+Open data
-Basic information
Entry | Database: PDB / ID: 3cs1 | ||||||
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Title | Flagellar Calcium-binding Protein (FCaBP) from T. cruzi | ||||||
Components | Flagellar calcium-binding protein | ||||||
Keywords | METAL BINDING PROTEIN / flagella / calcium-binding / myristoylated / palmitoylated / sensor / membrane targeting / EF-hand / Cell projection / Cilium / Flagellum | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Trypanosoma cruzi (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SAD / Resolution: 2 Å | ||||||
Authors | Ames, J.B. / Ladner, J.E. / Wingard, J.N. / Robinson, H. / Fisher, A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2008 Title: Structural Insights into Membrane Targeting by the Flagellar Calcium-binding Protein (FCaBP), a Myristoylated and Palmitoylated Calcium Sensor in Trypanosoma cruzi. Authors: Wingard, J.N. / Ladner, J. / Vanarotti, M. / Fisher, A.J. / Robinson, H. / Buchanan, K.T. / Engman, D.M. / Ames, J.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3cs1.cif.gz | 50.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3cs1.ent.gz | 39.1 KB | Display | PDB format |
PDBx/mmJSON format | 3cs1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3cs1_validation.pdf.gz | 429.9 KB | Display | wwPDB validaton report |
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Full document | 3cs1_full_validation.pdf.gz | 432 KB | Display | |
Data in XML | 3cs1_validation.xml.gz | 10 KB | Display | |
Data in CIF | 3cs1_validation.cif.gz | 13 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cs/3cs1 ftp://data.pdbj.org/pub/pdb/validation_reports/cs/3cs1 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 24955.055 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma cruzi (eukaryote) / Gene: FCABP / Plasmid: pET23d / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P07749 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.76 Å3/Da / Density % sol: 29.92 % |
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Crystal grow | Temperature: 298 K / pH: 6 Details: well solution: 2.88M ammonium sulfate, 0.09M MES pH 6.0, 0.075 magnesium chloride, 0.01M sodium acetate pH 4.6., hanging drop vapor diffusion, temperature 298K, pH 6.00 |
-Data collection
Diffraction | Mean temperature: 105 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Jan 1, 2005 |
Radiation | Monochromator: MSC BLUE CONFOCAL OPTICS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→29.84 Å / Num. obs: 12558 / % possible obs: 99.8 % |
Reflection shell | Resolution: 2→2.07 Å / Rmerge(I) obs: 0.308 / Mean I/σ(I) obs: 4.1 / % possible all: 97.9 |
-Phasing
Phasing | Method: SAD |
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-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2→20 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.904 / SU B: 12.718 / SU ML: 0.179 / TLS residual ADP flag: LIKELY RESIDUAL / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31 Å2
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.11 Å
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Refinement TLS params. | Method: refined / Origin x: 13.0352 Å / Origin y: -1.4832 Å / Origin z: -16.7111 Å
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