BMRB Entry 18852
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PDB ID: 2m1a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18852
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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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:
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 Vector: p(H)GB1-derived vector
Entity Sequences (FASTA):
Rev_ARM_peptide: GAMATRQARRNRRRRWRERQ
RAAAAR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 100 |
| 15N chemical shifts | 28 |
| 1H chemical shifts | 174 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HIV-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 | 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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SPARKY: Backbone
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