+Open data
-Basic information
Entry | Database: PDB / ID: 1baz | ||||||
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Title | ARC REPRESSOR MUTANT PHE10VAL | ||||||
Components | ARC REPRESSOR | ||||||
Keywords | TRANSCRIPTION REGULATION | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Enterobacteria phage P22 (virus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Schildbach, J.F. / Raumann, B.E. / Sauer, R.T. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1999 Title: Origins of DNA-binding specificity: role of protein contacts with the DNA backbone. Authors: Schildbach, J.F. / Karzai, A.W. / Raumann, B.E. / Sauer, R.T. #1: Journal: Nature / Year: 1994 Title: DNA Recognition by Beta-Sheets in the Arc Repressor-Operator Crystal Structure Authors: Raumann, B.E. / Rould, M.A. / Pabo, C.O. / Sauer, R.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1baz.cif.gz | 47.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1baz.ent.gz | 34.9 KB | Display | PDB format |
PDBx/mmJSON format | 1baz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ba/1baz ftp://data.pdbj.org/pub/pdb/validation_reports/ba/1baz | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 6190.229 Da / Num. of mol.: 4 / Mutation: F10V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage P22 (virus) / Genus: P22-like viruses / Gene: ARC / Plasmid: PTA200-FV10 / Gene (production host): ARC / Production host: Escherichia coli (E. coli) / Strain (production host): UA2F / References: UniProt: P03050 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.69 % Description: THE ARC MUTANT FV10 CRYSTALLIZED NEARLY ISOMORPHOUSLY WITH THE WILD TYPE WHEN CRYSTALLIZING USING MACROSEEDING. THEREFORE, THE WILD TYPE ARC STRUCTURE WAS USED AS THE INITIAL MODEL FOR THE MUTANT. | |||||||||||||||
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Crystal grow | pH: 8 Details: PROTEIN WAS CRYSTALLIZED FROM 40-45% SATURATED AMMONIUM PHOSPHATE, PH 8.0, BY MACROSEEDING USING CRYSTALS OF THE WILD TYPE PROTEIN | |||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Oct 1, 1993 / Details: COLLIMATOR |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.9 Å / Num. obs: 16796 / % possible obs: 90 % / Observed criterion σ(I): 0 / Redundancy: 2.6 % / Rmerge(I) obs: 0.087 |
Reflection shell | Resolution: 1.9→1.97 Å / % possible all: 50.7 |
Reflection | *PLUS % possible obs: 89.9 % |
Reflection shell | *PLUS % possible obs: 50.7 % |
-Processing
Software |
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Refinement | Resolution: 1.9→6 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: SCALE UNCONVENTIONAL ORTHORHOMBIC CELL, WITH A AND C SWAPPED.
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Displacement parameters | Biso mean: 31.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.97 Å / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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