+Open data
-Basic information
Entry | Database: PDB / ID: 5j9p | ||||||
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Title | KcsA in vitro | ||||||
Components |
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Keywords | METAL TRANSPORT / Membrane Protein / Ion Channel / In vitro | ||||||
Function / homology | Function and homology information monoatomic ion transmembrane transport / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Streptomyces lividans (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.85 Å | ||||||
Authors | Matulef, K. / Valiyaveetil, F.I. | ||||||
Funding support | United States, 1items
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Citation | Journal: Biochemistry / Year: 2016 Title: Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression. Authors: Focke, P.J. / Hein, C. / Hoffmann, B. / Matulef, K. / Bernhard, F. / Dotsch, V. / Valiyaveetil, F.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5j9p.cif.gz | 110.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5j9p.ent.gz | 88.6 KB | Display | PDB format |
PDBx/mmJSON format | 5j9p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j9/5j9p ftp://data.pdbj.org/pub/pdb/validation_reports/j9/5j9p | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Antibody | Mass: 23411.242 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Cell line (production host): Hybridoma Cells / Production host: Mus musculus (house mouse) | ||
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#2: Antibody | Mass: 23435.738 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Cell line (production host): Hybridoma Cells / Production host: Mus musculus (house mouse) | ||
#3: Protein | Mass: 10092.809 Da / Num. of mol.: 1 / Fragment: UNP residues 22-117 / Source method: obtained synthetically / Source: (synth.) Streptomyces lividans (bacteria) / References: UniProt: P0A334 | ||
#4: Chemical | ChemComp-K / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.98 Å3/Da / Density % sol: 69.1 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: PEG400 |
-Data collection
Diffraction | Mean temperature: 80 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: RDI CMOS_8M / Detector: CMOS / Date: Feb 9, 2014 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.85→50.962 Å / Num. all: 21104 / Num. obs: 21104 / % possible obs: 100 % / Redundancy: 7.6 % / Biso Wilson estimate: 56.24 Å2 / Rpim(I) all: 0.073 / Rrim(I) all: 0.202 / Rsym value: 0.188 / Net I/av σ(I): 3.717 / Net I/σ(I): 11.7 / Num. measured all: 160009 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: 0
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-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.85→42.638 Å / SU ML: 0.46 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 29.18 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 140.23 Å2 / Biso mean: 64.2734 Å2 / Biso min: 16.17 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.85→42.638 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14
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