BMRB Entry 30638

Title:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Deposition date:
2019-07-12
Original release date:
2019-09-11
Authors:
Jiang, Y.; Rossi, P.; Kalodimos, C.
Citation:

Citation: Jiang, Y.; Rossi, P.; Kalodimos, C.. "Structural basis for client recognition and activity of Hsp40 chaperones"  Science 365, 1313-1319 (2019).
PubMed: 31604242

Assembly members:

Assembly members:
entity_1, polymer, 280 residues, 31023.424 Da.
entity_2, polymer, 471 residues, 49492.367 Da.

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 300852   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Data sets:
Data typeCount
13C chemical shifts799
15N chemical shifts599
1H chemical shifts1328

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_22
3entity_1, 21

Entities:

Entity 1, entity_1, 1 280 residues - 31023.424 Da.

1   METALAALALYSLYSASPTYRTYRALAILE
2   LEUGLYVALPROARGASNALATHRGLNGLU
3   GLUILELYSARGALATYRLYSARGLEUALA
4   ARGGLNTYRHISPROASPVALASNLYSSER
5   PROGLUALAGLUGLULYSPHELYSGLUILE
6   ASNGLUALATYRALAVALLEUSERASPPRO
7   GLULYSARGARGILETYRASPTHRTYRGLY
8   THRTHRGLUALAPROPROPROPROPROPRO
9   GLYGLYTYRASPPHESERGLYPHEASPVAL
10   GLUASPPHESERGLUPHEPHEGLNGLULEU
11   PHEGLYPROGLYLEUPHEGLYGLYPHEGLY
12   ARGARGSERARGLYSGLYARGASPLEUARG
13   ALAGLULEUPROLEUTHRLEUGLUGLUALA
14   PHEHISGLYGLYGLUARGVALVALGLUVAL
15   ALAGLYARGARGVALSERVALARGILEPRO
16   PROGLYVALARGGLUGLYSERVALILEARG
17   VALPROGLYMETGLYGLYGLNGLYASNPRO
18   PROGLYASPLEULEULEUVALVALARGLEU
19   LEUPROHISPROVALPHEARGLEUGLUGLY
20   GLNASPLEUTYRALATHRLEUASPVALPRO
21   ALAPROILEALAVALVALGLYGLYLYSVAL
22   ARGALAMETTHRLEUGLUGLYPROVALGLU
23   VALALAVALPROPROARGTHRGLNALAGLY
24   ARGLYSLEUARGLEULYSGLYLYSGLYPHE
25   PROGLYPROALAGLYARGGLYASPLEUTYR
26   LEUGLUVALARGILETHRILEPROGLUARG
27   LEUTHRPROGLUGLUGLUALALEUTRPLYS
28   LYSLEUALAGLUALATYRTYRALAARGALA

Entity 2, entity_2 471 residues - 49492.367 Da.

1   METLYSGLNSERTHRILEALALEUALALEU
2   LEUPROLEULEUPHETHRPROVALTHRLYS
3   ALAARGTHRPROGLUMETPROVALLEUGLU
4   ASNARGALAALAGLNGLYASPILETHRALA
5   PROGLYGLYALAARGARGLEUTHRGLYASP
6   GLNTHRALAALALEUARGASPSERLEUSER
7   ASPLYSPROALALYSASNILEILELEULEU
8   ILEGLYASPGLYMETGLYASPSERGLUILE
9   THRALAALAARGASNTYRALAGLUGLYALA
10   GLYGLYPHEPHELYSGLYILEASPALALEU
11   PROLEUTHRGLYGLNTYRTHRHISTYRALA
12   LEUASNLYSLYSTHRGLYLYSPROASPTYR
13   VALTHRASPSERALAALASERALATHRALA
14   TRPSERTHRGLYVALLYSTHRTYRASNGLY
15   ALALEUGLYVALASPILEHISGLULYSASP
16   HISPROTHRILELEUGLUMETALALYSALA
17   ALAGLYLEUALATHRGLYASNVALSERTHR
18   ALAGLULEUGLNASPALATHRPROALAALA
19   LEUVALALAHISVALTHRSERARGLYSCYS
20   TYRGLYPROSERALATHRSERGLULYSCYS
21   PROGLYASNALALEUGLULYSGLYGLYLYS
22   GLYSERILETHRGLUGLNLEULEUASNALA
23   ARGALAASPVALTHRLEUGLYGLYGLYALA
24   LYSTHRPHEALAGLUTHRALATHRALAGLY
25   GLUTRPGLNGLYLYSTHRLEUARGGLUGLN
26   ALAGLNALAARGGLYTYRGLNLEUVALSER
27   ASPALAALASERLEUASNSERVALTHRGLU
28   ALAASNGLNGLNLYSPROLEULEUGLYLEU
29   PHEALAASPGLYASNMETPROVALARGTRP
30   LEUGLYPROLYSALATHRTYRHISGLYASN
31   ILEASPLYSPROALAVALTHRCYSTHRPRO
32   ASNPROGLNARGASNASPSERVALPROTHR
33   LEUALAGLNMETTHRASPLYSALAILEGLU
34   LEULEUSERLYSASNGLULYSGLYPHEPHE
35   LEUGLNVALGLUGLYALASERILEASPLYS
36   GLNASPHISALAALAASNPROCYSGLYGLN
37   ILEGLYGLUTHRVALASPLEUASPGLUALA
38   VALGLNARGALALEUGLUPHEALALYSLYS
39   GLUGLYASNTHRLEUVALILEVALTHRALA
40   ASPHISALAHISALASERGLNILEVALALA
41   PROASPTHRLYSALAPROGLYLEUTHRGLN
42   ALALEUASNTHRLYSASPGLYALAVALMET
43   VALMETSERTYRGLYASNSERGLUGLUASP
44   SERGLNGLUHISTHRGLYSERGLNLEUARG
45   ILEALAALATYRGLYPROHISALAALAASN
46   VALVALGLYLEUTHRASPGLNTHRASPLEU
47   PHETYRTHRMETLYSALAALALEUGLYLEU
48   LYS

Samples:

sample_1: PhoA_DnaJ, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; potassium chloride 75 mM; potassium phosphate 20 mM; sodium azide 0.04%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 25 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CNH-sofast hmqc-NOESY-hmqcsample_1isotropicsample_conditions_1
3D HNH-sofastNOESY-hmqcsample_1isotropicsample_conditions_1
3D HCH-sofastNOESY-hmqcsample_1isotropicsample_conditions_1
3D NCH-sofast hmqc-NOESY-hmqcsample_1isotropicsample_conditions_1
3D CCH-sofast hmqc-NOESY-hmqcsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

Sparky, Goddard - peak picking

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TopSpin, Bruker Biospin - collection

PSVS, Bhattacharya and Montelione - processing

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz

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