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 27412

Title: dASCIZ LC8 binding domain (residues 241-388)

Deposition date: 2018-02-27 Original release date: 2018-03-02

Authors: Clark, Sarah; Barbar, Elisar; Fiala, Radovan; Novacek, Jiri

Citation: Clark, Sarah; Fiala, Radovan; Novacek, Jiri; Barbar, Elisar. "Assigned Chemical Shifts for dASCIZ LC8 Binding Domain (241-388)"  Not known ., .-..

Assembly members:
dASCIZ, polymer, 148 residues, 17117.5 Da.

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):
dASCIZ: MDVSYALEMSSQKLDMETQT EEDDLNEIRNEVLAPLLRDI ETQTPDTRGDIGTMTDDFPE EQEPVAVGSHFHAYSETEPM FDLQTSAHMYTQTCDDLFEE LGLSHIQTQTHWPDGLYNTQ HTQTCDEIMDELFPDNFQST CTQTRWLD

Data sets:
Data typeCount
13C chemical shifts362
15N chemical shifts133
1H chemical shifts468

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1dASCIZ1

Entities:

Entity 1, dASCIZ 148 residues - 17117.5 Da.

1   METASPVALSERTYRALALEUGLUMETSER
2   SERGLNLYSLEUASPMETGLUTHRGLNTHR
3   GLUGLUASPASPLEUASNGLUILEARGASN
4   GLUVALLEUALAPROLEULEUARGASPILE
5   GLUTHRGLNTHRPROASPTHRARGGLYASP
6   ILEGLYTHRMETTHRASPASPPHEPROGLU
7   GLUGLNGLUPROVALALAVALGLYSERHIS
8   PHEHISALATYRSERGLUTHRGLUPROMET
9   PHEASPLEUGLNTHRSERALAHISMETTYR
10   THRGLNTHRCYSASPASPLEUPHEGLUGLU
11   LEUGLYLEUSERHISILEGLNTHRGLNTHR
12   HISTRPPROASPGLYLEUTYRASNTHRGLN
13   HISTHRGLNTHRCYSASPGLUILEMETASP
14   GLULEUPHEPROASPASNPHEGLNSERTHR
15   CYSTHRGLNTHRARGTRPLEUASP

Samples:

sample_1: dASCIZ, [U-100% 13C; U-100% 15N], 0.3 mM; beta-mercaptoethanol 10 mM; sodium phosphate 10 mM; sodium chloride 10 mM; DSS 0.01 mM; sodium azide 1 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 283.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
5D HN(CA)CoNHsample_1isotropicsample_conditions_1
5D HabCabCONHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 800 MHz

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