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Yorodumi- PDB-1elw: Crystal structure of the TPR1 domain of HOP in complex with a HSC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1elw | ||||||
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Title | Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide | ||||||
Components |
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Keywords | CHAPERONE / Hop / Tpr-Domain / Peptide-Complex / Helical Repeat / Hsc70 / Hsp70 / Protein Binding | ||||||
Function / homology | Function and homology information dynein axonemal particle / protein folding chaperone complex / cellular response to interleukin-7 / RND1 GTPase cycle / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Hsp90 protein binding / Golgi apparatus / protein-containing complex / RNA binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.6 Å | ||||||
Authors | Scheufler, C. / Brinker, A. / Hartl, F.U. / Moarefi, I. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2000 Title: Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Authors: Scheufler, C. / Brinker, A. / Bourenkov, G. / Pegoraro, S. / Moroder, L. / Bartunik, H. / Hartl, F.U. / Moarefi, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1elw.cif.gz | 67.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1elw.ent.gz | 50.6 KB | Display | PDB format |
PDBx/mmJSON format | 1elw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/el/1elw ftp://data.pdbj.org/pub/pdb/validation_reports/el/1elw | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 13446.996 Da / Num. of mol.: 2 / Fragment: N-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PPRO EX HTA / Production host: Escherichia coli (E. coli) / References: UniProt: P31948 #2: Protein/peptide | Mass: 858.890 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: This sequence occurs naturally in humans #3: Chemical | ChemComp-NI / #4: Chemical | ChemComp-TRS / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 42.38 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG MME 2000, TRIS, Nickel Chloride, Xylitol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 45 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.5 / Details: used to microseeding | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12B / Wavelength: 0.949 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Oct 2, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.949 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→20 Å / % possible obs: 95.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 21.8 Å2 / Rmerge(I) obs: 0.041 / Net I/σ(I): 32.5 |
Reflection shell | Resolution: 1.6→1.66 Å / Rmerge(I) obs: 0.305 / Num. unique all: 0 / % possible all: 75.2 |
Reflection shell | *PLUS % possible obs: 75.2 % / Mean I/σ(I) obs: 3.3 |
-Processing
Software |
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Refinement | Resolution: 1.6→18.87 Å / Rfactor Rfree error: 0.004 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 46.36 Å2 / ksol: 0.423 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.6→18.87 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.6→1.7 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 10.1 % / Rfactor obs: 0.18 / Rfactor Rwork: 0.18 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 22.2 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.264 / % reflection Rfree: 10 % / Rfactor Rwork: 0.244 |