BMRB Entry 18851
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18851
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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:
HIV-1_Rev_ARM, polymer, 26 residues, Formula weight is not available
Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HIV-1_Rev_ARM: GAMATRQARRNRRRRWRERQ
RAAAAR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 103 |
| 15N chemical shifts | 27 |
| 1H chemical shifts | 163 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HIV-1 Rev ARM peptide | 1 |
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 | GLY | ALA | MET | ALA | THR | ARG | GLN | ALA | ARG | ARG | ||||
| 2 | ASN | ARG | ARG | ARG | ARG | TRP | ARG | GLU | ARG | GLN | ||||
| 3 | ARG | ALA | ALA | ALA | ALA | ARG |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Rev_ARM_15N | isotropic | Experiments_at_283K |
| 2D 1H-13C HSQC | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D HNCO | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D HNCA | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D HN(CO)CA | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D CBCA(CO)NH | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D HNCACB | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D HBHA(CO)NH | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D H(CCO)NH | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D 1H-15N NOESY | Rev_ARM_15N | isotropic | Experiments_at_283K |
| 3D 1H-13C NOESY | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D HCCH-TOCSY | Rev_ARM_15N-13C | isotropic | Experiments_at_283K |
| 3D HNHA | Rev_ARM_15N | isotropic | Experiments_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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts