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- PDB-1aty: DETERMINATION OF LOCAL PROTEIN STRUCTURE BY SPIN LABEL DIFFERENCE... -

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Entry
Database: PDB / ID: 1aty
TitleDETERMINATION OF LOCAL PROTEIN STRUCTURE BY SPIN LABEL DIFFERENCE 2D NMR: THE REGION NEIGHBORING ASP61 OF SUBUNIT C OF THE F1FO ATP SYNTHASE
ComponentsF1F0 ATP SYNTHASE (SUBUNIT C)
KeywordsMEMBRANE 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 motive force-driven ATP synthesis / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / lipid binding / plasma membrane
Similarity search - Function
F1F0 ATP synthase subunit C / F1FO ATP Synthase / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C ...F1F0 ATP synthase subunit C / F1FO ATP Synthase / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
ATP synthase subunit c
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR
AuthorsGirvin, M.E. / Fillingame, R.H.
Citation
Journal: Biochemistry / Year: 1995
Title: Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase.
Authors: Girvin, M.E. / Fillingame, R.H.
#1: Journal: Biochemistry / Year: 1994
Title: Hairpin Folding of Subunit C of F1Fo ATP Synthase: 1H Distance Measurements to Nitroxide-Derivatized Aspartyl-61
Authors: Girvin, M.E. / Fillingame, R.H.
#2: Journal: Biochemistry / Year: 1993
Title: Helical Structure and Folding of Subunit C of F1Fo ATP Synthase: 1H NMR Resonance Assignments and Noe Analysis
Authors: Girvin, M.E. / Fillingame, R.H.
History
DepositionOct 5, 1994Processing site: BNL
Revision 1.0Dec 20, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 27, 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details

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Structure viewerMolecule:
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Assembly

Deposited unit
A: F1F0 ATP SYNTHASE (SUBUNIT C)


Theoretical massNumber of molelcules
Total (without water)8,2911
Polymers8,2911
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)9 / -
Representative

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Components

#1: Protein F1F0 ATP SYNTHASE (SUBUNIT C)


Mass: 8291.129 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: UNCE / Plasmid: PCP35 (PBR322 DERIVATIV / References: UniProt: P68699, EC: 3.6.1.34

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR softwareName: X-PLOR / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 9

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