BMRB Entry 25239

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25239

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Title:
NMR Chemical Shift Assignments of La-RRM1 of La protein.
Deposition date:
2014-09-19
Original release date:
2015-06-04
Authors:
Bouras, Georgios; Argyriou, Aikaterini; Apostolidi, Maria; Chasapis, Christos; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios
Citation:

Citation: Chasapis, Christos; Argyriou, Aikaterini; Apostolidi, Maria; Konstantinidou, Parthena; Bentrop, Detlef; Stathopoulos, Constantinos; Spyroulias, Georgios. "1H, 13C and 15N backbone and side-chain resonance assignment of the LAM-RRM1 N-terminal module of La protein from Dictyostelium discoideum"  Biomol. NMR Assign. 9, 303-307 (2015).
PubMed: 25687647

Assembly members:

Assembly members:
La-RRM1, polymer, 191 residues, 22032.90 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
La-RRM1: MSEETSTQILKQVEYYFSDS NFPRDKFLRSEAAKNVDNYI SIDVIASFNRMKTISTDLQL ITEALKKSTRLQVSEDGKMV RRLDPLPENIDCGKTLYSKG WPEDTTIEKVQEFFNANGGY KVVSVRLRKKSDKSFKGSFL ADFETEEIVNKIITEAPKLG EKELIYQTFKQFSDEKKDEK EKFFASTNGDK

Data sets:
Data typeCount
13C chemical shifts822
15N chemical shifts195
1H chemical shifts1136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 191 residues - 22032.90 Da.

1   METSERGLUGLUTHRSERTHRGLNILELEU
2   LYSGLNVALGLUTYRTYRPHESERASPSER
3   ASNPHEPROARGASPLYSPHELEUARGSER
4   GLUALAALALYSASNVALASPASNTYRILE
5   SERILEASPVALILEALASERPHEASNARG
6   METLYSTHRILESERTHRASPLEUGLNLEU
7   ILETHRGLUALALEULYSLYSSERTHRARG
8   LEUGLNVALSERGLUASPGLYLYSMETVAL
9   ARGARGLEUASPPROLEUPROGLUASNILE
10   ASPCYSGLYLYSTHRLEUTYRSERLYSGLY
11   TRPPROGLUASPTHRTHRILEGLULYSVAL
12   GLNGLUPHEPHEASNALAASNGLYGLYTYR
13   LYSVALVALSERVALARGLEUARGLYSLYS
14   SERASPLYSSERPHELYSGLYSERPHELEU
15   ALAASPPHEGLUTHRGLUGLUILEVALASN
16   LYSILEILETHRGLUALAPROLYSLEUGLY
17   GLULYSGLULEUILETYRGLNTHRPHELYS
18   GLNPHESERASPGLULYSLYSASPGLULYS
19   GLULYSPHEPHEALASERTHRASNGLYASP
20   LYS

Samples:

sample_1: La-RRM1, [U-99% 15N], 0,5 mM; H2O 90%; D2O 10%

sample_2: La-RRM1, [U-99% 13C; U-99% 15N], 0,5 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 CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance III 700 MHz

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