BMRB Entry 51310

Click here to enlarge.

PDB ID: 7v06
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51310
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Encoded Conformational Dynamics of the HIV Splice Site A3 Regulatory Locus: Implications for differential binding of hnRNP Splicing Auxiliary Factors

Deposition date:

2022-02-06

Original release date:

2022-06-22

Authors:

Chiu, Liang-Yuan; Jain, Niyati; Sugarman, Andrew; Tolbert, Blanton

Citation:

Citation: Chiu, Liang-Yuan; Emery, Ann; Jain, Niyati; Sugarman, Andrew; Kendrick, Nashea; Luo, Le; Ford, William; Swanstrom, Ronald; Tolbert, Blanton. "Encoded Conformational Dynamics of the HIV Splice Site A3 Regulatory Locus: Implications for Differential Binding of hnRNP Splicing Auxiliary Factors" J. Mol. Biol. 434, 167728-167728 (2022).
PubMed: 35870649

Assembly members:

Assembly members:
entity_1, polymer, 43 residues, Formula weight is not available

Natural source:

Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1

Experimental source:

Experimental source: Production method: In vitro transcription Host organism: n/a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGUGCUGUUUAUCCAUUUCA GAAUUGGGUGUCGACAUAGC ACC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	137

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 43 residues - Formula weight is not available

1

G

U

G

C

U

G

U

2

A

U

C

A

U

C

A

3

G

A

U

G

U

G

4

U

C

G

A

C

A

U

A

G

C

5

A

C

Samples:

sample_1: ESS2p Equimolar mix, selective deuteration, 450 uM

sample_2: ESS2p fully protonated 400 uM

sample_3: ESS2p_N15_HSQC, [U-100% 15N] on GTP and UTP, 300 uM

sample_4: ESS2p_uniform_N15, [U-100% 13C; U-100% 15N], 300 uM

sample_5: ESS2p_uniform_N15_C13, [U-100% 13C; U-100% 15N] on ATP and GTP, 200 uM

sample_conditions_1: ionic strength: 5 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 5 mM; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HMQC	sample_5	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_2
2D 1H-15N HNN-COSY	sample_4	isotropic	sample_conditions_2

Software:

AMBER - refinement

NMRDraw - Data processing

NMRPipe - Data processing

TOPSPIN - Data collection

NMRViewJ - chemical shift assignment

X-PLOR NIH - structure calculation

NMR spectrometers:

Bruker Avance II 900 MHz
Bruker AVANCE II 800 MHz
Bruker AVANCE NEO 700 MHz