+Open data
-Basic information
Entry | Database: PDB / ID: 3mf6 | ||||||
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Title | Computationally designed endo-1,4-beta-xylanase | ||||||
Components | Endo-1,4-beta-xylanaseXylanase | ||||||
Keywords | HYDROLASE / peptide binding / jelly-role / designed / computational / family 11 / thumb / Glycosidase / Xylan degradation | ||||||
Function / homology | Function and homology information polysaccharide binding / endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process Similarity search - Function | ||||||
Biological species | Thermopolyspora flexuosa (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.28 Å | ||||||
Authors | Morin, A. / Harp, J.M. | ||||||
Citation | Journal: Protein Eng.Des.Sel. / Year: 2011 Title: Computational design of an endo-1,4-{beta}-xylanase ligand binding site. Authors: Morin, A. / Kaufmann, K.W. / Fortenberry, C. / Harp, J.M. / Mizoue, L.S. / Meiler, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3mf6.cif.gz | 98 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3mf6.ent.gz | 76.1 KB | Display | PDB format |
PDBx/mmJSON format | 3mf6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mf/3mf6 ftp://data.pdbj.org/pub/pdb/validation_reports/mf/3mf6 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 21337.061 Da / Num. of mol.: 1 / Fragment: UNP residues 44-234 / Mutation: W21R,N47L,V49L,Y75R,E88S,Y90H,F134Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermopolyspora flexuosa (bacteria) / Gene: xyn11A / Plasmid: pET29b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: Q8GMV7, endo-1,4-beta-xylanase | ||
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#2: Chemical | #3: 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: 2.98 Å3/Da / Density % sol: 58.68 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 10mg.mL protein conc., 0.1 M NaCl, 1.125 M ammonium sulfate, 0.1 M Bis-Tris pH 5.5, 3% Jeffamine M600 pH 7.0 , VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Feb 1, 2009 |
Radiation | Monochromator: double crystal si-220 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.28→55.3 Å / Num. all: 62659 / Num. obs: 62177 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.284→1.317 Å / % possible all: 99.78 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.28→55.3 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.978 / SU B: 0.868 / SU ML: 0.017 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.033 / ESU R Free: 0.032 / 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: 12.476 Å2
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Refinement step | Cycle: LAST / Resolution: 1.28→55.3 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.284→1.317 Å / Total num. of bins used: 20
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