Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17449

Title: Solution Structure of the human Anti-codon Stem and loop(hASL) of transfer RNA Lysine III (tRNALys3)   PubMed: 22227389

Authors: Vendeix, Franck; Murphy, Frank; Leszczynska, Grazyna; Cantara, William; Gustilo, Estella; Sproat, Brian; Malkiewicz, Andrzej; Agris, Paul

Citation: Vendeix, Franck; Murphy, Frank; Cantara, William; Leszczyska, Grayna; Gustilo, Estella; Sproat, Brian; Malkiewicz, Andrzej; Agris, Paul. "Human tRNA(Lys3)(UUU) Is Pre-Structured by Natural Modifications for Cognate and Wobble Codon Binding through Keto-Enol Tautomerism."  J. Mol. Biol. 416, 467-485 (2012).

Assembly members:
RNA_(5'-R(*GP*CP*AP*GP*AP*CP*UP*(70U)P*UP*UP*(12A)P*AP*UP*CP*UP*GP*C)-3')_, polymer, 17 residues, 5644.569 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):

Data sets:
Data typeCount
1H chemical shifts131

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID


Entity 1, tRNALys3UUU 17 residues - 5644.569 Da.



sample_1: tRNALys3UUU 1.50 mM; H2O 90%; D2O 10%

Sample_2: tRNALys3UUU 1.50 mM; D2O 100%

sample_conditions_1: ionic strength: . M; pH: 6.2; pressure: 1 atm; temperature: 275 K

sample_conditions_2: ionic strength: . M; pD: 6.2 pD; pressure: 1 atm; temperature: 295 K

sample_conditions_3: ionic strength: . M; pH: 6.2; pressure: 1 atm; temperature: 295 K


NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_3
2D 1H-1H COSYSample_2isotropicsample_conditions_2
2D DQF-COSYSample_2isotropicsample_conditions_2
2D 1H-1H NOESYSample_2isotropicsample_conditions_2
2D 1H-1H TOCSYSample_2isotropicsample_conditions_2
2D 1H-13C HSQCSample_2isotropicsample_conditions_2
2D 1H-31P HETCORSample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_conditions_3


xwinnmr, Bruker Biospin - collection, processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Varian Unity 600 MHz

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