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NMR processing:
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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
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UNIO ATNOS-Candid
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Fragment-based:
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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)
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d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
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NMR model quality:
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RDCs:
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Pseudocontact shifts:
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SAVES2 or SAVES4
Vadar
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MetaMQAPII
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Ramachandran Plot
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Verify_3D
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
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ArShift- Aromatic
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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
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camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
sedNMR


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Old 11-19-2010, 08:32 PM
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Default Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approa

Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approach for stereospecific NMR assignments of CH3 groups in Val and Leu residues.

Related Articles Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approach for stereospecific NMR assignments of CH3 groups in Val and Leu residues.

J Biomol NMR. 2001 Mar;19(3):267-72

Authors: Atreya HS, Chary KV

A novel methodology for stereospecific NMR assignments of methyl (CH3) groups of Val and Leu residues in fractionally 13C-labeled proteins is presented. The approach is based on selective 'unlabeling' of specific amino acids in proteins while fractionally 13C-labeling the rest. A 2D [13C-1H] HSQC spectrum recorded on such a sample is devoid of peaks belonging to the 'unlabeled' amino acid residues. Such spectral simplification aids in unambiguous stereospecific assignment of diastereotopic CH3 groups in Val and Leu residues in large proteins. This methodology has been demonstrated on a 15 kDa calcium binding protein from Entamoeba histolytica (Eh-CaBP).

PMID: 11330814 [PubMed - indexed for MEDLINE]



Source: PubMed
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