+Open data
-Basic information
Entry | Database: PDB / ID: 1vqb | |||||||||
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Title | GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN) | |||||||||
Components | GENE V PROTEIN | |||||||||
Keywords | DNA BINDING PROTEIN / DNA-BINDING PROTEIN / GENE V | |||||||||
Function / homology | Function and homology information rolling circle single-stranded viral DNA replication / single-stranded DNA binding / DNA replication Similarity search - Function | |||||||||
Biological species | Enterobacteria phage f1 (virus) | |||||||||
Method | X-RAY DIFFRACTION / MAD / Resolution: 1.8 Å | |||||||||
Authors | Skinner, M.M. / Zhang, H. / Leschnitzer, D.H. / Guan, Y. / Bellamy, H. / Sweet, R.M. / Gray, C.W. / Konings, R.N.H. / Wang, A.H.-J. / Terwilliger, T.C. | |||||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 Title: Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein. Authors: Skinner, M.M. / Zhang, H. / Leschnitzer, D.H. / Guan, Y. / Bellamy, H. / Sweet, R.M. / Gray, C.W. / Konings, R.N. / Wang, A.H. / Terwilliger, T.C. #1: Journal: To be Published Title: Context-Dependence of Mutational Effects in a Protein: The Crystal Structures of the V35I, I47V and V35I/I47V Gene V Protein Core Mutants Authors: Zhang, H. / Skinner, M.M. / Sandberg, W.S. / Wang, A.H.-J. / Terwilliger, T.C. #2: Journal: Acta Crystallogr.,Sect.D / Year: 1995 Title: Difference Refinement: Obtaining Differences between Two Related Structures Authors: Terwilliger, T.C. / Berendzen, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1vqb.cif.gz | 32 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1vqb.ent.gz | 21.3 KB | Display | PDB format |
PDBx/mmJSON format | 1vqb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vq/1vqb ftp://data.pdbj.org/pub/pdb/validation_reports/vq/1vqb | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 9699.214 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage f1 (virus) / Genus: Inovirus / Species: Enterobacteria phage M13 / Production host: Escherichia coli (E. coli) / References: UniProt: P69543 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 45 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.6 / Method: vapor diffusion | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 8113 / % possible obs: 98.8 % / Redundancy: 6 % / Rmerge(I) obs: 0.061 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.8→5 Å / σ(F): 2 Details: SIDE CHAIN DISORDERED DENSITY FOR GLN 12 IS MODELED STEREOCHEMICALLY.
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Displacement parameters | Biso mean: 20 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.18 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→5 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |