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Yorodumi- PDB-3a0j: Crystal structure of cold shock protein 1 from Thermus thermophil... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3a0j | ||||||
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Title | Crystal structure of cold shock protein 1 from Thermus thermophilus HB8 | ||||||
Components | Cold shock protein | ||||||
Keywords | TRANSCRIPTION / OB-fold / Cytoplasm / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | ||||||
Authors | Miyazaki, T. / Nakagawa, N. / Kuramitsu, S. / Masui, R. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: The Biological Action of Cold Shock Protein 1 from Thermus thermophilus HB8 Authors: Miyazaki, T. / Mega, R. / Kim, K. / Shikai, A. / Masui, R. / Kuramitsu, S. / Nakagawa, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3a0j.cif.gz | 45 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3a0j.ent.gz | 31.3 KB | Display | PDB format |
PDBx/mmJSON format | 3a0j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3a0j_validation.pdf.gz | 437 KB | Display | wwPDB validaton report |
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Full document | 3a0j_full_validation.pdf.gz | 441.9 KB | Display | |
Data in XML | 3a0j_validation.xml.gz | 10.7 KB | Display | |
Data in CIF | 3a0j_validation.cif.gz | 15 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a0/3a0j ftp://data.pdbj.org/pub/pdb/validation_reports/a0/3a0j | HTTPS FTP |
-Related structure data
Related structure data | 1hzaS S: Starting model for refinement |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 8197.178 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus thermophilus (bacteria) / Strain: HB8 / Gene: TTHA0175 / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q5SLW8 #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: 1.777856 Å3/Da / Density % sol: 30.815542 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.2 Details: 32% PEG 1500, 0.1M Tris HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44B2 / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 23, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→50 Å / Num. all: 12948 / Num. obs: 12948 / % possible obs: 95.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.9 % / Biso Wilson estimate: 14.7 Å2 / Rmerge(I) obs: 0.031 / Net I/σ(I): 46.9 |
Reflection shell | Resolution: 1.65→1.71 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.095 / Mean I/σ(I) obs: 13.9 / Num. unique all: 1166 / % possible all: 87.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1HZA Resolution: 1.65→21.56 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 306025.72 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): -3 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 54.0224 Å2 / ksol: 0.410312 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.65→21.56 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.65→1.75 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Xplor file |
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