BMRB Entry 15319

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PDB ID: 2jr4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15319
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR SOLUTION STRUCTURE OF THE ANTICODON OF E.coli TRNA-VAL3 WITH NO MODIFICATIONS PubMed: 18473483

Deposition date: 2007-06-20 Original release date: 2008-06-12

Authors: Vendeix, Franck; Dziergowska, Agnieszka; Gustilo, Estella; Graham, William; Sproat, Brian; Malkiewicz, Andrzej; Agris, Paul

Citation: Vendeix, Franck; Dziergowska, Agnieszka; Gustilo, Estella; Graham, William; Sproat, Brian; Malkiewicz, Andrzej; Agris, Paul. "Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding" Biochemistry 47, 6117-6129 (2008).

Assembly members:
RNA_ASLval, polymer, 17 residues, 5402.314 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: chemical synthesis

Entity Sequences (FASTA):
RNA_ASLval: CCUCCCUUACAAGGAGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ASLval	1

Entities:

Entity 1, ASLval 17 residues - 5402.314 Da.

1

C

U

C

U

A

C

2

A

G

A

G

Samples:

Unmodified_ASLval3_H2O: RNA 17mer1.5 – 2 mM; H2O 90%; D2O 10%

Unmodified_ASLval3_D2O: RNA 17mer1.5 – 2 mM; D2O 100%

sample_conditions_1: pH: 6.2; pressure: 1 atm; temperature: 295 K

sample_conditions_2: pH: 6.2; pressure: 1 atm; temperature: 275 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H COSY	Unmodified_ASLval3_D2O	isotropic	sample_conditions_1
2D DQF-COSY	Unmodified_ASLval3_D2O	isotropic	sample_conditions_1
2D 1H-1H TOCSY	Unmodified_ASLval3_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC	Unmodified_ASLval3_D2O	isotropic	sample_conditions_1
2D 1H-1H NOESY	Unmodified_ASLval3_D2O	isotropic	sample_conditions_1
2D 1H-1H NOESY	Unmodified_ASLval3_H2O	isotropic	sample_conditions_2
2D 1H-31P HETCOR	Unmodified_ASLval3_D2O	isotropic	sample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

VNMR, Varian - collection

NMRDraw v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Bruker Avance 500 MHz
Varian INOVA 600 MHz