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- PDB-1abv: N-TERMINAL DOMAIN OF THE DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE F... -

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Entry
Database: PDB / ID: 1abv
TitleN-TERMINAL DOMAIN OF THE DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsDELTA SUBUNIT OF THE F1F0-ATP SYNTHASE
KeywordsATP SYNTHESIS / ATP SYNTHASE / F1-ATPASE / DELTA SUBUNIT / NMR SPECTROSCOPY
Function / homology
Function and homology information


proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton motive force-driven ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / plasma membrane
Similarity search - Function
N-terminal domain of the delta subunit of the F1F0-ATP synthase / ATPase, OSCP/delta subunit, conserved site / ATP synthase delta (OSCP) subunit signature. / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / Peroxidase; domain 1 / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
ATP synthase subunit delta
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / DG, SA, MD
AuthorsWilkens, S. / Dunn, S.D. / Chandler, J. / Dahlquist, F.W. / Capaldi, R.A.
CitationJournal: Nat.Struct.Biol. / Year: 1997
Title: Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase.
Authors: Wilkens, S. / Dunn, S.D. / Chandler, J. / Dahlquist, F.W. / Capaldi, R.A.
History
DepositionJan 29, 1997Processing site: BNL
Revision 1.0Jul 7, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 27, 2021Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_representative / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.authors / _pdbx_nmr_software.classification / _pdbx_nmr_software.version / _pdbx_nmr_spectrometer.manufacturer / _pdbx_nmr_spectrometer.model
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Assembly

Deposited unit
A: DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE


Theoretical massNumber of molelcules
Total (without water)14,6771
Polymers14,6771
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 30ALL
RepresentativeModel #1

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Components

#1: Protein DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE


Mass: 14676.533 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1 - 134
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PJC1 / Gene (production host): UNCH / Production host: Escherichia coli (E. coli) / Strain (production host): MM294 AND 594 / References: UniProt: P0ABA4, 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
1113D NOESY-HSMQC
1213D TOCSY-HSMQC
1313D C(CO)NH
1413D H(CCO)NH
151SIMULTANEOUS 13C/15N RESOLVED NOESY
161VARIOUS 2D EXPERIMENTS

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Sample preparation

Sample conditionspH: 7.2 / Temperature: 293 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
GE GNGEGN5001
Varian UNITYVarianUNITY5002

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLOR3.1BRUNGERstructure calculation
RefinementMethod: DG, SA, MD / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. THIS ENTRY CONTAINS THE MINIMIZED AVERAGE OVER 30 FILES. THE AVERAGE RMS DIFFERENCE TO THE MEAN STRUCTURE FOR NON-HYDROGEN ATOMS ...Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. THIS ENTRY CONTAINS THE MINIMIZED AVERAGE OVER 30 FILES. THE AVERAGE RMS DIFFERENCE TO THE MEAN STRUCTURE FOR NON-HYDROGEN ATOMS IS 1.25067. THE AVERAGE RMS DIFFERENCE TO THE MEAN STRUCTURE FOR THE BACKBONE IS 0.795004. THE B VALUE FIELD (COLUMNS 61 =66) CONTAINS THE RMS DIFFERENCE FROM THE MEAN.
NMR ensembleConformer selection criteria: ALL / Conformers calculated total number: 30 / Conformers submitted total number: 1

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