BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17837

Title: The assigned chemical shifts for the structured forms of apo-IscU   PubMed: 22203963

Deposition date: 2011-08-07 Original release date: 2012-02-28

Authors: Kim, Jin Hae; Tonelli, Marco; Markley, John

Citation: Kim, Jin Hae; Tonelli, Marco; Markley, John. "Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase"  Proc. Natl. Acad. Sci. U. S. A. 109, 454-459 (2012).

Assembly members:
IscU, polymer, 128 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
IscU: MAYSEKVIDHYENPRNVGSF DNNDENVGSGMVGAPACGDV MKLQIKVNDEGIIEDARFKT YGCGSAIASSSLVTEWVKGK SLDEAQAIKNTDIAEELELP PVKIHCSILAEDAIKAAIAD YKSKREAK

Data sets:
Data typeCount
13C chemical shifts69
15N chemical shifts91
1H chemical shifts96

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IscU1

Entities:

Entity 1, IscU 128 residues - Formula weight is not available

1   METALATYRSERGLULYSVALILEASPHIS
2   TYRGLUASNPROARGASNVALGLYSERPHE
3   ASPASNASNASPGLUASNVALGLYSERGLY
4   METVALGLYALAPROALACYSGLYASPVAL
5   METLYSLEUGLNILELYSVALASNASPGLU
6   GLYILEILEGLUASPALAARGPHELYSTHR
7   TYRGLYCYSGLYSERALAILEALASERSER
8   SERLEUVALTHRGLUTRPVALLYSGLYLYS
9   SERLEUASPGLUALAGLNALAILELYSASN
10   THRASPILEALAGLUGLULEUGLULEUPRO
11   PROVALLYSILEHISCYSSERILELEUALA
12   GLUASPALAILELYSALAALAILEALAASP
13   TYRLYSSERLYSARGGLUALALYS

Samples:

sample_1: IscU, [U-13C; U-15N], 1.5 mM; TRIS 50 mM; DTT 5 mM; DSS 0.7 mM; EDTA 0.5 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: . M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

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

VNMRJ, Varian - collection

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz

Related Database Links:

BMRB 15967 16245 16603 17282 17836 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

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