Micelles Determined by NMR Spectroscopy

Specific Binding of Adamantane Drugs and Direction of Their Polar Amines in the Pore of the Influenza M2 Transmembrane Domain in Lipid Bilayers and Dodecylphosphocholine Micelles Determined by NMR Spectroscopy

Sarah D. Cady, Jun Wang, Yibing Wu, William F. DeGrado and Mei Hong



Journal of the American Chemical Society
DOI: 10.1021/ja102581n




Source: Journal of the American Chemical Society
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