+Open data
-Basic information
Entry | Database: PDB / ID: 1ned | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION | ||||||
Components | HSLVHslVU | ||||||
Keywords | HYDROLASE / HSLV / CLPQ / HSLVU / CLPQY / ATP-DEPENDENT PROTEASE / PROTEASOME | ||||||
Function / homology | Function and homology information HslU-HslV peptidase / protein denaturation / HslUV protease complex / proteasome core complex / threonine-type endopeptidase activity / proteolysis involved in protein catabolic process / cellular response to heat / response to heat / protein domain specific binding / magnesium ion binding ...HslU-HslV peptidase / protein denaturation / HslUV protease complex / proteasome core complex / threonine-type endopeptidase activity / proteolysis involved in protein catabolic process / cellular response to heat / response to heat / protein domain specific binding / magnesium ion binding / proteolysis / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 3.8 Å | ||||||
Authors | Bochtler, M. / Ditzel, L. / Groll, M. / Huber, R. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1997 Title: Crystal structure of heat shock locus V (HslV) from Escherichia coli. Authors: Bochtler, M. / Ditzel, L. / Groll, M. / Huber, R. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1ned.cif.gz | 129.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1ned.ent.gz | 102.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ned.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ne/1ned ftp://data.pdbj.org/pub/pdb/validation_reports/ne/1ned | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 20091.811 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: XL-1 BLUE / Cellular location: CYTOPLASM / Production host: Escherichia coli (E. coli) / References: UniProt: P0A7B8, EC: 3.4.99.- |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 51 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 7.5 Details: 100MM HEPES/NAOH PH 7.5 200MM SODIUM ACETATE 0.02 % SODIUM AZIDE 9-14% ETHANOL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 293 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.8→15 Å / Num. obs: 6404 / % possible obs: 99.8 % / Redundancy: 5.7 % / Rsym value: 0.073 |
Reflection shell | Resolution: 3.8→3.93 Å / Redundancy: 6.2 % / Mean I/σ(I) obs: 3.8 / Rsym value: 0.205 / % possible all: 99.4 |
Reflection | *PLUS Num. measured all: 36796 / Rmerge(I) obs: 0.073 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MIR / Resolution: 3.8→15 Å / σ(F): 2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.8→15 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints NCS | Rms dev Biso : 3.5 Å2 / Rms dev position: 0.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Version: 3.842 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|