BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18975

Title: Unmodified 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:
RNA, polymer, 19 residues, 6077.715 Da.

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

Experimental source:   Production method: enzymatic semisynthesis

Entity Sequences (FASTA):
RNA: GGCCGUAACUAUAACGGUC

Data sets:
Data typeCount
13C chemical shifts128
1H chemical shifts160

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNA1

Entities:

Entity 1, RNA 19 residues - 6077.715 Da.

1   GGCCGUAACU
2   AUAACGGUC

Samples:

sample_1: RNA 1.0 mM; Potassium Phosphate 10 mM; Potassium Chloride 50 mM; EDTA 0.1 mM; D20 100%

sample_2: RNA 1.0 mM; Potassium Phosphate 10 mM; Potassium Chloride 50 mM; EDTA 0.1 mM; D20 90%; H2O 10%

sample_3: RNA, [U-100% 13C; U-100% 15N], 1.0 mM; Potassium Phosphate 10 mM; Potassium Chloride 50 mM; EDTA 0.1 mM; D20 100%

sample_conditions_1: ionic strength: 70 mM; pH: 7.3; pressure: 1 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C NATURAL ABUNDANCE HMQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
3D 1H-1H-1H TOCSY-NOESYsample_1isotropicsample_conditions_1
2D 1H-31P HETCORsample_1isotropicsample_conditions_1
1D 31Psample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-13C-1H HCCH-COSYsample_3isotropicsample_conditions_1
3D 1H-13C-1H HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C-13C HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-1H-13C NOESY-HMQCsample_3isotropicsample_conditions_1

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