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Yorodumi- PDB-1vpb: CRYSTAL STRUCTURE OF A PUTATIVE MODULATOR OF DNA GYRASE (BT3649) ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1vpb | ||||||
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Title | CRYSTAL STRUCTURE OF A PUTATIVE MODULATOR OF DNA GYRASE (BT3649) FROM BACTEROIDES THETAIOTAOMICRON VPI-5482 AT 1.75 A RESOLUTION | ||||||
Components | putative modulator of DNA gyrase | ||||||
Keywords | HYDROLASE / PUTATIVE MODULATOR OF DNA GYRASE / STRUCTURAL GENOMICS / JOINT CENTER FOR STRUCTURAL GENOMICS / JCSG / PROTEIN STRUCTURE INITIATIVE / PSI | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Bacteroides thetaiotaomicron (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.75 Å | ||||||
Authors | Joint Center for Structural Genomics (JCSG) | ||||||
Citation | Journal: To be Published Title: Crystal structure of Putative modulator of DNA gyrase (bt3649) from Bacteroides thetaiotaomicron vpi-5482 at 1.75 A resolution Authors: Joint Center for Structural Genomics (JCSG) | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1vpb.cif.gz | 109.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1vpb.ent.gz | 82.7 KB | Display | PDB format |
PDBx/mmJSON format | 1vpb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1vpb_validation.pdf.gz | 411.1 KB | Display | wwPDB validaton report |
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Full document | 1vpb_full_validation.pdf.gz | 411.8 KB | Display | |
Data in XML | 1vpb_validation.xml.gz | 10.5 KB | Display | |
Data in CIF | 1vpb_validation.cif.gz | 17.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vp/1vpb ftp://data.pdbj.org/pub/pdb/validation_reports/vp/1vpb | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 49845.000 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacteroides thetaiotaomicron (bacteria) Strain: VPI-5482 / Gene: bt3649 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8A1L2 | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal |
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Crystal grow |
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.74→99 Å / Num. obs: 61062 / % possible obs: 98.69 % / Redundancy: 4.73 % / Biso Wilson estimate: 32.84 Å2 / Rmerge(I) obs: 0.052 / Net I/σ(I): 30.27 | ||||||||||||||||||
Reflection shell | Resolution: 1.74→1.77 Å / Redundancy: 3.37 % / Rmerge(I) obs: 0.428 / Mean I/σ(I) obs: 3.61 / Num. unique all: 2652 / % possible all: 86.87 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.75→43.78 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.951 / SU B: 3.635 / SU ML: 0.062 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.096 / ESU R Free: 0.094 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS ELECTRON DENSITY FOR RESIDUES ALA42 AND LYS43 ARE POOR, SO THESE TWO RESIDUES ARE NOT INCLUDED IN THE FINAL MODEL. THE DATA USED IN THE ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS ELECTRON DENSITY FOR RESIDUES ALA42 AND LYS43 ARE POOR, SO THESE TWO RESIDUES ARE NOT INCLUDED IN THE FINAL MODEL. THE DATA USED IN THE FINAL REFINEMENT WAS FROM A NATIVE CRYSTAL. THE REFINEMENT OF THE COORDINATES WAS RESTRAINED WITH THE EXPERIMENTAL PHASES FROM A SELENOMETHIONINE MAD EXPERIMENT FROM A SECOND CRYSTAL.
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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: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.34 Å2
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Refinement step | Cycle: LAST / Resolution: 1.75→43.78 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.75→1.795 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 12.6584 Å / Origin y: 20.6205 Å / Origin z: 35.9151 Å
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Refinement TLS group | Selection: ALL |