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- PDB-2jb0: CRYSTAL STRUCTURE OF THE MUTANT H573A OF THE NUCLEASE DOMAIN OF C... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2jb0 | ||||||
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Title | CRYSTAL STRUCTURE OF THE MUTANT H573A OF THE NUCLEASE DOMAIN OF COLE7 IN COMPLEX WITH IM7 | ||||||
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![]() | HYDROLASE/INHIBITOR / HYDROLASE-INHIBITOR COMPLEX / ZINC / TOXIN / PLASMID / NUCLEASE / HYDROLASE / ANTIBIOTIC / H-N-H MOTIF / BACTERIOCIN / ENDONUCLEASE / METAL-BINDING / ANTIMICROBIAL / DNA HYDROLYSIS / BACTERIOCIN IMMUNITY / HIS METAL FINGER MOTIF | ||||||
Function / homology | ![]() extrachromosomal circular DNA / bacteriocin immunity / toxic substance binding / endonuclease activity / killing of cells of another organism / Hydrolases; Acting on ester bonds / defense response to bacterium / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Huang, H. / Yuan, H.S. | ||||||
![]() | ![]() Title: The Conserved Asparagine in the Hnh Motif Serves an Important Structural Role in Metal Finger Endonucleases. Authors: Huang, H. / Yuan, H.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 59.9 KB | Display | ![]() |
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PDB format | ![]() | 43.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.2 KB | Display | ![]() |
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Full document | ![]() | 437.2 KB | Display | |
Data in XML | ![]() | 12.4 KB | Display | |
Data in CIF | ![]() | 17.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2jazC ![]() 2jbgC ![]() 7ceiS 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 9906.963 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q03708, Hydrolases; Acting on ester bonds |
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#2: Protein | Mass: 14995.036 Da / Num. of mol.: 1 / Fragment: NUCLEASE DOMAIN, RESIDUES 446-576 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q47112, Hydrolases; Acting on ester bonds |
#3: Chemical | ChemComp-ZN / |
#4: Water | ChemComp-HOH / |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 57.02 % |
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Crystal grow | pH: 7 Details: 20 % W/V PEG3350 AND 0.2 M DI-AMMONIUM HYDROGEN CITRATE, pH 7.00 |
-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: May 24, 2005 / Details: MIRRORS |
Radiation | Monochromator: SI / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.91→25.46 Å / Num. obs: 21837 / % possible obs: 97.4 % / Observed criterion σ(I): 0 / Redundancy: 6.3 % / Biso Wilson estimate: 20.7 Å2 / Rsym value: 0.04 / Net I/σ(I): 39.2 |
Reflection shell | Resolution: 1.91→1.98 Å / Redundancy: 3.5 % / Mean I/σ(I) obs: 4.8 / Rsym value: 0.27 / % possible all: 86.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 7CEI Resolution: 1.91→25.46 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 506787.59 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 53.7618 Å2 / ksol: 0.350635 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.91→25.46 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.91→2.03 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 6
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Xplor file |
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