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Yorodumi- PDB-5k39: THE TYPE II COHESIN DOCKERIN COMPLEX FROM CLOSTRIDIUM THERMOCELLUM -
+Open data
-Basic information
Entry | Database: PDB / ID: 5k39 | ||||||
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Title | THE TYPE II COHESIN DOCKERIN COMPLEX FROM CLOSTRIDIUM THERMOCELLUM | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN / S-LAYER / SECRETED / CELL WALL / MEMBRANE PROTEIN | ||||||
Function / homology | Function and homology information S-layer / cellulose catabolic process / polysaccharide catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate binding / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Ruminiclostridium thermocellum 27405 (bacteria) Clostridium thermocellum 27405 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.98 Å | ||||||
Authors | Viegas, A. / Pinheiro, B. / Bras, J.L.A. / Romao, M.J. / Alves, V. / Carvalho, A.L. / Fontes, C.M.G.A. | ||||||
Citation | Journal: Sci Rep / Year: 2016 Title: Diverse specificity of cellulosome attachment to the bacterial cell surface. Authors: Bras, J.L. / Pinheiro, B.A. / Cameron, K. / Cuskin, F. / Viegas, A. / Najmudin, S. / Bule, P. / Pires, V.M. / Romao, M.J. / Bayer, E.A. / Spencer, H.L. / Smith, S. / Gilbert, H.J. / Alves, V. ...Authors: Bras, J.L. / Pinheiro, B.A. / Cameron, K. / Cuskin, F. / Viegas, A. / Najmudin, S. / Bule, P. / Pires, V.M. / Romao, M.J. / Bayer, E.A. / Spencer, H.L. / Smith, S. / Gilbert, H.J. / Alves, V.D. / Carvalho, A.L. / Fontes, C.M. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE ...SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5k39.cif.gz | 85.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5k39.ent.gz | 62.2 KB | Display | PDB format |
PDBx/mmJSON format | 5k39.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k3/5k39 ftp://data.pdbj.org/pub/pdb/validation_reports/k3/5k39 | HTTPS FTP |
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-Related structure data
Related structure data | 5g5dC 5m0yC 2b59S 2mb3S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 18947.541 Da / Num. of mol.: 1 / Fragment: COHESION 2 DOMAIN, RESIDUES 205-364 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Ruminiclostridium thermocellum 27405 (bacteria) Gene: AD2_00639 / Plasmid: pCF1 / Details (production host): altered pET21 plasmid / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: A0A0U3TQ90, UniProt: Q06853*PLUS | ||
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#2: Protein | Mass: 18245.408 Da / Num. of mol.: 1 / Fragment: RESIDUES 2015-2177 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium thermocellum 27405 (bacteria) Gene: Cthe_1806 / Production host: Escherichia coli (E. coli) / References: UniProt: A3DGE8 | ||
#3: Chemical | #4: 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: 2.2 Å3/Da / Density % sol: 43.13 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 12% (m/v) polyethyleneglycol (PEG) 3350, 4% tacsimate, pH 5.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9735 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 28, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9735 Å / Relative weight: 1 |
Reflection | Resolution: 1.98→39.31 Å / Num. obs: 21909 / % possible obs: 97.8 % / Observed criterion σ(I): 4 / Redundancy: 3.6 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 13.1 |
Reflection shell | Resolution: 1.98→2.09 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 5.5 / % possible all: 98.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRIES 2MB3 AND 2B59 Resolution: 1.98→18.83 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.906 / SU B: 7.842 / SU ML: 0.124 / Cross valid method: THROUGHOUT / ESU R: 0.225 / ESU R Free: 0.194 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.01 Å2
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Refinement step | Cycle: LAST / Resolution: 1.98→18.83 Å
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Refine LS restraints |
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