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- PDB-4uys: X-ray structure of the N-terminal domain of the flocculin Flo11 f... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4uys | ||||||
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Title | X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae | ||||||
![]() | FLOCCULATION PROTEIN FLO11 | ||||||
![]() | CELL ADHESION / 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 | ![]() ![]() ![]() | ||||||
![]() | Kraushaar, T. / Veelders, M. / 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 95.3 KB | Display | ![]() |
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PDB format | ![]() | 77.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 420.1 KB | Display | ![]() |
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Full document | ![]() | 421.5 KB | Display | |
Data in XML | ![]() | 12 KB | Display | |
Data in CIF | ![]() | 18.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 20563.312 Da / Num. of mol.: 1 / Fragment: FLO11 DOMAIN, UNP RESIDUES 30-211 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: S288C / Description: GERMAN COLLECTION OF MICROORGANISMS (DSM) / Plasmid: PET28A / Production host: ![]() ![]() | ||||
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#2: Chemical | ChemComp-NA / #3: Chemical | ChemComp-MG / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.45 % / Description: NONE |
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Crystal grow | pH: 7.5 Details: PROTEIN WAS CRYSTALLIZED FROM 100 MM NAHEPES, PH 7.5, 100 MM MGCL2, 30% PEG 400, THEN SOAKED IN THIS CONDITION CONTAINING 50 MM CACL2 ADDITIONALLY FOR 5 MIN; FOR CRYOPROTECTION THE PROTEIN ...Details: PROTEIN WAS CRYSTALLIZED FROM 100 MM NAHEPES, PH 7.5, 100 MM MGCL2, 30% PEG 400, THEN SOAKED IN THIS CONDITION CONTAINING 50 MM CACL2 ADDITIONALLY FOR 5 MIN; FOR CRYOPROTECTION THE PROTEIN WAS SOAKED IN THE LATTER CONDITION CONTAINING 35% PEG 400 INSTEAD OF 30%. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 3, 2013 / Details: MIRRORS |
Radiation | Monochromator: KMC-1 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.799905 Å / Relative weight: 1 |
Reflection | Resolution: 1.05→28.5 Å / Num. obs: 85769 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 5.8 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 1.05→1.11 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 2.5 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
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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: 12.7 Å2
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Refinement step | Cycle: LAST / Resolution: 1.05→28.51 Å
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Refine LS restraints |
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