BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18621

Title: NMR Chemical Shift Assignments of N terminal La motif domain of La protein   PubMed: 23239108

Deposition date: 2012-07-27 Original release date: 2013-02-14

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

Citation: Apostolidi, Maria; Vourtsis, Dionysios; Chasapis, Christos; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios. "H, 15N, 13C assignment and secondary structure determination of two domains of La protein from D. discoideum."  Biomol. NMR Assignments 8, 47-51 (2014).

Assembly members:
La_motif, polymer, 91 residues, 10534.9 Da.

Natural source:   Common Name: Dictyostelium discoideum   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):
La_motif: MSEETSTQILKQVEYYFSDS NFPRDKFLRSEAAKNVDNYI SIDVIASFNRMKTISTDLQL ITEALKKSTRLQVSEDGKMV RRLDPLPENID

Data sets:
Data typeCount
13C chemical shifts383
15N chemical shifts88
1H chemical shifts514

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1La-type RNA-binding domain1

Entities:

Entity 1, La-type RNA-binding domain 91 residues - 10534.9 Da.

1   METSERGLUGLUTHRSERTHRGLNILELEU
2   LYSGLNVALGLUTYRTYRPHESERASPSER
3   ASNPHEPROARGASPLYSPHELEUARGSER
4   GLUALAALALYSASNVALASPASNTYRILE
5   SERILEASPVALILEALASERPHEASNARG
6   METLYSTHRILESERTHRASPLEUGLNLEU
7   ILETHRGLUALALEULYSLYSSERTHRARG
8   LEUGLNVALSERGLUASPGLYLYSMETVAL
9   ARGARGLEUASPPROLEUPROGLUASNILE
10   ASP

Samples:

sample_1: La-type RNA-binding domain, [U-98% 15N], 0.37 mM; buffer salts 50 mM

sample_2: La-type RNA-binding domain, [U-98% 13C; U-98% 15N], 0.37 mM; buffer salts 50 mM

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

sample_conditions_2: ionic strength: 50 mM; pH: 7; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

EMBL Q54TG6

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