+Open data
-Basic information
Entry | Database: PDB / ID: 3etx | |||||||||
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Title | Crystal structure of bacterial adhesin FadA L14A mutant | |||||||||
Components | Adhesin A | |||||||||
Keywords | CELL ADHESION / antiparallel helix-loop-helix / FadA L14A mutant / Cell adhesin | |||||||||
Function / homology | Adhesion protein FadA / Adhesion protein FadA / Helix Hairpins - #1700 / Helix Hairpins / Orthogonal Bundle / Mainly Alpha / Adhesion A Function and homology information | |||||||||
Biological species | Fusobacterium nucleatum (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | |||||||||
Authors | Nithianantham, S. / Xu, M. / Wu, N. / Shoham, M. / Han, Y.W. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2009 Title: Crystal Structure of FadA Adhesin from Fusobacterium nucleatum Reveals a Novel Oligomerization Motif, the Leucine Chain. Authors: Nithianantham, S. / Xu, M. / Yamada, M. / Ikegami, A. / Shoham, M. / Han, Y.W. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2006 Title: Crystallization and preliminary X-ray data of the FadA adhesin from Fusobacterium nucleatum Authors: Nithianantham, S. / Xu, M. / Wu, N. / Han, Y.W. / Shoham, M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3etx.cif.gz | 76.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3etx.ent.gz | 57.9 KB | Display | PDB format |
PDBx/mmJSON format | 3etx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/et/3etx ftp://data.pdbj.org/pub/pdb/validation_reports/et/3etx | HTTPS FTP |
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-Related structure data
Related structure data | 3etwSC 3etyC 3etzC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain: (Details: chain A,B,C, using restrain) |
-Components
#1: Protein | Mass: 13627.759 Da / Num. of mol.: 3 / Mutation: L14A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Fusobacterium nucleatum (bacteria) / Gene: fadA / Plasmid: pET21(b) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q5I6B0 #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: 4.39 Å3/Da / Density % sol: 72 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1M Imidazole pH 7.5, and 0.5M sodium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.97934 Å |
Detector | Type: SBC-2 / Detector: CCD / Date: Mar 25, 2005 / Details: 3 x 3 mosaic |
Radiation | Monochromator: Double crystal (Si-111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97934 Å / Relative weight: 1 |
Reflection | Resolution: 3→38.8 Å / Num. all: 14001 / Num. obs: 13703 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 62.6 Å2 / Rmerge(I) obs: 0.097 / Χ2: 0.898 |
Reflection shell | Resolution: 3→3.11 Å / Redundancy: 3 % / Rmerge(I) obs: 0.426 / Mean I/σ(I) obs: 2.4 / Num. unique all: 1284 / Χ2: 0.839 / % possible all: 93.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3ETW Resolution: 3→38.8 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.778 / Isotropic thermal model: Restrained / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 50.81 Å2 | ||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 118.33 Å2 / Biso mean: 68.09 Å2 / Biso min: 23.02 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3→38.8 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell | Resolution: 3→3.04 Å /
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Xplor file |
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