BMRB Entry 17210

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17210

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Backbone 1H, 13C, and 15N chemical shift assignments for the nucleotide-binding domain of E.coli DnaK in the ATP-bound state
Deposition date:
2010-09-27
Original release date:
2011-05-05
Authors:
Zhuravleva, Anastasia; Gierasch, Lila
Citation:

Citation: Zhuravleva, Anastasia; Gierasch, Lila. "Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones."  Proc. Natl. Acad. Sci. U.S.A. 108, 6987-6992 (2011).
PubMed: 21482798

Assembly members:

Assembly members:
the_nucleotide-binding_domain_of_DnaK, polymer, 392 residues, Formula weight is not available
ATP, non-polymer, 507.181 Da.
AGS, non-polymer, 523.247 Da.
MG, non-polymer, 24.305 Da.

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: pMS119-EH

Entity Sequences (FASTA):

Entity Sequences (FASTA):
the_nucleotide-binding_domain_of_DnaK: MGKIIGIDLGTTNSCVAIMD GTTPRVLENAEGDRTTPSII AYTQDGETLVGQPAKRQAVT NPQNTLFAIKRLIGRRFQDE EVQRDVSIMPFKIIAADNGD AWVEVKGQKMAPPQISAEVL KKMKKTAEDYLGEPVTEAVI TVPAYFNDAQRQATKDAGRI AGLEVKRIINEPTAAALAYG LDKGTGNRTIAVYDLGGGAF DISIIEIDEVDGEKTFEVLA TNGDTHLGGEDFDSRLINYL VEEFKKDQGIDLRNDPLAMQ RLKEAAEKAKIELSSAQQTD VNLPYITADATGPKHMNIKV TRAKLESLVEDLVNRSIEPL KVALQDAGLSVSDIDDVILV GGQTRMPMVQKKVAEFFGKE PRKDVNPDEAVAIGAAVQGG VLTGDVKDVLLL

Data sets:
Data typeCount
13C chemical shifts1026
15N chemical shifts331
1H chemical shifts331

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NBD1
2ATP2
3ATPgS3
4MG4

Entities:

Entity 1, NBD 392 residues - Formula weight is not available

1   METGLYLYSILEILEGLYILEASPLEUGLY
2   THRTHRASNSERCYSVALALAILEMETASP
3   GLYTHRTHRPROARGVALLEUGLUASNALA
4   GLUGLYASPARGTHRTHRPROSERILEILE
5   ALATYRTHRGLNASPGLYGLUTHRLEUVAL
6   GLYGLNPROALALYSARGGLNALAVALTHR
7   ASNPROGLNASNTHRLEUPHEALAILELYS
8   ARGLEUILEGLYARGARGPHEGLNASPGLU
9   GLUVALGLNARGASPVALSERILEMETPRO
10   PHELYSILEILEALAALAASPASNGLYASP
11   ALATRPVALGLUVALLYSGLYGLNLYSMET
12   ALAPROPROGLNILESERALAGLUVALLEU
13   LYSLYSMETLYSLYSTHRALAGLUASPTYR
14   LEUGLYGLUPROVALTHRGLUALAVALILE
15   THRVALPROALATYRPHEASNASPALAGLN
16   ARGGLNALATHRLYSASPALAGLYARGILE
17   ALAGLYLEUGLUVALLYSARGILEILEASN
18   GLUPROTHRALAALAALALEUALATYRGLY
19   LEUASPLYSGLYTHRGLYASNARGTHRILE
20   ALAVALTYRASPLEUGLYGLYGLYALAPHE
21   ASPILESERILEILEGLUILEASPGLUVAL
22   ASPGLYGLULYSTHRPHEGLUVALLEUALA
23   THRASNGLYASPTHRHISLEUGLYGLYGLU
24   ASPPHEASPSERARGLEUILEASNTYRLEU
25   VALGLUGLUPHELYSLYSASPGLNGLYILE
26   ASPLEUARGASNASPPROLEUALAMETGLN
27   ARGLEULYSGLUALAALAGLULYSALALYS
28   ILEGLULEUSERSERALAGLNGLNTHRASP
29   VALASNLEUPROTYRILETHRALAASPALA
30   THRGLYPROLYSHISMETASNILELYSVAL
31   THRARGALALYSLEUGLUSERLEUVALGLU
32   ASPLEUVALASNARGSERILEGLUPROLEU
33   LYSVALALALEUGLNASPALAGLYLEUSER
34   VALSERASPILEASPASPVALILELEUVAL
35   GLYGLYGLNTHRARGMETPROMETVALGLN
36   LYSLYSVALALAGLUPHEPHEGLYLYSGLU
37   PROARGLYSASPVALASNPROASPGLUALA
38   VALALAILEGLYALAALAVALGLNGLYGLY
39   VALLEUTHRGLYASPVALLYSASPVALLEU
40   LEULEU

Entity 2, ATP - C10 H16 N5 O13 P3 - 507.181 Da.

1   ATP

Entity 3, ATPgS - C10 H16 N5 O12 P3 S - 523.247 Da.

1   AGS

Entity 4, MG - Mg - 24.305 Da.

1   MG

Samples:

DnaK392_ATP: potassium phosphate 10 mM; magnesium chloride 10 mM; AEBSF protease inhibitor 1 uM; DTT 5 mM; DSS 0.5 mM; ATP 10 mM; potassium chloride 10 mM; the nucleotide-binding domain of DnaK, [U-97% 2H; U-95% 13C; U-95% 15N], 0.5 mM; H2O 95%; D2O 5%

DnaK392_ATPgS: potassium phosphate 10 mM; magnesium chloride 10 mM; AEBSF protease inhibitor 1 uM; DTT 5 mM; DSS 0.5 mM; ATPgS 10 mM; potassium chloride 10 mM; the nucleotide-binding domain of DnaK, [U-97% 2H; U-95% 13C; U-95% 15N], 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.050 M; pH: 7.0; pressure: 1 atm; temperature: 299 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYDnaK392_ATPisotropicsample_conditions_1
3D TROSY-HNCODnaK392_ATPisotropicsample_conditions_1
3D TROSY-HNCACBDnaK392_ATPisotropicsample_conditions_1
3D TROSY-HN(CO)CACBDnaK392_ATPisotropicsample_conditions_1
2D 1H-15N TROSYDnaK392_ATPgSisotropicsample_conditions_1
3D TROSY-HNCODnaK392_ATPgSisotropicsample_conditions_1
3D TROSY-HN(CA)CODnaK392_ATPgSisotropicsample_conditions_1
3D TROSY-HNCACBDnaK392_ATPgSisotropicsample_conditions_1
3D TROSY-HNCADnaK392_ATPgSisotropicsample_conditions_1

Software:

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking

CARA, Keller, Wuthrich - chemical shift assignment

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17208 17209
PDB
DBJ BAA01595 BAB33437 BAB96589 BAG75537 BAI23377
EMBL CAD01165 CAP74584 CAQ30531 CAQ87598 CAQ96905
GB AAA23694 AAB02910 AAC73125 AAG54314 AAL18976
PIR AE0503
REF NP_308041 NP_414555 NP_454622 NP_459017 NP_705973
SP A1A766 A7MIK5 A7ZHA4 A7ZVV7 A8ALU3
AlphaFold A1A766 A7MIK5 A7ZHA4 A7ZVV7 A8ALU3

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