BMRB Entry 6229

Title:
Backbone 1H, 13C, and 15N Chemical Shift assignments for the Nucleotide-binding domain of Thermus Thermophilus DnaK
Deposition date:
2004-06-10
Original release date:
2005-11-14
Authors:
Revington, Matthew; Zuiderweg, Erik
Citation:

Citation: Revington, Matthew; Zuiderweg, Erik. "Letter to the Editor: TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone."  J. Biomol. NMR 30, 113-114 (2004).
PubMed: 15452445

Assembly members:

Assembly members:
DnaK NBD, polymer, 401 residues, Formula weight is not available
ADENOSINE-5'-DIPHOSPHATE, non-polymer, 427.201 Da.

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Data sets:
Data typeCount
1H chemical shifts330
13C chemical shifts1009
15N chemical shifts330

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DnaK nucleotide binding domain, Dnak NBD1

Entities:

Entity 1, DnaK nucleotide binding domain, Dnak NBD 401 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALALYSALAVALGLYILEASPLEUGLY
4   THRTHRASNSERVALILEALAVALLEUGLU
5   GLYGLYLYSPROVALVALLEUGLUASNALA
6   GLUGLYGLUARGVALTHRPROSERVALVAL
7   ALAPHEARGASPGLYGLUTHRLEUVALGLY
8   ARGMETALALYSARGGLNALAVALLEUASN
9   PROGLUGLYTHRILEPHEGLUILELYSARG
10   PHEILEGLYARGARGPHEGLUGLUVALGLN
11   GLUGLUALALYSARGVALPROTYRLYSVAL
12   VALPROGLYPROASPGLYGLYVALARGVAL
13   GLUVALLYSGLYLYSLEUTYRTHRPROGLU
14   GLUILESERALAMETILELEUARGLYSLEU
15   VALGLUASPALASERLYSLYSLEUGLYGLU
16   LYSILETHRLYSALAVALILETHRVALPRO
17   ALATYRPHEASNASNALAGLNARGGLUALA
18   THRALAASNALAGLYARGILEALAGLYLEU
19   GLUVALLEUARGILEILEASNGLUPROTHR
20   ALAALAALALEUALATYRGLYLEUASPLYS
21   LYSGLYASNGLUTHRVALLEUVALPHEASP
22   LEUGLYGLYGLYTHRPHEASPVALTHRILE
23   LEUGLUILEGLYGLUGLYVALPHEGLUVAL
24   LYSALATHRSERGLYASPTHRHISLEUGLY
25   GLYSERASPMETASPHISALAILEVALASN
26   TRPLEUALAGLUGLUPHELYSLYSGLUHIS
27   GLYVALASPLEULYSALAASPARGGLNALA
28   LEUGLNARGLEUILEGLUALAALAGLULYS
29   ALALYSILEGLULEUSERSERTHRLEUGLU
30   THRTHRILESERLEUPROPHEILEALALEU
31   ASPPROALASERLYSTHRPROLEUHISLEU
32   GLULYSLYSLEUTHRARGALALYSPHEGLU
33   GLULEUILEGLNPROLEULEULYSARGLEU
34   ARGGLYPROVALGLUGLNALALEULYSASP
35   ALAGLYLEUTHRPROALAGLNILEASPGLU
36   VALILELEUVALGLYGLYALATHRARGVAL
37   PROALAVALGLNGLNVALVALARGGLULEU
38   LEUGLYLYSGLUPROASNARGSERVALASN
39   PROASPGLUVALVALALAMETGLYALAALA
40   ILEGLNALAGLYVALLEUMETGLYGLUVAL
41   ARG

Samples:

Sample_1: DnaK NBD, [U-97% 2H; U-95% 13C; U-95% 15N], 0.4 – 0.6 mM; HEPES50 – 50 mM; Potassium Chloride10 – 10 mM; magnesium chloride5 – 5 mM; ADP5 – 5 mM; Sodium phosphate5 – 5 mM

Cond-1: pH: 7.4 na; temperature: 328 K; ionic strength: 0.1 M

Experiments:

NameSampleSample stateSample conditions
1H-15N TROSYSample_1not availableCond-1
TROSY-HNCASample_1not availableCond-1
TROSY-HNCOSample_1not availableCond-1
TROSY-HN(CA)COSample_1not availableCond-1
TROSY-HN(CO)CASample_1not availableCond-1
TROSY-HNCACBSample_1not availableCond-1
TROSY-HN(CO)CACBSample_1not availableCond-1
1H-15N NOESYSample_1not availableCond-1

Software:

NMRPIPE - Data processing

XEASY - Assignment

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

DBJ BAA12280 BAA81741 BAA96089 BAD71314
EMBL CAA69159
GB AAB04676 AAS81469 AEG33909 AFH38459
REF WP_011173541 WP_011228715 WP_014510666 WP_014629205 WP_024119965
SP Q56235 Q72IK5
AlphaFold Q56235 Q72IK5

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