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Open data
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Basic information
Entry | Database: PDB / ID: 1fxk | ||||||
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Title | CRYSTAL STRUCTURE OF ARCHAEAL PREFOLDIN (GIMC). | ||||||
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![]() | CHAPERONE / ARCHAEAL PROTEIN | ||||||
Function / homology | ![]() prefoldin complex / unfolded protein binding / protein folding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Siegert, R. / Scheufler, C. / Moarefi, I. | ||||||
![]() | ![]() Title: Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Authors: Siegert, R. / Leroux, M.R. / Scheufler, C. / Hartl, F.U. / Moarefi, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83.3 KB | Display | ![]() |
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PDB format | ![]() | 67.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.8 KB | Display | ![]() |
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Full document | ![]() | 442.6 KB | Display | |
Data in XML | ![]() | 18.6 KB | Display | |
Data in CIF | ![]() | 27.1 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 12725.708 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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#2: Protein | Mass: 12782.761 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
#3: Protein | Mass: 14377.448 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.27 Å3/Da / Density % sol: 62.33 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / Method: vapor diffusion, hanging dropDetails: temperature was shifted to 4 degrees after one week of incubation | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92801 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / % possible obs: 99.6 % / Observed criterion σ(I): 3 / Biso Wilson estimate: 25.4 Å2 / Rsym value: 4.4 / Net I/σ(I): 24.5 |
Reflection shell | Resolution: 2.3→2.38 Å / Mean I/σ(I) obs: 6.5 / Rsym value: 18.8 / % possible all: 99.6 |
Reflection | *PLUS Rmerge(I) obs: 0.044 |
Reflection shell | *PLUS % possible obs: 99.6 % / Rmerge(I) obs: 0.188 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 39.77 Å2 / ksol: 0.32 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→19.84 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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