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- PDB-1a11: NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1a11 | ||||||
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Title | NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE RECEPTOR IN DPC MICELLES, 10 STRUCTURES | ||||||
![]() | ACETYLCHOLINE RECEPTOR M2 | ||||||
![]() | ACETYLCHOLINE RECEPTOR / M2 / MICELLE | ||||||
Function / homology | ![]() Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine-gated channel complex / acetylcholine receptor activity / acetylcholine binding / acetylcholine-gated monoatomic cation-selective channel activity / acetylcholine receptor signaling pathway / postsynaptic specialization membrane / monoatomic cation transport ...Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine-gated channel complex / acetylcholine receptor activity / acetylcholine binding / acetylcholine-gated monoatomic cation-selective channel activity / acetylcholine receptor signaling pathway / postsynaptic specialization membrane / monoatomic cation transport / membrane depolarization / ligand-gated monoatomic ion channel activity / skeletal muscle contraction / regulation of membrane potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / neuromuscular junction / neuron projection / synapse / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING | ||||||
![]() | Gesell, J.J. / Sun, W. / Montal, M. / Opella, S.J. | ||||||
![]() | ![]() Title: Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Authors: Opella, S.J. / Marassi, F.M. / Gesell, J.J. / Valente, A.P. / Kim, Y. / Oblatt-Montal, M. / Montal, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 81.4 KB | Display | ![]() |
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PDB format | ![]() | 51.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1cekC ![]() 1eq8C ![]() 2nr1C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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/peptide | Mass: 2666.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 5.5 / Temperature: 313 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
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NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 30 / Conformers submitted total number: 10 |