BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18852

Title: HIV-1 Rev ARM peptide (residues T34-R50)   PubMed: 23972852

Deposition date: 2012-11-21 Original release date: 2013-09-04

Authors: Casu, Fabio; Duggan, Brendan; Hennig, Mirko

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).

Assembly members:
Rev_ARM_peptide, polymer, 26 residues, 3219.751 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Rev_ARM_peptide: GAMATRQARRNRRRRWRERQ RAAAAR

Data sets:
Data typeCount
13C chemical shifts100
15N chemical shifts28
1H chemical shifts174

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-1 Rev ARM peptide (residues T34-R50)1

Entities:

Entity 1, HIV-1 Rev ARM peptide (residues T34-R50) 26 residues - 3219.751 Da.

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: Rev ARM peptide, [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 40.0%; TFE 50.0%

Rev_ARM_15N-13C: Rev ARM peptide, [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 40.0%; TFE, [U-99% 2H], 50.0%

Experiments_at_283K: pH: 7.4; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCRev_ARM_15NisotropicExperiments_at_283K
2D 1H-15N HSQC NH2 onlyRev_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:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS+, Cornilescu, Delaglio and Bax - structure solution

NMR spectrometers:

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

Related Database Links:

BMRB 18851
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts