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Open data
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Basic information
Entry | Database: PDB / ID: 1efu | ||||||
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Title | ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI | ||||||
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![]() | COMPLEX (TWO ELONGATION FACTORS) / ELONGATION FACTOR | ||||||
Function / homology | ![]() guanyl-nucleotide exchange factor complex / translational elongation / guanosine tetraphosphate binding / translation elongation factor activity / guanyl-nucleotide exchange factor activity / response to antibiotic / GTPase activity / GTP binding / RNA binding / zinc ion binding ...guanyl-nucleotide exchange factor complex / translational elongation / guanosine tetraphosphate binding / translation elongation factor activity / guanyl-nucleotide exchange factor activity / response to antibiotic / GTPase activity / GTP binding / RNA binding / zinc ion binding / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kawashima, T. / Berthet-Colominas, C. / Wulff, M. / Cusack, S. / Leberman, R. | ||||||
![]() | ![]() Title: The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Authors: Kawashima, T. / Berthet-Colominas, C. / Wulff, M. / Cusack, S. / Leberman, R. #1: ![]() Title: Interconversion of Crystals of the Escherichia Coli EF-TU.EF-Ts Complex between High-and Low-Diffraction Forms Authors: Kawashima, T. / Berthet-Colominas, C. / Cusack, S. / Leberman, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 281.2 KB | Display | ![]() |
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PDB format | ![]() | 223.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 453.2 KB | Display | ![]() |
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Full document | ![]() | 475.8 KB | Display | |
Data in XML | ![]() | 60.4 KB | Display | |
Data in CIF | ![]() | 88.9 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: Protein | Mass: 42230.168 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 30332.795 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: THE CPC40 WITH THE TSF GENE INSERTED WAS USED TO TRANSFORM N4830-1. THIS LEAD TO THE COPURIFICATION OF EF-TU AND EF-TS. Plasmid: CPC40 / Gene (production host): TSF / Production host: ![]() ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 43 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.7 / Details: pH 7.7 | ||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19-20 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 13, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.883 Å / Relative weight: 1 |
Reflection | Resolution: 2.48→44.28 Å / Num. obs: 51804 / % possible obs: 98.2 % / Observed criterion σ(I): 4 / Redundancy: 3.8 % / Biso Wilson estimate: 47.66 Å2 / Rsym value: 0.043 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 2.48→2.55 Å / Redundancy: 3.2 % / Mean I/σ(I) obs: 4.9 / Rsym value: 0.151 / % possible all: 80.3 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 37.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati sigma a obs: 0.01 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.61 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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