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- PDB-4b2l: Humanised monomeric RadA in complex with L-methylester tryptophan -
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Open data
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Basic information
Entry | Database: PDB / ID: 4b2l | ||||||
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Title | Humanised monomeric RadA in complex with L-methylester tryptophan | ||||||
![]() | DNA REPAIR AND RECOMBINATION PROTEIN RADA | ||||||
![]() | HYDROLASE / RECOMBINASE / THERMOSTABLE / PEPTIDE-BINDING | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Scott, D.E. / Ehebauer, M.T. / Pukala, T. / Marsh, M. / Blundell, T.L. / Venkitaraman, A.R. / Abell, C. / Hyvonen, M. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.2 KB | Display | ![]() |
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PDB format | ![]() | 45 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 454.7 KB | Display | ![]() |
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Full document | ![]() | 456.5 KB | Display | |
Data in XML | ![]() | 13.7 KB | Display | |
Data in CIF | ![]() | 20.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4b2iC ![]() 4b32C ![]() 4b33C ![]() 4b34C ![]() 4b35C ![]() 4b3bC ![]() 4b3cC ![]() 4b3dC ![]() 1pznS S: Starting model for refinement C: citing same article ( |
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Similar 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: 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.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-TR7 / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Dec 10, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9728 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→32.09 Å / Num. obs: 31779 / % possible obs: 96.7 % / Observed criterion σ(I): 2 / Redundancy: 3.8 % / Biso Wilson estimate: 23.63 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 19.16 |
Reflection shell | Resolution: 1.5→1.59 Å / Redundancy: 3.78 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 3.78 / % possible all: 94.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1PZN CHAIN A Resolution: 1.5→39.31 Å / SU ML: 0.18 / σ(F): 2 / Phase error: 22.35 / 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: 42.538 Å2 / ksol: 0.344 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.5→39.31 Å
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Refine LS restraints |
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LS refinement shell |
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