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Yorodumi- PDB-5ewu: Crystal structure of the Arabidopsis thaliana C-terminal Chlh at 1.25A -
+Open data
-Basic information
Entry | Database: PDB / ID: 5ewu | ||||||
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Title | Crystal structure of the Arabidopsis thaliana C-terminal Chlh at 1.25A | ||||||
Components | Magnesium-chelatase subunit ChlH, chloroplastic | ||||||
Keywords | LIGASE / MG-CHELATASE / GUN5 / METAL BINDING PROTEIN / Magnesium-chelatase subunit ChlH / ABAR / CCH / RTL1 | ||||||
Function / homology | Function and homology information magnesium chelatase complex / magnesium chelatase / magnesium chelatase activity / chloroplast inner membrane / chlorophyll biosynthetic process / plastid / chloroplast stroma / photosynthesis / chloroplast / mRNA binding ...magnesium chelatase complex / magnesium chelatase / magnesium chelatase activity / chloroplast inner membrane / chlorophyll biosynthetic process / plastid / chloroplast stroma / photosynthesis / chloroplast / mRNA binding / mitochondrion / ATP binding Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.25 Å | ||||||
Authors | Chen, Z. / Zhang, X. / Liu, Y. / Jiang, L. | ||||||
Citation | Journal: To Be Published Title: Crystal structure of the Arabidopsis thaliana C-terminal Chlh at 1.25A Authors: Chen, Z. / Zhang, X. / Liu, Y. / Jiang, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ewu.cif.gz | 354.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ewu.ent.gz | 290.2 KB | Display | PDB format |
PDBx/mmJSON format | 5ewu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ew/5ewu ftp://data.pdbj.org/pub/pdb/validation_reports/ew/5ewu | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 43765.984 Da / Num. of mol.: 2 / Fragment: UNP residues 994-1381 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: CHLH, ABAR, CCH, GUN5, RTL1, At5g13630, MSH12.9 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9FNB0, magnesium chelatase #2: Chemical | #3: Chemical | ChemComp-MG / #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: 1.97 Å3/Da / Density % sol: 37.6 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: PEG, NaCl |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NE3A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 4, 2009 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→50 Å / Num. all: 187584 / Num. obs: 168362 / % possible obs: 89.8 % / Redundancy: 5.9 % / Net I/σ(I): 45 |
-Processing
Software |
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Refinement | Resolution: 1.25→50 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.962 / SU B: 1.458 / SU ML: 0.029 / Cross valid method: THROUGHOUT / ESU R: 0.061 / ESU R Free: 0.051 / 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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.411 Å2
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Refinement step | Cycle: LAST / Resolution: 1.25→50 Å
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Refine LS restraints |
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