BMRB Entry 18381

Title:
The backbone chemical shifts of IscU complexed with HscA
Deposition date:
2012-04-08
Original release date:
2012-09-14
Authors:
Kim, Jin Hae; Tonelli, Marco; Markley, John
Citation:

Citation: Kim, Jin Hae; Tonelli, Marco; Frederick, Ronnie; Chow, Darius C-F; Markley, John. "Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU)."  J. Biol. Chem. 287, 31406-31413 (2012).
PubMed: 22782893

Assembly members:

Assembly members:
IscU, polymer, 128 residues, Formula weight is not available
HscA, polymer, 616 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: pTrc99a

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts71
1H chemical shifts71

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IscU1
2HscA2

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

Entity 2, HscA 616 residues - Formula weight is not available

1   METALALEULEUGLNILESERGLUPROGLY
2   LEUSERALAALAPROHISGLNARGARGLEU
3   ALAALAGLYILEASPLEUGLYTHRTHRASN
4   SERLEUVALALATHRVALARGSERGLYGLN
5   ALAGLUTHRLEUALAASPHISGLUGLYARG
6   HISLEULEUPROSERVALVALHISTYRGLN
7   GLNGLNGLYHISSERVALGLYTYRASPALA
8   ARGTHRASNALAALALEUASPTHRALAASN
9   THRILESERSERVALLYSARGLEUMETGLY
10   ARGSERLEUALAASPILEGLNGLNARGTYR
11   PROHISLEUPROTYRGLNPHEGLNALASER
12   GLUASNGLYLEUPROMETILEGLUTHRALA
13   ALAGLYLEULEUASNPROVALARGVALSER
14   ALAASPILELEULYSALALEUALAALAARG
15   ALATHRGLUALALEUALAGLYGLULEUASP
16   GLYVALVALILETHRVALPROALATYRPHE
17   ASPASPALAGLNARGGLNGLYTHRLYSASP
18   ALAALAARGLEUALAGLYLEUHISVALLEU
19   ARGLEULEUASNGLUPROTHRALAALAALA
20   ILEALATYRGLYLEUASPSERGLYGLNGLU
21   GLYVALILEALAVALTYRASPLEUGLYGLY
22   GLYTHRPHEASPILESERILELEUARGLEU
23   SERARGGLYVALPHEGLUVALLEUALATHR
24   GLYGLYASPSERALALEUGLYGLYASPASP
25   PHEASPHISLEULEUALAASPTYRILEARG
26   GLUGLNALAGLYILEPROASPARGSERASP
27   ASNARGVALGLNARGGLULEULEUASPALA
28   ALAILEALAALALYSILEALALEUSERASP
29   ALAASPSERVALTHRVALASNVALALAGLY
30   TRPGLNGLYGLUILESERARGGLUGLNPHE
31   ASNGLULEUILEALAPROLEUVALLYSARG
32   THRLEULEUALACYSARGARGALALEULYS
33   ASPALAGLYVALGLUALAASPGLUVALLEU
34   GLUVALVALMETVALGLYGLYSERTHRARG
35   VALPROLEUVALARGGLUARGVALGLYGLU
36   PHEPHEGLYARGPROPROLEUTHRSERILE
37   ASPPROASPLYSVALVALALAILEGLYALA
38   ALAILEGLNALAASPILELEUVALGLYASN
39   LYSPROASPSERGLUMETLEULEULEUASP
40   VALILEPROLEUSERLEUGLYLEUGLUTHR
41   METGLYGLYLEUVALGLULYSVALILEPRO
42   ARGASNTHRTHRILEPROVALALAARGALA
43   GLNASPPHETHRTHRPHELYSASPGLYGLN
44   THRALAMETSERILEHISVALMETGLNGLY
45   GLUARGGLULEUVALGLNASPCYSARGSER
46   LEUALAARGPHEALALEUARGGLYILEPRO
47   ALALEUPROALAGLYGLYALAHISILEARG
48   VALTHRPHEGLNVALASPALAASPGLYLEU
49   LEUSERVALTHRALAMETGLULYSSERTHR
50   GLYVALGLUALASERILEGLNVALLYSPRO
51   SERTYRGLYLEUTHRASPSERGLUILEALA
52   SERMETILELYSASPSERMETSERTYRALA
53   GLUGLNASPVALLYSALAARGMETLEUALA
54   GLUGLNLYSVALGLUALAALAARGVALLEU
55   GLUSERLEUHISGLYALALEUALAALAASP
56   ALAALALEULEUSERALAALAGLUARGGLN
57   VALILEASPASPALAALAALAHISLEUSER
58   GLUVALALAGLNGLYASPASPVALASPALA
59   ILEGLULYSALAILELYSASNVALASPLYS
60   GLNTHRGLNASPPHEALAALAARGARGMET
61   ASPGLNSERVALARGARGALALEULYSGLY
62   HISSERVALASPGLUVAL

Samples:

sample_1: IscU, [U-13C; U-15N], 1.0 – 1.5 mM; TRIS 50 mM; DTT 5 mM; EDTA 0.5 mM; HscA2.0 – 3.0 mM; DSS 0.7 mM; D2O, [U-99% 2H], 7%; sodium azide 0.02%; D2O, [U-99% 2H], 7%

sample_conditions_1: ionic strength: 0 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 HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_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
  • Varian VNMRS 900 MHz

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