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Yorodumi- PDB-4kkl: Structure of the E148A mutant of CLC-ec1 delta NC construct in 10... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4kkl | ||||||
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Title | Structure of the E148A mutant of CLC-ec1 delta NC construct in 100mM fluoride | ||||||
Components |
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Keywords | tranport protein / membrane protein / membrane transporter | ||||||
Function / homology | Function and homology information chloride:proton antiporter activity / cellular stress response to acidic pH / voltage-gated chloride channel activity / chloride transmembrane transport / proton transmembrane transport / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å | ||||||
Authors | Stockbridge, R.B. / Lim, H.-H. / Miller, C. | ||||||
Citation | Journal: Nat.Chem.Biol. / Year: 2013 Title: Fluoride-dependent interruption of the transport cycle of a CLC Cl(-)/H(+) antiporter. Authors: Lim, H.H. / Stockbridge, R.B. / Miller, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4kkl.cif.gz | 327 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4kkl.ent.gz | 274.4 KB | Display | PDB format |
PDBx/mmJSON format | 4kkl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kk/4kkl ftp://data.pdbj.org/pub/pdb/validation_reports/kk/4kkl | HTTPS FTP |
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-Related structure data
Related structure data | 4kjpC 4kjqC 4kjwC 4kk5C 4kk6C 4kk8C 4kk9C 4kkaC 4kkbC 4kkcC C: citing same article (ref.) |
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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: 47560.367 Da / Num. of mol.: 2 / Fragment: unp residues 17-460 / Mutation: E148A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: clcA, eriC, yadQ, b0155, JW5012 / Production host: Escherichia coli (E. coli) / References: UniProt: P37019 #2: Antibody | Mass: 23823.031 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Cell line (production host): hybridoma / Production host: MUS MUSCULUS (house mouse) #3: Antibody | Mass: 23088.443 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Cell line (production host): hybridoma / Production host: MUS MUSCULUS (house mouse) #4: Chemical | ChemComp-F / |
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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: 3.89 Å3/Da / Density % sol: 68.36 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 22% PEG400, 50mM Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 77 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD |
Radiation | Monochromator: Double crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.85→25 Å / Num. all: 71808 / Num. obs: 71781 / % possible obs: 99.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.85→25 Å / SU ML: 0.42 / σ(F): 1.35 / Phase error: 34.4 / 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.85→25 Å
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Refine LS restraints |
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LS refinement shell |
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