BMRB Entry 18852

Name: HIV-1 Rev ARM peptide (residues T34-R50)
Published: 2013-09-04

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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
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:
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:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	100
15N chemical shifts	28
1H chemical shifts	174

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

2

ASN

ARG

TRP

ARG

GLU

ARG

GLN

3

ARG

ALA

ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	Rev_ARM_15N	isotropic	Experiments_at_283K
2D 1H-15N HSQC NH2 only	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:

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

Biological Magnetic Resonance Data Bank