+
Open data
-
Basic information
Entry | Database: PDB / ID: 1ii8 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of the P. furiosus Rad50 ATPase domain | ||||||
![]() | (Rad50 ABC-ATPase) x 2 | ||||||
![]() | REPLICATION / Rad50 / Mre11 / DNA double-strand break repair / ATP | ||||||
Function / homology | ![]() double-strand break repair / ATP hydrolysis activity / zinc ion binding / ATP binding / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hopfner, K.-P. / Karcher, A. / Craig, L. / Woo, T.T. / Carney, J.P. / Tainer, J.A. | ||||||
![]() | ![]() Title: Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase. Authors: Hopfner, K.P. / Karcher, A. / Craig, L. / Woo, T.T. / Carney, J.P. / Tainer, J.A. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 91.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 67.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 385.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 404.1 KB | Display | |
Data in XML | ![]() | 11.2 KB | Display | |
Data in CIF | ![]() | 16 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ii7C ![]() 1f2tS C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 22672.248 Da / Num. of mol.: 1 / Fragment: N-terminal fragment Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
---|---|---|---|
#2: Protein | Mass: 19981.195 Da / Num. of mol.: 1 / Fragment: C-terminal fragment Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.9 Å3/Da / Density % sol: 68.47 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 300 K / Method: vapor diffusion, sitting drop / pH: 6.2 Details: 100 mM Na-Acetate, 8% PEG 6K, 10 mM Ca-Acetate, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 300K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 26, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 3→30 Å / Num. all: 119376 / Num. obs: 119376 / % possible obs: 83 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.8 % / Rmerge(I) obs: 0.057 / Net I/σ(I): 7.1 |
Reflection shell | Resolution: 3→3.11 Å / Redundancy: 2 % / Rmerge(I) obs: 0.348 / % possible all: 47.3 |
Reflection | *PLUS Num. obs: 13527 / Num. measured all: 119376 |
Reflection shell | *PLUS % possible obs: 47.3 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 1F2T Resolution: 3.02→28.84 Å / Rfactor Rfree error: 0.012 / Data cutoff high absF: 1889335.26 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 0 / Stereochemistry target values: Engh&Huber
| ||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 63.72 Å2 / ksol: 0.22 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 90.5 Å2
| ||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.02→28.84 Å
| ||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||
LS refinement shell | Highest resolution: 3.02 Å / Total num. of bins used: 6 /
| ||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 2 / % reflection Rfree: 5.1 % | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 90.5 Å2 | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|