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Yorodumi- PDB-1c9o: CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1c9o | ||||||
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Title | CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP | ||||||
Components | COLD-SHOCK PROTEIN | ||||||
Keywords | TRANSCRIPTION / BETA BARREL / HOMODIMER | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Bacillus caldolyticus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / AB INITIO / Resolution: 1.17 Å | ||||||
Authors | Mueller, U. / Perl, D. / Schmid, F.X. / Heinemann, U. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein. Authors: 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 | 1c9o.cif.gz | 81.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c9o.ent.gz | 62 KB | Display | PDB format |
PDBx/mmJSON format | 1c9o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c9/1c9o ftp://data.pdbj.org/pub/pdb/validation_reports/c9/1c9o | HTTPS FTP |
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-Related structure data
Related structure data | |
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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 on special symmetry positions |
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-Components
#1: Protein | Mass: 7341.187 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bacillus caldolyticus (bacteria) / References: UniProt: P41016 #2: Chemical | #3: Chemical | #4: 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 Å3/Da / Density % sol: 48.22 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: MPD, HEPES, pH 7.5. VAPOR DIFFUSION, HANGING DROP at 293 | |||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 2.05 % | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||||||||||||
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: BW7A / Wavelength: 0.9493 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 20, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9493 Å / Relative weight: 1 |
Reflection | Resolution: 1.17→15 Å / Num. all: 45174 / Num. obs: 45174 / % possible obs: 96.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Biso Wilson estimate: 11 Å2 / Rmerge(I) obs: 0.041 / Net I/σ(I): 33.4 |
Reflection shell | Resolution: 1.17→1.18 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.301 / % possible all: 38.8 |
Reflection | *PLUS Lowest resolution: 15 Å |
Reflection shell | *PLUS % possible obs: 38.8 % / Mean I/σ(I) obs: 2.1 |
-Processing
Software |
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Refinement | Method to determine structure: AB INITIO / Resolution: 1.17→15 Å / Num. parameters: 1266 / Num. restraintsaints: 1481 / Cross valid method: FREE R / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER Details: USED RESTRAINED ANISOTROPIC DISPLACEMENT-FACTOR REFINEMENT
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Refine analyze | Num. disordered residues: 1 / Occupancy sum hydrogen: 976 / Occupancy sum non hydrogen: 1321 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.17→15 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 5 % | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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