|Entry||Database: PDB / ID: 1jfw|
|Title||HOMONUCLEAR AND HETERONUCLEAR 1H-13C NUCLEAR MAGNETIC RESONANCE ASSIGNMENT AND STRUCTURAL CHARACTERIZATION OF A HIV-1 TAT PROTEIN|
|Keywords||VIRAL PROTEIN / TAT / HIV-1 / HETERONUCLEAR / DRUG DESIGN|
|Function / homology|
Function and homology information
modulation of transcription in other organism involved in symbiotic interaction / trans-activation response element binding / modulation by virus of host PP1 activity / RNA-binding transcription regulator activity / negative regulation of cellular respiration / modulation by virus of host chromatin organization / host cell nucleolus / membrane hyperpolarization / actinin binding / positive regulation of viral transcription ...modulation of transcription in other organism involved in symbiotic interaction / trans-activation response element binding / modulation by virus of host PP1 activity / RNA-binding transcription regulator activity / negative regulation of cellular respiration / modulation by virus of host chromatin organization / host cell nucleolus / membrane hyperpolarization / actinin binding / positive regulation of viral transcription / negative regulation of peptidyl-threonine phosphorylation / cyclin binding / positive regulation of transcription elongation from RNA polymerase II promoter / positive regulation of protein localization to nucleus / positive regulation of NF-kappaB transcription factor activity / suppression by virus of host type I interferon-mediated signaling pathway / transcription, DNA-templated / host cell cytoplasm / protein domain specific binding / extracellular region / metal ion binding
Similarity search - Function
HIV-1 Transactivator Protein / Tat domain / Tat domain superfamily / Transactivating regulatory protein (Tat) / Immunodeficiency virus transactivating regulatory protein (Tat) / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Similarity search - Component
|Method||SOLUTION NMR / SIMULATED ANNEALING, RANDOM LOOP RESEARCH VALIDATED WITH NOE BACK-CALCULATION ENERGY MINIMIZATION, MOLECULAR DYNAMIC|
|Authors||Peloponese, J.M. / Gregoire, C. / Opi, S. / Esquieu, D.|
|Citation||Journal: C.R.Acad.Sci.III / Year: 2000|
Title: 1H-13C nuclear magnetic resonance assignment and structural characterization of HIV-1 Tat protein.
Authors: Peloponese Jr., J.M. / Gregoire, C. / Opi, S. / Esquieu, D. / Sturgis, J. / Lebrun, E. / Meurs, E. / Collette, Y. / Olive, D. / Aubertin, A.M. / Witvrow, M. / Pannecouque, C. / De Clercq, E. ...Authors: Peloponese Jr., J.M. / Gregoire, C. / Opi, S. / Esquieu, D. / Sturgis, J. / Lebrun, E. / Meurs, E. / Collette, Y. / Olive, D. / Aubertin, A.M. / Witvrow, M. / Pannecouque, C. / De Clercq, E. / Bailly, C. / Lebreton, J. / Loret, E.P.
|Structure viewer||Molecule: |
Downloads & links
A: TAT PROTEIN
|#1: Protein|| |
Mass: 9789.319 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: THIS PEPTIDE WAS SYNTHESIZED (SOLID PHASE SYNTHESIS). THE SEQUENCE OF THIS PEPTIDE OCCURS NATURALLY IN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
References: UniProt: P04610
|Experiment||Method: SOLUTION NMR|
|Details||Contents: SPECIFIC 13C LABELLING OF GLYCINE 15,44,48,61,79,83|
|Sample conditions||pH: 4.50 / Temperature: 298.00 K|
*PLUSMethod: other / Details: NMR
|NMR spectrometer||Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz|
|Refinement||Method: SIMULATED ANNEALING, RANDOM LOOP RESEARCH VALIDATED WITH NOE BACK-CALCULATION ENERGY MINIMIZATION, MOLECULAR DYNAMIC|
Software ordinal: 1
Details: THE STRUCTURES ARE BASED ON A TOTAL OF 915 RESTRAINTS AND 272 ARE LONG-RANGE NOES.
|NMR ensemble||Conformer selection criteria: BACK CALCULATED DATA AGREE WITH EXPERIMEN TAL NOESY SPECTRUM, STRUCTURES WITH ACCEPTABLE COVALENT GEOMETRY,STRUCTURES WITH FAVORABLE NON-BOND ENERGY,STRUCTURES WITH THE ...Conformer selection criteria: BACK CALCULATED DATA AGREE WITH EXPERIMEN TAL NOESY SPECTRUM, STRUCTURES WITH ACCEPTABLE COVALENT GEOMETRY,STRUCTURES WITH FAVORABLE NON-BOND ENERGY,STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS,STRUCTURES WITH THE LOWEST ENERGY, TARGET FUNCTION|
Conformers calculated total number: 100 / Conformers submitted total number: 11
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