BMRB Entry 34429

Title:
Mouse RBM20 RRM domain
Deposition date:
2019-08-29
Original release date:
2019-11-01
Authors:
Mackereth, C.; Upadhyay, S.
Citation:

Citation: Upadhyay, Santosh Kumar; Mackereth, Cameron. "Structural basis of UCUU RNA motif recognition by splicing factor RBM20"  Nucleic Acids Res. 48, 4538-4550 (2020).
PubMed: 32187365

Assembly members:

Assembly members:
entity_1, polymer, 112 residues, 12571.588 Da.

Natural source:

Natural source:   Common Name: House mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET-His1a

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts119
1H chemical shifts821

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 112 residues - 12571.588 Da.

1   GLYALAMETALAGLNARGLYSGLYALAGLY
2   ARGVALVALHISILECYSASNLEUPROGLU
3   GLYSERCYSTHRGLUASNASPVALILEASN
4   LEUGLYLEUPROPHEGLYLYSVALTHRASN
5   TYRILELEUMETLYSSERTHRASNGLNALA
6   PHELEUGLUMETALATYRTHRGLUALAALA
7   GLNALAMETVALGLNTYRTYRGLNGLULYS
8   PROALAILEILEASNGLYGLULYSLEULEU
9   ILEARGMETSERTHRARGTYRLYSGLULEU
10   GLNLEULYSLYSPROGLYLYSASNVALALA
11   ALAILEILEGLNASPILEHISSERGLNARG
12   GLUARG

Samples:

sample_1: Mouse RBM20 RRM domain, [U-99% 13C; U-99% 15N], 400 uM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM

sample_2: Mouse RBM20 RRM domain 500 uM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM

sample_3: Mouse RBM20 RRM domain, [U-99% 13C], 170 uM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM

sample_4: Mouse RBM20 RRM domain, [U-10% 13C; U-99% 15N], 100 uM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D H(C)(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D (H)C(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC CTsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

Sparky, Goddard - chemical shift assignment

ARIA, Linge, O'Donoghue and Nilges - structure calculation

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

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz
  • Bruker AVANCE III 800 MHz

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