BMRB Entry 27670

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27670

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Title:
HuR GGS
Deposition date:
2018-10-30
Original release date:
2018-11-14
Authors:
Pabis, Marta; Popowicz, Grzegorz; Schlundt, Andreas; Sattler, Michael
Citation:

Citation: Pabis, Marta; Popowicz, Grzegorz; Stehle, Ralf; Fernandez-Ramos, David; Asami, Sam; Warner, Lisa; Garcia-Maurino, Sofia; Schlundt, Andreas; Martinez-Chantar, Maria; Diaz-Moreno, Irene; Sattler, Michael. "HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs."  Nucleic Acids Res. 47, 1011-1029 (2019).
PubMed: 30418581

Assembly members:

Assembly members:
HuR_GGS, polymer, 329 residues, 34020.76 Da.

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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HuR_GGS: GAMASNGYEDHMAEDCRGDI GRTNLIVNYLPQNMTQDELR SLFSSIGEVESAKLIRDKVA GHSLGYGFVNYVTAKDAERA INTLNGLRLQSKTIKVSYAR PSSEVIKDANLYISGLPRTM TQKDVEDMFSRFGRIINSRV LVDQTTGLSRGVAFIRFDKR SEAEEAITSFNGHKPPGSSE PITVKFAATGGSGGSGGSGG SGGSGGSGGSGGSGGSGGSG GSGGSGGSGGSGGSGGSGGS GGASSGWCIFIYNLGQDADE GILWQMFGPFGAVTNVKVIR DFNTNKCKGFGFVTMTNYEE AAMAIASLNGYRLGDKILQV SFKTNKSHK

Data sets:
Data typeCount
15N chemical shifts220
1H chemical shifts220

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HuR GGS1

Entities:

Entity 1, HuR GGS 329 residues - 34020.76 Da.

GAMA is from cloning

1   GLYALAMETALASERASNGLYTYRGLUASP
2   HISMETALAGLUASPCYSARGGLYASPILE
3   GLYARGTHRASNLEUILEVALASNTYRLEU
4   PROGLNASNMETTHRGLNASPGLULEUARG
5   SERLEUPHESERSERILEGLYGLUVALGLU
6   SERALALYSLEUILEARGASPLYSVALALA
7   GLYHISSERLEUGLYTYRGLYPHEVALASN
8   TYRVALTHRALALYSASPALAGLUARGALA
9   ILEASNTHRLEUASNGLYLEUARGLEUGLN
10   SERLYSTHRILELYSVALSERTYRALAARG
11   PROSERSERGLUVALILELYSASPALAASN
12   LEUTYRILESERGLYLEUPROARGTHRMET
13   THRGLNLYSASPVALGLUASPMETPHESER
14   ARGPHEGLYARGILEILEASNSERARGVAL
15   LEUVALASPGLNTHRTHRGLYLEUSERARG
16   GLYVALALAPHEILEARGPHEASPLYSARG
17   SERGLUALAGLUGLUALAILETHRSERPHE
18   ASNGLYHISLYSPROPROGLYSERSERGLU
19   PROILETHRVALLYSPHEALAALATHRGLY
20   GLYSERGLYGLYSERGLYGLYSERGLYGLY
21   SERGLYGLYSERGLYGLYSERGLYGLYSER
22   GLYGLYSERGLYGLYSERGLYGLYSERGLY
23   GLYSERGLYGLYSERGLYGLYSERGLYGLY
24   SERGLYGLYSERGLYGLYSERGLYGLYSER
25   GLYGLYALASERSERGLYTRPCYSILEPHE
26   ILETYRASNLEUGLYGLNASPALAASPGLU
27   GLYILELEUTRPGLNMETPHEGLYPROPHE
28   GLYALAVALTHRASNVALLYSVALILEARG
29   ASPPHEASNTHRASNLYSCYSLYSGLYPHE
30   GLYPHEVALTHRMETTHRASNTYRGLUGLU
31   ALAALAMETALAILEALASERLEUASNGLY
32   TYRARGLEUGLYASPLYSILELEUGLNVAL
33   SERPHELYSTHRASNLYSSERHISLYS

Samples:

sample_1: HuR GGS, [U-15N], 70 uM; sodium phosphate 20 mM; sodium chloride 200 mM; DTT 5 mM; EDTA 1 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CCPNMR_Analysis v2.4, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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