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Yorodumi- PDB-2wpw: Tandem GNAT protein from the clavulanic acid biosynthesis pathway... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 2wpw | ||||||
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| Title | Tandem GNAT protein from the clavulanic acid biosynthesis pathway (without AcCoA) | ||||||
Components | ORF14 | ||||||
Keywords | TRANSFERASE / ACETYL TRANSFERASE / ANTIBIOTIC BIOSYNTHESIS | ||||||
| Function / homology | Function and homology informationclavulanic acid biosynthetic process / acyltransferase activity, transferring groups other than amino-acyl groups Similarity search - Function | ||||||
| Biological species | STREPTOMYCES CLAVULIGERUS (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.38 Å | ||||||
Authors | Iqbal, A. / Arunlanantham, H. / McDonough, M.A. / Chowdhury, R. / Clifton, I.J. | ||||||
Citation | Journal: Proteins / Year: 2010Title: Crystallographic and mass spectrometric analyses of a tandem GNAT protein from the clavulanic acid biosynthesis pathway. Authors: Iqbal, A. / Arunlanantham, H. / Brown, T. / Chowdhury, R. / Clifton, I.J. / Kershaw, N.J. / Hewitson, K.S. / McDonough, M.A. / Schofield, C.J. | ||||||
| History |
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| Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. 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 | 2wpw.cif.gz | 287.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2wpw.ent.gz | 236.2 KB | Display | PDB format |
| PDBx/mmJSON format | 2wpw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2wpw_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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| Full document | 2wpw_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 2wpw_validation.xml.gz | 78.4 KB | Display | |
| Data in CIF | 2wpw_validation.cif.gz | 104 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wp/2wpw ftp://data.pdbj.org/pub/pdb/validation_reports/wp/2wpw | 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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| 2 | ![]()
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| 3 | ![]()
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| 4 | ![]()
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS oper:
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Components
| #1: Protein | Mass: 36664.973 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: SELENO-METHIONINE LABELLED / Source: (gene. exp.) STREPTOMYCES CLAVULIGERUS (bacteria) / Production host: ![]() References: UniProt: Q8KRB5, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups #2: Chemical | ChemComp-ACO / #3: Water | ChemComp-HOH / | Has protein modification | Y | |
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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: 3.05 Å3/Da / Density % sol: 59.7 % / Description: NONE |
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| Crystal grow | pH: 6 Details: 3 MG/ML PROTEIN, 10% PEG8000, 0.1M CACODYLATE PH6, 0.2M SODIUM ACETATE |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX14.2 / Wavelength: 0.97976 |
| Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 9, 2003 / Details: RH COATED MIRRORS |
| Radiation | Monochromator: SI (1 1 1) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.97976 Å / Relative weight: 1 |
| Reflection | Resolution: 2.38→32.4 Å / Num. obs: 68408 / % possible obs: 92.2 % / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 44.8 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 6.5 |
| Reflection shell | Resolution: 2.38→2.51 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 3 / % possible all: 71.9 |
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Processing
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| Refinement | Method to determine structure: MADStarting model: NONE Resolution: 2.38→32.4 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.915 / SU B: 18.005 / SU ML: 0.196 / Cross valid method: THROUGHOUT / ESU R: 0.429 / ESU R Free: 0.282 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 29.885 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.38→32.4 Å
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About Yorodumi



STREPTOMYCES CLAVULIGERUS (bacteria)
X-RAY DIFFRACTION
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