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NMR processing:
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NMR assignment:
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PINE
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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ASDP
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Fragment-based:
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Template-based:
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Refinement:
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Structure from chemical shifts:
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WeNMR CS-Rosetta
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Torsion angles from chemical shifts:
Preditor
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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
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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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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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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Default 129Xe NMR Relaxation-Based Macromolecular Sensing

129Xe NMR Relaxation-Based Macromolecular Sensing

Muller D. Gomes, Phuong Dao, Keunhong Jeong, Clancy C. Slack, Christophoros C. Vassiliou, Joel A. Finbloom, Matthew B. Francis, David E. Wemmer and Alexander Pines



Journal of the American Chemical Society
DOI: 10.1021/jacs.6b02758




Source: Journal of the American Chemical Society
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