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 17282

Title: Solution Structure of apo-IscU(WT)   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, polymer, 128 residues, 13865.679 Da.

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 shifts394
15N chemical shifts98
1H chemical shifts645
heteronuclear NOE values81
residual dipolar couplings74
T1 relaxation values79
T2 relaxation values79

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IscU1

Entities:

Entity 1, IscU 128 residues - 13865.679 Da.

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:

15N-IscU: IscU, [U-15N], 0.7 – 0.8 mM; TRIS 20 mM; DTT 5 mM; sodium chloride 150 mM; DSS 0.7 mM; EDTA 0.5 mM; H2O 93%; D2O 7%

15N-13C-IscU: IscU, [U-13C; U-15N], 1.4 mM; TRIS 20 mM; DTT 5 mM; DSS 0.7 mM; sodium chloride 150 mM; EDTA 0.5 mM; H2O 93%; D2O 7%

15N-IscU_aniso: IscU, [U-15N], 0.7 – 0.8 mM; TRIS 20 mM; DTT 5 mM; sodium chloride 150 mM; DSS 0.7 mM; EDTA 0.5 mM; Pf1 phage 12 mg/ml; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 150 mM; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESY15N-13C-IscUisotropicsample_conditions_1
3D 1H-13C NOESY15N-13C-IscUisotropicsample_conditions_1
2D 1H-15N HSQC15N-IscUisotropicsample_conditions_1
2D 1H-13C HSQC15N-13C-IscUisotropicsample_conditions_1
3D CBCA(CO)NH15N-13C-IscUisotropicsample_conditions_1
3D C(CO)NH15N-13C-IscUisotropicsample_conditions_1
3D HNCO15N-13C-IscUisotropicsample_conditions_1
3D HNCACB15N-13C-IscUisotropicsample_conditions_1
3D HBHA(CO)NH15N-13C-IscUisotropicsample_conditions_1
3D H(CCO)NH15N-13C-IscUisotropicsample_conditions_1
3D HCCH-TOCSY15N-13C-IscUisotropicsample_conditions_1
2D IPAP 1H-15N HSQC15N-IscU_anisoanisotropicsample_conditions_1

Software:

CYANA_3.0_intel v3.0_intel, P.GUNTERT ET AL. - refinement, structure solution

VNMRJ, Varian - collection

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

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz
  • Bruker DMX 750 MHz

Related Database Links:

BMRB 15967 16245 16603 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