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Open data
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Basic information
Entry | Database: PDB / ID: 3jtp | ||||||
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Title | crystal structure of the C-terminal domain of MecA | ||||||
![]() | Adapter protein mecA 1 | ||||||
![]() | PROTEIN BINDING / MecA / adaptor protein / degradation tag / Competence / Sporulation | ||||||
Function / homology | ![]() negative regulation of establishment of competence for transformation / negative regulation of sporulation resulting in formation of a cellular spore / establishment of competence for transformation / sporulation resulting in formation of a cellular spore / protein-macromolecule adaptor activity Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wang, F. / Mei, Z. / Qi, Y. / Yan, C. / Wang, J. / Shi, Y. | ||||||
![]() | ![]() Title: crystal structure of the MecA degradation tag Authors: Wang, F. / Mei, Z. / Qi, Y. / Yan, C. / Xiang, S. / Zhou, Z. / Hu, Q. / Wang, J. / Shi, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 89.7 KB | Display | ![]() |
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PDB format | ![]() | 69.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 457 KB | Display | ![]() |
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Full document | ![]() | 473.7 KB | Display | |
Data in XML | ![]() | 18.5 KB | Display | |
Data in CIF | ![]() | 25.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 11565.924 Da / Num. of mol.: 4 / Fragment: c-terminal domain, UNP residues 121-218 / Mutation: N50D, L63M, T68N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-IOD / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44.3 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.2 Details: 14% PEG 3350, 300mM calcium chloride, 4% ethylene glycol,0.1M Bis-Tris pH6.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction source | Source: ![]() |
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Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Nov 16, 2008 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.17→20.52 Å / Num. obs: 43892 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.5 % / Biso Wilson estimate: 50.3 Å2 / Rmerge(I) obs: 0.069 / Net I/σ(I): 36.75 |
Reflection shell | Resolution: 2.17→2.25 Å / Redundancy: 7.9 % / Rmerge(I) obs: 0.431 / Mean I/σ(I) obs: 4.55 / Num. unique all: 21946 / % possible all: 98.7 |
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Processing
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Refinement | Method to determine structure: ![]() Details: The file contains friedel pairs in the _refln.pdbx_F_plus and _refln.pdbx_F_minus columns.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 66.589 Å2 / ksol: 0.366 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 122.08 Å2 / Biso mean: 51.536 Å2 / Biso min: 23.55 Å2
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Refinement step | Cycle: LAST / Resolution: 2.17→20.52 Å
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Refine LS restraints |
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LS refinement shell |
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