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- PDB-1o9g: rRNA methyltransferase aviRa from Streptomyces viridochromogenes ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1o9g | ||||||
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Title | rRNA methyltransferase aviRa from Streptomyces viridochromogenes at 1.5A | ||||||
![]() | RRNA METHYLTRANSFERASE | ||||||
![]() | ![]() ![]() | ||||||
Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mosbacher, T.G. / Schulz, G.E. | ||||||
![]() | ![]() Title: Crystal Structure of the Avilamycin Resistance-Conferring Methyltransferase Avira from Streptomyces Viridochromogenes Authors: Mosbacher, T.G. / Bechthold, A. / Schulz, G.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 113.9 KB | Display | ![]() |
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PDB format | ![]() | 92.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 26833.492 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PRSETB / Production host: ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / ![]() |
Compound details | ENGINEERED MUTATION ILE 11 MET, ARG 190 GLY AND LEU 239 MET. ALSO SEE REMARK 999 FOR MORE DETAILS ...ENGINEERED |
Sequence details | SEQUENCE IN DATABASE INCORRECT FROM RESIDUE 180 TO 195. THE SWISS-PROT ACCESSION Q9F5K5 HAS THE ...SEQUENCE IN DATABASE INCORRECT FROM RESIDUE 180 TO 195. THE SWISS-PROT ACCESSION Q9F5K5 HAS THE SEQUENCE SARTGKGRCP |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 39 % | ||||||||||||||||||||||||
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Crystal grow![]() | pH: 6.9 / Details: PEG 20000 9%, MES 6.6, pH 6.90 | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / PH range low: 6.9 / PH range high: 6.6 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Sep 8, 2002 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.5→37.8 Å / Num. obs: 64711 / % possible obs: 97 % / Observed criterion σ(I): 2 / Redundancy: 4.3 % / Rsym value: 0.034 / Net I/σ(I): 38.7 |
Reflection shell | Resolution: 1.5→1.52 Å / Redundancy: 3.4 % / Mean I/σ(I) obs: 6.6 / Rsym value: 0.2 / % possible all: 90 |
Reflection | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 15 Å / % possible obs: 97 % / Redundancy: 4.3 % / Num. measured all: 289006 / Rmerge(I) obs: 0.039 |
Reflection shell | *PLUS % possible obs: 90 % / Redundancy: 3.4 % / Num. unique obs: 1482 / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 6.6 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Displacement parameters | Biso mean: 9.096 Å2
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Refinement step | Cycle: LAST / Resolution: 1.5→37.8 Å
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Refinement | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 25 Å / Num. reflection obs: 33212 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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