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- PDB-3cp0: Crystal structure of the soluble domain of membrane protein impli... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3cp0 | ||||||
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Title | Crystal structure of the soluble domain of membrane protein implicated in regulation of membrane protease activity from Corynebacterium glutamicum | ||||||
![]() | Membrane protein implicated in regulation of membrane protease activity | ||||||
![]() | MEMBRANE PROTEIN / beta barrel / Structural Genomics / PSI-2 / Protein Structure Initiative / Midwest Center for Structural Genomics / MCSG / Protease | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kim, Y. / Tesar, C. / Abdullah, J. / Joachimiak, A. / Midwest Center for Structural Genomics (MCSG) | ||||||
![]() | ![]() Title: The crystal structure of the soluble domain of membrane protein implicated in regulation of membrane protease activity from Corynebacterium glutamicum. Authors: Kim, Y. / Tesar, C. / Abdullah, J. / Joachimiak, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 24.8 KB | Display | ![]() |
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PDB format | ![]() | 18.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.1 KB | Display | ![]() |
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Full document | ![]() | 425.1 KB | Display | |
Data in XML | ![]() | 5.6 KB | Display | |
Data in CIF | ![]() | 6.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 8923.986 Da / Num. of mol.: 1 / Fragment: CG1731 domain: Residues 64-142 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Species: Corynebacterium glutamicum / Strain: DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / Gene: cg1731 / Plasmid: pMCSG7 / Species (production host): Escherichia coli / Production host: ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-CL / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.59 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop Details: 0.05 M Zinc acetate dihydrate, 20% w/v PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 12, 2008 / Details: Mirrors |
Radiation | Monochromator: Double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→40 Å / Num. all: 9137 / Num. obs: 9137 / % possible obs: 98.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.6 % / Biso Wilson estimate: 20.43 Å2 / Rsym value: 0.113 / Net I/σ(I): 13.6 |
Reflection shell | Resolution: 1.65→1.68 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.436 / Mean I/σ(I) obs: 2.22 / % possible all: 86.3 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.127 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→33.2 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.65→1.693 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 19.7791 Å / Origin y: 3.1642 Å / Origin z: 25.9387 Å
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