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NMR processing:
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NMR assignment:
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PINE
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
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
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RPF scores
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Chemical shifts:
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iCing
RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
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PSVS
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SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
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STAN
Ramachandran Plot
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ERRAT
Verify_3D
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
Backbone S2
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 Computer-aided assignment of the 1H-NMR spectrum of the viral-protein-genome-linked p

Computer-aided assignment of the 1H-NMR spectrum of the viral-protein-genome-linked polypeptide from cowpea mosaic virus.

Related Articles Computer-aided assignment of the 1H-NMR spectrum of the viral-protein-genome-linked polypeptide from cowpea mosaic virus.

Eur J Biochem. 1990 Jul 5;190(3):583-91

Authors: van de Ven FJ, Lycksell PO, van Kammen A, Hilbers CW

The 1H-NMR spectrum of the viral-protein-genome-linked (VPg) polypeptide from cowpea mosaic virus, has been interpreted via application of 2-dimensional (2D) NMR techniques. The interpretation of the data was performed by a computer program called 'PROSPECT' (PROtein SPECTra), which detects the cross-peak patterns of the amino acid residues in the spectra, assigns these patterns to amino acid types, and finally performs the sequential assignments using the well-known 'sequential walks' obtained from the NOE spectrum. Due to the severe overlap of resonances in the NMR spectrum of the VPg polypeptide, several ways of performing these walks existed. The program detected six alternatives for the sequential assignments of backbone N alpha H-C beta H-C beta H moieties.

PMID: 2373083 [PubMed - indexed for MEDLINE]



Source: PubMed
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