BMRB Entry 25059

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25059

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Title:
Backbone assignment for cold shock domain 1 of Drosophila Upstream of N-ras
Deposition date:
2014-07-01
Original release date:
2014-11-07
Authors:
Wang, Iren; Hennig, Janosch; Sattler, Michael
Citation:

Citation: Hennig, Janosch; Militti, Cristina; Popowicz, Grzegorz; Wang, Iren; Sonntag, Miriam; Geerlof, Arie; Gabel, Frank; Gebauer, Fatima; Sattler, Michael. "Structural basis for the assembly of the Sxl-Unr translation regulatory complex"  Nature 515, 287-290 (2014).
PubMed: 25209665

Assembly members:

Assembly members:
dCSD1, polymer, 72 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Fruit Fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETtrx-1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
dCSD1: GAMATRETGIIEKLLHSYGF IQCCERQARLFFHFSQFSGN IDHLKIGDPVEFEMTYDRRT GKPIASQVSKIA

Data sets:
Data typeCount
1H chemical shifts425
13C chemical shifts270
15N chemical shifts72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cold shock domain 1 of drosophila UNR1

Entities:

Entity 1, cold shock domain 1 of drosophila UNR 72 residues - Formula weight is not available

Residues 1-4 represent a residual non-native tag

1   GLYALAMETALATHRARGGLUTHRGLYILE
2   ILEGLULYSLEULEUHISSERTYRGLYPHE
3   ILEGLNCYSCYSGLUARGGLNALAARGLEU
4   PHEPHEHISPHESERGLNPHESERGLYASN
5   ILEASPHISLEULYSILEGLYASPPROVAL
6   GLUPHEGLUMETTHRTYRASPARGARGTHR
7   GLYLYSPROILEALASERGLNVALSERLYS
8   ILEALA

Samples:

sample_1: CSD1, [U-99% 13C; U-99% 15N], 0.1 – 0.8 mM; potassium phosphate 10 mM; sodium chloride 50 mM; DTT 10 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: temperature: 298 K; pH: 6; pressure: 1 atm; ionic strength: 0.05 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - data analysis, peak picking

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

GB AAF50415.2
BMRB 25060 25078
PDB

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