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 17308

Title: drosophila CstF-50 (1-65)   PubMed: 21233223

Authors: Mackereth, Cameron

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).

Assembly members:
dCstF-50, polymer, 68 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
dCstF-50: MRDEILDPSNLVKNREILYR LMISQLMYDGLEKFAMELSM LVKADQCAPSERLLHVMIAG MQTLSLGS

Data sets:
Data typeCount
13C chemical shifts198
15N chemical shifts65
1H chemical shifts117
heteronuclear NOE values58
T1 relaxation values55
T2 relaxation values52

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1

Entities:

Entity 1, protein 68 residues - Formula weight is not available

C-terminal -LGS 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   METGLNTHRLEUSERLEUGLYSER

Samples:

sample_1: dCstF-50, [U-99% 13C; U-99% 15N], 2 mM; d-Tris 50 mM; NaCl 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 295 K

sample_conditions_2: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 298 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 HN(CO)CAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQC hetnoesample_1isotropicsample_conditions_2
2D 1H-15N HSQC T1sample_1isotropicsample_conditions_2
2D 1H-15N HSQC T2sample_1isotropicsample_conditions_2

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 17313
PDB
GB AAF57183 AAM11155 ACL84511 ACL89448 ALC45969
REF NP_651883 XP_001358995 XP_001964574 XP_001981061 XP_002013189