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Yorodumi- PDB-2vi5: LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO N-6-(r... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2vi5 | ||||||
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Title | LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-yl-propionamide | ||||||
Components | 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE | ||||||
Keywords | TRANSFERASE / LUMAZINE SYNTHASE / RIBOFLAVIN BIOSYNTHESIS / MYCOBACTERIUM TUBERCULOSIS | ||||||
Function / homology | Function and homology information 6,7-dimethyl-8-ribityllumazine synthase / 6,7-dimethyl-8-ribityllumazine synthase activity / riboflavin synthase complex / riboflavin biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | MYCOBACTERIUM TUBERCULOSIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Morgunova, E. / Zhang, Y. / Jin, G. / Illarionov, B. / Bacher, A. / Fischer, M. / Cushman, M. / Ladenstein, R. | ||||||
Citation | Journal: J.Org.Chem. / Year: 2008 Title: A New Series of N-[2,4-Dioxo-6-D-Ribitylamino-1,2, 3,4-Tetrahydropyrimidin-5-Yl]Oxalamic Acid Derivatives as Inhibitors of Lumazine Syntase and Riboflavin Synthase: Design, Synthesis, ...Title: A New Series of N-[2,4-Dioxo-6-D-Ribitylamino-1,2, 3,4-Tetrahydropyrimidin-5-Yl]Oxalamic Acid Derivatives as Inhibitors of Lumazine Syntase and Riboflavin Synthase: Design, Synthesis, Biochemical Evaluation, Crystallography and Mechanistic Implications. Authors: Zhang, Y. / Illarionov, B. / Morgunova, E. / Bacher, A. / Fischer, M. / Ladenstein, R. / Cushman, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2vi5.cif.gz | 292.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2vi5.ent.gz | 237.7 KB | Display | PDB format |
PDBx/mmJSON format | 2vi5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2vi5_validation.pdf.gz | 3.2 MB | Display | wwPDB validaton report |
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Full document | 2vi5_full_validation.pdf.gz | 3.2 MB | Display | |
Data in XML | 2vi5_validation.xml.gz | 64.3 KB | Display | |
Data in CIF | 2vi5_validation.cif.gz | 85.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vi/2vi5 ftp://data.pdbj.org/pub/pdb/validation_reports/vi/2vi5 | HTTPS FTP |
-Related structure data
Related structure data | 1w19S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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-Components
#1: Protein | Mass: 16387.559 Da / Num. of mol.: 10 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MYCOBACTERIUM TUBERCULOSIS (bacteria) / Plasmid: PNCO-MT-LS / Production host: ESCHERICHIA COLI (E. coli) / Variant (production host): XL1-BLUE References: UniProt: P66034, UniProt: P9WHE9*PLUS, riboflavin synthase #2: Chemical | ChemComp-Y19 / #3: Chemical | ChemComp-K / #4: Chemical | ChemComp-PO4 / #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: 2.5 Å3/Da / Density % sol: 50 % / Description: NONE |
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Crystal grow | pH: 7 / Details: pH 7 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.97873 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: May 7, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97873 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. obs: 62709 / % possible obs: 97.7 % / Observed criterion σ(I): 2 / Redundancy: 2.7 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 6.9 |
Reflection shell | Resolution: 2.3→2.36 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 1.3 / % possible all: 96.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1W19 Resolution: 2.3→30 Å / Cor.coef. Fo:Fc: 0.904 / Cor.coef. Fo:Fc free: 0.881 / SU B: 19.706 / SU ML: 0.27 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.534 / ESU R Free: 0.305 / 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: 39.41 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→30 Å
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Refine LS restraints |
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