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Yorodumi- PDB-6k5i: Crystal structure of the E148D/R147A/F317A mutant CLC-ec1 in the ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6k5i | |||||||||
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Title | Crystal structure of the E148D/R147A/F317A mutant CLC-ec1 in the presence of 20 mM NaBr | |||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Cl-/H+ antiporter / CLC transporter | |||||||||
Function / homology | Function and homology information voltage-gated chloride channel activity / antiporter activity / plasma membrane Similarity search - Function | |||||||||
Biological species | Escherichia coli MS 117-3 (bacteria) Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.022 Å | |||||||||
Authors | Park, K. / Lim, H.H. | |||||||||
Funding support | Korea, Republic Of, 2items
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2019 Title: Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC Cl-/H+antiporter. Authors: Park, K. / Lee, B.C. / Lim, H.H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6k5i.cif.gz | 333.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6k5i.ent.gz | 269.8 KB | Display | PDB format |
PDBx/mmJSON format | 6k5i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k5/6k5i ftp://data.pdbj.org/pub/pdb/validation_reports/k5/6k5i | HTTPS FTP |
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-Related structure data
Related structure data | 6ad7C 6ad8C 6adaC 6adbC 6adcC 6k5aC 6k5dC 6k5fC 4eneS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 50214.168 Da / Num. of mol.: 2 / Mutation: R147A, E148D, F317A Source method: isolated from a genetically manipulated source Details: SF file contains Friedel pairs. / Source: (gene. exp.) Escherichia coli MS 117-3 (bacteria) / Gene: clcA, eriC, HMPREF9542_03540 / Production host: Escherichia coli (E. coli) / References: UniProt: E9TIA0 #2: Antibody | Mass: 23823.031 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: SF file contains Friedel pairs. / Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) #3: Antibody | Mass: 23088.443 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: SF file contains Friedel pairs. / Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) #4: Chemical | |
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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: 3.74 Å3/Da / Density % sol: 67.11 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 400 23% (v/v), 20 mM Na/K tartrate, 100 mM Tris-SO4 |
-Data collection
Diffraction | Mean temperature: 77.36 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 5C (4A) / Wavelength: 0.92 Å |
Detector | Type: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Apr 2, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 3.02→42.9 Å / Num. obs: 109854 / % possible obs: 99.9 % / Redundancy: 3.5 % / CC1/2: 0.96 / Rmerge(I) obs: 0.074 / Net I/σ(I): 20.2 |
Reflection shell | Resolution: 3.02→3.07 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.569 / Mean I/σ(I) obs: 1.69 / Num. unique obs: 5476 / CC1/2: 0.813 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4ENE Resolution: 3.022→42.886 Å / SU ML: 0.44 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 28.81
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.022→42.886 Å
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Refine LS restraints |
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LS refinement shell |
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