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- PDB-1vtx: DELTA-ATRACOTOXIN-HV1 (VERSUTOXIN) FROM HADRONYCHE VERSUTA, NMR, ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1vtx | ||||||
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Title | DELTA-ATRACOTOXIN-HV1 (VERSUTOXIN) FROM HADRONYCHE VERSUTA, NMR, 20 STRUCTURES | ||||||
![]() | DELTA-ATRACOTOXIN-HV1 | ||||||
![]() | NEUROTOXIN / SODIUM CHANNEL TOXIN / CYSTEINE KNOT / VENOM | ||||||
Function / homology | ![]() sodium channel inhibitor activity / : / toxin activity / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, DYNAMICAL SIMULATED ANNEALING | ||||||
![]() | Fletcher, J.I. / Chapman, B.E. / King, G.F. | ||||||
![]() | ![]() Title: The structure of versutoxin (delta-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel. Authors: Fletcher, J.I. / Chapman, B.E. / Mackay, J.P. / Howden, M.E. / King, G.F. #1: ![]() Title: Selective Alteration of Sodium Channel Gating by Australian Funnel-Web Spider Toxins Authors: Nicholson, G.M. / Little, M.J. / Tyler, M. / Narahashi, T. #2: ![]() Title: Erratum. Amino Acid Sequence of Versutoxin, a Lethal Neurotoxin from the Venom of the Funnel-Web Spider Atrax Versutus Authors: Brown, M.R. / Sheumack, D.D. / Tyler, M.I. / Howden, M.E. #3: ![]() Title: Amino Acid Sequence of Versutoxin, a Lethal Neurotoxin from the Venom of the Funnel-Web Spider Atrax Versutus Authors: Brown, M.R. / Sheumack, D.D. / Tyler, M.I. / Howden, M.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 252.9 KB | Display | ![]() |
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PDB format | ![]() | 218.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 339.4 KB | Display | ![]() |
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Full document | ![]() | 457.8 KB | Display | |
Data in XML | ![]() | 20.5 KB | Display | |
Data in CIF | ![]() | 31.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 4862.720 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 2.6 / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
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NMR software |
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Refinement | Method: DISTANCE GEOMETRY, DYNAMICAL SIMULATED ANNEALING / Software ordinal: 1 Details: SEE PRIMARY REFERENCE ABOVE. OTHER PROGRAM USED DIANA VERSION 2.8 BY GUNTERT. | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 75 / Conformers submitted total number: 20 |