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Yorodumi- PDB-1csq: CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTE... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1csq | ||||||
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| Title | CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN | ||||||
Components | COLD SHOCK PROTEIN B(CSPB) | ||||||
Keywords | TRANSCRIPTION REGULATION | ||||||
| Function / homology | Function and homology informationnucleoid / regulation of gene expression / nucleic acid binding / DNA binding / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 2.7 Å | ||||||
Authors | Schindelin, H. / Heinemann, U. | ||||||
Citation | Journal: Nature / Year: 1993Title: Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Authors: Schindelin, H. / Marahiel, M.A. / Heinemann, U. #1: Journal: Proteins / Year: 1992Title: Overproduction, Crystallization, and Preliminary X-Ray Diffraction Studies of the Major Cold Shock Protein from Bacillus Subtilis, Cspb Authors: Schindelin, H. / Herrler, M. / Willimsky, G. / Marahiel, M.A. / Heinemann, U. | ||||||
| History |
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| Remark 700 | SHEET STRANDS 1 TO 4 OF THE BETA-SHEET HAVE GREEK-KEY TOPOLOGY. THE SHEET FORMS A FIVE-STRANDED ...SHEET STRANDS 1 TO 4 OF THE BETA-SHEET HAVE GREEK-KEY TOPOLOGY. THE SHEET FORMS A FIVE-STRANDED BETA-BARREL WITH BULGES IN STRANDS 3 AND 5. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1csq.cif.gz | 22.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1csq.ent.gz | 14.5 KB | Display | PDB format |
| PDBx/mmJSON format | 1csq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1csq_validation.pdf.gz | 408.2 KB | Display | wwPDB validaton report |
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| Full document | 1csq_full_validation.pdf.gz | 409.6 KB | Display | |
| Data in XML | 1csq_validation.xml.gz | 4.9 KB | Display | |
| Data in CIF | 1csq_validation.cif.gz | 5.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cs/1csq ftp://data.pdbj.org/pub/pdb/validation_reports/cs/1csq | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 7372.126 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 3.07 Å3/Da / Density % sol: 59.93 % |
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-Data collection
| Radiation | Scattering type: x-ray |
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| Radiation wavelength | Relative weight: 1 |
| Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 12 Å / Num. obs: 2252 / % possible obs: 94 % / Rmerge(I) obs: 0.039 |
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Processing
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| Refinement | Resolution: 2.7→10 Å / σ(F): 1 /
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| Refinement step | Cycle: LAST / Resolution: 2.7→10 Å
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| Refine LS restraints |
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| Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS |
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