+Open data
-Basic information
Entry | Database: PDB / ID: 4b2i | ||||||
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Title | Humanised monomeric RadA in complex with indazole | ||||||
Components | DNA REPAIR AND RECOMBINATION PROTEIN RADA | ||||||
Keywords | HYDROLASE / RECOMBINASE / THERMOSTABLE / PEPTIDE-BINDING | ||||||
Function / homology | Function and homology information DNA recombinase assembly / mitotic recombination / DNA strand invasion / DNA strand exchange activity / ATP-dependent DNA damage sensor activity / single-stranded DNA binding / double-stranded DNA binding / damaged DNA binding / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | PYROCOCCUS FURIOSUS (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.3 Å | ||||||
Authors | Scott, D.E. / Ehebauer, M.T. / Pukala, T. / Marsh, M. / Blundell, T.L. / Venkitaraman, A.R. / Abell, C. / Hyvonen, M. | ||||||
Citation | Journal: Chembiochem / Year: 2013 Title: Using a Fragment-Based Approach to Target Protein-Protein Interactions. Authors: Scott, D.E. / Ehebauer, M.T. / Pukala, T. / Marsh, M. / Blundell, T.L. / Venkitaraman, A.R. / Abell, C. / Hyvonen, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4b2i.cif.gz | 66 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4b2i.ent.gz | 46.7 KB | Display | PDB format |
PDBx/mmJSON format | 4b2i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4b2i_validation.pdf.gz | 450.8 KB | Display | wwPDB validaton report |
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Full document | 4b2i_full_validation.pdf.gz | 452.8 KB | Display | |
Data in XML | 4b2i_validation.xml.gz | 14.4 KB | Display | |
Data in CIF | 4b2i_validation.cif.gz | 21.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b2/4b2i ftp://data.pdbj.org/pub/pdb/validation_reports/b2/4b2i | HTTPS FTP |
-Related structure data
Related structure data | 4b2lC 4b32C 4b33C 4b34C 4b35C 4b3bC 4b3cC 4b3dC 1pznS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 25502.150 Da / Num. of mol.: 1 / Fragment: ATPASE, RESIDUES 108-349 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) PYROCOCCUS FURIOSUS (archaea) / Plasmid: PBAT4 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CONTAINING PUBS520 PLASMID / References: UniProt: O74036 |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-LZ1 / |
#4: Water | ChemComp-HOH / |
Compound details | ENGINEERED RESIDUE IN CHAIN A, ILE 169 TO MET ENGINEERED RESIDUE IN CHAIN A, TYR 201 TO ALA ...ENGINEERED |
Sequence details | DELETION 1-107,HUMANISING |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.46 % / Description: NONE |
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Crystal grow | pH: 6.2 / Details: 10-15% PEG-1000, 50 MM NAKPHOSPHATE, PH 6.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9795 |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 4, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.3→39.38 Å / Num. obs: 49540 / % possible obs: 99 % / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Biso Wilson estimate: 20.2 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 18.2 |
Reflection shell | Resolution: 1.3→1.38 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 2.6 / % possible all: 99 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1PZN CHAIN A Resolution: 1.3→33.064 Å / SU ML: 0.15 / σ(F): 2 / Phase error: 22.56 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 59.964 Å2 / ksol: 0.379 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.3→33.064 Å
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Refine LS restraints |
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LS refinement shell |
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