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 34067

Title: Solution structure of the RBM5 OCRE domain in complex with polyproline SmN peptide.   PubMed: 27894420

Deposition date: 2016-11-17 Original release date: 2016-12-05

Authors: Mourao, A.; Sattler, M.; Bonnal, S.; Komal, S.; Warner, L.; Bordonne, R.; Valcarcel, J.

Citation: Mourao, A.; Bonnal, S.; Komal, S.; Warner, L.; Bordonne, R.; Valcarcel, J.; Sattler, M.. "Structural basis for the recognition ofspliceosomal SmN B B proteins by theRBM5 OCRE domain in splicing regulation"  Elife 5, 1-25 (2016).

Assembly members:
entity_1, polymer, 64 residues, 7436.785 Da.
entity_2, polymer, 11 residues, 1136.371 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: GAMGTKYAVPDTSTYQYDES SGYYYDPTTGLYYDPNSQYY YNSLTQQYLYWDGEKETYVP AAES
entity_2: GMRPPPPGIRG

Data sets:
Data typeCount
13C chemical shifts292
15N chemical shifts65
1H chemical shifts443

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 64 residues - 7436.785 Da.

1   GLYALAMETGLYTHRLYSTYRALAVALPRO
2   ASPTHRSERTHRTYRGLNTYRASPGLUSER
3   SERGLYTYRTYRTYRASPPROTHRTHRGLY
4   LEUTYRTYRASPPROASNSERGLNTYRTYR
5   TYRASNSERLEUTHRGLNGLNTYRLEUTYR
6   TRPASPGLYGLULYSGLUTHRTYRVALPRO
7   ALAALAGLUSER

Entity 2, entity_2 11 residues - 1136.371 Da.

1   GLYMETARGPROPROPROPROGLYILEARG
2   GLY

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 2 mM; entity_1, [U-99% 15N], 2 mM; entity_1, [U-13C; U-15N], 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_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 HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement

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

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX500 500 MHz
  • Bruker DRX600 600 MHz
  • Bruker DRX900 900 MHz

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