+Open data
-Basic information
Entry | Database: PDB / ID: 3jtp | ||||||
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Title | crystal structure of the C-terminal domain of MecA | ||||||
Components | Adapter protein mecA 1 | ||||||
Keywords | PROTEIN BINDING / MecA / adaptor protein / degradation tag / Competence / Sporulation | ||||||
Function / homology | Function and homology information 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 | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SAD / Resolution: 2.17 Å | ||||||
Authors | Wang, F. / Mei, Z. / Qi, Y. / Yan, C. / Wang, J. / Shi, Y. | ||||||
Citation | Journal: To be Published 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3jtp.cif.gz | 86.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3jtp.ent.gz | 71.1 KB | Display | PDB format |
PDBx/mmJSON format | 3jtp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jt/3jtp ftp://data.pdbj.org/pub/pdb/validation_reports/jt/3jtp | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-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: 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.) Bacillus subtilis (bacteria) / Gene: mecA / Plasmid: pGEX-6P-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P37958 #2: Chemical | ChemComp-IOD / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: ROTATING ANODE / Type: RIGAKU FR-E SUPERBRIGHT / Wavelength: 1.5418 Å |
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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 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.17→20.52 Å / Occupancy max: 1 / Occupancy min: 0.25 / FOM work R set: 0.774 / SU ML: 0.38 / σ(F): 0.04 / Phase error: 29.38 / Stereochemistry target values: ML 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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