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NMR processing:
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NMR assignment:
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Side-chains:
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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:
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GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
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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:
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NMR model quality:
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Chemical shifts:
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RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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PSVS
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SAVES2 or SAVES4
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NMR spectrum prediction:
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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
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ShiftS
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PPM
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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
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
sedNMR


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Default Objective identification of residue ranges for the superposition of protein ... - 7thSpace Interactive (press release)

Objective identification of residue ranges for the superposition of protein ... - 7thSpace Interactive (press release)



Objective identification of residue ranges for the superposition of protein ...
7thSpace Interactive (press release)
Results: We present an automated and objective method for finding amino acid residue ranges for the superposition and analysis of protein structures, in particular for structure bundles resulting from NMR structure calculations. ...


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