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Yorodumi- PDB-1j2b: Crystal Structure Of Archaeosine tRNA-Guanine Transglycosylase Co... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1j2b | ||||||
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Title | Crystal Structure Of Archaeosine tRNA-Guanine Transglycosylase Complexed With lambda-form tRNA(Val) | ||||||
Components |
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Keywords | transferase/RNA / transferase / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics / transferase-RNA COMPLEX | ||||||
Function / homology | Function and homology information tRNA-guanine15 transglycosylase / pentosyltransferase activity / tRNA modification / RNA binding / metal ion binding Similarity search - Function | ||||||
Biological species | Pyrococcus horikoshii (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å | ||||||
Authors | Ishitani, R. / Nureki, O. / Nameki, N. / Okada, N. / Nishimura, S. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2003 Title: Alternative Tertiary Structure of tRNA for Recognition by a Posttranscriptional Modification Enzyme Authors: Ishitani, R. / Nureki, O. / Nameki, N. / Okada, N. / Nishimura, S. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1j2b.cif.gz | 321.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1j2b.ent.gz | 256.1 KB | Display | PDB format |
PDBx/mmJSON format | 1j2b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j2/1j2b ftp://data.pdbj.org/pub/pdb/validation_reports/j2/1j2b | HTTPS FTP |
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-Related structure data
Related structure data | 1iq8S S: Starting model for refinement |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: RNA chain | Mass: 24827.746 Da / Num. of mol.: 2 / Source method: obtained synthetically Details: synthetic tRNA transcript; sequence from Pyrococcus horikoshii #2: Protein | Mass: 66700.141 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus horikoshii (archaea) / Plasmid: pET3a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: O58843, tRNA-guanosine34 preQ1 transglycosylase #3: Chemical | ChemComp-MG / #4: Chemical | #5: 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: 3.95 Å3/Da / Density % sol: 68.58 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 300 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: citrate, ammonium phosphate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 300K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 30 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 13, 2002 / Details: mirrors |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→50 Å / Num. all: 334265 / Num. obs: 334265 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.1 % / Biso Wilson estimate: 40.6 Å2 / Rmerge(I) obs: 0.099 / Rsym value: 0.099 / Net I/σ(I): 16.7 |
Reflection shell | Resolution: 3.3→3.42 Å / Rmerge(I) obs: 0.487 / Mean I/σ(I) obs: 2.31 / Num. unique all: 4055 / Rsym value: 0.487 / % possible all: 99.8 |
Reflection | *PLUS Lowest resolution: 50 Å / Num. obs: 41049 / Num. measured all: 334265 |
Reflection shell | *PLUS % possible obs: 99.8 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1IQ8 Resolution: 3.3→48.54 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 14348606.6 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 21.895 Å2 / ksol: 0.265241 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 88.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.3→48.54 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: CONSTR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 3.3→3.51 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 3.3 Å / Lowest resolution: 50 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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