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NMR processing:
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NMR assignment:
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PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
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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:
WeNMR CS-Rosetta
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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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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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What-If
iCing
PSVS
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SAVES2 or SAVES4
Vadar
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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+
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
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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 The SARS-CoV-2 Spike Glycoprotein Directly Binds Exogeneous Sialic Acids: A NMR View

The SARS-CoV-2 Spike Glycoprotein Directly Binds Exogeneous Sialic Acids: A NMR View

The interaction of the SARS CoV2 spike glycoprotein with two sialic acid-containing trisaccharides (a2,3 and a2,6 sialyl N-Acetyllactosamine) has been demonstrated by NMR. The NMR-based distinction between the signals of those sialic acids in the glycans covalently attached to the spike protein and those belonging to the exogenous a2,3 and a2,6 sialyl N-Acetyllactosamine ligands has been achieved by synthesizing uniformly 13C-labelled trisaccharides at the sialic acid and galactose moieties....

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