BMRB Entry 17313

Title:
drosophila CstF-50 (1-92)
Deposition date:
2010-11-22
Original release date:
2011-01-18
Authors:
Mackereth, Cameron
Citation:

Citation: Moreno-Morcillo, Maria; Minvielle-Sebastia, Lionel; Mackereth, Cameron; Fribourg, Sebastien. "Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure."  RNA 17, 412-418 (2011).
PubMed: 21233223

Assembly members:

Assembly members:
dCstF-50, polymer, 94 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: pET

Data sets:
Data typeCount
13C chemical shifts259
15N chemical shifts82
1H chemical shifts82

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1dCstF-501

Entities:

Entity 1, dCstF-50 94 residues - Formula weight is not available

C-terminal -GS arises from the cloning site in the vector Protein is expressed with an N-terminal His6-tag which is removed by TEV protease, leaving a GH- at the N-terminus

1   METARGASPGLUILELEUASPPROSERASN
2   LEUVALLYSASNARGGLUILELEUTYRARG
3   LEUMETILESERGLNLEUMETTYRASPGLY
4   LEUGLULYSPHEALAMETGLULEUSERMET
5   LEUVALLYSALAASPGLNCYSALAPROSER
6   GLUARGLEULEUHISVALMETILEALAGLY
7   METGLNTHRLEUSERASPLYSASPLYSTHR
8   ASNSERASPASPVALLEUPROGLYILEASP
9   LEUGLUPHEGLUPROGLUALASERALALEU
10   ALAPROGLYSER

Samples:

sample_1: dCstF-50, [U-99% 13C; U-99% 15N], 0.7 – 2 mM; KH2PO4 1.05 mM; Na2HPO4 3 mM; NaCl 154 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 170 mM; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 17308
PDB
GB AAF57183 AAM11155 ACL84511 ACL89448 EDV52931
REF NP_651883 XP_001981061 XP_002043730 XP_002105645

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