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- PDB-1lxg: Solution structure of alpha-cobratoxin complexed with a cognate p... -
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Basic information
Entry | Database: PDB / ID: 1lxg | ||||||
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Title | Solution structure of alpha-cobratoxin complexed with a cognate peptide (structure ensemble) | ||||||
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![]() | TOXIN / alpha-cobratoxin / nicotinic acetylcholine receptor / protein-protein interaction | ||||||
Function / homology | ![]() acetylcholine receptor inhibitor activity / ion channel regulator activity / acetylcholine-gated monoatomic cation-selective channel activity / transmembrane signaling receptor activity / toxin activity / postsynaptic membrane / neuron projection / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
![]() | Zeng, H. / Hawrot, E. | ||||||
![]() | ![]() Title: NMR-based Binding Screen and Structural Analysis of the Complex Formed between alpha-Cobratoxin and an 18-mer Cognate Peptide Derived from the alpha1 Subunit of the Nicotinic Acetylcholine ...Title: NMR-based Binding Screen and Structural Analysis of the Complex Formed between alpha-Cobratoxin and an 18-mer Cognate Peptide Derived from the alpha1 Subunit of the Nicotinic Acetylcholine Receptor from Torpedo californica Authors: Zeng, H. / Hawrot, 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 | ![]() | 274.6 KB | Display | ![]() |
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PDB format | ![]() | 232.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 353.5 KB | Display | ![]() |
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Full document | ![]() | 534.1 KB | Display | |
Data in XML | ![]() | 24 KB | Display | |
Data in CIF | ![]() | 36.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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 | Mass: 7842.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Protein/peptide | Mass: 2424.732 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PET-31B(+) / Species (production host): Escherichia coli / Production host: ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.6 mM alpha-cobratoxin/alpha18-mer complex, alpha18-mer is U-15N, 50 mM perdeuterated potassium acetate buffer (pH 4.0) with 5% D2O and 0.05% sodium azide Solvent system: 95% H2O/5% D2O |
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Sample conditions | pH: 4.0 / Pressure: AMBIENT / Temperature: 308 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |