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Yorodumi- PDB-1ecr: ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED W... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ecr | ||||||
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Title | ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA | ||||||
Components |
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Keywords | REPLICATION/DNA / DNA-BINDING / DNA REPLICATION / COMPLEX (DNA-BINDING PROTEIN-DNA) / REPLICATION-DNA COMPLEX | ||||||
Function / homology | Function and homology information replication fork arrest involved in DNA replication termination / DNA replication termination / sequence-specific DNA binding / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR, ANOMALOUS SCATTERING / Resolution: 2.7 Å | ||||||
Authors | Kamada, K. / Morikawa, K. | ||||||
Citation | Journal: Nature / Year: 1996 Title: Structure of a replication-terminator protein complexed with DNA. Authors: Kamada, K. / Horiuchi, T. / Ohsumi, K. / Shimamoto, N. / Morikawa, K. #1: Journal: Proteins / Year: 1996 Title: Crystallization and Preliminary X-Ray Analysis of the Escherichia Coli Replication Terminator Protein Complexed with DNA Authors: Kamada, K. / Ohsumi, K. / Horiuchi, T. / Shimamoto, N. / Morikawa, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ecr.cif.gz | 93.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ecr.ent.gz | 68.9 KB | Display | PDB format |
PDBx/mmJSON format | 1ecr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ecr_validation.pdf.gz | 379.5 KB | Display | wwPDB validaton report |
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Full document | 1ecr_full_validation.pdf.gz | 395.3 KB | Display | |
Data in XML | 1ecr_validation.xml.gz | 9.9 KB | Display | |
Data in CIF | 1ecr_validation.cif.gz | 14.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ec/1ecr ftp://data.pdbj.org/pub/pdb/validation_reports/ec/1ecr | HTTPS FTP |
-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
#1: DNA chain | Mass: 4856.191 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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#2: DNA chain | Mass: 4927.225 Da / Num. of mol.: 1 / Source method: obtained synthetically |
#3: Protein | Mass: 35843.188 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: B / Plasmid: PHO100 / Gene (production host): TUS / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: P16525 |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: microdialysis / pH: 5.3 / Details: pH 5.30, MICRODIALYSIS, temperature 293.00K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.3 Details: Kamada, K., (1996) Proteins: Struct.,Funct., Genet., 24, 402. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 288 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Dec 13, 1994 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 14018 / % possible obs: 90.4 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 3.3 % / Rsym value: 0.06 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 2.6 % / Rsym value: 0.217 / % possible all: 75.1 |
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 50 Å / % possible obs: 90.4 % / Rmerge(I) obs: 0.06 |
-Processing
Software |
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Refinement | Method to determine structure: MIR, ANOMALOUS SCATTERING / Resolution: 2.7→10 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.7→10 Å
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Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 10 Å / σ(F): 0 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |