+Open data
-Basic information
Entry | Database: PDB / ID: 1tuh | ||||||
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Title | Structure of Bal32a from a Soil-Derived Mobile Gene Cassette | ||||||
Components | hypothetical protein EGC068 | ||||||
Keywords | UNKNOWN FUNCTION / uncultured | ||||||
Function / homology | SnoaL-like domain / SnoaL-like domain / Nuclear Transport Factor 2; Chain: A, - #50 / NTF2-like domain superfamily / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta / ACETATE ION / SnoaL-like domain-containing protein Function and homology information | ||||||
Biological species | uncultured bacterium (environmental samples) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 1.85 Å | ||||||
Authors | Robinson, A. / Wu, P.S.-C. / Harrop, S.J. / Schaeffer, P.M. / Dixon, N.E. / Gillings, M.R. / Holmes, A.J. / Nevalainen, K.M.H. / Otting, G. / Stokes, H.W. ...Robinson, A. / Wu, P.S.-C. / Harrop, S.J. / Schaeffer, P.M. / Dixon, N.E. / Gillings, M.R. / Holmes, A.J. / Nevalainen, K.M.H. / Otting, G. / Stokes, H.W. / Curmi, P.M.G. / Mabbutt, B.C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 Title: Integron-associated Mobile Gene Cassettes Code for Folded Proteins: The Structure of Bal32a, a New Member of the Adaptable alpha+beta Barrel Family Authors: Robinson, A. / Wu, P.S.-C. / Harrop, S.J. / Schaeffer, P.M. / Dosztanyi, Z. / Gillings, M.R. / Holmes, A.J. / Nevalainen, K.M.H. / Stokes, H.W. / Otting, G. / Dixon, N.E. / Curmi, P.M.G. / Mabbutt, B.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tuh.cif.gz | 41.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tuh.ent.gz | 28.6 KB | Display | PDB format |
PDBx/mmJSON format | 1tuh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tuh_validation.pdf.gz | 439.4 KB | Display | wwPDB validaton report |
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Full document | 1tuh_full_validation.pdf.gz | 440.3 KB | Display | |
Data in XML | 1tuh_validation.xml.gz | 8.2 KB | Display | |
Data in CIF | 1tuh_validation.cif.gz | 10.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tu/1tuh ftp://data.pdbj.org/pub/pdb/validation_reports/tu/1tuh | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The second part of the biological assembly is generated by the two fold axis: y, x, 1-z. |
-Components
#1: Protein | Mass: 17767.822 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) uncultured bacterium (environmental samples) Gene: EGC068 / Plasmid: pETMCIII / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: Q99IU3 |
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#2: Chemical | ChemComp-ACT / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: ammonium sulfate, sodium acetate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: ENRAF-NONIUS / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 25, 2003 / Details: mirrors |
Radiation | Monochromator: RIGAKU MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→22.5 Å / Num. all: 14962 / Num. obs: 14962 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.85→1.898 Å / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 1.85→22.47 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.953 / SU B: 2.605 / SU ML: 0.08 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.121 / ESU R Free: 0.113 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.676 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→22.47 Å
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Refine LS restraints |
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LS refinement shell | Highest resolution: 1.85 Å / Num. reflection Rwork: 1034 / Total num. of bins used: 20 |