[English] 日本語
![](img/lk-miru.gif)
- PDB-4uyr: X-ray structure of the N-terminal domain of the flocculin Flo11 f... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 4uyr | ||||||
---|---|---|---|---|---|---|---|
Title | X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae | ||||||
![]() | FLOCCULATION PROTEIN FLO11 | ||||||
![]() | CELL ADHESION / SACCHAROMYCES CEREVISIAE / FLO11 / ADHESIN / FLOCCULATION / HYDROPHOBIC PATCHES / HOMOTYPIC BINDING | ||||||
Function / homology | ![]() cell-cell self recognition / single-species surface biofilm formation / flocculation / pseudohyphal growth / homotypic cell-cell adhesion / invasive growth in response to glucose limitation / filamentous growth / cellular bud neck / cell adhesion involved in single-species biofilm formation / fungal-type vacuole ...cell-cell self recognition / single-species surface biofilm formation / flocculation / pseudohyphal growth / homotypic cell-cell adhesion / invasive growth in response to glucose limitation / filamentous growth / cellular bud neck / cell adhesion involved in single-species biofilm formation / fungal-type vacuole / side of membrane / cell-cell adhesion / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Veelders, M. / Kraushaar, T. / Brueckner, S. / Rhinow, D. / Moesch, H.U. / Essen, L.O. | ||||||
![]() | ![]() Title: Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-Like Adhesin Domain Girdled by Aromatic Bands. Authors: Kraushaar, T. / Bruckner, S. / Veelders, M. / Rhinow, D. / Schreiner, F. / Birke, R. / Pagenstecher, A. / Mosch, H. / Essen, L. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 99.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 81 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 437.3 KB | Display | |
Data in XML | ![]() | 12.2 KB | Display | |
Data in CIF | ![]() | 18.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 23748.949 Da / Num. of mol.: 1 / Fragment: FLO11 DOMAIN, UNP RESIDUES 22-211 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: S288C / Description: GERMAN COLLECTION OF MICROORGANISMS (DSM) / Production host: ![]() ![]() | ||||||
---|---|---|---|---|---|---|---|
#2: Chemical | #3: Chemical | ChemComp-MG / | #4: Chemical | ChemComp-PO4 / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.06 % / Description: NONE |
---|---|
Crystal grow | pH: 7.5 Details: PROTEIN WAS CRYSTALLIZED FROM 30% PEG 400, 100 MM MGCL2, 100 MM NAHEPES, PH 7.5. |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 18, 2011 / Details: MIRRORS |
Radiation | Monochromator: SI(311) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.70847 Å / Relative weight: 1 |
Reflection | Resolution: 0.89→40.76 Å / Num. obs: 156350 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 5.1 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 13.1 |
Reflection shell | Resolution: 0.89→0.94 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.78 / Mean I/σ(I) obs: 2 / % possible all: 99.6 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 0.89→40.76 Å / Cor.coef. Fo:Fc: 0.98 / Cor.coef. Fo:Fc free: 0.98 / SU B: 0.374 / SU ML: 0.01 / Cross valid method: THROUGHOUT / ESU R: 0.013 / ESU R Free: 0.013 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.747 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 0.89→40.76 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|