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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:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
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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
iCing
PSVS
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SAVES2 or SAVES4
Vadar
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MetaMQAPII
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Verify_3D
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V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
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Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
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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 Primary and NMR three-dimensional structure determination of a novel crustacean toxin

Primary and NMR three-dimensional structure determination of a novel crustacean toxin from the venom of the scorpion Centruroides limpidus limpidus Karsch.

Related Articles Primary and NMR three-dimensional structure determination of a novel crustacean toxin from the venom of the scorpion Centruroides limpidus limpidus Karsch.

Biochemistry. 1994 Sep 20;33(37):11135-49

Authors: Lebreton F, Delepierre M, Ram├*rez AN, Balderas C, Possani LD

A crustacean-specific toxin from the Mexican scorpion Centruroides limpidus limpidus was purified, and its primary sequence was determined, including disulfide bonds. This toxin has 66 amino acid residues and is stabilized by four disulfide bridges (Cys12-Cys65, Cys16-Cys41, Cys25-Cys46, and Cys29-Cys48). A detailed nuclear magnetic resonance structure of this protein was obtained using a combination of two-dimensional proton NMR experiments. The NMR parameters that gave 69 dihedral restraints and 418 distance constraints were used in molecular dynamics calculations in order to determine the solution conformation of the toxin. It is composed of a short alpha-helix and a three-stranded antiparallel beta-sheet. Although the regular secondary structure of this crustacean toxin is common to the structural motif of other scorpion toxins, detailed conformational analysis was performed in order to highlight structural features that might be responsible for the differential modulation of the toxin on sodium channels of distinct tissues: mammalian versus crustacean.

PMID: 7727365 [PubMed - indexed for MEDLINE]



Source: PubMed
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