+Open data
-Basic information
Entry | Database: PDB / ID: 1qu9 | ||||||
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Title | 1.2 A CRYSTAL STRUCTURE OF YJGF GENE PRODUCT FROM E. COLI | ||||||
Components | YJGF PROTEIN | ||||||
Keywords | STRUCTURAL GENOMICS | ||||||
Function / homology | Function and homology information 2-iminobutanoate/2-iminopropanoate deaminase / 2-iminobutanoate/2-iminopropanoate deaminase / : / deaminase activity / isoleucine biosynthetic process / protein homotrimerization / response to toxic substance / unfolded protein binding / identical protein binding / membrane ...2-iminobutanoate/2-iminopropanoate deaminase / 2-iminobutanoate/2-iminopropanoate deaminase / : / deaminase activity / isoleucine biosynthetic process / protein homotrimerization / response to toxic substance / unfolded protein binding / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.2 Å | ||||||
Authors | Volz, K. | ||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: A test case for structure-based functional assignment: the 1.2 A crystal structure of the yjgF gene product from Escherichia coli Authors: Volz, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qu9.cif.gz | 83.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qu9.ent.gz | 67.9 KB | Display | PDB format |
PDBx/mmJSON format | 1qu9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qu9_validation.pdf.gz | 415 KB | Display | wwPDB validaton report |
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Full document | 1qu9_full_validation.pdf.gz | 417.5 KB | Display | |
Data in XML | 1qu9_validation.xml.gz | 20.7 KB | Display | |
Data in CIF | 1qu9_validation.cif.gz | 27.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qu/1qu9 ftp://data.pdbj.org/pub/pdb/validation_reports/qu/1qu9 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 13705.514 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P39330, UniProt: P0AF93*PLUS #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: 2.29 Å3/Da / Density % sol: 46.27 % | |||||||||||||||
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Crystal grow | Temperature: 277 K / Method: microdialysis / pH: 8.1 Details: 50 mM tris HCL, 2.35 M ammonium sulphate, pH 8.1, microdialysis, temperature 4K | |||||||||||||||
Crystal grow | *PLUS Method: unknown / PH range low: 8.5 / PH range high: 7.9 | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 75 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 0.961 |
Detector | Type: BRUKER / Detector: CCD / Date: May 31, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.961 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→30 Å / Num. all: 118474 / Num. obs: 112350 / % possible obs: 94.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 |
Reflection shell | Resolution: 1.2→1.27 Å / Num. unique all: 18335 / % possible all: 90.6 |
Reflection shell | *PLUS % possible obs: 90.6 % |
-Processing
Software |
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Refinement | Resolution: 1.2→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 9.61 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 1.2 Å / Lowest resolution: 1.27 Å / Rfactor Rwork: 0.141 / Num. reflection obs: 18335 |