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- PDB-2xzr: Escherichia coli Immunoglobulin-binding protein EibD 391-438 FUSE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xzr | ||||||
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Title | Escherichia coli Immunoglobulin-binding protein EibD 391-438 FUSED TO GCN4 ADAPTORS | ||||||
![]() | IMMUNOGLOBULIN-BINDING PROTEIN EIBD | ||||||
![]() | CELL ADHESION / TRIMERIC AUTOTRANSPORTER ADHESIN / TAA / PROTEIN EXPORT | ||||||
Function / homology | ![]() protein secretion by the type V secretion system / cell outer membrane / cell surface / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hartmann, M.D. / Hernandez Alvarez, B. / Ridderbusch, O. / Deiss, S. / Lupas, A.N. | ||||||
![]() | ![]() Title: The Structure of E. Coli Igg-Binding Protein D Suggests a General Model for Bending and Binding in Trimeric Autotransporter Adhesins. Authors: Leo, J.C. / Lyskowski, A. / Hattula, K. / Hartmann, M.D. / Schwarz, H. / Butcher, S.J. / Linke, D. / Lupas, A.N. / Goldman, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 58.7 KB | Display | ![]() |
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PDB format | ![]() | 44.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 419.3 KB | Display | ![]() |
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Full document | ![]() | 419.2 KB | Display | |
Data in XML | ![]() | 6.1 KB | Display | |
Data in CIF | ![]() | 7.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xqhC ![]() 2wpqS C: citing same article ( S: Starting model for refinement |
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Similar 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: 13552.596 Da / Num. of mol.: 1 / Fragment: RESIDUES 391-438 Source method: isolated from a genetically manipulated source Details: N- AND C-TERMINAL IN-REGISTER FUSION TO GCN4 ADAPTORS Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-CL / #3: Water | ChemComp-HOH / | Sequence details | MKQIEDKIEEILSKIYHIENEIARIKKLI IS AN N-TERMINAL TAG BASED ON THE SEQUENCE OF A GCN4 ADAPTOR DOMAIN. ...MKQIEDKIEE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.5 Å3/Da / Density % sol: 64 % / Description: NONE |
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Crystal grow | pH: 7.5 Details: 20% (V/V) 2-PROPANOL, 200 MM SODIUM CITRATE, 100 MM HEPES PH 7.5. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→38.1 Å / Num. obs: 4931 / % possible obs: 98.8 % / Observed criterion σ(I): -3 / Redundancy: 2.81 % / Biso Wilson estimate: 49.2 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 9.77 |
Reflection shell | Resolution: 2.8→2.97 Å / Redundancy: 2.92 % / Rmerge(I) obs: 0.25 / Mean I/σ(I) obs: 4.09 / % possible all: 99.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2WPQ Resolution: 2.8→38.1 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.913 / SU B: 36.008 / SU ML: 0.308 / Cross valid method: THROUGHOUT / ESU R: 0.765 / ESU R Free: 0.402 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.006 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→38.1 Å
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Refine LS restraints |
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