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Yorodumi- PDB-1eq8: THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF T... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1eq8 | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT | ||||||
Components | ACETYLCHOLINE RECEPTOR PROTEIN | ||||||
Keywords | SIGNALING PROTEIN / NEUROTRANSMITTER RECEPTOR / M2 / LIPID BILAYERS / ION-CHANNEL / HELICAL BUNDLE / PENTAMERIC BUNDLE | ||||||
Function / homology | Function and homology information acetylcholine-gated monoatomic cation-selective channel activity / transmembrane signaling receptor activity / postsynaptic membrane / neuron projection Similarity search - Function | ||||||
Biological species | Torpedo californica (Pacific electric ray) | ||||||
Method | SOLID-STATE NMR / X-PLOR 3.1, distance geometry, simulated annealing, molecular dynamics, FISI, FINGERPRINT, HOLE | ||||||
Authors | Marassi, F.M. / Gesell, J.J. / Kim, Y. / Valente, A.P. / Oblatt-Montal, M. / Montal, M. / Opella, S.J. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1999 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. #1: Journal: J.BIOMOL.NMR / Year: 1999 Title: Dilute Spin-Exchange Assignment of Solid-State NMR Spectra of Oriented Proteins: Acetylcholine M2 in Bilayers Authors: Marassi, F.M. / Gesell, J.J. / Valente, A.P. / Kim, Y. / Oblatt-Montal, M. / Montal, M. / Opella, S.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eq8.cif.gz | 43.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eq8.ent.gz | 34.7 KB | Display | PDB format |
PDBx/mmJSON format | 1eq8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1eq8_validation.pdf.gz | 307.4 KB | Display | wwPDB validaton report |
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Full document | 1eq8_full_validation.pdf.gz | 307.2 KB | Display | |
Data in XML | 1eq8_validation.xml.gz | 3 KB | Display | |
Data in CIF | 1eq8_validation.cif.gz | 4.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eq/1eq8 ftp://data.pdbj.org/pub/pdb/validation_reports/eq/1eq8 | HTTPS FTP |
-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/peptide | Mass: 2522.013 Da / Num. of mol.: 5 / Fragment: M2 SEGMENT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Torpedo californica (Pacific electric ray) Cell: NEURON / Cellular location: POST-SYNAPTIC MEMBRANE / Organ: BRAIN / Plasmid: PMAL / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P02718 #2: Chemical | ChemComp-OH / | |
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-Experimental details
-Experiment
Experiment | Method: SOLID-STATE NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: The orientation of each monomer in the pentameric bundle was obtained from the combination of the solution NMR (PDB file 1a11) and solid-state NMR (PDB file 1cek) structures |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: X-PLOR 3.1, distance geometry, simulated annealing, molecular dynamics, FISI, FINGERPRINT, HOLE Software ordinal: 1 Details: The backbone coordinates obtained from solution NMR were superimposed on the coordinates obtained from solid-state NMR to fix the helix orientation and rotation in the membrane. The ...Details: The backbone coordinates obtained from solution NMR were superimposed on the coordinates obtained from solid-state NMR to fix the helix orientation and rotation in the membrane. The pentameric array was then optimized using molecular dynamics. Pore contours were calculated with the program HOLE. | ||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with favorable non-bond energy Conformers calculated total number: 30 / Conformers submitted total number: 1 |