BMRB Entry 18851

Title:
HIV-1 Rev ARM peptide (residues T34-R50)
Deposition date:
2012-11-21
Original release date:
2013-09-04
Authors:
Casu, Fabio; Duggan, Brendan; Hennig, Mirko
Citation:

Citation: Casu, Fabio; Duggan, Brendan; Hennig, Mirko. "The Arginine-Rich RNA-Binding Motif of HIV-1 Rev Is Intrinsically Disordered and Folds upon RRE Binding"  Biophys. J. 105, 1004-1017 (2013).
PubMed: 23972852

Assembly members:

Assembly members:
HIV-1_Rev_ARM, polymer, 26 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p(H)GB1-derived vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HIV-1_Rev_ARM: GAMATRQARRNRRRRWRERQ RAAAAR

Data sets:
Data typeCount
13C chemical shifts103
15N chemical shifts27
1H chemical shifts163

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-1 Rev ARM peptide1

Entities:

Entity 1, HIV-1 Rev ARM peptide 26 residues - Formula weight is not available

Residues 1-4 and 22-26 are non-native residues added for expression (TEV-cleavable hexahistidine-GB1 expression tag) and to enhance helical stability.

1   GLYALAMETALATHRARGGLNALAARGARG
2   ASNARGARGARGARGTRPARGGLUARGGLN
3   ARGALAALAALAALAARG

Samples:

Rev_ARM_15N: HIV-1 Rev ARM, [U-15N], 1.0 mM; sodium phosphate 50 mM; potassium chloride 150 mM; EDTA 1 mM; DTT 1 mM; sodium azide 0.02%; D2O, [U-99% 2H], 10.0%; H2O 90.0%

Rev_ARM_15N-13C: HIV-1 Rev ARM, [U-13C; U-15N], 1.0 mM; sodium phosphate 50 mM; potassium chloride 150 mM; EDTA 1 mM; DTT 1 mM; sodium azide 0.02%; D2O, [U-99% 2H], 10.0%; H2O 90.0%

Experiments_at_283K: pH: 7.4; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCRev_ARM_15NisotropicExperiments_at_283K
2D 1H-13C HSQCRev_ARM_15N-13CisotropicExperiments_at_283K
3D HNCORev_ARM_15N-13CisotropicExperiments_at_283K
3D HNCARev_ARM_15N-13CisotropicExperiments_at_283K
3D HN(CO)CARev_ARM_15N-13CisotropicExperiments_at_283K
3D CBCA(CO)NHRev_ARM_15N-13CisotropicExperiments_at_283K
3D HNCACBRev_ARM_15N-13CisotropicExperiments_at_283K
3D HBHA(CO)NHRev_ARM_15N-13CisotropicExperiments_at_283K
3D H(CCO)NHRev_ARM_15N-13CisotropicExperiments_at_283K
3D 1H-15N NOESYRev_ARM_15NisotropicExperiments_at_283K
3D 1H-13C NOESYRev_ARM_15N-13CisotropicExperiments_at_283K
3D HCCH-TOCSYRev_ARM_15N-13CisotropicExperiments_at_283K
3D HNHARev_ARM_15NisotropicExperiments_at_283K

Software:

TOPSPIN, Bruker Biospin - collection

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNMR, CCPN - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 18852
PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks