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- PDB-5h66: Crystal structure of the Bacillus subtilis SMC head domain comple... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5h66 | ||||||
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Title | Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain | ||||||
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![]() | DNA BINDING PROTEIN/CELL CYCLE / SMC protein / DNA BINDING PROTEIN-CELL CYCLE complex | ||||||
Function / homology | ![]() cohesin loader activity / chromosome condensation / mitotic sister chromatid cohesion / chromosome segregation / chromosome / double-stranded DNA binding / DNA replication / cell division / ATP hydrolysis activity / ATP binding ...cohesin loader activity / chromosome condensation / mitotic sister chromatid cohesion / chromosome segregation / chromosome / double-stranded DNA binding / DNA replication / cell division / ATP hydrolysis activity / ATP binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kamada, K. / Hirano, T. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Overall Shapes of the SMC-ScpAB Complex Are Determined by Balance between Constraint and Relaxation of Its Structural Parts Authors: Kamada, K. / Su'etsugu, M. / Takada, H. / Miyata, M. / Hirano, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 125.8 KB | Display | ![]() |
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PDB format | ![]() | 77.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449 KB | Display | ![]() |
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Full document | ![]() | 452.7 KB | Display | |
Data in XML | ![]() | 18.1 KB | Display | |
Data in CIF | ![]() | 25.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5h67C ![]() 5h68C ![]() 5h69C ![]() 1xewS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 22517.609 Da / Num. of mol.: 1 / Fragment: N-terminal, UNP residues 1-199 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: 168 / Gene: smc, ylqA, BSU15940 / Plasmid: pET-22b / Details (production host): coexpression / Production host: ![]() ![]() |
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#2: Protein | Mass: 21466.559 Da / Num. of mol.: 1 / Fragment: C-terminal, UNP residues 1000-1186 / Mutation: E1118Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: 168 / Gene: smc, ylqA, BSU15940 / Plasmid: pET-22b / Details (production host): coexpression / Production host: ![]() ![]() |
#3: Protein | Mass: 9289.652 Da / Num. of mol.: 1 / Fragment: UNP residues 176-251 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: 168 / Gene: scpA, ypuG, BSU23220 / Plasmid: pET-28m / Details (production host): modified / Production host: ![]() ![]() |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.73 Å3/Da / Density % sol: 67.03 % / Description: Orthogonal plate |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.4 / Details: 3.5M sodium formate (pH 7.4) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 1, 2012 |
Radiation | Monochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.82→50 Å / Num. obs: 65862 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.5 % / Biso Wilson estimate: 23.509975769 Å2 / Rmerge(I) obs: 0.05 / Rsym value: 0.05 / Net I/av σ(I): 30.2 / Net I/σ(I): 14.1 |
Reflection shell | Resolution: 1.82→1.89 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.258 / Rsym value: 0.258 / % possible all: 99.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1XEW Resolution: 1.82194772804→34.5967717027 Å / SU ML: 0.18789881426 / Cross valid method: FREE R-VALUE / σ(F): 1.33778337783 / Phase error: 23.7348302365
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.5291876369 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.82194772804→34.5967717027 Å
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Refine LS restraints |
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LS refinement shell |
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