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NMR processing:
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Side-chains:
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NOEs:
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UNIO Candid
ASDP
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
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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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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 spectrum prediction:
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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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PPM
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From sequence:
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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:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
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Isotope labeling:
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Solid-state NMR:
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Default Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1

Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1



Source: Journal of Biomolecular NMR
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