BMRB Entry 18974

Name: Modified Helix 69
Published: 2014-01-02

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PDB ID: 2mer
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18974
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Modified Helix 69 PubMed: 24371282

Deposition date: 2013-01-25 Original release date: 2014-01-02

Authors: JIANG, JUN; ADURI, RAVIPRASAD; CHOW, CHRISTINE; SANTALUCIA, JOHN

Citation: Jiang, Jun; Aduri, Raviprasad; Chow, Christine; Santalucia, John. "Structure modulation of helix 69 from Escherichia coli 23S ribosomal RNA by pseudouridylations." Nucleic Acids Res. ., .-. (2013).

Assembly members:
HELIX_69, polymer, 19 residues, 6077.715 Da.

Natural source: Common Name: Enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
HELIX_69: GGCCGXAACXAXAACGGUC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	46
1H chemical shifts	155

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HELIX_69	1

Entities:

Entity 1, HELIX_69 19 residues - 6077.715 Da.

1

G

C

G

PSU

A

C

PSU

2

A

PSU

A

C

G

U

C

Samples:

sample_1: HELIX_69 1.0 mM; Potassium Phosphate 10 mM; Potassium Chloride 50 mM; EDTA 0.1 mM; D2O 100%

sample_2: HELIX_69 1.0 mM; Potassium Phosphate 10 mM; Potassium Chloride 50 mM; EDTA 0.1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 70 mM; pH: 7.3; pressure: 1 atm; temperature: 310.2 K

sample_conditions_2: ionic strength: 70 mM; pH: 7.3; pressure: 1 atm; temperature: 283.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C NATURAL ABUNDANCE HMQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-1H-1H TOCSY-NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-31P HETCOR	sample_1	isotropic	sample_conditions_1
1D 31P	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 700 MHz
Varian Mercury 400 MHz