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 25023

Title: 15N HSQC assignment of Drosophila ELF domain from FANCL   PubMed: 26149689

Deposition date: 2014-06-16 Original release date: 2016-07-01

Authors: Miles, Jennifer; Carroll, Ellis; Rowe, Michelle; Howard, Mark; Sihu, Ateesh; Frost, Mark; Williamson, Richard; Alpi, Arno; Walden, Helen

Citation: Miles, Jennifer; Carroll, Ellis; Rowe, Michelle; Howard, Mark; Sidhu, Ateesh; Frost, Mark; Williamson, Richard; Alpi, Arno; Walden, Helen. "The Fanconi Anemia DNA Repair Pathway Is Regulated by an Interaction between Ubiquitin and the E2-like Fold Domain of FANCL"  J. Biol. Chem. 290, 20995-21006 (2015).

Assembly members:
ELF, polymer, 104 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):
ELF: MESNEDVERLLCQKYPGLAA ELQPSGACIIRGVLGSEDTW RRLKLYLPHHPALHGFQLYV QESLEYKLYTSANLKLQDDW LLEDFLDHLPKILPAQKAPT VPKE

Data sets:
Data typeCount
15N chemical shifts74
1H chemical shifts81

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ELF1

Entities:

Entity 1, ELF 104 residues - Formula weight is not available

1   METGLUSERASNGLUASPVALGLUARGLEU
2   LEUCYSGLNLYSTYRPROGLYLEUALAALA
3   GLULEUGLNPROSERGLYALACYSILEILE
4   ARGGLYVALLEUGLYSERGLUASPTHRTRP
5   ARGARGLEULYSLEUTYRLEUPROHISHIS
6   PROALALEUHISGLYPHEGLNLEUTYRVAL
7   GLNGLUSERLEUGLUTYRLYSLEUTYRTHR
8   SERALAASNLEULYSLEUGLNASPASPTRP
9   LEULEUGLUASPPHELEUASPHISLEUPRO
10   LYSILELEUPROALAGLNLYSALAPROTHR
11   VALPROLYSGLU

Samples:

sample_1: ELF, [U-99% 15N], 0.6 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian Unity 600 MHz

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