+Open data
-Basic information
Entry | Database: PDB / ID: 1vmp | ||||||
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Title | STRUCTURE OF THE ANTI-HIV CHEMOKINE VMIP-II | ||||||
Components | PROTEIN (ANTI-HIV CHEMOKINE MIP VII) | ||||||
Keywords | ANTIVIRAL PROTEIN / VMIP-II / CHEMOKINE / MONOMER / SARCOMA / HERPESVIRUS / HHV-8 / KAPOSI'S | ||||||
Function / homology | Function and homology information CXCR chemokine receptor binding / chemokine activity / immune response / protein-containing complex / extracellular space Similarity search - Function | ||||||
Biological species | Human herpesvirus 8 | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Liwang, A.C. / Wang, Z.-X. / Sun, Y. / Peiper, S.C. / Liwang, P.J. | ||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: The solution structure of the anti-HIV chemokine vMIP-II. Authors: Liwang, A.C. / Wang, Z.X. / Sun, Y. / Peiper, S.C. / Liwang, P.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1vmp.cif.gz | 35.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1vmp.ent.gz | 24.5 KB | Display | PDB format |
PDBx/mmJSON format | 1vmp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vm/1vmp ftp://data.pdbj.org/pub/pdb/validation_reports/vm/1vmp | HTTPS FTP |
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-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 | Mass: 8142.661 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human herpesvirus 8 / Genus: Rhadinovirus / Description: SYNTHETIC GENE / Plasmid: PET32A+ / Cell line (production host): BL21 / Production host: Escherichia coli (E. coli) / References: UniProt: Q98157 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: MEAN STRUCTURE. THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED VMIP-II |
-Sample preparation
Sample conditions | Ionic strength: 0.01 / pH: 5.4 / Pressure: 1 atm / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM XPLOR 3.1 ( BRUNGER) MODIFIED TO INCORPORATE COUPLING ...Details: THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM XPLOR 3.1 ( BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANTS (GARRETT EL AL. (1984) J. MAGN. RESON. SER. B 104, 99-103) AND A CONFORMATIONAL DATA BASE POTENTIAL ( KUSZEWSKI ET AL. (1996) PROTEIN SCI 5, 1067- 1080 AND (1997) J. MAGN. RESON. 125, 171-177). | ||||||||||||
NMR ensemble | Conformer selection criteria: MINIMIZED MEAN STRUCTURE / Conformers calculated total number: 30 / Conformers submitted total number: 1 |