BMRB Entry 36582

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36582
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Solution structure of full-length HtpG in complex with D131D
Deposition date:
2023-07-13
Original release date:
2025-12-12
Authors:
Qu, X.; Huang, C.
Citation:

Citation: Qu, Xiaozhan; Zhao, Shuo; Wan, Chanjuan; Zhu, Lei; Ji, Tuo; Rossi, Paolo; Wang, Junfeng; Kalodimos, Charalampos; Wang, Chao; Xu, Weiya; Huang, Chengdong. "Structural basis for the dynamic chaperoning of disordered clients by Hsp90."  Nat. Struct. Mol. Biol. 31, 1482-1491 (2024).
PubMed: 38890550

Assembly members:

Assembly members:
Chaperone protein HtpG, polymer, 624 residues, 71519.422 Da.
Nuclease A, polymer, 132 residues, 15033.458 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: not available   Kingdom: Pseudomonadati   Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Chaperone protein HtpG: MKGQETRGFQSEVKQLLHLM IHSLYSNKEIFLRELISNAS DAADKLRFRALSNPDLYEGD GELRVRVSFDKDKRTLTISD NGVGMTRDEVIDHLGTIAKS GTKSFLESLGSDQAKDSQLI GQFGVGFYSAFIVADKVTVR TRAAGEKPENGVFWESAGEG EYTVADITKEDRGTEITLHL REGEDEFLDDWRVRSIISKY SDHIALPVEIEKREEKDGET VISWEKINKAQALWTRNKSE ITDEEYKEFYKHIAHDFNDP LTWSHNRVEGKQEYTSLLYI PSQAPWDMWNRDHKHGLKLY VQRVFIMDDAEQFMPNYLRF VRGLIDSSDLPLNVSREILQ DSTVTRNLRNALTKRVLQML EKLAKDDAEKYQTFWQQFGL VLKEGPAEDFANQEAIAKLL RFASTHTDSSAQTVSLEDYV SRMKEGQEKIYYITADSYAA AKSSPHLELLRKKGIEVLLL SDRIDEWMMNYLTEFDGKPF QSVSKVDESLEKLADEVDES AKEAEKALTPFIDRVKALLG ERVKDVRLTHRLTDTPAIVS TDADEMSTQMAKLFAAAGQK VPEVKYIFELNPDHVLVKRA ADTEDEAKFSEWVELLLDQA LLAERGTLEDPNLFIRRMNQ LLVS
Nuclease A: MATSTLIKAIDGDTVKLMYK GQPMTFRLLLVDTPETKHPK KGVEKYGPEASAFTKKMVEN AKKIEVEFDKGQRTDKYGRG LAYIYADGKMVNEALVRQGL AKVAYVYKPNNTHEQHLRKS EAQAKKEKLNIW

Data sets:
Data typeCount
13C chemical shifts859
15N chemical shifts414
1H chemical shifts414

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_1_11
2entity_1_21
3entity_22

Entities:

Entity 1, entity_1_1 624 residues - 71519.422 Da.

