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- PDB-2byp: Crystal structure of Aplysia californica AChBP in complex with al... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2byp | ||||||
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Title | Crystal structure of Aplysia californica AChBP in complex with alpha- conotoxin ImI | ||||||
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![]() | RECEPTOR / RECEPTOR COMPLEX / NICOTINIC ACETYLCHOLINE RECEPTOR COMPLEX / CONOTOXIN | ||||||
Function / homology | ![]() host cell postsynaptic membrane / acetylcholine receptor inhibitor activity / ion channel regulator activity / acetylcholine receptor activity / acetylcholine-gated monoatomic cation-selective channel activity / response to nicotine / toxin activity / neuron projection / synapse / extracellular region ...host cell postsynaptic membrane / acetylcholine receptor inhibitor activity / ion channel regulator activity / acetylcholine receptor activity / acetylcholine-gated monoatomic cation-selective channel activity / response to nicotine / toxin activity / neuron projection / synapse / extracellular region / identical protein binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hansen, S.B. / Sulzenbacher, G. / Huxford, T. / Marchot, P. / Taylor, P. / Bourne, Y. | ||||||
![]() | ![]() Title: Structures of Aplysia Achbp Complexes with Nicotinic Agonists and Antagonists Reveal Distinctive Binding Interfaces and Conformations. Authors: Hansen, S.B. / Sulzenbacher, G. / Huxford, T. / Marchot, P. / Taylor, P. / Bourne, Y. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 256.1 KB | Display | ![]() |
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PDB format | ![]() | 210.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 508.7 KB | Display | ![]() |
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Full document | ![]() | 521.4 KB | Display | |
Data in XML | ![]() | 53.3 KB | Display | |
Data in CIF | ![]() | 78.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2bynSC ![]() 2byqC ![]() 2byrC ![]() 2bysC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 24320.039 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Cell: SENSORY CELL / Cell line (production host): HEK293 / Production host: ![]() #2: Protein/peptide | Mass: 1357.609 Da / Num. of mol.: 5 / Source method: obtained synthetically / Source: (synth.) ![]() #3: Sugar | ChemComp-NAG / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.25 % |
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Crystal grow | pH: 7.5 / Details: 11-14% PEG-4000, 0.1 M TRIS, PH 7.5, 0.4 M MGCL2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.976 Å / Relative weight: 1 |
Reflection | Resolution: 2.07→50 Å / Num. obs: 86601 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 29.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2BYN Resolution: 2.07→20 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.949 / SU B: 7.782 / SU ML: 0.122 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.176 / ESU R Free: 0.155 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.98 Å2
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Refinement step | Cycle: LAST / Resolution: 2.07→20 Å
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Refine LS restraints |
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