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NMR processing:
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NMR assignment:
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PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
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Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
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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Promega- Proline
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:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
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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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What-If
iCing
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SAVES2 or SAVES4
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MetaMQAPII
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ERRAT
Verify_3D
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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
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
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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 Site-SpecificInternal Motions in GB1 Protein MicrocrystalsRevealed by 3D 2H–13C–13C Solid-State NMR Spectroscopy

Site-SpecificInternal Motions in GB1 Protein MicrocrystalsRevealed by 3D 2H–13C–13C Solid-State NMR Spectroscopy

Xiangyan Shi and Chad M. Rienstra



Journal of the American Chemical Society
DOI: 10.1021/jacs.5b12974




Source: Journal of the American Chemical Society
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