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 19967

Title: Solution NMR assignment of C-terminal RRM domain of La protein from D. discoideum.   PubMed: 25281001

Deposition date: 2014-05-12 Original release date: 2018-02-27

Authors: Bouras, Georgios; Argyriou, Aikaterini; Makrynitsa, Garyfallia; Apostolidi, Maria; Chasapis, Christos; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios

Citation: Argyriou, Aikaterini; Chasapis, Christos; Apostolidi, Maria; Konstantinidou, Parthena; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios. "Backbone and side chain NMR assignment, along with the secondary structure prediction of RRM2 domain of La protein from a lower eukaryote exhibiting identical structural organization with its human homolog"  Biomol NMR Assign. 9, 219-222 (2015).

Assembly members:
CRRM, polymer, 105 residues, 12027.6 Da.

Natural source:   Common Name: cellular slime mold   Taxonomy ID: 44689   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Dictyostelium discoideum

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

Entity Sequences (FASTA):
CRRM: KDVKKEVEEEEVMIPGVILC FKGVGKGLHRGDIKEIFSQY GEVQFVGYNSDEENGSVRYK TAESCKRAIESLTETKKEIG GQIPTYNLLEGEEEKKEWEK IIERK

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts108
1H chemical shifts743

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CRRM domain1

Entities:

Entity 1, CRRM domain 105 residues - 12027.6 Da.

1   LYSASPVALLYSLYSGLUVALGLUGLUGLU
2   GLUVALMETILEPROGLYVALILELEUCYS
3   PHELYSGLYVALGLYLYSGLYLEUHISARG
4   GLYASPILELYSGLUILEPHESERGLNTYR
5   GLYGLUVALGLNPHEVALGLYTYRASNSER
6   ASPGLUGLUASNGLYSERVALARGTYRLYS
7   THRALAGLUSERCYSLYSARGALAILEGLU
8   SERLEUTHRGLUTHRLYSLYSGLUILEGLY
9   GLYGLNILEPROTHRTYRASNLEULEUGLU
10   GLYGLUGLUGLULYSLYSGLUTRPGLULYS
11   ILEILEGLUARGLYS

Samples:

sample_1: CRRM, [U-99% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: CRRM, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_3: CRRM 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III 700 MHz

Related Database Links:

UNP Q54TG6

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