+Open data
-Basic information
Entry | Database: PDB / ID: 1tiv | ||||||
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Title | STRUCTURAL STUDIES OF HIV-1 TAT PROTEIN | ||||||
Components | HIV-1 TRANSACTIVATOR PROTEIN | ||||||
Keywords | TRANSCRIPTION ACTIVATION | ||||||
Function / homology | Function and homology information viral gene expression / trans-activation response element binding / regulatory region RNA binding / positive regulation of viral transcription / protein serine/threonine phosphatase inhibitor activity / modulation by virus of host chromatin organization / symbiont-mediated suppression of host translation initiation / host cell nucleolus / actinin binding / negative regulation of peptidyl-threonine phosphorylation ...viral gene expression / trans-activation response element binding / regulatory region RNA binding / positive regulation of viral transcription / protein serine/threonine phosphatase inhibitor activity / modulation by virus of host chromatin organization / symbiont-mediated suppression of host translation initiation / host cell nucleolus / actinin binding / negative regulation of peptidyl-threonine phosphorylation / RNA-binding transcription regulator activity / cyclin binding / positive regulation of transcription elongation by RNA polymerase II / host cell cytoplasm / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / protein domain specific binding / virus-mediated perturbation of host defense response / DNA-templated transcription / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Human immunodeficiency virus 1 | ||||||
Method | SOLUTION NMR | ||||||
Authors | Bayer, P. / Kraft, M. / Frank, R. / Roesch, P. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Structural studies of HIV-1 Tat protein. Authors: Bayer, P. / Kraft, M. / Ejchart, A. / Westendorp, M. / Frank, R. / Rosch, P. #1: Journal: Science / Year: 1994 Title: Structure of the Equine Infectious Anemia Virus Tat Protein Authors: Willbold, D. / Rosin-Arbesfeld, R. / Sticht, H. / Frank, R. / Roesch, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tiv.cif.gz | 271.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tiv.ent.gz | 220.2 KB | Display | PDB format |
PDBx/mmJSON format | 1tiv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tiv_validation.pdf.gz | 353.5 KB | Display | wwPDB validaton report |
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Full document | 1tiv_full_validation.pdf.gz | 467.3 KB | Display | |
Data in XML | 1tiv_validation.xml.gz | 21.8 KB | Display | |
Data in CIF | 1tiv_validation.cif.gz | 34 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ti/1tiv ftp://data.pdbj.org/pub/pdb/validation_reports/ti/1tiv | 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 | Mass: 9785.232 Da / Num. of mol.: 1 / Mutation: THR 40 LYS Source method: isolated from a genetically manipulated source Details: NMR, 10 STRUCTURES / Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Gene: POTENTIAL / Production host: Escherichia coli (E. coli) / References: UniProt: P12506 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software | Name: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement | ||||||||||||
NMR ensemble | Conformers submitted total number: 10 |