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Open data
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Basic information
Entry | Database: PDB / ID: 7cs9 | ||||||
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Title | AtPrR1 in apo form | ||||||
![]() | Pinoresinol reductase 1 | ||||||
![]() | OXIDOREDUCTASE / AtPrR1 / dimer / PLANT PROTEIN | ||||||
Function / homology | (+)-pinoresinol reductase / (-)-pinoresinol reductase / lignan biosynthetic process / pinoresinol reductase activity / Phenylcoumaran benzylic ether reductase-like / NmrA-like domain / NmrA-like family / NAD(P)-binding domain superfamily / Pinoresinol reductase 1![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Shao, K. / Zhang, P. | ||||||
![]() | ![]() Title: Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases. Authors: Xiao, Y. / Shao, K. / Zhou, J. / Wang, L. / Ma, X. / Wu, D. / Yang, Y. / Chen, J. / Feng, J. / Qiu, S. / Lv, Z. / Zhang, L. / Zhang, P. / Chen, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 297 KB | Display | ![]() |
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PDB format | ![]() | 196.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 451.5 KB | Display | ![]() |
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Full document | ![]() | 480.6 KB | Display | |
Data in XML | ![]() | 44.8 KB | Display | |
Data in CIF | ![]() | 61.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7cs2C ![]() 7cs3C ![]() 7cs4C ![]() 7cs5C ![]() 7cs6C ![]() 7cs7C ![]() 7cs8C ![]() 7csaC ![]() 7csbC ![]() 7cscC ![]() 7csdC ![]() 7cseC ![]() 7csfC ![]() 7csgC ![]() 7cshC ![]() 1qydS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 35594.844 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9FVQ6, (+)-pinoresinol reductase, (-)-pinoresinol reductase |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.27 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: 0.2 M lithium chloride, 20% w/v PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MAR555 FLAT PANEL / Detector: IMAGE PLATE / Date: Dec 18, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9798 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→39.271 Å / Num. obs: 39296 / % possible obs: 99.9 % / Redundancy: 12.1 % / Biso Wilson estimate: 58.8908106247 Å2 / Rmerge(I) obs: 0.152 / Net I/σ(I): 19.3 |
Reflection shell | Resolution: 2.8→2.9 Å / Rmerge(I) obs: 1.283 / Num. unique obs: 3860 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1QYD Resolution: 2.80114138241→39.270799393 Å / SU ML: 0.432085596789 / Cross valid method: FREE R-VALUE / σ(F): 1.32663843817 / Phase error: 33.0036151099 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 66.4159313122 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.80114138241→39.270799393 Å
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Refine LS restraints |
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LS refinement shell |
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