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Open data
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Basic information
Entry | Database: PDB / ID: 9l55 | ||||||
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Title | Plastid Localized Exonuclease 1 (D249A) complexed with DNA | ||||||
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![]() | PLANT PROTEIN/DNA / Exonuclease / PLANT PROTEIN-DNA complex | ||||||
Function / homology | ![]() DNA replication, Okazaki fragment processing / 5'-flap endonuclease activity / 5'-3' exonuclease activity / DNA-directed DNA polymerase activity / DNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() synthetic construct (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Shi, G. / Zhang, Y. | ||||||
Funding support | ![]()
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![]() | ![]() Title: PEN1 catalyses RNA primer removal during plastid DNA replication in maize. Authors: Huang, X. / Shi, G. / Xiao, Q. / Feng, J. / Huang, Y. / Shi, H. / Wang, Q. / Su, Y. / Wang, J. / Wu, X. / Cao, Y. / Wang, H. / Wang, W. / Zhang, Y. / Wu, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 254.5 KB | Display | ![]() |
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PDB format | ![]() | 197.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 464 KB | Display | ![]() |
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Full document | ![]() | 478.1 KB | Display | |
Data in XML | ![]() | 27.9 KB | Display | |
Data in CIF | ![]() | 36.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9l56C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 36697.551 Da / Num. of mol.: 2 / Mutation: D249A Source method: isolated from a genetically manipulated source Details: Expression using the pET28a-His-SUMOstar plasmid.Deleted the first 91 amino acids of the original sequence and the D249 mutation became A249(the deleted sequence was the signal peptide). Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-DNA chain , 3 types, 3 molecules EFG
#2: DNA chain | Mass: 5379.520 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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#3: DNA chain | Mass: 3099.052 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
#4: DNA chain | Mass: 2506.665 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 2 types, 50 molecules 


#5: Chemical | ChemComp-MG / #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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Has protein modification | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.5 Å3/Da / Density % sol: 64.87 % |
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Crystal grow | Temperature: 295.15 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.2 M ammonium acetate, 0.01 M MgCl2, 0.05 M Sodium cacodylate pH 6.5, 10% w/v PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 20, 2024 |
Radiation | Monochromator: Si111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979183 Å / Relative weight: 1 |
Reflection | Resolution: 2.87→30.38 Å / Num. obs: 51965 / % possible obs: 99.8 % / Redundancy: 12.8 % / CC1/2: 0.999 / Rmerge(I) obs: 0.139 / Rpim(I) all: 0.04 / Rrim(I) all: 0.145 / Net I/σ(I): 19.3 |
Reflection shell | Resolution: 2.87→2.94 Å / Redundancy: 13.2 % / Rmerge(I) obs: 1.79 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 26697 / CC1/2: 0.739 / Rpim(I) all: 0.647 / Rsym value: 1.69 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 97.24 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.87→30.38 Å
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Refine LS restraints |
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LS refinement shell |
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