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Yorodumi- PDB-1l4w: NMR structure of an AChR-peptide (Torpedo Californica, alpha-subu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1l4w | ||||||
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Title | NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin | ||||||
Components |
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Keywords | Receptor / Toxin / protein-protein complex / intermolecular beta sheet / bungarotoxin / acetylcholine receptor | ||||||
Function / homology | Function and homology information acetylcholine receptor inhibitor activity / acetylcholine-gated monoatomic cation-selective channel activity / ion channel regulator activity / transmembrane signaling receptor activity / toxin activity / postsynaptic membrane / extracellular region Similarity search - Function | ||||||
Biological species | Bungarus multicinctus (many-banded krait) | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing energy minimization | ||||||
Model type details | minimized average | ||||||
Authors | Samson, A.O. / Scherf, T. / Rodriguez, E. / Eisenstein, M. / Anglister, J. | ||||||
Citation | Journal: Neuron / Year: 2002 Title: The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR. Authors: Samson, A. / Scherf, T. / Eisenstein, M. / Chill, J. / Anglister, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1l4w.cif.gz | 40.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1l4w.ent.gz | 31.8 KB | Display | PDB format |
PDBx/mmJSON format | 1l4w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l4/1l4w ftp://data.pdbj.org/pub/pdb/validation_reports/l4/1l4w | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8005.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bungarus multicinctus (many-banded krait) / Secretion: venom / Strain: Banded krait / References: UniProt: P60615 |
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#2: Protein/peptide | Mass: 3137.432 Da / Num. of mol.: 1 / Fragment: Acetylcholine receptor peptide (residues 206-226) / Source method: obtained synthetically / Details: synthesized peptide / References: UniProt: P02711 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: Mixing times of 40, 70 and 150 ms were measured for the NOESY experiment |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 50 mM Ac / pH: 4 / Pressure: ambient / Temperature: 303 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 |
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-Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing energy minimization Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |