+Open data
-Basic information
Entry | Database: PDB / ID: 1ety | ||||||
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Title | THE CRYSTAL STRUCTURE OF E. COLI WILD-TYPE FIS | ||||||
Components | FACTOR FOR INVERSION STIMULATION | ||||||
Keywords | TRANSCRIPTION ACTIVATOR / DNA-BINDING PROTEIN | ||||||
Function / homology | Function and homology information invertasome / positive regulation of DNA recombination / sequence-specific DNA binding, bending / provirus excision / nucleoid / DNA-binding transcription repressor activity / DNA-binding transcription activator activity / chromosome organization / core promoter sequence-specific DNA binding / protein-DNA complex ...invertasome / positive regulation of DNA recombination / sequence-specific DNA binding, bending / provirus excision / nucleoid / DNA-binding transcription repressor activity / DNA-binding transcription activator activity / chromosome organization / core promoter sequence-specific DNA binding / protein-DNA complex / response to radiation / nucleosome / sequence-specific DNA binding / transcription cis-regulatory region binding / DNA-templated transcription / regulation of DNA-templated transcription / protein homodimerization activity / DNA binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Cheng, Y.S. / Yang, W.Z. / Johnson, R.C. / Yuan, H.S. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Structural analysis of the transcriptional activation on Fis: crystal structures of six Fis mutants with different activation properties. Authors: Cheng, Y.S. / Yang, W.Z. / Johnson, R.C. / Yuan, H.S. | ||||||
History |
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Remark 300 | THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAINS THAT GIVE ONE ... THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAINS THAT GIVE ONE BIOLOGICAL DIMER MOLECULE. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ety.cif.gz | 43.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ety.ent.gz | 31.5 KB | Display | PDB format |
PDBx/mmJSON format | 1ety.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/et/1ety ftp://data.pdbj.org/pub/pdb/validation_reports/et/1ety | HTTPS FTP |
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-Related structure data
Related structure data | 1etkC 1etoC 1etqC 1etvC 1etwC 1etxC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a dimer constructed from chain A and a symmetry partner (chain B) generated by the non-crystallographic two-fold |
-Components
#1: Protein | Mass: 11252.918 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET11A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (-FIS) / References: UniProt: P0A6R3 #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: 2.07 Å3/Da / Density % sol: 40.49 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 10 mg/ml protein, 0.5 M sodium chloride, 0.1 M sodium acetate, 0.05 M sodium cacodylate(pH 6.5), 15% PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Sep 2, 1999 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→40 Å / Num. all: 70772 / Num. obs: 13174 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.37 % / Biso Wilson estimate: 17.7 Å2 / Rsym value: 0.062 / Net I/σ(I): 25.1 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 6.39 % / Num. unique all: 1279 / Rsym value: 0.254 / % possible all: 99.6 |
Reflection | *PLUS Num. measured all: 70772 / Rmerge(I) obs: 0.062 |
Reflection shell | *PLUS % possible obs: 99.6 % / Rmerge(I) obs: 0.254 / Mean I/σ(I) obs: 6.4 |
-Processing
Software |
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Refinement | Starting model: The wild-type FIS Resolution: 2→19.4 Å / Rfactor Rfree error: 0.008 / Data cutoff high rms absF: 450184.2 / Isotropic thermal model: restrained / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: flat model / Bsol: 50.0204 Å2 / ksol: 0.342513 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→19.4 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.13 Å / Rfactor Rfree error: 0.021 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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