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Yorodumi- PDB-3adg: Structure of Arabidopsis HYL1 and its molecular implications for ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3adg | ||||||
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Title | Structure of Arabidopsis HYL1 and its molecular implications for miRNA processing | ||||||
Components | F21M12.9 protein | ||||||
Keywords | GENE REGULATION / HYL1 / miRNA processing mechanism / RNA BINDING PROTEIN | ||||||
Function / homology | Function and homology information nuclear dicing body / leaf proximal/distal pattern formation / response to cytokinin / ta-siRNA processing / leaf vascular tissue pattern formation / miRNA-mediated gene silencing by mRNA destabilization / response to auxin / response to abscisic acid / miRNA processing / pre-miRNA processing ...nuclear dicing body / leaf proximal/distal pattern formation / response to cytokinin / ta-siRNA processing / leaf vascular tissue pattern formation / miRNA-mediated gene silencing by mRNA destabilization / response to auxin / response to abscisic acid / miRNA processing / pre-miRNA processing / miRNA binding / double-stranded RNA binding / nuclear speck / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Yuan, Y.A. / Chen, H.Y. | ||||||
Citation | Journal: Structure / Year: 2010 Title: Structure of arabidopsis HYPONASTIC LEAVES1 and its molecular implications for miRNA processing Authors: Yang, S.W. / Chen, H.Y. / Yang, J. / Machida, S. / Chua, N.H. / Yuan, Y.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3adg.cif.gz | 29.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3adg.ent.gz | 18.8 KB | Display | PDB format |
PDBx/mmJSON format | 3adg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3adg_validation.pdf.gz | 396.3 KB | Display | wwPDB validaton report |
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Full document | 3adg_full_validation.pdf.gz | 397.3 KB | Display | |
Data in XML | 3adg_validation.xml.gz | 3.5 KB | Display | |
Data in CIF | 3adg_validation.cif.gz | 5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ad/3adg ftp://data.pdbj.org/pub/pdb/validation_reports/ad/3adg | HTTPS FTP |
-Related structure data
Related structure data | 3adiC 3adjC 3adlC 1di2S C: citing same article (ref.) S: Starting model for refinement |
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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
#1: Protein | Mass: 8238.390 Da / Num. of mol.: 1 / Fragment: HYL1 dsRBD1, UNP residues 15-84 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: HYL1 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O04492 |
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#2: 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: 2.15 Å3/Da / Density % sol: 42.66 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG400, MgCl2, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.54 Å |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→40 Å / Num. obs: 7709 / % possible obs: 98.4 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5.7 % / Rsym value: 0.032 / Net I/σ(I): 40 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 5.5 % / Mean I/σ(I) obs: 9 / Num. unique all: 779 / Rsym value: 0.182 / % possible all: 97.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1DI2 Resolution: 1.7→26.25 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.932 / SU B: 4.52 / SU ML: 0.099 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(I): 2 / ESU R: 0.136 / ESU R Free: 0.133 / 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: 31.04 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→26.25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.701→1.745 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 10.08 Å / Origin y: -6.2199 Å / Origin z: -11.9658 Å
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