BMRB Entry 34079

Title:
Solution NMR structure of hnRNP A1 RRM1 in complex with 5'-UUAGGUC-3' RNA
Deposition date:
2016-12-16
Original release date:
2017-11-29
Authors:
Barraud, P.; Allain, F.
Citation:

Citation: Beusch, Irene; Barraud, Pierre; Moursy, Ahmed; Clery, Antoine; Allain, Frederic Hai-Trieu. "Tandem hnRNP A1 RNA recognition motifs act in concert to repress the splicing of survival motor neuron exon 7"  Elife 6, e25736-e25736 (2017).
PubMed: 28650318

Assembly members:

Assembly members:
entity_1, polymer, 97 residues, 11003.271 Da.
entity_2, polymer, 7 residues, 2198.339 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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts293
15N chemical shifts93
1H chemical shifts637

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 97 residues - 11003.271 Da.

1   ALASERLYSSERGLUSERPROLYSGLUPRO
2   GLUGLNLEUARGLYSLEUPHEILEGLYGLY
3   LEUSERPHEGLUTHRTHRASPGLUSERLEU
4   ARGSERHISPHEGLUGLNTRPGLYTHRLEU
5   THRASPCYSVALVALMETARGASPPROASN
6   THRLYSARGSERARGGLYPHEGLYPHEVAL
7   THRTYRALATHRVALGLUGLUVALASPALA
8   ALAMETASNALAARGPROHISLYSVALASP
9   GLYARGVALVALGLUPROLYSARGALAVAL
10   SERARGGLUASPSERGLNARG

Entity 2, entity_2 7 residues - 2198.339 Da.

1   UUAGGUC

Samples:

sample_3: hnRNP A1 RRM1, [U-99% 15N], 1.0 mM; RNA UUAGGUC 1.0 mM

sample_4: hnRNP A1 RRM1, [U-99% 13C; U-99% 15N], 1.0 mM; RNA UUAGGUC 1.0 mM

sample_1: hnRNP A1 RRM1, [U-99% 15N], 1.0 mM; RNA UUAGGUC 1.0 mM

sample_2: hnRNP A1 RRM1, [U-99% 13C; U-99% 15N], 1.0 mM; RNA UUAGGUC 1.0 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1not availablesample_conditions_1
2D 1H-13C HSQC aliphaticsample_4not availablesample_conditions_1
2D 1H-13C HSQC aromaticsample_4not availablesample_conditions_1
3D HNCAsample_2not availablesample_conditions_1
3D HNCACBsample_2not availablesample_conditions_1
3D CBCA(CO)NHsample_2not availablesample_conditions_1
3D HNCOsample_2not availablesample_conditions_1
3D HCc(CO)NH TOCSYsample_2not availablesample_conditions_1
3D hCC(CO)NH TOCSYsample_2not availablesample_conditions_1
3D 1H-15N NOESYsample_1not availablesample_conditions_1
3D 1H-13C NOESY aliphaticsample_2not availablesample_conditions_1
3D F1eF3f 13C-filtered/edited NOESYsample_4not availablesample_conditions_1
2D F1fF2f 13C-filtered NOESYsample_4not availablesample_conditions_1
2D 1H-1H TOCSYsample_3not availablesample_conditions_1
2D 1H-1H NOESYsample_3not availablesample_conditions_1
3D 1H-13C NOESY aromaticsample_2not availablesample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker AvanceIII 500 MHz
  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 700 MHz
  • Bruker AvanceIII 750 MHz
  • Bruker Avance 900 MHz

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