+Open data
-Basic information
Entry | Database: PDB / ID: 5zme | ||||||
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Title | Nucleotide-free form of C. reinhardtii ArsA1 | ||||||
Components | ATPase ARSA1 | ||||||
Keywords | HYDROLASE/TRANSPORT PROTEIN / ATPase / Transport / chloroplast / HYDROLASE-TRANSPORT PROTEIN complex | ||||||
Function / homology | Function and homology information Hydrolases; Acting on acid anhydrides / ATP hydrolysis activity / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Chlamydomonas reinhardtii (plant) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.603 Å | ||||||
Authors | Lin, T.W. / Hsiao, C.D. / Chang, H.Y. | ||||||
Citation | Journal: Plant J. / Year: 2019 Title: Structural analysis of chloroplast tail-anchored membrane protein recognition by ArsA1. Authors: Lin, T.W. / Chen, C.C. / Wu, S.M. / Chang, Y.C. / Li, Y.C. / Su, Y.W. / Hsiao, C.D. / Chang, H.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5zme.cif.gz | 131.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5zme.ent.gz | 105.9 KB | Display | PDB format |
PDBx/mmJSON format | 5zme.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zm/5zme ftp://data.pdbj.org/pub/pdb/validation_reports/zm/5zme | HTTPS FTP |
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-Related 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: 74435.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chlamydomonas reinhardtii (plant) / Gene: ARSA1, AS1, CHLREDRAFT_132949 / Production host: Escherichia coli (E. coli) References: UniProt: A8JGB0, Hydrolases; Acting on acid anhydrides |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.28 Å3/Da / Density % sol: 71.26 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 100 mM Sodium HEPES pH7.5, 20% Glycerol, 10% PEG6000 and 3% 2-Methyl-2,4-pentanediol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: BL15A1 / Wavelength: 1 Å |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Feb 25, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.6→29.86 Å / Num. obs: 15761 / % possible obs: 99.53 % / Redundancy: 7.6 % / Net I/σ(I): 29.9 |
Reflection shell | Resolution: 3.6→3.73 Å |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 3.603→29.861 Å / SU ML: 0.6 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 36.6 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.603→29.861 Å
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Refine LS restraints |
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LS refinement shell |
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