BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30077

Title: Structural model of a apo G-protein alpha subunit determined with NMR residual dipolar couplings and SAXS   PubMed: 27298341

Deposition date: 2016-05-07 Original release date: 2016-06-24

Authors: Goricanec, D.; Stehle, R.; Grigoriu, S.; Wagner, G.; Hagn, F.

Citation: Goricanec, D.; Stehle, R.; Egloff, P.; Grigori, S.; Plueckthun, A.; Wagner, G.; Hagn, F.. "Conformational dynamics of a G-protein alpha subunit is tightly regulated by nucleotide binding"  Proc. Natl. Acad. Sci. U. S. A. 113, E3629-E3638 (2016).

Assembly members:
Guanine nucleotide-binding protein G(i) subunit alpha-1, polymer, 326 residues, 37247.414 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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
Guanine nucleotide-binding protein G(i) subunit alpha-1: GASREVKLLLLGAGESGKST IVKQMKIIHEAGYSEEECKQ YKAVVYSNTIQSIIAIIRAM GRLKIDFGDSARADDARQLF VLAGAAEEGFMTAELAGVIK RLWKDSGVQACFNRSREYQL NDSAAYYLNDLDRIAQPNYI PTQQDVLRTRVKTTGIVETH FTFKDLHFKMFDVGGQRSER KKWIHCFEGVAAIIFCVALS DYDLVLAEDEEMNRMHESMK LFDSICNNKWFTDTSIILFL NKKDLFEEKIKKSPLTICYQ EYAGSNTYEEAAAYIQCQFE DLNKRKDTKEIYTHFTCATD TKNVQFVFDAVTDVIIKNNL KDCGLF

Data sets:
Data typeCount
15N chemical shifts244
1H chemical shifts244

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 326 residues - 37247.414 Da.

1   GLYALASERARGGLUVALLYSLEULEULEU
2   LEUGLYALAGLYGLUSERGLYLYSSERTHR
3   ILEVALLYSGLNMETLYSILEILEHISGLU
4   ALAGLYTYRSERGLUGLUGLUCYSLYSGLN
5   TYRLYSALAVALVALTYRSERASNTHRILE
6   GLNSERILEILEALAILEILEARGALAMET
7   GLYARGLEULYSILEASPPHEGLYASPSER
8   ALAARGALAASPASPALAARGGLNLEUPHE
9   VALLEUALAGLYALAALAGLUGLUGLYPHE
10   METTHRALAGLULEUALAGLYVALILELYS
11   ARGLEUTRPLYSASPSERGLYVALGLNALA
12   CYSPHEASNARGSERARGGLUTYRGLNLEU
13   ASNASPSERALAALATYRTYRLEUASNASP
14   LEUASPARGILEALAGLNPROASNTYRILE
15   PROTHRGLNGLNASPVALLEUARGTHRARG
16   VALLYSTHRTHRGLYILEVALGLUTHRHIS
17   PHETHRPHELYSASPLEUHISPHELYSMET
18   PHEASPVALGLYGLYGLNARGSERGLUARG
19   LYSLYSTRPILEHISCYSPHEGLUGLYVAL
20   ALAALAILEILEPHECYSVALALALEUSER
21   ASPTYRASPLEUVALLEUALAGLUASPGLU
22   GLUMETASNARGMETHISGLUSERMETLYS
23   LEUPHEASPSERILECYSASNASNLYSTRP
24   PHETHRASPTHRSERILEILELEUPHELEU
25   ASNLYSLYSASPLEUPHEGLUGLULYSILE
26   LYSLYSSERPROLEUTHRILECYSTYRGLN
27   GLUTYRALAGLYSERASNTHRTYRGLUGLU
28   ALAALAALATYRILEGLNCYSGLNPHEGLU
29   ASPLEUASNLYSARGLYSASPTHRLYSGLU
30   ILETYRTHRHISPHETHRCYSALATHRASP
31   THRLYSASNVALGLNPHEVALPHEASPALA
32   VALTHRASPVALILEILELYSASNASNLEU
33   LYSASPCYSGLYLEUPHE

Samples:

sample_1: G protein alpha subunit subtype i1, GNAI1, [U-98% 2H; U-99% 13C; U-99% 15N], 400 uM; H2O 95%; D2O 5%; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; magnesium chloride 5 mM

sample_2: G protein alpha subunit subtype i1, GNAI1, [U-98% 15N; U-90% 2H], 250 uM; H2O 95%; D2O 5%; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; magnesium chloride 5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

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

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts