BioNMR - FAQ

BioNMR

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NMR processing:

NMR assignment:

Backbone:

Side-chains:

UNIO ATNOS-Ascan

NOEs:

UNIO ATNOS-Candid

Structure from NMR restraints:

Ab initio:

UNIO ATNOS-Candid

Fragment-based:

BMRB CS-Rosetta

Rosetta-NMR (Robetta)

Template-based:

Refinement:

Structure from chemical shifts:

Fragment-based:

WeNMR CS-Rosetta

BMRB CS-Rosetta

Homology-based:

Torsion angles from chemical shifts:

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

MICS caps, β-turns

Flexibility from chemical shifts:

Interactions from chemical shifts:

Chemical shifts re-referencing:

UNIO Shiftinspector

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

Resolution-by-Proxy

SAVES2 or SAVES4

Ramachandran Plot

Quality Control Check

NMR spectrum prediction:

Flexibility from structure:

Molecular dynamics:

Chemical shifts prediction:

From structure:

CH3shift- Methyl

ArShift- Aromatic

CheShift-2- Cα

From sequence:

Disordered proteins:

Format conversion & validation:

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

Protein solubility:

Isotope labeling:

Solid-state NMR:

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