+Open data
-Basic information
Entry | Database: PDB / ID: 1eqq | ||||||
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Title | SINGLE STRANDED DNA BINDING PROTEIN AND SSDNA COMPLEX | ||||||
Components |
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Keywords | REPLICATION/RNA / BETA BARREL / PROTEIN-DNA COMPLEX / REPLICATION-RNA COMPLEX | ||||||
Function / homology | Function and homology information single-stranded DNA-binding protein complex / nucleoid / recombinational repair / replisome / positive regulation of catalytic activity / SOS response / mismatch repair / enzyme activator activity / DNA-templated DNA replication / single-stranded DNA binding ...single-stranded DNA-binding protein complex / nucleoid / recombinational repair / replisome / positive regulation of catalytic activity / SOS response / mismatch repair / enzyme activator activity / DNA-templated DNA replication / single-stranded DNA binding / DNA recombination / DNA replication / DNA repair / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.2 Å | ||||||
Authors | Matsumoto, T. / Morimoto, Y. / Shibata, N. / Yasuoka, N. / Shimamoto, N. | ||||||
Citation | Journal: J.Biochem.(Tokyo) / Year: 2000 Title: Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by X-Ray structure analysis Authors: Matsumoto, T. / Morimoto, Y. / Shibata, N. / Kinebuchi, T. / Shimamoto, N. / Tsukihara, T. / Yasuoka, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eqq.cif.gz | 106.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eqq.ent.gz | 81.1 KB | Display | PDB format |
PDBx/mmJSON format | 1eqq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eq/1eqq ftp://data.pdbj.org/pub/pdb/validation_reports/eq/1eqq | 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: RNA chain | Mass: 915.621 Da / Num. of mol.: 2 / Source method: obtained synthetically #2: Protein | Mass: 18991.939 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P02339, UniProt: P0AGE0*PLUS #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 10 |
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-Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 51.8 % | ||||||||||||
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 9 Details: ammonium sulfate, pH 9.0, VAPOR DIFFUSION, HANGING DROP at 288K | ||||||||||||
Components of the solutions |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Type: PHOTON FACTORY / Wavelength: 0.7 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 10, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.7 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→45 Å / Num. all: 28599 / % possible obs: 100 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 6 % / Biso Wilson estimate: 25 Å2 / Rmerge(I) obs: 0.091 / Net I/σ(I): 12 |
-Processing
Software |
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Refinement | Resolution: 3.2→15 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3.2→15 Å
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Refine LS restraints |
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