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 25885

Title: RBM24 RRM domain   PubMed: 27002326

Deposition date: 2015-11-09 Original release date: 2016-06-15

Authors: Upadhyay, Santosh Kumar; Mackereth, Cameron

Citation: Upadhyay, Santosh Kumar; Mackereth, Cameron. "1H, 15N and 13C backbone and side chain resonance assignments of the RRM domain from human RBM24"  Biomol. NMR Assign. 10, 237-240 (2016).

Assembly members:
RBM24, polymer, 105 residues, Formula weight is not available

Natural source:   Common Name: humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
RBM24: GAMAHTTQKDTTYTKIFVGG LPYHTTDASLRKYFEVFGEI EEAVVITDRQTGKSRGYGFV TMADRAAAERACKDPNPIID GRKANVNLAYLGAKPRIMQP GFAFG

Data sets:
Data typeCount
13C chemical shifts450
15N chemical shifts104
1H chemical shifts708

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RBM241

Entities:

Entity 1, RBM24 105 residues - Formula weight is not available

The N-terminal Gly-Ala-Met-Ala remains following removal of the His6-tag by TEV potease

1   GLYALAMETALAHISTHRTHRGLNLYSASP
2   THRTHRTYRTHRLYSILEPHEVALGLYGLY
3   LEUPROTYRHISTHRTHRASPALASERLEU
4   ARGLYSTYRPHEGLUVALPHEGLYGLUILE
5   GLUGLUALAVALVALILETHRASPARGGLN
6   THRGLYLYSSERARGGLYTYRGLYPHEVAL
7   THRMETALAASPARGALAALAALAGLUARG
8   ALACYSLYSASPPROASNPROILEILEASP
9   GLYARGLYSALAASNVALASNLEUALATYR
10   LEUGLYALALYSPROARGILEMETGLNPRO
11   GLYPHEALAPHEGLY

Samples:

sample_1: RBM24, [U-99% 13C; U-99% 15N], 0.25 mM; sodium phosphate 20 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

sample_2: RBM24, [U-10% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O 100%

sample_conditions_1: ionic strength: 320 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCC(CO)-TOCSYsample_1isotropicsample_conditions_1
3D HCC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC CTsample_2isotropicsample_conditions_1
D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - Visualisation, collection

NMRPipe v2014, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.115, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

SP Q9BX46

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