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Yorodumi- PDB-1a11: NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE... -
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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 | ||||||
Components | ACETYLCHOLINE RECEPTOR M2 | ||||||
Keywords | ACETYLCHOLINE RECEPTOR / M2 / MICELLE | ||||||
| Function / homology | Function and homology informationHighly sodium permeable postsynaptic acetylcholine nicotinic receptors / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine receptor activity / acetylcholine-gated channel complex / acetylcholine-gated monoatomic cation-selective channel activity / acetylcholine binding / acetylcholine receptor signaling pathway / ligand-gated monoatomic ion channel activity / postsynaptic specialization membrane ...Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine receptor activity / acetylcholine-gated channel complex / acetylcholine-gated monoatomic cation-selective channel activity / acetylcholine binding / acetylcholine receptor signaling pathway / ligand-gated monoatomic ion channel activity / postsynaptic specialization membrane / monoatomic cation transport / membrane depolarization / skeletal muscle contraction / regulation of membrane potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / neuromuscular junction / monoatomic ion transmembrane transport / chemical synaptic transmission / neuron projection / synapse / plasma membrane Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING | ||||||
Authors | Gesell, J.J. / Sun, W. / Montal, M. / Opella, S.J. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1999Title: 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. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1a11.cif.gz | 81.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1a11.ent.gz | 51.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1a11.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1a11_validation.pdf.gz | 344.5 KB | Display | wwPDB validaton report |
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| Full document | 1a11_full_validation.pdf.gz | 406.7 KB | Display | |
| Data in XML | 1a11_validation.xml.gz | 6.6 KB | Display | |
| Data in CIF | 1a11_validation.cif.gz | 9.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/1a11 ftp://data.pdbj.org/pub/pdb/validation_reports/a1/1a11 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1cekC ![]() 1eq8C ![]() 2nr1C C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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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 |
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