+Open data
-Basic information
Entry | Database: PDB / ID: 3zkw | ||||||
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Title | Periplasmic Binding Protein CeuE apo form | ||||||
Components | (ENTEROCHELIN UPTAKE PERIPLASMIC BINDING PROTEIN) x 2 | ||||||
Keywords | METAL BINDING PROTEIN / ENTEROBACTIN UPTAKE / SIDEROPHORE | ||||||
Function / homology | Function and homology information iron ion transport / outer membrane-bounded periplasmic space / metal ion binding Similarity search - Function | ||||||
Biological species | CAMPYLOBACTER JEJUNI (Campylobacter) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.71 Å | ||||||
Authors | Raines, D.J. / Moroz, O.V. / Wilson, K.S. / Duhme-Klair, A.K. | ||||||
Citation | Journal: Angew.Chem.Int.Ed.Engl. / Year: 2013 Title: Interactions of a Periplasmic Binding Protein with a Tetradentate Siderophore Mimic. Authors: Raines, D.J. / Moroz, O.V. / Wilson, K.S. / Duhme-Klair, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3zkw.cif.gz | 330.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3zkw.ent.gz | 269.1 KB | Display | PDB format |
PDBx/mmJSON format | 3zkw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3zkw_validation.pdf.gz | 446.9 KB | Display | wwPDB validaton report |
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Full document | 3zkw_full_validation.pdf.gz | 466.9 KB | Display | |
Data in XML | 3zkw_validation.xml.gz | 33.3 KB | Display | |
Data in CIF | 3zkw_validation.cif.gz | 45.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zk/3zkw ftp://data.pdbj.org/pub/pdb/validation_reports/zk/3zkw | HTTPS FTP |
-Related structure data
Related structure data | 5a1jC 2chuS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 31725.551 Da / Num. of mol.: 2 / Fragment: RESIDUES 44-330 Source method: isolated from a genetically manipulated source Details: N-TERMINAL TRUNCATION / Source: (gene. exp.) CAMPYLOBACTER JEJUNI (Campylobacter) / Plasmid: PET-YSBLIC / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q0P8Q4 #2: Protein | | Mass: 31725.551 Da / Num. of mol.: 1 / Fragment: RESIDUES 44-330 Source method: isolated from a genetically manipulated source Details: N-TERMINAL TRUNCATION / Source: (gene. exp.) CAMPYLOBACTER JEJUNI (Campylobacter) / Plasmid: PET-YSBLIC / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q0P8Q4 #3: 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: 2.46 Å3/Da / Density % sol: 49.9 % / Description: NONE |
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Crystal grow | pH: 5 Details: 0.1 M MIB (SODIUM MALONATE, IMIDAZOLE, BORIC ACID) BUFFER, PH 5, 25% (W/V) PEG 1500 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.976 |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 7, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.976 Å / Relative weight: 1 |
Reflection | Resolution: 1.69→14.7 Å / Num. obs: 95173 / % possible obs: 96.8 % / Observed criterion σ(I): 2 / Redundancy: 2.4 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 1.69→1.74 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 1.9 / % possible all: 95.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2CHU Resolution: 1.71→65.93 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.949 / SU B: 5.031 / SU ML: 0.078 / Cross valid method: THROUGHOUT / ESU R: 0.113 / ESU R Free: 0.11 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.407 Å2
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Refinement step | Cycle: LAST / Resolution: 1.71→65.93 Å
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Refine LS restraints |
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