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 27669

Title: Amide chemical shifts of full-length human HuR   PubMed: 30418581

Deposition date: 2018-10-30 Original release date: 2018-11-14

Authors: Sattler, Michael; Schlundt, Andreas; Pabis, Marta; Popowicz, Grzegorz

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).

Assembly members:
HuR_FL, polymer, 329 residues, 36317.13 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   Vector: pETM44

Entity Sequences (FASTA):
HuR_FL: GPMASNGYEDHMAEDCRGDI GRTNLIVNYLPQNMTQDELR SLFSSIGEVESAKLIRDKVA GHSLGYGFVNYVTAKDAERA INTLNGLRLQSKTIKVSYAR PSSEVIKDANLYISGLPRTM TQKDVEDMFSRFGRIINSRV LVDQTTGLSRGVAFIRFDKR SEAEEAITSFNGHKPPGSSE PITVKFAANPNQNKNVALLS QLYHSPARRFGGPVHHQAQR FRFSPMGVDHMSGLSGVNVP GNASSGWCIFIYNLGQDADE GILWQMFGPFGAVTNVKVIR DFNTNKCKGFGFVTMTNYEE AAMAIASLNGYRLGDKILQV SFKTNKSHK

Data sets:
Data typeCount
15N chemical shifts212
1H chemical shifts212

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HuR FL1

Entities:

Entity 1, HuR FL 329 residues - 36317.13 Da.

GPMA is from cloning

1   GLYPROMETALASERASNGLYTYRGLUASP
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   PROILETHRVALLYSPHEALAALAASNPRO
20   ASNGLNASNLYSASNVALALALEULEUSER
21   GLNLEUTYRHISSERPROALAARGARGPHE
22   GLYGLYPROVALHISHISGLNALAGLNARG
23   PHEARGPHESERPROMETGLYVALASPHIS
24   METSERGLYLEUSERGLYVALASNVALPRO
25   GLYASNALASERSERGLYTRPCYSILEPHE
26   ILETYRASNLEUGLYGLNASPALAASPGLU
27   GLYILELEUTRPGLNMETPHEGLYPROPHE
28   GLYALAVALTHRASNVALLYSVALILEARG
29   ASPPHEASNTHRASNLYSCYSLYSGLYPHE
30   GLYPHEVALTHRMETTHRASNTYRGLUGLU
31   ALAALAMETALAILEALASERLEUASNGLY
32   TYRARGLEUGLYASPLYSILELEUGLNVAL
33   SERPHELYSTHRASNLYSSERHISLYS

Samples:

sample_1: HuR FL, [U-15N; U-2H], 20 uM; sodium phosphate 20 mM; sodium chloride 200 mM; DTT, [U-2H], 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, processing

CCPNMR_Analysis v2.4, CCPN - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 800 MHz

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