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NMR processing:
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Side-chains:
UNIO ATNOS-Ascan
NOEs:
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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ASDP
UNIO ATNOS-Candid
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Fragment-based:
BMRB CS-Rosetta
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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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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:
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NMR model quality:
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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Proshift
PPM
CheShift-2- Cα
From sequence:
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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
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Isotope labeling:
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Solid-state NMR:
sedNMR


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Old 02-11-2011, 08:31 AM
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Default NMR paper in Nature Structural & Molecular Biology

NMR paper in Nature Structural & Molecular Biology

L.A. Freiburger, O.M. Baettig, T. Sprules, A.M. Berghuis, K. Auclair, A.K. Mittermaier, "Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme," Nature Structural & Molecular Biology (2011) online. http://dx.doi.org/10.1038/nsmb.1978


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