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Open data
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Basic information
| Entry | Database: PDB / ID: 3m8k | ||||||
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| Title | Protein structure of type III plasmid segregation TubZ | ||||||
Components | FtsZ/tubulin-related protein | ||||||
Keywords | STRUCTURAL PROTEIN / tubulin-like protein / plasmid segregation / GTP-binding / Nucleotide-binding | ||||||
| Function / homology | Function and homology informationplasmid partitioning / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / GTPase activity / GTP binding / metal ion binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.3 Å | ||||||
Authors | Schumacher, M.A. / Ni, L. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2010Title: From the Cover: Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition. Authors: Ni, L. / Xu, W. / Kumaraswami, M. / Schumacher, M.A. | ||||||
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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 | 3m8k.cif.gz | 159.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3m8k.ent.gz | 129.5 KB | Display | PDB format |
| PDBx/mmJSON format | 3m8k.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3m8k_validation.pdf.gz | 422.9 KB | Display | wwPDB validaton report |
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| Full document | 3m8k_full_validation.pdf.gz | 433.8 KB | Display | |
| Data in XML | 3m8k_validation.xml.gz | 19.4 KB | Display | |
| Data in CIF | 3m8k_validation.cif.gz | 25.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m8/3m8k ftp://data.pdbj.org/pub/pdb/validation_reports/m8/3m8k | 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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| Unit cell |
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Components
| #1: Protein | Mass: 48609.066 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 1-428 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.86 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 4 M NaFormate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
| Diffraction | Mean temperature: 100 K | ||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 0.97963,1.01995,0.97974 | ||||||||||||
| Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 1, 2009 / Details: KOHZU: Double Crystal Si(111) | ||||||||||||
| Radiation | Monochromator: KHOZU Double flat crystal / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
| Radiation wavelength |
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| Reflection | Resolution: 2.3→65.79 Å / Num. all: 21805 / Num. obs: 21740 / % possible obs: 99.7 % / Observed criterion σ(I): 3 / Redundancy: 6.1 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 19.4 | ||||||||||||
| Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.271 / Mean I/σ(I) obs: 4.6 / % possible all: 100 |
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Processing
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| Refinement | Method to determine structure: MAD / Resolution: 2.3→65.79 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.921 / SU B: 13.341 / SU ML: 0.182 / Cross valid method: THROUGHOUT / ESU R: 0.32 / ESU R Free: 0.232 / 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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 53.279 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.3→65.79 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.3→2.36 Å / Total num. of bins used: 20
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group |
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