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Yorodumi- PDB-2wld: Crystallographic analysis of the polysialic acid O-acetyltransfer... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 2wld | ||||||
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| Title | Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY | ||||||
Components | POLYSIALIC ACID O-ACETYLTRANSFERASE | ||||||
Keywords | TRANSFERASE / ENZYME / ACETYLTRANSFERASE / LEFT-HANDED BETA HELIX | ||||||
| Function / homology | Function and homology informationpolysialic-acid O-acetyltransferase activity / protein homotrimerization / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups Similarity search - Function | ||||||
| Biological species | NEISSERIA MENINGITIDIS SEROGROUP Y (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Lee, H.J. / Rakic, B. / Gilbert, M. / Wakarchuk, W.W. / Withers, S.G. / Strynadka, N.C.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2009Title: Structural and Kinetic Characterizations of the Polysialic Acid O-Acetyltransferase Oatwy from Neisseria Meningitidis. Authors: Lee, H.J. / Rakic, B. / Gilbert, M. / Wakarchuk, W.W. / Withers, S.G. / Strynadka, N.C.J. | ||||||
| History |
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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 | 2wld.cif.gz | 137.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2wld.ent.gz | 110.1 KB | Display | PDB format |
| PDBx/mmJSON format | 2wld.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2wld_validation.pdf.gz | 476.1 KB | Display | wwPDB validaton report |
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| Full document | 2wld_full_validation.pdf.gz | 489 KB | Display | |
| Data in XML | 2wld_validation.xml.gz | 27.5 KB | Display | |
| Data in CIF | 2wld_validation.cif.gz | 38.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wl/2wld ftp://data.pdbj.org/pub/pdb/validation_reports/wl/2wld | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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| Components on special symmetry positions |
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| Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: TYR / Beg label comp-ID: TYR / End auth comp-ID: TYR / End label comp-ID: TYR / Refine code: 6 / Auth seq-ID: 6 - 214 / Label seq-ID: 6 - 214
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Components
| #1: Protein | Mass: 23731.191 Da / Num. of mol.: 3 / Mutation: YES Source method: isolated from a genetically manipulated source Details: LEFT-HANDED BETA HELIX Source: (gene. exp.) NEISSERIA MENINGITIDIS SEROGROUP Y (bacteria)Strain: 406Y / Plasmid: PET-28 / Production host: ![]() #2: Chemical | #3: Chemical | ChemComp-EDO / #4: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, ASN 67 TO ILE ENGINEERED RESIDUE IN CHAIN B, ASN 67 TO ILE ...ENGINEERED | |
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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: 2.7 Å3/Da / Density % sol: 54 % Description: STARTING MODEL WAS MY NAI SOAKING SIRAS STRUCTURE SOLVED BY SHELX-CDE. |
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| Crystal grow | pH: 4.6 Details: 100 MM SODIUM ACETATE, PH 4.6, 2.25 M AMMONIUM ACETATE |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1 |
| Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 24, 2007 / Details: MIRRORS |
| Radiation | Monochromator: DOUBLE CRYSTAL, SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 2.2→40 Å / Num. obs: 39235 / % possible obs: 100 % / Observed criterion σ(I): 6 / Redundancy: 8.1 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 42.8 |
| Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 8.2 % / Rmerge(I) obs: 0.27 / Mean I/σ(I) obs: 6.5 / % possible all: 100 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: IN-HOUSE STRUCTURE Resolution: 2.2→40 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.928 / SU B: 11.32 / SU ML: 0.132 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.23 / ESU R Free: 0.195 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES RESIDUAL ONLY.
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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: 16.881 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.2→40 Å
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| Refine LS restraints |
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NEISSERIA MENINGITIDIS SEROGROUP Y (bacteria)
X-RAY DIFFRACTION
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