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Yorodumi- PDB-4mvm: Structural Basis for Ca2+ Selectivity of a Voltage-gated Calcium ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4mvm | ||||||
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Title | Structural Basis for Ca2+ Selectivity of a Voltage-gated Calcium Channel | ||||||
Components | Ion transport proteinIon transporter | ||||||
Keywords | METAL TRANSPORT / Tetrameric / Voltage-gated Ion Channel / Voltage-gated Calcium Channel / Calcium Selective / Transport Protein / Membrane | ||||||
Function / homology | Function and homology information monoatomic cation channel activity / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Arcobacter butzleri (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1997 Å | ||||||
Authors | Tang, L. / Gamal El-Din, T.M. / Payandeh, J. / Martinez, G.Q. / Heard, T.M. / Scheuer, T. / Zheng, N. / Catterall, W.A. | ||||||
Citation | Journal: Nature / Year: 2014 Title: Structural basis for Ca2+ selectivity of a voltage-gated calcium channel. Authors: Tang, L. / Gamal El-Din, T.M. / Payandeh, J. / Martinez, G.Q. / Heard, T.M. / Scheuer, T. / Zheng, N. / Catterall, W.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4mvm.cif.gz | 197.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4mvm.ent.gz | 156.2 KB | Display | PDB format |
PDBx/mmJSON format | 4mvm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mv/4mvm ftp://data.pdbj.org/pub/pdb/validation_reports/mv/4mvm | HTTPS FTP |
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-Related structure data
Related structure data | 4ms2C 4mtfC 4mtgC 4mtoC 4mvoC 4mvqC 4mvrC 4mvsC 4mvuC 4mvzC 4mw3C 4mw8C 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 27457.590 Da / Num. of mol.: 4 / Fragment: Voltage-gated Calcium Channel (Residues 1-219) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arcobacter butzleri (bacteria) / Strain: RM4018 / Gene: Abu_1752 / Plasmid: PFASTBAC DUAL / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: A8EVM5 #2: Chemical | ChemComp-PX4 / #3: Chemical | ChemComp-CA / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.75 Details: CHAPSO:DMPC BICELLES,0.1M Na-Acetate ,pH4.75, 2M Ammonium Sulfate, 28% Glucose, 10mM Calcium Chloride., VAPOR DIFFUSION, HANGING DROP, temperature 298K |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1.75 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 15, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.75 Å / Relative weight: 1 |
Reflection | Resolution: 3.1997→30 Å / Num. all: 47534 / Num. obs: 47534 / % possible obs: 96.6 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 5.1 % / Rmerge(I) obs: 0.901 |
Reflection shell | Resolution: 3.1997→3.37 Å / % possible all: 98.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.1997→29.879 Å / SU ML: 0.39 / σ(F): 0.96 / Phase error: 28.37 / 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: 3.1997→29.879 Å
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Refine LS restraints |
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LS refinement shell |
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