BMRB Entry 5812

Title:
1H Chemical Shift Assignments for quasi-repetitive arginine/glycine/ tyrosine-rich domains within glycine-rich RNA binding proteins
Deposition date:
2003-05-27
Original release date:
2005-06-09
Authors:
Kumaki, Yasuhiro
Citation:

Citation: Kumaki, Yasuhiro; Nitta, K.; Hikichi, K.; Matsumoto, T.; Matsushima, N.. "Side chain-side chain interactions of arginine with tyrosine and aspartic acid in Arg/Gly/Tyr-rich domains within plant glycine-rich RNA binding proteins"  J. Biochem. 136, 29-37 (2004).
PubMed: 15269237

Assembly members:

Assembly members:
glycine-rich RNA-binding proteins, polymer, 10 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Zea mays   Taxonomy ID: 4577   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Zea mays

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
glycine-rich RNA-binding proteins: GGYGGGRRDG

Data sets:
Data typeCount
1H chemical shifts47
coupling constants4

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GGYGGGRRDG subunit 11

Entities:

Entity 1, GGYGGGRRDG subunit 1 10 residues - Formula weight is not available

1   GLYGLYTYRGLYGLYGLYARGARGASPGLY

Samples:

sample_1: glycine-rich RNA-binding proteins 12 mM

sample_cond_1: pH: 4.3; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
not availablesample_1not availablesample_cond_1

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz