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 27002

Title: Assignment of HuR RRM1-RRM2 tandem domain   PubMed: 28934484

Deposition date: 2017-01-19 Original release date: 2017-11-16

Authors: Lal, Preet; Cerofolini, Linda; D'Agostino, Vito Giuseppe; Zucal, Chiara; Fuccio, Carmelo; Bonomo, Isabelle; Luchinat, Claudio; Di Maio, Danilo; Novellino, Ettore; Biasini, Emiliano; Elezgarai, Saioa; Manzoni, Leonardo; Seneci, Pierfausto; Marinelli, Luciana; Fragai, Marco; Provenzani, Alessandro

Citation: Lal, Preet; Cerofolini, Linda; D'Agostino, Vito Giuseppe; Zucal, Chiara; Fuccio, Carmelo; Bonomo, Isabelle; Dassi, Erik; Giuntini, Stefano; Di Maio, Danilo; Vishwakarma, Vikalp; Preet, Ranjan; Williams, Sha Neisha; Fairlamb, Max; Munk, Rachel; Lehrmann, Elin; Abdelmohsen, Kotb; Elezgarai, Saioa; Luchinat, Claudio; Novellino, Ettore; Quattrone, Alessandro; Biasini, Emiliano; Manzoni, Leonardo; Gorospe, Myriam; Dixon, Dan; Seneci, Pierfausto; Marinelli, Luciana; Fragai, Marco; Provenzani, Alessandro. "Regulation of HuR structure and function by dihydrotanshinone-I."  Nucleic Acids Res. 45, 9514-9527 (2017).

Assembly members:
HuR_RRM1-RRM2, polymer, 210 residues, Formula weight is not available

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):
HuR_RRM1-RRM2: MSNGYEDHMAEDCRGDIGRT NLIVNYLPQNMTQDELRSLF SSIGEVESAKLIRDKVAGHS LGYGFVNYVTAKDAERAINT LNGLRLQSKTIKVSYARPSS EVIKDANLYISGLPRTMTQK DVEDMFSRFGRIINSRVLVD QTTGLSRGVAFIRFDKRSEA EEAITSFNGHKPPGSSEPIA VKFAANPNQNKNVALLSPRA PPPPPPPLID

Data sets:
Data typeCount
13C chemical shifts581
15N chemical shifts193
1H chemical shifts195

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HuR RRM-RRM21

Entities:

Entity 1, HuR RRM-RRM2 210 residues - Formula weight is not available

1   METSERASNGLYTYRGLUASPHISMETALA
2   GLUASPCYSARGGLYASPILEGLYARGTHR
3   ASNLEUILEVALASNTYRLEUPROGLNASN
4   METTHRGLNASPGLULEUARGSERLEUPHE
5   SERSERILEGLYGLUVALGLUSERALALYS
6   LEUILEARGASPLYSVALALAGLYHISSER
7   LEUGLYTYRGLYPHEVALASNTYRVALTHR
8   ALALYSASPALAGLUARGALAILEASNTHR
9   LEUASNGLYLEUARGLEUGLNSERLYSTHR
10   ILELYSVALSERTYRALAARGPROSERSER
11   GLUVALILELYSASPALAASNLEUTYRILE
12   SERGLYLEUPROARGTHRMETTHRGLNLYS
13   ASPVALGLUASPMETPHESERARGPHEGLY
14   ARGILEILEASNSERARGVALLEUVALASP
15   GLNTHRTHRGLYLEUSERARGGLYVALALA
16   PHEILEARGPHEASPLYSARGSERGLUALA
17   GLUGLUALAILETHRSERPHEASNGLYHIS
18   LYSPROPROGLYSERSERGLUPROILEALA
19   VALLYSPHEALAALAASNPROASNGLNASN
20   LYSASNVALALALEULEUSERPROARGALA
21   PROPROPROPROPROPROPROLEUILEASP

Samples:

sample_1: HuR RRM1-RRM2, [U-100% 13C; U-100% 15N], 0.4 mM; MES 20 mM; sodium chloride 100 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
2D CACOsample_1isotropicsample_conditions_1
2D CBCACOsample_1isotropicsample_conditions_1
3D CBCANCOsample_1isotropicsample_conditions_1
3D CBCACONsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker DRX 500 MHz

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