[English] 日本語
Yorodumi- PDB-1wck: Crystal structure of the C-terminal domain of BclA, the major ant... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wck | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of the C-terminal domain of BclA, the major antigen of the exosporium of the Bacillus anthracis spore. | ||||||
Components | BCLA PROTEIN | ||||||
Keywords | STRUCTURAL PROTEIN / COLLAGEN-LIKE PROTEIN / BACTERIAL SURFACE ANTIGEN / JELLY-ROLL TOPOLOGY | ||||||
Function / homology | Function and homology information extracellular matrix structural constituent conferring tensile strength / extracellular matrix organization / extracellular space Similarity search - Function | ||||||
Biological species | BACILLUS ANTHRACIS (anthrax bacterium) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 1.36 Å | ||||||
Authors | Rety, S. / Salamitou, S. / Augusto, L.A. / Chaby, R. / Lehegarat, F. / Lewit-Bentley, A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: The Crystal Structure of the Bacillus Anthracis Spore Surface Protein Bcla Shows Remarkable Similarity to Mammalian Proteins. Authors: Rety, S. / Salamitou, S. / Garcia-Verdugo, I. / Hulmes, D.J. / Lehegarat, F. / Chaby, R. / Lewit-Bentley, A. | ||||||
History |
| ||||||
Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1wck.cif.gz | 40.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1wck.ent.gz | 30.3 KB | Display | PDB format |
PDBx/mmJSON format | 1wck.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1wck_validation.pdf.gz | 438.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1wck_full_validation.pdf.gz | 439.4 KB | Display | |
Data in XML | 1wck_validation.xml.gz | 9.8 KB | Display | |
Data in CIF | 1wck_validation.cif.gz | 13.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wc/1wck ftp://data.pdbj.org/pub/pdb/validation_reports/wc/1wck | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||||||||||
Unit cell |
| ||||||||||||||||||||||||
Components on special symmetry positions |
|
-Components
#1: Protein | Mass: 21397.006 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACILLUS ANTHRACIS (anthrax bacterium) / Strain: CEB 9732 / Plasmid: PET9SNI / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): ROSETTA / References: UniProt: Q83WA5, UniProt: Q83WB0*PLUS |
---|---|
#2: Chemical | ChemComp-CAC / |
#3: Water | ChemComp-HOH / |
Sequence details | THE STRAIN USED IN THIS WORK HAS NOT BEEN DEPOSITED WITH A SEQUENCE DATABASE, BUT IS EXTREMELY ...THE STRAIN USED IN THIS WORK HAS NOT BEEN DEPOSITED WITH A SEQUENCE DATABASE, BUT IS EXTREMELY CLOSE TO UNIPROT ENTRY Q83WA5. ALL SEQUENCE DIFFERENCE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.1 % |
---|---|
Crystal grow | Method: vapor diffusion Details: 20% PEG 4000, 20% ISOPROPANOL, 0.1M NA-CACODYLATE PH = 6.5, 10 MG/ML PROTEIN, VAPOUR DIFFUSION TECHNIQUE |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 30, 2004 / Details: MIRRORS |
Radiation | Monochromator: CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.36→40 Å / Num. obs: 48836 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 18.5 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 35.4 |
Reflection shell | Resolution: 1.36→1.45 Å / Redundancy: 9.9 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 4.24 / % possible all: 96 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: SIRAS / Resolution: 1.36→81.65 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.969 / SU B: 0.669 / SU ML: 0.027 / Cross valid method: THROUGHOUT / ESU R: 0.042 / ESU R Free: 0.042 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 79 N-TERMINAL RESIDUES AND 5 C-TERMINAL RESIDUES (HIS-TAG) ARE DISORDERED
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 17.98 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.36→81.65 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|