+Open data
-Basic information
Entry | Database: PDB / ID: 2d35 | ||||||
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Title | Solution structure of Cell Division Reactivation Factor, CedA | ||||||
Components | Cell division activator cedA | ||||||
Keywords | CELL CYCLE / cell division activator / DNA binding motif | ||||||
Function / homology | Function and homology information regulation of cell division / double-stranded DNA binding / cell cycle / cell division Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics | ||||||
Authors | Abe, Y. / Watanabe, N. / Matsuda, Y. / Yoshida, Y. / Katayama, T. / Ueda, T. | ||||||
Citation | Journal: To be Published Title: Structural Analysis and Molecular Interaction of Cell Division Reactivation Factor, CedA from Escherichia coli Authors: Abe, Y. / Watanabe, N. / Matsuda, Y. / Yoshida, Y. / Katayama, T. / Ueda, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2d35.cif.gz | 195.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2d35.ent.gz | 168.4 KB | Display | PDB format |
PDBx/mmJSON format | 2d35.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d3/2d35 ftp://data.pdbj.org/pub/pdb/validation_reports/d3/2d35 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7147.088 Da / Num. of mol.: 1 / Fragment: Residues 1-62 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: cedA / Plasmid: pET-22b(+) / Production host: Escherichia coli (E. coli) / References: UniProt: P0AE60 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 3D heteronuclear techniques. |
-Sample preparation
Details | Contents: 0.5mM CedA U-15N,13C; 10mM AcONa U-2H; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: No salt / pH: 5.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, molecular dynamics Software ordinal: 1 Details: the structures are based on a total of 596 restraints, 496 are NOE-derived distance constraints, 66 dihedral angle restraints,34 distance restraints from hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 10 |