+Open data
-Basic information
Entry | Database: PDB / ID: 1eoe | ||||||
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Title | CRYSTAL STRUCTURE OF THE V135R MUTANT OF A SHAKER T1 DOMAIN | ||||||
Components | POTASSIUM CHANNEL KV1.1 | ||||||
Keywords | MEMBRANE PROTEIN / POTASSIUM CHANNELS / APLYSIA KV1.1 / PROTON TRANSPORT | ||||||
Function / homology | Function and homology information monoatomic ion-gated channel activity / voltage-gated potassium channel activity / voltage-gated potassium channel complex / protein homooligomerization Similarity search - Function | ||||||
Biological species | Aplysia californica (California sea hare) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.704 Å | ||||||
Authors | Nanao, M.H. / Cushman, S.J. / Jahng, A.W. / DeRubeis, D. / Choe, S. / Pfaffinger, P.J. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2000 Title: Voltage dependent activation of potassium channels is coupled to T1 domain structure. Authors: Cushman, S.J. / Nanao, M.H. / Jahng, A.W. / DeRubeis, D. / Choe, S. / Pfaffinger, P.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eoe.cif.gz | 54.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eoe.ent.gz | 40.4 KB | Display | PDB format |
PDBx/mmJSON format | 1eoe.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eo/1eoe ftp://data.pdbj.org/pub/pdb/validation_reports/eo/1eoe | HTTPS FTP |
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-Related 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: 12155.516 Da / Num. of mol.: 1 / Fragment: SHAKER T1 DOMAIN / Mutation: V135R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aplysia californica (California sea hare) Plasmid: PET20 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q16968 |
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#2: 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: 2.73 Å3/Da / Density % sol: 54.92 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 30% Isopropanol, .1 M Hepes 7.5, .2 M MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 4K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / Details: Bixby, K.A., (1999) Nature Struct. Biol., 6, 38. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Sep 27, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. all: 15106 / Num. obs: 15106 / % possible obs: 92.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8 % / Biso Wilson estimate: 20.316 Å2 / Rmerge(I) obs: 0.078 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 1.7→1.73 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.234 / % possible all: 80.7 |
Reflection | *PLUS Num. measured all: 130025 |
-Processing
Software |
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Refinement | Resolution: 1.704→19.84 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: KONNERT-HENDRICKSON
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Refinement step | Cycle: LAST / Resolution: 1.704→19.84 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS σ(F): 0 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 22.5 Å2 | ||||||||||||||||||||
Refine LS restraints | *PLUS
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