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 19298

Title: RBPMS2-Nter   PubMed: 25064856

Deposition date: 2013-06-12 Original release date: 2014-10-13

Authors: YANG, Yinshan

Citation: Sagnol, Sebastien; Yang, Yinshan; Bessin, Yannick; Allemand, Frederic; Hapkova, Ilona; Notarnicola, Cecile; Guichou, Jean-Francois; Faure, Sandrine; Labesse, Gilles; de Santa Barbara, Pascal. "Homodimerization of RBPMS2 through a new RRM-interaction motif is necessary to control smooth muscle plasticity"  Nucleic Acids Res. 42, 10173-10184 (2014).

Assembly members:
entity, polymer, 93 residues, 10501.271 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   Vector: Ecoli

Entity Sequences (FASTA):
entity: MEEEVRTLFVSGLPVDIKPR ELYLLFRPFKGYEGSLIKLT ARQPVGFVIFDSRAGAEAAK NALNGIRFDPENPQTLRLEF AKANTKMAKSKLE

Data sets:
Data typeCount
13C chemical shifts256
15N chemical shifts85
1H chemical shifts182

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RBPMS2-Nter, 11
2RBPMS2-Nter, 21

Entities:

Entity 1, RBPMS2-Nter, 1 93 residues - 10501.271 Da.

1   METGLUGLUGLUVALARGTHRLEUPHEVAL
2   SERGLYLEUPROVALASPILELYSPROARG
3   GLULEUTYRLEULEUPHEARGPROPHELYS
4   GLYTYRGLUGLYSERLEUILELYSLEUTHR
5   ALAARGGLNPROVALGLYPHEVALILEPHE
6   ASPSERARGALAGLYALAGLUALAALALYS
7   ASNALALEUASNGLYILEARGPHEASPPRO
8   GLUASNPROGLNTHRLEUARGLEUGLUPHE
9   ALALYSALAASNTHRLYSMETALALYSSER
10   LYSLEUGLU

Samples:

sample_1: entity, [U-100% 15N], 0.4-0.8 mM; entity, [U-100% 13C; U-100% 15N], 0.7 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.3; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1anisotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization

NMR spectrometers:

  • Bruker DRX 700 MHz

Related Database Links:

PDB
DBJ BAB26834 BAC87172 BAE25995 BAE33785 BAI47052
GB AAH21788 AAI69038 AAI72373 AAQ73311 ABQ82149
REF NP_001166897 NP_082306 NP_919248 XP_001174270 XP_002718127
SP Q6ZRY4 Q8VC52
AlphaFold Q6ZRY4 Q8VC52

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