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Basic information

Entry
Database: PDB / ID: 1ifj
TitleMOLECULAR MODELS AND STRUCTURAL COMPARISONS OF NATIVE AND MUTANT CLASS I FILAMENTOUS BACTERIOPHAGES FF (FD, F1, M13), IF1 AND IKE
ComponentsINOVIRUSFf phages
KeywordsVIRUS / Helical virus
Function / homology
Function and homology information


helical viral capsid / host cell membrane / membrane
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #80 / Phage major coat protein, Gp8 / Bacteriophage M13, G8P, capsid domain superfamily / Capsid protein G8P / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesEnterobacteria phage fd (virus)
MethodFIBER DIFFRACTION / Resolution: 3.3 Å
AuthorsMarvin, D.A.
Citation
Journal: J.Mol.Biol. / Year: 1994
Title: Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages Ff (fd, f1, M13), If1 and IKe.
Authors: Marvin, D.A. / Hale, R.D. / Nave, C. / Helmer-Citterich, M.
#1: Journal: Int.J.Biol.Macromol. / Year: 1990
Title: Model-Building Studies of Inovirus: Genetic Variations on a Geometric Theme
Authors: Marvin, D.A.
#2: Journal: Int.J.Biol.Macromol. / Year: 1989
Title: Dynamics of Telescoping Inovirus: A Mechanism for Assembly at Membrane Adhesions
Authors: Marvin, D.A.
#3: Journal: Nature / Year: 1981
Title: Structure of the Protein and DNA in Fd Filamentous Bacterial Virus
Authors: Banner, D.W. / Nave, C. / Marvin, D.A.
#4: Journal: J.Mol.Biol. / Year: 1974
Title: Filamentous Bacterial Viruses Xii. Molecular Architecture of the Class I (Fd, If1, Ike) Virion
Authors: Marvin, D.A. / Pigram, W.J. / Wiseman, R.L. / Wachtel, E.J. / Marvin, F.J.
History
DepositionJan 31, 1994Processing site: BNL
Revision 1.0Jul 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 7, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / 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_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: INOVIRUS


Theoretical massNumber of molelcules
Total (without water)5,2441
Polymers5,2441
Non-polymers00
Water0
1
A: INOVIRUS
x 55


Theoretical massNumber of molelcules
Total (without water)288,42055
Polymers288,42055
Non-polymers00
Water0
TypeNameSymmetry operationNumber
helical symmetry operation54
identity operation1_555x,y,z1
2


  • Idetical with deposited unit in distinct coordinate
  • helical asymmetric unit
TypeNameSymmetry operationNumber
helical symmetry operation1
3


  • Idetical with deposited unit
  • helical asymmetric unit, std helical frame
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)1.000, 1.000, 1.000
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number1
Space group name H-MP1
SymmetryHelical symmetry: (Circular symmetry: 5 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 55 / Rise per n subunits: 16.15 Å / Rotation per n subunits: -33.23 °)

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Components

#1: Protein/peptide INOVIRUS / Ff phages


Mass: 5244.000 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Enterobacteria phage fd (virus) / Genus: InovirusFf phages / Species: Enterobacteria phage M13 / Strain: FD MAJOR / References: UniProt: P69539

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Experimental details

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Experiment

ExperimentMethod: FIBER DIFFRACTION

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Sample preparation

Crystal grow
*PLUS
Method: fibre diffraction

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Data collection

Radiation wavelengthRelative weight: 1

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Processing

SoftwareName: EREF / Classification: refinement
RefinementHighest resolution: 3.3 Å
Details: THE TEMPERATURE FACTOR WAS NOT REFINED AND IS GIVEN THE ARBITRARY VALUE OF 10.
Refinement stepCycle: LAST / Highest resolution: 3.3 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms370 0 0 0 370

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