BMRB Entry 15178

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15178

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Title:
Backbone, C' and CB 13C, 15N and 1H chemical shift assignments for the RGS domain of the human Regulator of G-protein Signalling 3(RGS3)protein
Deposition date:
2007-03-16
Original release date:
2007-03-30
Authors:
Higman, Victoria; Leidert, Martina; Schmieder, Peter; Bray, James; Elkins, Jon; Phillips, Claire; Fedorov, Oleg; Johannson, Catrine; Smee, Carol; Burgess, Nicola; Doyle, Declan; Yang, Xiaowen; Berridge, Georgine; Diehl, Annette; Sundstrom, Michael; Arrowsmith, Cheryl; Weigelt, Johan; Edwards, Aled; Oschkinat, Hartmut; Ball, Linda
Citation:

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).
PubMed: 18434541

Assembly members:

Assembly members:
RGS3, polymer, 144 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21 (DE3) - Rosetta (Novagen)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RGS3: SMDLSWLDLEKPTSEEALKW GESLEKLLVHKYGLAVFQAF LRTEFSEENLEFWLACEDFK KVKSQSKMASKAKKIFAEYI AIQACKEVNLDSYTREHTKD NLQSVTRGCFDLAQKRIFGL MEKDSYPRFLRSDLYLDLIN QKKM

Data sets:
Data typeCount
13C chemical shifts418
15N chemical shifts140
1H chemical shifts325

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1RGS31

Entities:

Entity 1, RGS3 144 residues - Formula weight is not available

The N terminal SM residues are an artefact from the vector. The next 8 residues 'DLSWLDLE' are a non-natural, inserted sequence, engineered into the construct as an interaction site for 14-3-3 proteins (included for use in later studies).

1   SERMETASPLEUSERTRPLEUASPLEUGLU
2   LYSPROTHRSERGLUGLUALALEULYSTRP
3   GLYGLUSERLEUGLULYSLEULEUVALHIS
4   LYSTYRGLYLEUALAVALPHEGLNALAPHE
5   LEUARGTHRGLUPHESERGLUGLUASNLEU
6   GLUPHETRPLEUALACYSGLUASPPHELYS
7   LYSVALLYSSERGLNSERLYSMETALASER
8   LYSALALYSLYSILEPHEALAGLUTYRILE
9   ALAILEGLNALACYSLYSGLUVALASNLEU
10   ASPSERTYRTHRARGGLUHISTHRLYSASP
11   ASNLEUGLNSERVALTHRARGGLYCYSPHE
12   ASPLEUALAGLNLYSARGILEPHEGLYLEU
13   METGLULYSASPSERTYRPROARGPHELEU
14   ARGSERASPLEUTYRLEUASPLEUILEASN
15   GLNLYSLYSMET

Samples:

sample_1: RGS3, [U-98% 13C; U-98% 15N], 0.2 ± 0.05 mM; H2O 90%; D2O 10%; potassium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02%

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - processing

ANALYSIS v1.0.13, CCPNMR - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAB70766 BAC87285 BAE90824 BAF82355 BAG53374
GB AAC50394 AAH18072 AAH19039 AAH42555 AAI23616
PRF 2206475A
REF NP_001071441 NP_001263189 NP_001263190 NP_001263191 NP_001269851
SP P49796
TPG DAA26468
AlphaFold P49796

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks