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Yorodumi- PDB-1hz9: BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hz9 | ||||||
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Title | BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY | ||||||
Components | COLD SHOCK PROTEIN CSPB | ||||||
Keywords | TRANSCRIPTION / BETA BARREL / HOMODIMER | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Bacillus caldolyticus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 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 | 1hz9.cif.gz | 40.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hz9.ent.gz | 28.2 KB | Display | PDB format |
PDBx/mmJSON format | 1hz9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hz9_validation.pdf.gz | 434.5 KB | Display | wwPDB validaton report |
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Full document | 1hz9_full_validation.pdf.gz | 436.3 KB | Display | |
Data in XML | 1hz9_validation.xml.gz | 9 KB | Display | |
Data in CIF | 1hz9_validation.cif.gz | 11.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hz/1hz9 ftp://data.pdbj.org/pub/pdb/validation_reports/hz/1hz9 | HTTPS FTP |
-Related structure data
Related structure data | 1hzaC 1hzbC 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: 7283.151 Da / Num. of mol.: 2 / Mutation: E46A 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: 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: 2.41 Å3/Da / Density % sol: 48.9 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: MPD, Na-Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 1, 1999 / Details: mirros |
Radiation | Monochromator: Goebel-Mirror System / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→28 Å / Num. all: 12265 / Num. obs: 12265 / % possible obs: 94.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3 % / Biso Wilson estimate: 23.7 Å2 / Rmerge(I) obs: 0.035 / Net I/σ(I): 17.9 |
Reflection shell | Resolution: 1.8→1.83 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.287 / Mean I/σ(I) obs: 1.1 / Num. unique all: 462 / % possible all: 74.4 |
Reflection | *PLUS Lowest resolution: 28 Å / Redundancy: 3.1 % |
Reflection shell | *PLUS % possible obs: 68.3 % / Rmerge(I) obs: 0.297 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1C9O Resolution: 1.8→28 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 28.9 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→28 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 28 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor all: 0.2 / Rfactor obs: 0.185 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 28.9 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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