+
Open data
-
Basic information
Entry | Database: PDB / ID: 3ety | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Crystal structure of bacterial adhesin FadA L14A mutant | |||||||||
![]() | Adhesin A | |||||||||
![]() | 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![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() ![]() | |||||||||
![]() | Nithianantham, S. / Xu, M. / Wu, N. / Shoham, M. / Han, Y.W. | |||||||||
![]() | ![]() 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: ![]() 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 32.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 22 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 429.2 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 431.6 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Data in CIF | ![]() | 7.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3etwSC ![]() 3etxC ![]() 3etzC S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 13627.759 Da / Num. of mol.: 1 / Mutation: L14A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.16 Å3/Da / Density % sol: 61.11 % |
---|---|
Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.1M Sodium citrate pH 7.0, 0.5M potassium thiocyanate, and 5% dioxane, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: SBC-3 / Detector: CCD / Date: Mar 1, 2006 / 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: 0.96112 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→32.3 Å / Num. all: 3823 / Num. obs: 3801 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Biso Wilson estimate: 71.9 Å2 / Rmerge(I) obs: 0.088 / Χ2: 0.946 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.453 / Mean I/σ(I) obs: 2 / Num. unique all: 374 / Χ2: 0.725 / % possible all: 32.3 |
-Phasing
Phasing | Method: ![]() |
---|
-
Processing
Software |
| ||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 3ETW Resolution: 2.9→32.3 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.77 / Isotropic thermal model: Restrained / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||||||||||||||
Solvent computation | Bsol: 39.331 Å2 | ||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 106.9 Å2 / Biso mean: 64.589 Å2 / Biso min: 24.02 Å2
| ||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→32.3 Å
| ||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.9→3.03 Å /
| ||||||||||||||||||||||||||||||||
Xplor file |
|