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Open data
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Basic information
Entry | Database: PDB / ID: 1hgz | ||||||
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Title | Filamentous Bacteriophage PH75 | ||||||
![]() | PH75 INOVIRUS MAJOR COAT PROTEIN | ||||||
![]() | VIRUS / VIRUS COAT PROTEIN / HELICAL VIRUS COAT PROTEIN / SSDNA VIRUSES / INOVIRUS / FILAMENTOUS BACTERIOPHAGE / THERMOPHILES / MEMBRANE PROTEINS / HELICAL VIRUS | ||||||
Function / homology | Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #80 / Bacteriophage M13, G8P, capsid domain superfamily / helical viral capsid / host cell membrane / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha / membrane / Capsid protein G8P![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pederson, D.M. / Welsh, L.C. / Marvin, D.A. / Sampson, M. / Perham, R.N. / Yu, M. / Slater, M.R. | ||||||
![]() | ![]() Title: The Protein Capsid of Filamentous Bacteriophage Ph75 from Thermus Thermophilus Authors: Pederson, D.M. / Welsh, L.C. / Marvin, D.A. / Sampson, M. / Perham, R.N. / Yu, M. / Slater, M.R. #1: ![]() Title: The Molecular Structure and Structural Transition of the Alpha-Helical Capsid in Filamentous Bacteriophage Pf1 Authors: Welsh, L.C. / Symmons, M.F. / Marvin, D.A. #2: ![]() Title: Structure of the Capsid of Pf3 Filamentous Phage Determined from X-Ray Fibre Diffraction Data at 3.1 A Resolution Authors: Welsh, L.C. / Symmons, M.F. / Sturtevant, J.M. / Marvin, D.A. / Perham, R.N. #3: ![]() Title: Pf1 Filamentous Bacteriophage: Refinement of a Molecular Model by Simulated Annealing Using 3.3 Angstroms Resolution X-Ray Fibre Diffraction Data Authors: Gonzalez, A. / Nave, C. / Marvin, D.A. #4: ![]() Title: Model-Building Studies of Inovirus: Genetic Variations on a Geometric Theme Authors: Marvin, D.A. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 26.5 KB | Display | ![]() |
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PDB format | ![]() | 17.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 342.7 KB | Display | ![]() |
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Full document | ![]() | 347.7 KB | Display | |
Data in XML | ![]() | 3 KB | Display | |
Data in CIF | ![]() | 3.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1hgvC ![]() 1hh0C ![]() 1ifnS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 |
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3 | ![]()
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Unit cell |
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Symmetry | Helical symmetry: (Circular symmetry: 1 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 35 / Rise per n subunits: 2.9 Å / Rotation per n subunits: 66.667 °) |
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Components
#1: Protein/peptide | Mass: 4816.578 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: MAJOR COAT PROTEIN ASSEMBLY / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Description: THE DATA IS DERIVED FROM CONTINUOUS TRANSFORM DATA AND THEREFORE THE NUMBER OF UNIQUE REFLECTIONS IS A MEANINGLESS NUMBER. THE STRUCTURE WAS REFINED AGAI THE SAME STRUCTURE FACTORS AS ...Description: THE DATA IS DERIVED FROM CONTINUOUS TRANSFORM DATA AND THEREFORE THE NUMBER OF UNIQUE REFLECTIONS IS A MEANINGLESS NUMBER. THE STRUCTURE WAS REFINED AGAI THE SAME STRUCTURE FACTORS AS PDB ENTRY 1HGV, USING DIFFERENT REFINEMENT PROTOCOL. THEREFORE, THE STRUCT FACTORS FOR 1HGZ, CAN BE TAKEN FROM R1HGVSF |
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Crystal grow | pH: 7.5 / Details: pH 7.50 |
Crystal grow | *PLUS Method: unknown |
-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 15, 1999 / Details: MIRRORS |
Radiation | Monochromator: GE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / % possible obs: 100 % |
Reflection | *PLUS % possible obs: 100 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1IFN Resolution: 2.4→50 Å / σ(F): 0 Details: THE MODEL WAS DERIVED FROM PDB ENTRY 1IFN, REFERENCE 1, BY MOLECULAR REPLACEMENT
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Refinement step | Cycle: LAST / Resolution: 2.4→50 Å
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Refine LS restraints |
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Software | *PLUS Name: FXPLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.22 / Rfactor Rfree: 0.4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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