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Yorodumi- PDB-2m7x: Structural and Functional Analysis of Transmembrane Segment IV of... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2m7x | ||||||
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Title | Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2 | ||||||
Components | Na(+)/H(+) antiporter | ||||||
Keywords | MEMBRANE PROTEIN / sod2 / transmembrane | ||||||
Function / homology | Function and homology information plasma membrane of cell tip / intracellular pH reduction / prospore membrane / sodium:proton antiporter activity / perinuclear endoplasmic reticulum membrane / sodium ion export across plasma membrane / intracellular potassium ion homeostasis / intracellular sodium ion homeostasis / nuclear outer membrane-endoplasmic reticulum membrane network / plasma membrane => GO:0005886 ...plasma membrane of cell tip / intracellular pH reduction / prospore membrane / sodium:proton antiporter activity / perinuclear endoplasmic reticulum membrane / sodium ion export across plasma membrane / intracellular potassium ion homeostasis / intracellular sodium ion homeostasis / nuclear outer membrane-endoplasmic reticulum membrane network / plasma membrane => GO:0005886 / sodium ion transmembrane transport / proton transmembrane transport / plasma membrane Similarity search - Function | ||||||
Biological species | Schizosaccharomyces pombe (fission yeast) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Ullah, A. / Kemp, G. / Lee, B. / Alves, C. / Young, H. / Sykes, B.D. / Fliegel, L. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2013 Title: Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2. Authors: Ullah, A. / Kemp, G. / Lee, B. / Alves, C. / Young, H. / Sykes, B.D. / Fliegel, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m7x.cif.gz | 224 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m7x.ent.gz | 186.6 KB | Display | PDB format |
PDBx/mmJSON format | 2m7x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2m7x_validation.pdf.gz | 468 KB | Display | wwPDB validaton report |
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Full document | 2m7x_full_validation.pdf.gz | 600.5 KB | Display | |
Data in XML | 2m7x_validation.xml.gz | 15.4 KB | Display | |
Data in CIF | 2m7x_validation.cif.gz | 23.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m7/2m7x ftp://data.pdbj.org/pub/pdb/validation_reports/m7/2m7x | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3992.854 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schizosaccharomyces pombe (fission yeast) Strain: 972 / ATCC 24843 / Description: Maltose Binding Protein fusion / Gene: sod2, SPAC977.10 / Production host: Escherichia coli (E. coli) / Strain (production host): XL1-Blue / References: UniProt: P36606 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: NMR solution model of transmembrane segment IV Sod2 in organic solvent | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.2-0.7 mM [U-99% 15N] Sod2, 50 v/v CDCl3, 50 v/v 2-propanol, CDCl3/2-propanol Solvent system: CDCl3/2-propanol | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: not measured / Pressure: ambient / Temperature: 303.15 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 25 |