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 5811

Title: 1H Chemical Shift Assignments for quasi-repetitive arginine/glycine/ tyrosine-rich domains within glycine-rich RNA binding proteins   PubMed: 15269237

Deposition date: 2003-05-27 Original release date: 2005-05-26

Authors: Kumaki, Yasuhiro

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).

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

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

Experimental source:   Production method: chemical synthesis

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

Data sets:
Data typeCount
1H chemical shifts47
coupling constants4

Additional metadata:

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Entity Assembly IDEntity NameEntity ID
1GGRRDGGYGG subunit 11


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



sample_1: glycine-rich RNA-binding proteins 12 mM

sample_cond_1: pH: 4.3; temperature: 278 K


NameSampleSample stateSample conditions
TOCSYnot availablenot availablenot available
NOESYnot availablenot availablenot available
ROESYnot availablenot availablenot available
DQF-COSYnot availablenot availablenot available


No software information available

NMR spectrometers:

  • JEOL ALPHA 500 MHz