BMRB Entry 15541

Title:
NMR study of the interaction of HscB with apo-IscU
Deposition date:
2007-10-31
Original release date:
2008-08-18
Authors:
Fuezery, Anna; Tonelli, Marco; Ta, Dennis; Cornilescu, Gabriel; Vickery, Larry; Markley, John
Citation:

Citation: Fuezery, Anna; Tonelli, Marco; Ta, Dennis; Cornilescu, Gabriel; Vickery, Larry; Markley, John. "Solution Structure of the Iron-Sulfur Cluster Cochaperone HscB and Its Binding Surface for the Iron-Sulfur Assembly Scaffold Protein IscU"  Biochemistry 47, 9394-9404 (2008).
PubMed: 18702525

Assembly members:

Assembly members:
HscB, polymer, 171 residues, 20137 Da.
IscU, polymer, 127 residues, Formula weight is not available

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: pTrcIscU

Data typeCount
13C chemical shifts469
15N chemical shifts276
1H chemical shifts698
heteronuclear NOE values229
residual dipolar couplings274
T1 relaxation values228
T2 relaxation values228

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IscU2
2HscB1

Entities:

Entity 2, IscU 127 residues - Formula weight is not available

1   ALATYRSERGLULYSVALILEASPHISTYR
2   GLUASNPROARGASNVALGLYSERPHEASP
3   ASNASNASPGLUASNVALGLYSERGLYMET
4   VALGLYALAPROALACYSGLYASPVALMET
5   LYSLEUGLNILELYSVALASNASPGLUGLY
6   ILEILEGLUASPALAARGPHELYSTHRTYR
7   GLYCYSGLYSERALAILEALASERSERSER
8   LEUVALTHRGLUTRPVALLYSGLYLYSSER
9   LEUASPGLUALAGLNALAILELYSASNTHR
10   ASPILEALAGLUGLULEUGLULEUPROPRO
11   VALLYSILEHISCYSSERILELEUALAGLU
12   ASPALAILELYSALAALAILEALAASPTYR
13   LYSSERLYSARGGLUALALYS

Entity 1, HscB 171 residues - 20137 Da.

1   METASPTYRPHETHRLEUPHEGLYLEUPRO
2   ALAARGTYRGLNLEUASPTHRGLNALALEU
3   SERLEUARGPHEGLNASPLEUGLNARGGLN
4   TYRHISPROASPLYSPHEALASERGLYSER
5   GLNALAGLUGLNLEUALAALAVALGLNGLN
6   SERALATHRILEASNGLNALATRPGLNTHR
7   LEUARGHISPROLEUMETARGALAGLUTYR
8   LEULEUSERLEUHISGLYPHEASPLEUALA
9   SERGLUGLNHISTHRVALARGASPTHRALA
10   PHELEUMETGLUGLNLEUGLULEUARGGLU
11   GLULEUASPGLUILEGLUGLNALALYSASP
12   GLUALAARGLEUGLUSERPHEILELYSARG
13   VALLYSLYSMETPHEASPTHRARGHISGLN
14   LEUMETVALGLUGLNLEUASPASNGLUTHR
15   TRPASPALAALAALAASPTHRVALARGLYS
16   LEUARGPHELEUASPLYSLEUARGSERSER
17   ALAGLUGLNLEUGLUGLULYSLEULEUASP
18   PHE

Samples:

sample_1: HscB, [U-13C; U-15N], 1 mM; TRIS 18 mM; DTT 10 mM; EDTA 0.2 mM; H20 93%; D2O 7%

sample_2: HscB, [U-13C; U-15N], 1 mM; TRIS 18 mM; DTT 10 mM; EDTA 0.2 mM; sodium azide 0.08 mM; DSS 0.1 mM; H20 93%; D2O 7%

sample_3: HscB, [U-13C; U-15N], 1 mM; TRIS 16 mM; Pf1 phage 11 mg/mL; H20 93%; D2O 7%

sample_4: HscB, [U-15N], 0.9 mM; TRIS 22 mM; DTT 9 mM; H20 93%; D2O 7%

sample_5: HscB, [U-15N], 0.4 mM; TRIS 19 mM; DTT 10 mM; DSS 1 mM; IscU 0.9 mM; H20 93%; D2O 7%

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
3D HN-coupled HNCOsample_2isotropicsample_conditions_1
3D HN-coupled HNCOsample_3anisotropicsample_conditions_1
3D HA-coupled HN(CO)CAsample_2isotropicsample_conditions_1
3D HA-coupled HN(CO)CAsample_3anisotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1

Software:

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

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

VNMR, Varian - collection

VNMRJ, Varian - collection

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Varian Unity-INOVA 600 MHz
  • Varian Unity-INOVA 800 MHz
  • Varian Unity-INOVA 900 MHz
  • Bruker DMX-Avance 600 MHz

Related Database Links:

PDB
DBJ BAA16421 BAB36816 BAG78337 BAI26772 BAI31801 BAA16423 BAB36818 BAG78339 BAH64655 BAI26774
EMBL CAP76979 CAQ32900 CAQ88189 CAQ99418 CAR03969 CAD02745 CAP76981 CAQ32902 CAQ88187 CAQ99420
GB AAA18299 AAC75580 AAG57641 AAN44073 AAN81502 AAC75582 AAG57643 AAL21436 AAN44075 AAN81505
PIR E85897 AE0824
REF NP_311420 NP_417022 NP_708366 WP_000384389 WP_000384404 NP_289086 NP_311422 NP_417024 NP_457073 NP_461477
SP A1AE64 A7ZPX0 A8A333 B1IWD4 B1LNI2 P0ACD4 P0ACD5 P0ACD6 P0ACD7
BMRB 15967 16245 16603 17282 17836 17837 17844 18359 18360 18361 18362 18381 18750 18754 7432
AlphaFold B1LNI2 B1IWD4 A8A333 A7ZPX0 A1AE64 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