BMRB Entry 17209

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17209

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Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the nucleotide-binding domain of E.coli DnaK in the nucleotide-free 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, 388 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: 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 TRAKLESLVEDLVNRSIELL KVALQDAGLSVSDIDDVILV GGQTRMPMVQKKVAEFFGKE PRKDVNPDEAVAIGAAVQGG VLTGDVKD

Data sets:
Data typeCount
13C chemical shifts685
15N chemical shifts326
1H chemical shifts326

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NBD1

Entities:

Entity 1, NBD 388 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   ASPLEUVALASNARGSERILEGLULEULEU
33   LYSVALALALEUGLNASPALAGLYLEUSER
34   VALSERASPILEASPASPVALILELEUVAL
35   GLYGLYGLNTHRARGMETPROMETVALGLN
36   LYSLYSVALALAGLUPHEPHEGLYLYSGLU
37   PROARGLYSASPVALASNPROASPGLUALA
38   VALALAILEGLYALAALAVALGLNGLYGLY
39   VALLEUTHRGLYASPVALLYSASP

Samples:

DnaK388: potassium phosphate 10 mM; magnesium chloride 10 mM; AEBSF protease inhibitor 1 uM; DTT 5 mM; DSS 0.5 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 TROSYDnaK388isotropicsample_conditions_1
3D TROSY-HNCODnaK388isotropicsample_conditions_1
3D TROSY-HNCADnaK388isotropicsample_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 17210
PDB
DBJ BAA01595 BAB33437 BAB96589 BAG75537 BAI23377
EMBL CAP74584 CAQ30531 CAQ87598 CAQ96905 CAR01381
GB AAA23694 AAC73125 AAG54314 AAN41680 AAN78519
REF NP_308041 NP_414555 NP_705973 WP_000407451 WP_000516120
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