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 17088

Title: Solution structure of the pseudouridine modified P6.1 hairpin of human telomerase RNA   PubMed: 20554853

Deposition date: 2010-07-29 Original release date: 2010-08-18

Authors: Kim, Nak-Kyoon; Theimer, Carla; Mitchell, James; Collins, Kathleen; Feigon, Juli

Citation: Kim, Nak-Kyoon; Theimer, Carla; Mitchell, James; Collins, Kathleen; Feigon, Juli. "Effect of pseudouridylation on the structure and activity of the catalytically essential P6.1 hairpin in human telomerase RNA."  Nucleic Acids Res. 38, 6746-6756 (2010).

Assembly members:
RNA, polymer, 15 residues, 4824.931 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: enzymatic semisynthesis

Entity Sequences (FASTA):
RNA: GAGAGXXGGGCXCXC

Data sets:
Data typeCount
13C chemical shifts91
15N chemical shifts16
1H chemical shifts138

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P6.1 hairpin1

Entities:

Entity 1, P6.1 hairpin 15 residues - 4824.931 Da.

1   GAGAGPSUPSUGGG
2   CPSUCPSUC

Samples:

Unlabeled_HDO: RNA 0.6 mM; H2O 95%; D2O 5%

Unlabeled_D2O: RNA 0.6 mM; D2O 100%

ACG_labeled_HDO: RNA, [U-98% 13C; U-98% 15N], 0.8 mM; H2O 95%; D2O 5%

ACG_labeled_D2O: RNA, [U-98% 13C; U-98% 15N], 0.8 mM; D2O 100%

HDO: ionic strength: 5 mM; pH: 6.8; pressure: 1 atm; temperature: 283 K

D2O: ionic strength: 5 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCACG_labeled_HDOisotropicHDO
2D 1H-13C HSQCUnlabeled_D2OisotropicD2O
2D 1H-13C HSQCACG_labeled_D2OisotropicD2O
2D 1H-1H COSYACG_labeled_D2OisotropicD2O
2D 1H-1H NOESYUnlabeled_HDOisotropicHDO
2D 1H-1H NOESYUnlabeled_D2OisotropicD2O
2D 1H-1H Filter/Edited NOESYACG_labeled_D2OisotropicD2O
3D HCCH-TOCSYACG_labeled_D2OisotropicD2O
2D 1H-1H TOCSYUnlabeled_HDOisotropicHDO
2D 1H-1H TOCSYUnlabeled_D2OisotropicD2O

Software:

X-PLOR NIH v2.9.8, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

xwinnmr, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz