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Open data
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Basic information
Entry | Database: PDB / ID: 6ada | ||||||
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Title | Crystal structure of the E148D mutant CLC-ec1 in 200mM bromide | ||||||
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![]() | TRANSPORT PROTEIN / CLC Cl-/H+ antiporter / intermediate structure / external glutamate | ||||||
Function / homology | ![]() 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 | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Lim, H.-H. / Park, K. | ||||||
Funding support | ![]()
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![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 335.8 KB | Display | ![]() |
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PDB format | ![]() | 270.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 61.2 KB | Display | |
Data in CIF | ![]() | 83.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ad7C ![]() 6ad8C ![]() 6adbC ![]() 6adcC ![]() 6k5aC ![]() 6k5dC ![]() 6k5fC ![]() 6k5iC ![]() 4eneS S: Starting model for refinement C: citing same article ( |
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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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: LYS / Beg label comp-ID: LYS / End auth comp-ID: ALA / End label comp-ID: ALA / Auth seq-ID: 30 - 450 / Label seq-ID: 30 - 450
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Components
#1: Protein | Mass: 50376.375 Da / Num. of mol.: 2 / Mutation: E148D Source method: isolated from a genetically manipulated source Details: SF file contains Friedel pairs. Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: clcA, eriC, yadQ, b0155, JW5012 / Production host: ![]() ![]() #2: Antibody | Mass: 23823.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Antibody | Mass: 23088.443 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #4: Chemical | ChemComp-BR / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.92 Å3/Da / Density % sol: 68.61 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: PEG400 26%(w/v), 100mM tris-SO4, 200mM NaBr |
-Data collection
Diffraction | Mean temperature: 80 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 12, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.919 Å / Relative weight: 1 |
Reflection | Resolution: 3.15→50 Å / Num. obs: 98122 / % possible obs: 99.5 % / Redundancy: 6.3 % / Biso Wilson estimate: 87.47 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 18.1 |
Reflection shell | Resolution: 3.15→3.26 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 2.5 / Num. unique obs: 9800 / % possible all: 98.2 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4ENE Resolution: 3.153→33.969 Å / SU ML: 0.49 / Cross valid method: THROUGHOUT / σ(F): 0.07 / Phase error: 33.23
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 195.05 Å2 / Biso mean: 92.4991 Å2 / Biso min: 46.85 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 3.153→33.969 Å
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Refine LS restraints NCS |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30
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