+Open data
-Basic information
Entry | Database: PDB / ID: 2n1n | ||||||
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Title | Solution structure of VSTx1 | ||||||
Components | Kappa-theraphotoxin-Gr3a | ||||||
Keywords | TOXIN | ||||||
Function / homology | Function and homology information ion channel inhibitor activity / sodium channel regulator activity / potassium channel regulator activity / toxin activity / extracellular region Similarity search - Function | ||||||
Biological species | Grammostola rosea (Chilean rose tarantula) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Lau, H.Y. / King, G.F. / Mobli, M. | ||||||
Citation | Journal: Sci Rep Title: Molecular basis of the interaction between gating modifier spider toxins and the voltage sensor of voltage-gated ion channels. Authors: Lau, C.H. / King, G.F. / Mobli, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n1n.cif.gz | 245.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n1n.ent.gz | 213.7 KB | Display | PDB format |
PDBx/mmJSON format | 2n1n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n1/2n1n ftp://data.pdbj.org/pub/pdb/validation_reports/n1/2n1n | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4096.843 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Grammostola rosea (Chilean rose tarantula) Production host: Escherichia coli (E. coli) / References: UniProt: P60980 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 20 mM sodium acetate, 1.7 mM [U-99% 13C; U-99% 15N] VSTx1, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 900 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 / Details: Simulated annealing, with automated NOE assignment | ||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 694 / NOE intraresidue total count: 193 / NOE long range total count: 179 / NOE medium range total count: 116 / NOE sequential total count: 206 / Disulfide bond constraints total count: 3 / Hydrogen bond constraints total count: 2 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20 |