1   METLYSGLYGLNGLUTHRARGGLYPHEGLN
2   SERGLUVALLYSGLNLEULEUHISLEUMET
3   ILEHISSERLEUTYRSERASNLYSGLUILE
4   PHELEUARGGLULEUILESERASNALASER
5   ASPALAALAASPLYSLEUARGPHEARGALA
6   LEUSERASNPROASPLEUTYRGLUGLYASP
7   GLYGLULEUARGVALARGVALSERPHEASP
8   LYSASPLYSARGTHRLEUTHRILESERASP
9   ASNGLYVALGLYMETTHRARGASPGLUVAL
10   ILEASPHISLEUGLYTHRILEALALYSSER
11   GLYTHRLYSSERPHELEUGLUSERLEUGLY
12   SERASPGLNALALYSASPSERGLNLEUILE
13   GLYGLNPHEGLYVALGLYPHETYRSERALA
14   PHEILEVALALAASPLYSVALTHRVALARG
15   THRARGALAALAGLYGLULYSPROGLUASN
16   GLYVALPHETRPGLUSERALAGLYGLUGLY
17   GLUTYRTHRVALALAASPILETHRLYSGLU
18   ASPARGGLYTHRGLUILETHRLEUHISLEU
19   ARGGLUGLYGLUASPGLUPHELEUASPASP
20   TRPARGVALARGSERILEILESERLYSTYR
21   SERASPHISILEALALEUPROVALGLUILE
22   GLULYSARGGLUGLULYSASPGLYGLUTHR
23   VALILESERTRPGLULYSILEASNLYSALA
24   GLNALALEUTRPTHRARGASNLYSSERGLU
25   ILETHRASPGLUGLUTYRLYSGLUPHETYR
26   LYSHISILEALAHISASPPHEASNASPPRO
27   LEUTHRTRPSERHISASNARGVALGLUGLY
28   LYSGLNGLUTYRTHRSERLEULEUTYRILE
29   PROSERGLNALAPROTRPASPMETTRPASN
30   ARGASPHISLYSHISGLYLEULYSLEUTYR
31   VALGLNARGVALPHEILEMETASPASPALA
32   GLUGLNPHEMETPROASNTYRLEUARGPHE
33   VALARGGLYLEUILEASPSERSERASPLEU
34   PROLEUASNVALSERARGGLUILELEUGLN
35   ASPSERTHRVALTHRARGASNLEUARGASN
36   ALALEUTHRLYSARGVALLEUGLNMETLEU
37   GLULYSLEUALALYSASPASPALAGLULYS
38   TYRGLNTHRPHETRPGLNGLNPHEGLYLEU
39   VALLEULYSGLUGLYPROALAGLUASPPHE
40   ALAASNGLNGLUALAILEALALYSLEULEU
41   ARGPHEALASERTHRHISTHRASPSERSER
42   ALAGLNTHRVALSERLEUGLUASPTYRVAL
43   SERARGMETLYSGLUGLYGLNGLULYSILE
44   TYRTYRILETHRALAASPSERTYRALAALA
45   ALALYSSERSERPROHISLEUGLULEULEU
46   ARGLYSLYSGLYILEGLUVALLEULEULEU
47   SERASPARGILEASPGLUTRPMETMETASN
48   TYRLEUTHRGLUPHEASPGLYLYSPROPHE
49   GLNSERVALSERLYSVALASPGLUSERLEU
50   GLULYSLEUALAASPGLUVALASPGLUSER
51   ALALYSGLUALAGLULYSALALEUTHRPRO
52   PHEILEASPARGVALLYSALALEULEUGLY
53   GLUARGVALLYSASPVALARGLEUTHRHIS
54   ARGLEUTHRASPTHRPROALAILEVALSER
55   THRASPALAASPGLUMETSERTHRGLNMET
56   ALALYSLEUPHEALAALAALAGLYGLNLYS
57   VALPROGLUVALLYSTYRILEPHEGLULEU
58   ASNPROASPHISVALLEUVALLYSARGALA
59   ALAASPTHRGLUASPGLUALALYSPHESER
60   GLUTRPVALGLULEULEULEUASPGLNALA
61   LEULEUALAGLUARGGLYTHRLEUGLUASP
62   PROASNLEUPHEILEARGARGMETASNGLN
63   LEULEUVALSER

Entity 2, entity_2 132 residues - 15033.458 Da.

1   METALATHRSERTHRLEUILELYSALAILE
2   ASPGLYASPTHRVALLYSLEUMETTYRLYS
3   GLYGLNPROMETTHRPHEARGLEULEULEU
4   VALASPTHRPROGLUTHRLYSHISPROLYS
5   LYSGLYVALGLULYSTYRGLYPROGLUALA
6   SERALAPHETHRLYSLYSMETVALGLUASN
7   ALALYSLYSILEGLUVALGLUPHEASPLYS
8   GLYGLNARGTHRASPLYSTYRGLYARGGLY
9   LEUALATYRILETYRALAASPGLYLYSMET
10   VALASNGLUALALEUVALARGGLNGLYLEU
11   ALALYSVALALATYRVALTYRLYSPROASN
12   ASNTHRHISGLUGLNHISLEUARGLYSSER
13   GLUALAGLNALALYSLYSGLULYSLEUASN
14   ILETRP

Samples:

sample_1: Heat shock protein 90(HtpG M domain), [U-13C; U-15N; U-2H], 500 uM; Disordered protein(D131D), [U-100% 13C; U-100% 15N], 500 uM; Heat shock protein 90(HtpG M domain), [U-2H, 15N; Ala- 13CH3; Met- 13CH3; Ile-d1- 13CH3; Leu, Val- 13CH3/ 13CH3; Thr- 13CH3], 500 uM; H2O 93%; D2O, [U-2H], 7%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 Pa; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMRView, Johnson, One Moon Scientific - peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 850 MHz

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