+Open data
-Basic information
Entry | Database: PDB / ID: 5ec1 | ||||||
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Title | KcsA with V76ester mutation | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / alpha helical / channel / Fab | ||||||
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 / Resolution: 2.75 Å | ||||||
Model details | mutant1 | ||||||
Authors | Matulef, K. / Valiyaveetil, F.I. | ||||||
Funding support | United States, 1items
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Citation | Journal: Structure / Year: 2016 Title: Individual Ion Binding Sites in the K(+) Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation. Authors: Matulef, K. / Annen, A.W. / Nix, J.C. / 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 | 5ec1.cif.gz | 119.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ec1.ent.gz | 87.6 KB | Display | PDB format |
PDBx/mmJSON format | 5ec1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ec/5ec1 ftp://data.pdbj.org/pub/pdb/validation_reports/ec/5ec1 | HTTPS FTP |
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-Related structure data
Related structure data | 5eblC 5ebmC 5ebwC 5ec2C 1k4cS 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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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules C
#3: Protein | Mass: 13297.735 Da / Num. of mol.: 1 / Fragment: UNP residues 1-125 / Mutation: V76ester Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces lividans (bacteria) / Gene: kcsA, skc1 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A334 |
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-Antibody , 2 types, 2 molecules AB
#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 / Production host: Mus musculus (house mouse) |
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#2: Antibody | Mass: 23050.340 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 / Production host: Mus musculus (house mouse) |
-Non-polymers , 4 types, 24 molecules
#4: Chemical | ChemComp-F09 / | ||
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#5: Chemical | ChemComp-DGA / | ||
#6: Chemical | ChemComp-K / #7: 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: 4 Å3/Da / Density % sol: 69.23 % |
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Crystal grow | Temperature: 291 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: Jun 3, 2015 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.75→55.013 Å / Num. all: 23691 / Num. obs: 23691 / % possible obs: 100 % / Redundancy: 14.6 % / Biso Wilson estimate: 54.47 Å2 / Rmerge(I) obs: 0.204 / Rpim(I) all: 0.055 / Rrim(I) all: 0.212 / Rsym value: 0.204 / Net I/av σ(I): 3.687 / Net I/σ(I): 13.4 / Num. measured all: 344861 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: 0
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1K4C Resolution: 2.75→42.776 Å / FOM work R set: 0.7706 / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 29.73 / 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: 112.97 Å2 / Biso mean: 36.25 Å2 / Biso min: 0.05 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.75→42.776 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: 16
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