BMRB Entry 16245

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16245

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Title:
Assignment of the 1H and 15N Resonances of Escherichia coli IscU.
Deposition date:
2009-04-07
Original release date:
2009-04-13
Authors:
Pastore, Chiara; Prischi, Filippo; Au, Yunghan; Nair, Margie; Pastore, Annalisa
Citation:

Citation: Adinolfi, Salvatore; Rizzo, Francesca; Masino, Laura; Nair, Margie; Martin, Stephen; Pastore, Annalisa; Temussi, Piero Andrea. "Bacterial IscU is a well folded and functional single domain protein."  Eur. J. Biochem. 271, 2093-2100 (2004).
PubMed: 15153099

Assembly members:

Assembly members:
IscU, polymer, 130 residues, 13975 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: petm30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IscU: GAMAYSEKVIDHYENPRNVG SFDNNDENVGSGMVGAPACG DVMKLQIKVNDEGIIEDARF KTYGCGSAIASSSLVTEWVK GKSLDEAQAIKNTDIAEELE LPPVKIHCSILAEDAIKAAI ADYKSKREAK

Data sets:
Data typeCount
15N chemical shifts98
1H chemical shifts98

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IscU1
2ZN2

Entities:

Entity 1, IscU 130 residues - 13975 Da.

1   GLYALAMETALATYRSERGLULYSVALILE
2   ASPHISTYRGLUASNPROARGASNVALGLY
3   SERPHEASPASNASNASPGLUASNVALGLY
4   SERGLYMETVALGLYALAPROALACYSGLY
5   ASPVALMETLYSLEUGLNILELYSVALASN
6   ASPGLUGLYILEILEGLUASPALAARGPHE
7   LYSTHRTYRGLYCYSGLYSERALAILEALA
8   SERSERSERLEUVALTHRGLUTRPVALLYS
9   GLYLYSSERLEUASPGLUALAGLNALAILE
10   LYSASNTHRASPILEALAGLUGLULEUGLU
11   LEUPROPROVALLYSILEHISCYSSERILE
12   LEUALAGLUASPALAILELYSALAALAILE
13   ALAASPTYRLYSSERLYSARGGLUALALYS

Entity 2, ZN - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: IscU, [U-95% 15N], 0.43 mM; TRIS 20 mM; sodium chloride 150 mM; beta-mercaptoethanol 20 mM; H2O 90%; D2O 10%

sample_2: IscU, [U-95% 13C; U-90% 15N], 0.43 mM; TRIS 20 mM; sodium chloride 150 mM; beta-mercaptoethanol 20 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15967 16603 17282 17836 17837 17844 18359 18360 18361 18362 18381 18750 18754
PDB
DBJ BAA16423 BAB36818 BAG78339 BAH64655 BAI26774
EMBL CAD02745 CAP76981 CAQ32902 CAQ88187 CAQ99420
GB AAC75582 AAG57643 AAL21436 AAN44075 AAN81505
PIR AE0824
REF NP_311422 NP_417024 NP_457073 NP_461477 NP_708368
SP P0ACD4 P0ACD5 P0ACD6 P0ACD7
AlphaFold P0ACD4 P0ACD5 P0ACD6 P0ACD7

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