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- PDB-4f00: Crystal structure of the substrate binding domain of E.coli DnaK ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4f00 | ||||||
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Title | Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11) | ||||||
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![]() | CHAPERONE/IMMUNE SYSTEM / chaperone / peptide binding mode / CHAPERONE-IMMUNE SYSTEM complex | ||||||
Function / homology | ![]() stress response to copper ion / sigma factor antagonist activity / chaperone cofactor-dependent protein refolding / protein unfolding / cellular response to unfolded protein / inclusion body / protein folding chaperone / heat shock protein binding / ATP-dependent protein folding chaperone / ADP binding ...stress response to copper ion / sigma factor antagonist activity / chaperone cofactor-dependent protein refolding / protein unfolding / cellular response to unfolded protein / inclusion body / protein folding chaperone / heat shock protein binding / ATP-dependent protein folding chaperone / ADP binding / unfolded protein binding / protein-folding chaperone binding / protein refolding / response to heat / protein-containing complex assembly / DNA replication / defense response to bacterium / innate immune response / ATP hydrolysis activity / protein-containing complex / zinc ion binding / extracellular region / ATP binding / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Zahn, M. / Straeter, N. | ||||||
![]() | ![]() Title: Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK. Authors: Zahn, M. / Berthold, N. / Kieslich, B. / Knappe, D. / Hoffmann, R. / Strater, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98 KB | Display | ![]() |
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PDB format | ![]() | 76.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4eznC ![]() 4ezoC ![]() 4ezpC ![]() 4ezqC ![]() 4ezrC ![]() 4eztC ![]() 4ezwC ![]() 4ezxC ![]() 4ezyC ![]() 4ezzC ![]() 4f01C ![]() 4hy9C ![]() 4hybC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 |
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Unit cell |
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Components
#1: Protein | Mass: 23820.777 Da / Num. of mol.: 1 / Fragment: UNP residues 389-607 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1150.348 Da / Num. of mol.: 1 / Fragment: UNP residues 2-10 / Source method: obtained synthetically Details: This sequence occurs naturally in bumblebees. C-terminus is amidated. Source: (synth.) ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.58 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 4 Details: 2.4 M sodium malonate 0.1 M citric acid pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 27, 2011 |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→25 Å / Num. obs: 15317 / % possible obs: 99.9 % / Rmerge(I) obs: 0.056 |
Reflection shell | Resolution: 1.95→2.06 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.401 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: PDB ID 1DKZ / Resolution: 1.95→25 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.926 / SU B: 8.439 / SU ML: 0.126 / Cross valid method: THROUGHOUT / ESU R: 0.19 / ESU R Free: 0.17 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 30.409 Å2
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Refinement step | Cycle: LAST / Resolution: 1.95→25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.95→2 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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