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NMR processing:
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PINE
Side-chains:
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NOEs:
UNIO ATNOS-Candid
UNIO Candid
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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
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
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Torsion angles from chemical shifts:
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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:
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HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
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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
MolProbity
SAVES2 or SAVES4
Vadar
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MetaMQAPII
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STAN
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ERRAT
Verify_3D
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Quality Control Check
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:
UPLABEL
Solid-state NMR:
sedNMR


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Old 04-14-2011, 09:56 PM
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Default Special Issue of Solid State Nuclear Magnetic Resonance http://nmr900.ca/nmr_news.html#ssnmr

Special Issue of Solid State Nuclear Magnetic Resonance http://nmr900.ca/nmr_news.html#ssnmr

Published by nmr900 (Victor Terskikh) on 2011-04-14T21:20:42Z


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