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 27089

Title: ISCU(D39V)   PubMed: 29406711

Deposition date: 2017-04-30 Original release date: 2017-05-23

Authors: Cai, Kai; Markley, John

Citation: Cai, Kai; Frederick, Ronnie; Tonelli, Marco; Markley, John. "ISCU(M108I) and ISCU(D39V) Differ from Wild-Type ISCU in Their Failure To Form Cysteine Desulfurase Complexes Containing Both Frataxin and Ferredoxin"  Biochemistry 57, 1491-1500 (2018).

Assembly members:
ISCU, polymer, 135 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-SUMO

Entity Sequences (FASTA):
ISCU: RLYHKKVVDHYENPRNVGSL DKTSKNVGTGLVGAPACGVV MKLQIQVDEKGKIVDARFKT FGCGSAIASSSLATEWVKGK TVEEALTIKNTDIAKELCLP PVKLHCSMLAEDAIKAALAD YKLKQEPKKGEAEKK

Data sets:
Data typeCount
13C chemical shifts211
15N chemical shifts103
1H chemical shifts103

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ISCU monomer1

Entities:

Entity 1, ISCU monomer 135 residues - Formula weight is not available

1   ARGLEUTYRHISLYSLYSVALVALASPHIS
2   TYRGLUASNPROARGASNVALGLYSERLEU
3   ASPLYSTHRSERLYSASNVALGLYTHRGLY
4   LEUVALGLYALAPROALACYSGLYVALVAL
5   METLYSLEUGLNILEGLNVALASPGLULYS
6   GLYLYSILEVALASPALAARGPHELYSTHR
7   PHEGLYCYSGLYSERALAILEALASERSER
8   SERLEUALATHRGLUTRPVALLYSGLYLYS
9   THRVALGLUGLUALALEUTHRILELYSASN
10   THRASPILEALALYSGLULEUCYSLEUPRO
11   PROVALLYSLEUHISCYSSERMETLEUALA
12   GLUASPALAILELYSALAALALEUALAASP
13   TYRLYSLEULYSGLNGLUPROLYSLYSGLY
14   GLUALAGLULYSLYS

Samples:

sample_1: ISCU(D39V), [U-100% 13C; U-100% 15N], 0.5 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 3 mM; DSS 0.01 mM; EDTA 5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

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