+Open data
-Basic information
Entry | Database: PDB / ID: 4g1j | ||||||
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Title | Sortase C1 of GBS Pilus Island 1 | ||||||
Components | Sortase family protein | ||||||
Keywords | TRANSFERASE / CYSTEINE PROTEASE / EXTRACELLULAR | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Streptococcus agalactiae serogroup V (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | ||||||
Authors | Cozzi, R. / Prigozhin, D.M. / Alber, T. | ||||||
Citation | Journal: Plos One / Year: 2012 Title: Structural basis for group B streptococcus pilus 1 sortases C regulation and specificity. Authors: Cozzi, R. / Prigozhin, D. / Rosini, R. / Abate, F. / Bottomley, M.J. / Grandi, G. / Telford, J.L. / Rinaudo, C.D. / Maione, D. / Alber, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4g1j.cif.gz | 95.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4g1j.ent.gz | 73.9 KB | Display | PDB format |
PDBx/mmJSON format | 4g1j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4g1j_validation.pdf.gz | 419.6 KB | Display | wwPDB validaton report |
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Full document | 4g1j_full_validation.pdf.gz | 422.3 KB | Display | |
Data in XML | 4g1j_validation.xml.gz | 19.4 KB | Display | |
Data in CIF | 4g1j_validation.cif.gz | 28.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g1/4g1j ftp://data.pdbj.org/pub/pdb/validation_reports/g1/4g1j | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 24818.207 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 42-263 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus agalactiae serogroup V (bacteria) Gene: SAG0647 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8E0S7 #2: 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: 2.1 Å3/Da / Density % sol: 41.41 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.1159 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 20, 2010 |
Radiation | Monochromator: DOUBLE FLAT CRYSTAL, SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1159 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→46.25 Å / Num. obs: 31194 / Biso Wilson estimate: 20.56 Å2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.75→46.25 Å / SU ML: 0.2 / σ(F): 0.16 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 40.31 Å2 / ksol: 0.34 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.58 Å2
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Refinement step | Cycle: LAST / Resolution: 1.75→46.25 Å
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Refine LS restraints |
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LS refinement shell |
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