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- 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 | ||||||
![]() | COLD SHOCK PROTEIN B(CSPB) | ||||||
![]() | TRANSCRIPTION REGULATION | ||||||
Function / homology | ![]() nucleoid / regulation of gene expression / nucleic acid binding / DNA binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Schindelin, H. / Heinemann, U. | ||||||
![]() | ![]() Title: 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: ![]() Title: 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 22.5 KB | Display | ![]() |
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PDB format | ![]() | 14.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 408.2 KB | Display | ![]() |
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Full document | ![]() | 409.6 KB | Display | |
Data in XML | ![]() | 4.9 KB | Display | |
Data in CIF | ![]() | 5.8 KB | Display | |
Arichive directory | ![]() ![]() | 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: ![]() |
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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 |