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- PDB-1b9u: MEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE -

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Basic information

Entry
Database: PDB / ID: 1b9u
TitleMEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE
ComponentsPROTEIN (ATP SYNTHASE)
KeywordsHYDROLASE / ATP SYNTHASE / MEMBRANE PROTEIN
Function / homology
Function and homology information


proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / plasma membrane
Similarity search - Function
ATP synthase, F0 complex, subunit b, bacterial / F-type ATP synthase subunit B-like, membrane domain superfamily / ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast / ATP synthase B/B' CF(0)
Similarity search - Domain/homology
ATP synthase subunit b
Similarity search - Component
MethodSOLUTION NMR / simulated annealing
AuthorsDmitriev, O. / Jones, P.C. / Jiang, W. / Fillingame, R.H.
CitationJournal: J.Biol.Chem. / Year: 1999
Title: Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase.
Authors: Dmitriev, O. / Jones, P.C. / Jiang, W. / Fillingame, R.H.
History
DepositionFeb 15, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0Sep 15, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection / Category: atom_site / chem_comp_atom / chem_comp_bond / Item: _atom_site.auth_atom_id / _atom_site.label_atom_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (ATP SYNTHASE)


Theoretical massNumber of molelcules
Total (without water)3,8301
Polymers3,8301
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 / 200LOWEST TARGET FUNCTION VALUE
Representative

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Components

#1: Protein/peptide PROTEIN (ATP SYNTHASE) / E.C.3.6.1.34


Mass: 3829.722 Da / Num. of mol.: 1 / Fragment: MEMBRANE DOMAIN / Source method: obtained synthetically
Details: SEQUENCE CORRESPONDS TO RESIDUES 1-34 OF SUBUNIT B FROM GENE UNCF OF ESCHERICHIA COLI CYTOPLASMIC MEMBRANE
References: UniProt: P0ABA0, EC: 3.6.1.34

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DQF-COSY
121TOCSY
131NOESY
NMR detailsText: WATER SUPPESSION USING PULSED FIELD GRADIENTS

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Sample preparation

DetailsContents: CHLOROFORM/METHANOL/WATER=4/4/1
Sample conditionsIonic strength: 50 mM NACL / pH: 6.0 / Pressure: 1 atm / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DYANA, DISCOVER (MSI)1.5GUENTERT ET AL.refinement
DYANA1.5structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST TARGET FUNCTION VALUE / Conformers calculated total number: 200 / Conformers submitted total number: 10

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