BMRB Entry 26595

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26595

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Title:
Backbone 1H, 13C and 15N chemical shift assignments for hTRF1 bound to ADP-DnaK
Deposition date:
2015-06-30
Original release date:
2015-07-29
Authors:
Sekhar, Ashok; Rosenzweig, Rina; Bouvignies, Guillaume; Kay, Lewis
Citation:

Citation: Sekhar, Ashok; Rosenzweig, Rina; Bouvignies, Guillaume; Kay, Lewis. "Mapping the conformation of a client protein through the Hsp70 functional cycle"  Proc. Natl. Acad. Sci. U.S.A. 112, 10395-10400 (2015).
PubMed: 26240333

Assembly members:

Assembly members:
hTRF1, polymer, 53 residues, Formula weight is not available
DnaK, polymer, 638 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hTRF1: RKRQAWLWEEDKNLRSGVRK YGEGNWSKILLHYKFNNRTS VMLKDRWRTMKKL
DnaK: MGKIIGIDLGTTNSCVAIMD GTTPRVLENAEGDRTTPSII AYTQDGETLVGQPAKRQAVT NPQNTLFAIKRLIGRRFQDE EVQRDVSIMPFKIIAADNGD AWVEVKGQKMAPPQISAEVL KKMKKTAEDYLGEPVTEAVI TVPAYFNDAQRQATKDAGRI AGLEVKRIINEPTAAALAYG LDKGTGNRTIAVYDLGGGTF DISIIEIDEVDGEKTFEVLA TNGDTHLGGEDFDSRLINYL VEEFKKDQGIDLRNDPLAMQ RLKEAAEKAKIELSSAQQTD VNLPYITADATGPKHMNIKV TRAKLESLVEDLVNRSIEPL KVALQDAGLSVSDIDDVILV GGQTRMPMVQKKVAEFFGKE PRKDVNPDEAVAIGAAVQGG VLTGDVKDVLLLDVTPLSLG IETMGGVMTTLIAKNTTIPT KHSQVFSTAEDNQSAVTIHV LQGERKRAADNKSLGQFNLD GINPAPRGMPQIEVTFDIDA DGILHVSAKDKNSGKEQKIT IKASSGLNEDEIQKMVRDAE ANAEADRKFEELVQTRNQGD HLLHSTRKQVEEAGDKLPAD DKTAIESALTALETALKGED KAAIEAKMQELAQVSQKLME IAQQQHAQQQTAGADASANN AKDDDVVDAEFEEVKDKK

Data sets:
Data typeCount
13C chemical shifts120
15N chemical shifts42
1H chemical shifts42

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1hTRF11
2DnaK2

Entities:

Entity 1, hTRF1 53 residues - Formula weight is not available

1   ARGLYSARGGLNALATRPLEUTRPGLUGLU
2   ASPLYSASNLEUARGSERGLYVALARGLYS
3   TYRGLYGLUGLYASNTRPSERLYSILELEU
4   LEUHISTYRLYSPHEASNASNARGTHRSER
5   VALMETLEULYSASPARGTRPARGTHRMET
6   LYSLYSLEU

Entity 2, DnaK 638 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   ALAVALTYRASPLEUGLYGLYGLYTHRPHE
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   LEULEUASPVALTHRPROLEUSERLEUGLY
41   ILEGLUTHRMETGLYGLYVALMETTHRTHR
42   LEUILEALALYSASNTHRTHRILEPROTHR
43   LYSHISSERGLNVALPHESERTHRALAGLU
44   ASPASNGLNSERALAVALTHRILEHISVAL
45   LEUGLNGLYGLUARGLYSARGALAALAASP
46   ASNLYSSERLEUGLYGLNPHEASNLEUASP
47   GLYILEASNPROALAPROARGGLYMETPRO
48   GLNILEGLUVALTHRPHEASPILEASPALA
49   ASPGLYILELEUHISVALSERALALYSASP
50   LYSASNSERGLYLYSGLUGLNLYSILETHR
51   ILELYSALASERSERGLYLEUASNGLUASP
52   GLUILEGLNLYSMETVALARGASPALAGLU
53   ALAASNALAGLUALAASPARGLYSPHEGLU
54   GLULEUVALGLNTHRARGASNGLNGLYASP
55   HISLEULEUHISSERTHRARGLYSGLNVAL
56   GLUGLUALAGLYASPLYSLEUPROALAASP
57   ASPLYSTHRALAILEGLUSERALALEUTHR
58   ALALEUGLUTHRALALEULYSGLYGLUASP
59   LYSALAALAILEGLUALALYSMETGLNGLU
60   LEUALAGLNVALSERGLNLYSLEUMETGLU
61   ILEALAGLNGLNGLNHISALAGLNGLNGLN
62   THRALAGLYALAASPALASERALAASNASN
63   ALALYSASPASPASPVALVALASPALAGLU
64   PHEGLUGLUVALLYSASPLYSLYS

Samples:

sample_1: hTRF1, [U-13C; U-15N; U-2H], 0.5 mM; DnaK, [U-2H], 1.4 mM; MES 25 mM; KCl 25 mM; magnesium chloride 5 mM; adenosine diphosphate 5 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

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