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- PDB-1a11: NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE... -

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Basic information

Entry
Database: PDB / ID: 1a11
TitleNMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE RECEPTOR IN DPC MICELLES, 10 STRUCTURES
ComponentsACETYLCHOLINE RECEPTOR M2
KeywordsACETYLCHOLINE RECEPTOR / M2 / MICELLE
Function / homology
Function and homology information


Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine-gated channel complex / acetylcholine-gated monoatomic cation-selective channel activity / postsynaptic specialization membrane / acetylcholine binding / ligand-gated monoatomic ion channel activity / monoatomic cation transport / skeletal muscle contraction ...Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine-gated channel complex / acetylcholine-gated monoatomic cation-selective channel activity / postsynaptic specialization membrane / acetylcholine binding / ligand-gated monoatomic ion channel activity / monoatomic cation transport / skeletal muscle contraction / regulation of membrane potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / neuromuscular junction / transmembrane signaling receptor activity / neuron projection / synapse / plasma membrane
Similarity search - Function
Nicotinic acetylcholine receptor / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain
Similarity search - Domain/homology
Acetylcholine receptor subunit delta
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
AuthorsGesell, J.J. / Sun, W. / Montal, M. / Opella, S.J.
CitationJournal: 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.
History
DepositionDec 19, 1997Processing site: BNL
Revision 1.0Apr 8, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ACETYLCHOLINE RECEPTOR M2


Theoretical massNumber of molelcules
Total (without water)2,6661
Polymers2,6661
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 30LOWEST ENERGY
Representative

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Components

#1: Protein/peptide ACETYLCHOLINE RECEPTOR M2 / ACHR M2


Mass: 2666.143 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: BRAIN / Plasmid: PGEX FUSION / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P25110

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HMQC-NOESY
121HMQC-TOCSY
131HNCA
141HN(CO)CA
151HNHA

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Sample preparation

Sample conditionspH: 5.5 / Temperature: 313 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMX600BrukerDMX6006001
Bruker DMX750BrukerDMX7507502

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 30 / Conformers submitted total number: 10

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