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Yorodumi- PDB-1hzb: BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hzb | ||||||
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Title | BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY | ||||||
Components | COLD SHOCK PROTEIN CSPBCold shock response | ||||||
Keywords | TRANSCRIPTION / BETA BARREL / HOMODIMER | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Bacillus caldolyticus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.28 Å | ||||||
Authors | Delbrueck, H. / Mueller, U. / Perl, D. / Schmid, F.X. / Heinemann, U. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability. Authors: Delbruck, H. / Mueller, U. / Perl, D. / Schmid, F.X. / Heinemann, U. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hzb.cif.gz | 77.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hzb.ent.gz | 58.7 KB | Display | PDB format |
PDBx/mmJSON format | 1hzb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hz/1hzb ftp://data.pdbj.org/pub/pdb/validation_reports/hz/1hzb | HTTPS FTP |
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-Related structure data
Related structure data | 1hz9C 1hzaC 1hzcC 1i5fC 1c9oS 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: 7357.143 Da / Num. of mol.: 2 / Mutation: L66E Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus caldolyticus (bacteria) / Gene: CSPB / Production host: Escherichia coli (E. coli) / References: UniProt: P41016 #2: Chemical | ChemComp-NA / | #3: 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: 2.64 Å3/Da / Density % sol: 53.4 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: MPD, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7 | |||||||||||||||||||||||||
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: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.8428 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 31, 2000 / Details: crystal |
Radiation | Monochromator: crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8428 Å / Relative weight: 1 |
Reflection | Resolution: 1.27→20 Å / Num. all: 40862 / Num. obs: 40862 / % possible obs: 97.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Biso Wilson estimate: 15.7 Å2 / Rmerge(I) obs: 0.024 / Net I/σ(I): 41.4 |
Reflection shell | Resolution: 1.27→1.28 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.183 / Mean I/σ(I) obs: 1 / Num. unique all: 976 / % possible all: 94.7 |
Reflection | *PLUS Lowest resolution: 20 Å |
Reflection shell | *PLUS % possible obs: 94.7 % / Rmerge(I) obs: 0.185 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1C9O molecule A Resolution: 1.28→8 Å / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber / Details: Shelxl-97 (Sheldrick) was also used for refinement
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Refinement step | Cycle: LAST / Resolution: 1.28→8 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor obs: 0.158 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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