+Open data
-Basic information
Entry | Database: PDB / ID: 1jon | ||||||
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Title | GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345 | ||||||
Components | GROEL, HSP60 CLASS | ||||||
Keywords | CHAPERONE / CELL DIVISION / ATP-BINDING / PHOSPHORYLATION | ||||||
Function / homology | Function and homology information GroEL-GroES complex / chaperonin ATPase / virion assembly / chaperone cofactor-dependent protein refolding / isomerase activity / ATP-dependent protein folding chaperone / response to radiation / unfolded protein binding / protein folding / protein refolding ...GroEL-GroES complex / chaperonin ATPase / virion assembly / chaperone cofactor-dependent protein refolding / isomerase activity / ATP-dependent protein folding chaperone / response to radiation / unfolded protein binding / protein folding / protein refolding / response to heat / magnesium ion binding / ATP hydrolysis activity / ATP binding / identical protein binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Buckle, A.M. / Fersht, A.R. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1996 Title: Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. Authors: Zahn, R. / Buckle, A.M. / Perrett, S. / Johnson, C.M. / Corrales, F.J. / Golbik, R. / Fersht, A.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jon.cif.gz | 37.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jon.ent.gz | 25.6 KB | Display | PDB format |
PDBx/mmJSON format | 1jon.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jon_validation.pdf.gz | 422.9 KB | Display | wwPDB validaton report |
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Full document | 1jon_full_validation.pdf.gz | 424.5 KB | Display | |
Data in XML | 1jon_validation.xml.gz | 7.2 KB | Display | |
Data in CIF | 1jon_validation.cif.gz | 8.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jo/1jon ftp://data.pdbj.org/pub/pdb/validation_reports/jo/1jon | HTTPS FTP |
-Related structure data
Related structure data | 1oelS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 16642.238 Da / Num. of mol.: 1 Fragment: POLYPEPTIDE BINDING (APICAL) DOMAIN, RESIDUES 191 - 345 Mutation: A262L, I267M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: DH5 / Organ: TAIL / Plasmid: PRSET (INVITROGEN) Gene (production host): GROEL FRAGMENT COMPRISING RESIDUES 191 - 345 Production host: Escherichia coli (E. coli) / References: UniProt: P0A6F5 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 51 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / pH: 8.5 Details: 11% PEG 4000, 50 MM TRIS-HCL, PH 8.5, 200 MM LISO4, 23 MG/ML PROTEIN, 17 DEG. C., temperature 290K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.87 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 9, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→22 Å / Num. obs: 6564 / % possible obs: 99.4 % / Observed criterion σ(I): 3 / Redundancy: 3.3 % / Rmerge(I) obs: 0.099 / Net I/σ(I): 9.9 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 3 % / Rmerge(I) obs: 0.451 / Mean I/σ(I) obs: 1.8 / % possible all: 96.7 |
Reflection | *PLUS Num. measured all: 21762 |
Reflection shell | *PLUS % possible obs: 96.7 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1OEL Resolution: 2.5→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 42 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.214 / Rfactor Rfree: 0.291 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |