+Open data
-Basic information
Entry | Database: PDB / ID: 2jpx | ||||||
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Title | A18H Vpu TM structure in lipid bilayers | ||||||
Components | Vpu protein | ||||||
Keywords | VIRAL PROTEIN / A18H Vpu / trans-membrane / ion-channel / helix tilt / lipid bilayers | ||||||
Function / homology | Function and homology information receptor catabolic process / CD4 receptor binding / viral release from host cell / host cell membrane / monoatomic cation channel activity / suppression by virus of host tetherin activity / membrane => GO:0016020 / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / membrane Similarity search - Function | ||||||
Biological species | Human immunodeficiency virus 1 | ||||||
Method | SOLUTION NMR / structural fitting | ||||||
Authors | Park, S. / Opella, S.J. | ||||||
Citation | Journal: Protein Sci. / Year: 2007 Title: Conformational changes induced by a single amino acid substitution in the trans-membrane domain of Vpu: implications for HIV-1 susceptibility to channel blocking drugs Authors: Park, S.H. / Opella, S.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jpx.cif.gz | 44.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jpx.ent.gz | 22.2 KB | Display | PDB format |
PDBx/mmJSON format | 2jpx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2jpx_validation.pdf.gz | 318.4 KB | Display | wwPDB validaton report |
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Full document | 2jpx_full_validation.pdf.gz | 377.3 KB | Display | |
Data in XML | 2jpx_validation.xml.gz | 4.2 KB | Display | |
Data in CIF | 2jpx_validation.cif.gz | 7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jp/2jpx ftp://data.pdbj.org/pub/pdb/validation_reports/jp/2jpx | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3809.758 Da / Num. of mol.: 1 / Mutation: A18H Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Strain: BH 10 isolate / Gene: vpu / Production host: Escherichia coli (E. coli) / References: UniProt: Q76PP7, UniProt: P69699*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D 15N chemical shift/1H-15N dipolar coupling separated local field (SAMPI4) |
-Sample preparation
Details | Contents: 2 mg/mL [U-99% 15N] A18H Vpu TM, 100% H2O / Solvent system: 100% H2O |
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Sample | Conc.: 2 mg/mL / Component: A18H Vpu TM / Isotopic labeling: [U-99% 15N] |
Sample conditions | Ionic strength: 0 / pH: 4.0 / Pressure: ambient / Temperature: 313 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 750 MHz |
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-Processing
NMR software |
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Refinement | Method: structural fitting / Software ordinal: 1 Details: Nevzorov, A.A., and Opella, S.J. 2003. Structural fitting of PISEMA spectra of aligned proteins. J Magn Reson 160: 33-39. | |||||||||
NMR representative | Selection criteria: closest to the average | |||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 15 |