Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18851
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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:
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 Vector: p(H)GB1-derived vector
Entity Sequences (FASTA):
HIV-1_Rev_ARM: GAMATRQARRNRRRRWRERQ
RAAAAR
Data type | Count |
13C chemical shifts | 103 |
15N chemical shifts | 27 |
1H chemical shifts | 163 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HIV-1 Rev ARM peptide | 1 |
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 |
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