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 30155

Title: NMR solution structure of the RRM1 domain of the post-transcriptional regulator HuR

Deposition date: 2016-08-15 Original release date: 2017-08-04

Authors: Lixa, C.; Mujo, A.; Jendiroba, K.; Almeida, F.; Lima, L.; Pinheiro, A.

Citation: Lixa, C.; Mujo, A.; Jendiroba, K.; Almeida, F.; Lima, L.; Pinheiro, A.; Mujo, A.; Lixa, C.; Carneiro, L.; Anobom, C.; Almeida, F.; Pinheiro, A.. "Insights into HuR RRM1 domain self-association and mRNA recognition from solution NMR studies"  . ., .-..

Assembly members:
entity_1, polymer, 101 residues, 11220.585 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

Entity Sequences (FASTA):
entity_1: GHMSNGYEDHMAEDCRGDIG RTNLIVNYLPQNMTQDELRS LFSSIGEVESAKLIRDKVAG HSLGYGFVNYVTAKDAERAI NTLNGLRLQSKTIKVSYARP S

Data sets:
Data typeCount
13C chemical shifts412
15N chemical shifts106
1H chemical shifts666

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 101 residues - 11220.585 Da.

1   GLYHISMETSERASNGLYTYRGLUASPHIS
2   METALAGLUASPCYSARGGLYASPILEGLY
3   ARGTHRASNLEUILEVALASNTYRLEUPRO
4   GLNASNMETTHRGLNASPGLULEUARGSER
5   LEUPHESERSERILEGLYGLUVALGLUSER
6   ALALYSLEUILEARGASPLYSVALALAGLY
7   HISSERLEUGLYTYRGLYPHEVALASNTYR
8   VALTHRALALYSASPALAGLUARGALAILE
9   ASNTHRLEUASNGLYLEUARGLEUGLNSER
10   LYSTHRILELYSVALSERTYRALAARGPRO
11   SER

Samples:

sample_1: DTT 10 mM; HuR_RRM1, [U-15N], 1.5 mM; sodium chloride 100 mM; sodium phosphate 30 mM

sample_2: DTT 10 mM; HuR_RRM1, [U-100% 13C; U-100% 15N], 1.5 mM; sodium chloride 100 mM; sodium phosphate 30 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D (H)CC(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

CcpNMR, CCPN - data analysis

TOPSPIN v3.1, Bruker Biospin - processing

NMR spectrometers:

  • Bruker DRX 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