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Yorodumi- PDB-2zim: Pyrrolysyl-tRNA synthetase bound to adenylated pyrrolysine and py... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2zim | ||||||
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Title | Pyrrolysyl-tRNA synthetase bound to adenylated pyrrolysine and pyrophosphate | ||||||
Components | Pyrrolysyl-tRNA synthetasePyrrolysine—tRNAPyl ligase | ||||||
Keywords | LIGASE / tRNA synthetase bound to an adenylated intermediate / Aminoacyl-tRNA synthetase / ATP-binding / Nucleotide-binding / Protein biosynthesis | ||||||
Function / homology | Function and homology information pyrrolysine-tRNAPyl ligase / pyrrolysyl-tRNA synthetase activity / tRNA aminoacylation for protein translation / tRNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Methanosarcina mazei (archaea) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 2.1 Å | ||||||
Authors | Steitz, T.A. / Kavran, J.M. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2007 Title: Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation. Authors: Kavran, J.M. / Gundllapalli, S. / O'Donoghue, P. / Englert, M. / Soll, D. / Steitz, T.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2zim.cif.gz | 76.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2zim.ent.gz | 55.6 KB | Display | PDB format |
PDBx/mmJSON format | 2zim.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zi/2zim ftp://data.pdbj.org/pub/pdb/validation_reports/zi/2zim | 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: 33416.227 Da / Num. of mol.: 1 / Fragment: C-terminal Domain, UNP residues 185-454 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei (archaea) / Gene: pylS / Plasmid: pet15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 CODONPLUS RIL (DE3) / References: UniProt: Q8PWY1, pyrrolysine-tRNAPyl ligase | ||||||
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#2: Chemical | ChemComp-EDO / #3: Chemical | ChemComp-YLY / ( | #4: Chemical | ChemComp-POP / | #5: 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: 3.35 Å3/Da / Density % sol: 63.29 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion / pH: 7.5 Details: 100 MM TRIS, 10% PEG2000-MME, pH 7.5, VAPOR DIFFUSION, temperature 289 K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: OTHER / Wavelength: 1.514 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: May 17, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.514 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→40 Å / Num. obs: 25910 / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 11.2 % / Rmerge(I) obs: 0.087 / Net I/σ(I): 26.1 |
Reflection shell | Resolution: 2.1→2.18 Å / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 2.1→34.4 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.944 / SU B: 4.283 / SU ML: 0.113 / Cross valid method: THROUGHOUT / ESU R: 0.161 / ESU R Free: 0.153 / 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: 45.032 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→34.4 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.155 Å / Total num. of bins used: 20
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