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 18360

Title: The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(E111A)   PubMed: 22734684

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

Citation: Kim, Jin Hae; Tonelli, Marco; Kim, Taewook; Markley, John. "Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli."  Biochemistry 51, 5557-5563 (2012).

Assembly members:
IscU(E111A), 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(E111A): MAYSEKVIDHYENPRNVGSF DNNDENVGSGMVGAPACGDV MKLQIKVNDEGIIEDARFKT YGCGSAIASSSLVTEWVKGK SLDEAQAIKNTDIAEELELP PVKIHCSILAADAIKAAIAD YKSKREAK

Data sets:
Data typeCount
13C chemical shifts243
15N chemical shifts80
1H chemical shifts80
T1 relaxation values75
T2 relaxation values75
heteronuclear NOE values76

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1IscU(E111A)1

Entities:

Entity 1, IscU(E111A) 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   ALAASPALAILELYSALAALAILEALAASP
13   TYRLYSSERLYSARGGLUALALYS

Samples:

sample_1: IscU(E111A), [U-13C; U-15N], 1.5 – 2 mM; TRIS 20 mM; DTT 5 mM; EDTA 0.5 mM; sodium chloride 150 mM; DSS 0.7 mM; D2O, [U-99% 2H], 7%; sodium azide 0.02%; H2O, [U-99% 2H], 93%

sample_conditions_1: ionic strength: 0.15 M; pH: 8; 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 HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_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 VNMRS 600 MHz

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