+Open data
-Basic information
Entry | Database: PDB / ID: 1un1 | |||||||||
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Title | Xyloglucan endotransglycosylase native structure. | |||||||||
Components | XYLOGLUCAN ENDOTRANSGLYCOSYLASE | |||||||||
Keywords | TRANSFERASE / GLYCOSIDE HYDROLASE / XET / XTH / XEH / TRANSGLYCOSYLATION / XYLOGLUCAN / GLYCOSYLTRANSFERASE | |||||||||
Function / homology | Function and homology information xyloglucan:xyloglucosyl transferase / xyloglucan:xyloglucosyl transferase activity / xyloglucan metabolic process / cell wall biogenesis / apoplast / polysaccharide binding / hydrolase activity, hydrolyzing O-glycosyl compounds / cell wall organization / cytoplasm Similarity search - Function | |||||||||
Biological species | POPULUS TREMULA (European aspen) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 2.1 Å | |||||||||
Authors | Johansson, P. / Brumer, H. / Kallas, A. / Henriksson, H. / Denman, S. / Teeri, T.T. / Jones, T.A. | |||||||||
Citation | Journal: Plant Cell / Year: 2004 Title: Crystal Structures of a Poplar Xyloglucan Endotransglycosylase Reveal Details of Transglycosylation Acceptor Binding Authors: Johansson, P. / Brumer, H. / Baumann, M. / Kallas, A. / Henriksson, H. / Denman, S. / Teeri, T.T. / Jones, T.A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1un1.cif.gz | 123.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1un1.ent.gz | 100.5 KB | Display | PDB format |
PDBx/mmJSON format | 1un1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/un/1un1 ftp://data.pdbj.org/pub/pdb/validation_reports/un/1un1 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.8676, -0.4934, -0.0618), Vector: |
-Components
#1: Protein | Mass: 32531.570 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) POPULUS TREMULA (European aspen) / Production host: PICHIA PASTORIS (fungus) References: UniProt: Q8GZD5, xyloglucan:xyloglucosyl transferase #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-AU / | #4: Water | ChemComp-HOH / | |
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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: 4 Å3/Da / Density % sol: 68 % | ||||||||||||||||||||||||||||
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Crystal grow | pH: 7 Details: 10 MG ML-1 PROTEIN SOLUTION 1:1 WITH 1.0 M NAOAC AND 0.2 M IMIDAZOLE PH 6.5 | ||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.933 |
Detector | Type: ADSC CCD / Detector: CCD / Date: May 15, 2002 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: SI (111) / SI (311) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→25 Å / Num. obs: 106310 / % possible obs: 99.4 % / Observed criterion σ(I): 2 / Redundancy: 3.12 % / Rmerge(I) obs: 0.081 / Net I/σ(I): 12.4 |
Reflection shell | Resolution: 2.1→2.14 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 3.7 / % possible all: 95.5 |
Reflection | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 24.8 Å / Redundancy: 3.12 % / Rmerge(I) obs: 0.081 |
Reflection shell | *PLUS % possible obs: 95.5 % / Rmerge(I) obs: 0.261 / Mean I/σ(I) obs: 3.7 |
-Processing
Software |
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Refinement | Method to determine structure: SIRAS / Resolution: 2.1→24.77 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.931 / Cross valid method: THROUGHOUT / ESU R: 0.164 / ESU R Free: 0.148 / 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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.56 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→24.77 Å
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Refine LS restraints |
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