+Open data
-Basic information
Entry | Database: PDB / ID: 2l03 | ||||||
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Title | Spatial structure of water-soluble Lynx1 | ||||||
Components | Ly-6/neurotoxin-like protein 1 | ||||||
Keywords | NEUROPEPTIDE / Lynx1 / acetylcholine receptor / endogenic neuromodulator / three-finger toxins | ||||||
Function / homology | Function and homology information regulation of neurotransmitter receptor activity / acetylcholine receptor regulator activity / : / acetylcholine receptor inhibitor activity / acetylcholine receptor binding / synaptic transmission, cholinergic / ion channel inhibitor activity / dendrite / synapse / endoplasmic reticulum / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Authors | Mineev, K.S. / Shenkarev, Z.O. / Arseniev, A.S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: NMR structure and action on nicotinic acetylcholine receptors of water-soluble domain of human LYNX1 Authors: Lyukmanova, E.N. / Shenkarev, Z.O. / Shulepko, M.A. / Mineev, K.S. / D'Hoedt, D. / Kasheverov, I.E. / Filkin, S.Y. / Krivolapova, A.P. / Janickova, H. / Dolezal, V. / Dolgikh, D.A. / ...Authors: Lyukmanova, E.N. / Shenkarev, Z.O. / Shulepko, M.A. / Mineev, K.S. / D'Hoedt, D. / Kasheverov, I.E. / Filkin, S.Y. / Krivolapova, A.P. / Janickova, H. / Dolezal, V. / Dolgikh, D.A. / Arseniev, A.S. / Bertrand, D. / Tsetlin, V.I. / Kirpichnikov, M.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l03.cif.gz | 490.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l03.ent.gz | 430 KB | Display | PDB format |
PDBx/mmJSON format | 2l03.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l0/2l03 ftp://data.pdbj.org/pub/pdb/validation_reports/l0/2l03 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8418.714 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LYNX1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q9BZG9, UniProt: P0DP58*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 21 / pH: 5.3 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20 |