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NMR processing:
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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:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
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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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MICS caps, β-turns
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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
UNIO Shiftinspector
LACS
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RefDB
NMR model quality:
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iCing
RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
iCing
PSVS
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SAVES2 or SAVES4
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STAN
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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:
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 Zooming in on protons: Neutron structure of protein kinase A trapped in a product complex - Science Advances

Zooming in on protons: Neutron structure of protein kinase A trapped in a product complex - Science Advances

Zooming in on protons: Neutron structure of protein kinase A trapped in a product complex Science AdvancesThe question vis--vis the chemistry of phosphoryl group transfer catalyzed by protein kinases remains a major challenge. The neutron diffraction structure of the ...

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