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- PDB-1hf9: C-Terminal Coiled-Coil Domain from Bovine IF1 -

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Basic information

Entry
Database: PDB / ID: 1hf9
TitleC-Terminal Coiled-Coil Domain from Bovine IF1
ComponentsATPASE INHIBITOR (MITOCHONDRIAL)
KeywordsATPASE INHIBITOR / F1 ATPASE INHIBITOR / MITOCHONDRION / TRANSIT PEPTIDE
Function / homology
Function and homology information


angiostatin binding / ATPase inhibitor activity / negative regulation of hydrolase activity / heme biosynthetic process / : / negative regulation of endothelial cell proliferation / erythrocyte differentiation / ATPase binding / protein homotetramerization / calmodulin binding ...angiostatin binding / ATPase inhibitor activity / negative regulation of hydrolase activity / heme biosynthetic process / : / negative regulation of endothelial cell proliferation / erythrocyte differentiation / ATPase binding / protein homotetramerization / calmodulin binding / structural molecule activity / cell surface / protein homodimerization activity / protein-containing complex / mitochondrion / identical protein binding
Similarity search - Function
Single helix bin / Mitochondrial ATPase inhibitor / Mitochondrial ATPase inhibitor, IATP / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
ATPase inhibitor, mitochondrial
Similarity search - Component
Biological speciesBOS TAURUS (cattle)
MethodSOLUTION NMR / simulated annealing
AuthorsGordon-Smith, D.J. / Carbajo, R.J. / Yang, J.-C. / Videler, H. / Runswick, M.J. / Walker, J.E. / Neuhaus, D.
CitationJournal: J. Mol. Biol. / Year: 2001
Title: Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.
Authors: Gordon-Smith, D.J. / Carbajo, R.J. / Yang, J.C. / Videler, H. / Runswick, M.J. / Walker, J.E. / Neuhaus, D.
History
DepositionNov 30, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 31, 2001Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 17, 2018Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name
Revision 1.4Jan 15, 2020Group: Data collection / Other
Category: pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr ..._pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.5May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ATPASE INHIBITOR (MITOCHONDRIAL)
B: ATPASE INHIBITOR (MITOCHONDRIAL)


Theoretical massNumber of molelcules
Total (without water)9,9992
Polymers9,9992
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)35 / 50LOWEST ENERGIES
Representative

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Components

#1: Protein/peptide ATPASE INHIBITOR (MITOCHONDRIAL) / IF1


Mass: 4999.617 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN (44-84)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) BOS TAURUS (cattle) / Organ: HEART / Organelle: MITOCHONDRIA / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): C41(DE3) / References: UniProt: P01096

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 6.5 / Pressure: 1 atm / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMXBrukerAMX5001
Bruker DRXBrukerDRX5002
Bruker DMXBrukerDMX6003
Bruker AVANCEBrukerAVANCE8004

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
XwinNMRXWINNMRstructure solution
Felixstructure solution
Sparkystructure solution
Insightstructure solution
X-PLORstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: LOWEST ENERGIES / Conformers calculated total number: 50 / Conformers submitted total number: 35

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