+Open data
-Basic information
Entry | Database: PDB / ID: 1fi0 | ||||||
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Title | SOLUTION STRUCTURE OF HIV-1 VPR (13-33) PEPTIDE IN MICELLS | ||||||
Components | VPR PROTEIN | ||||||
Keywords | VIRAL PROTEIN / helix | ||||||
Function / homology | Function and homology information : / symbiont-mediated arrest of host cell cycle during G2/M transition / virion component => GO:0044423 / monoatomic ion transport / protein homooligomerization / viral penetration into host nucleus / host extracellular space / symbiont entry into host cell / cell cycle / DNA-templated transcription ...: / symbiont-mediated arrest of host cell cycle during G2/M transition / virion component => GO:0044423 / monoatomic ion transport / protein homooligomerization / viral penetration into host nucleus / host extracellular space / symbiont entry into host cell / cell cycle / DNA-templated transcription / host cell nucleus / regulation of DNA-templated transcription Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Engler, A. / Stangler, T. / Willbold, D. | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 2001 Title: Solution structure of human immunodeficiency virus type 1 Vpr(13-33) peptide in micelles. Authors: Engler, A. / Stangler, T. / Willbold, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fi0.cif.gz | 133.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fi0.ent.gz | 110.8 KB | Display | PDB format |
PDBx/mmJSON format | 1fi0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fi0_validation.pdf.gz | 346.8 KB | Display | wwPDB validaton report |
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Full document | 1fi0_full_validation.pdf.gz | 470.1 KB | Display | |
Data in XML | 1fi0_validation.xml.gz | 14.2 KB | Display | |
Data in CIF | 1fi0_validation.cif.gz | 21.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fi/1fi0 ftp://data.pdbj.org/pub/pdb/validation_reports/fi/1fi0 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2614.879 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The protein was chemically synthesized. The sequence is naturally found in Human immunodeficiency virus type 1 (RF/HAT isolate). References: UniProt: P05954 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
-Sample preparation
Details | Contents: 2.2mM Vpr(13-33); 100mM DPC; 90% H20, 10%D20 / Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 4 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Modified ab initio simulated annealing protocol which includes floating assignment of prochiral groups | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy Conformers calculated total number: 160 / Conformers submitted total number: 22 |