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- PDB-1ecr: ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED W... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ecr | ||||||
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Title | ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA | ||||||
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![]() | REPLICATION/DNA / DNA-BINDING / DNA REPLICATION / COMPLEX (DNA-BINDING PROTEIN-DNA) / REPLICATION-DNA COMPLEX | ||||||
Function / homology | ![]() replication fork arrest involved in DNA replication termination / DNA replication termination / sequence-specific DNA binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kamada, K. / Morikawa, K. | ||||||
![]() | ![]() Title: Structure of a replication-terminator protein complexed with DNA. Authors: Kamada, K. / Horiuchi, T. / Ohsumi, K. / Shimamoto, N. / Morikawa, K. #1: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 93.9 KB | Display | ![]() |
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PDB format | ![]() | 68.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 379.5 KB | Display | ![]() |
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Full document | ![]() | 395.3 KB | Display | |
Data in XML | ![]() | 9.9 KB | Display | |
Data in CIF | ![]() | 14.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() ![]() |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]()
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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 |