BMRB

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 15128

Title: Solution structure of the RGS domain of human RGS14   PubMed: 18434541

Deposition date: 2007-02-02 Original release date: 2007-08-23

Authors: Dowler, Elizabeth; Diehl, Annette; Bray, James; Elkins, Jon; Soundararajan, Meera; Doyle, Declan; Gileadi, Carina; Phillips, Claire; Schoch, Guillaume; Yang, Xiawen; Brockmann, Christoph; Leidert, Martina; Rehbein, Kristina; Schmieder, Peter; Kuhne, Ronald; Higman, Victoria; Sundstrom, Michael; Arrowsmith, Cheryl; Weigelt, Johan; Edwards, Aled; Oschkinat, Hartmut; Ball, Linda

Citation: Soundararajan, Meera; Willard, Francis; Kimple, Adam; Turnbull, Andrew; Ball, Linda; Schoch, Guillaume; Gileadi, Carina; Fedorov, Oleg; Dowler, Elizabeth; Higman, Victoria; Hutsell, Stephanie; Sundstrom, Michael; Doyle, Declan; Siderovski, David. "Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits"  Proc. Natl. Acad. Sci. USA 105, 6457-6462 (2008).

Assembly members:
RGS14, polymer, 154 residues, 17728.135 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
RGS14: SMTEEQPVASWALSFERLLQ DPLGLAYFTEFLKKEFSAEN VTFWKACERFQQIPASDTQQ LAQEARNIYQEFLSSQALSP VNIDRQAWLGEEVLAEPRPD MFRAQQLQIFNLMKFDSYAR FVKSPLYRECLLAEAEGRPL REPGSSRLGSPDAT

Data sets:
Data typeCount
13C chemical shifts567
15N chemical shifts151
1H chemical shifts1011

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

PDB 2JNU
DBJ BAJ20688
GB AAH14094 ADZ15921 EAW85011 EAW85012 EAW85013
REF NP_001179660 NP_006471 XP_001089197 XP_002744538 XP_003280558
SP O43566
TPG DAA27643

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