+Open data
-Basic information
Entry | Database: PDB / ID: 1mbv | ||||||
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Title | CRYSTAL STRUCTURE ANALYSIS OF ClpSN HETERODIMER TETRAGONAL FORM | ||||||
Components |
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Keywords | PROTEIN BINDING / Adaptors / Hsp100/Clp chaperone / AAA+ family ATP-dependent protease | ||||||
Function / homology | Function and homology information endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / molecular function inhibitor activity / protein unfolding / protein catabolic process / cellular response to heat / response to heat / protein-folding chaperone binding / response to oxidative stress ...endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / molecular function inhibitor activity / protein unfolding / protein catabolic process / cellular response to heat / response to heat / protein-folding chaperone binding / response to oxidative stress / ATP hydrolysis activity / proteolysis / ATP binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å | ||||||
Authors | Guo, F. / Esser, L. / Singh, S.K. / Maurizi, M.R. / Xia, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: Crystal Structure of the Heterodimeric Complex of the Adaptor, ClpS, with the N-domain of AAA+ Chaperone ClpA Authors: Guo, F. / Esser, L. / Singh, S.K. / Maurizi, M.R. / Xia, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mbv.cif.gz | 55.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mbv.ent.gz | 41.3 KB | Display | PDB format |
PDBx/mmJSON format | 1mbv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mb/1mbv ftp://data.pdbj.org/pub/pdb/validation_reports/mb/1mbv | HTTPS FTP |
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-Related structure data
Related structure data | 1mbuSC 1mbxC S: Starting model for refinement C: citing same article (ref.) |
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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: 16043.073 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: pBAD-yljA / Production host: Escherichia coli (E. coli) / Strain (production host): DH5alpha / References: UniProt: P0ABH9 |
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#2: Protein | Mass: 12193.038 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: pFG42 / Production host: Escherichia coli (E. coli) / Strain (production host): SG22176 / References: UniProt: P0A8Q6 |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
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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: X9B / Wavelength: 1.072 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 10, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.072 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→28 Å / Num. all: 13160 / Num. obs: 13160 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 14.4 % / Biso Wilson estimate: 96.4 Å2 / Rsym value: 0.061 / Net I/σ(I): 30.8 |
Reflection shell | Resolution: 3.3→3.42 Å / Redundancy: 14 % / Mean I/σ(I) obs: 4.7 / Num. unique all: 1273 / Rsym value: 0.594 / % possible all: 100 |
Reflection | *PLUS Highest resolution: 3.3 Å / Lowest resolution: 28 Å / Rmerge(I) obs: 0.061 |
Reflection shell | *PLUS % possible obs: 100 % / Rmerge(I) obs: 0.594 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1MBU Resolution: 3.3→14.98 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 615032.18 / Data cutoff high rms absF: 615032.18 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 10 Å2 / ksol: 0.216313 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 84.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.3→14.98 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.3→3.5 Å / Rfactor Rfree error: 0.035 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 3.3 Å / Lowest resolution: 12 Å / Rfactor Rfree: 0.28 / Rfactor Rwork: 0.258 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.442 / Rfactor Rwork: 0.571 |