BMRB Entry 26815

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26815

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Title:
Backbone and Methyl chemical shift assignments for Hsc70-1-386
Deposition date:
2016-06-14
Original release date:
2016-10-13
Authors:
Zuiderweg, Erik
Citation:

Citation: Zuiderweg, Erik; Gestwicki, Jason. "Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state"  Biomol. NMR Assign. ., .-. (2016).
PubMed: 27699616

Assembly members:

Assembly members:
Hsc-70, polymer, 386 residues, 42456 Da.
entity_ADP, non-polymer, 427.201 Da.

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: pET T7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hsc-70: MSKGPAVGIDLGTTYSCVGV FQHGKVEIIANDQGNRTTPS YVAFTDTERLIGDAAKNQVA MNPTNTVFDAKRLIGRRFDD AVVQSDMKHWPFMVVNDAGR PKVQVEYKGETKSFYPEEVS SMVLTKMKEIAEAYLGKTVT NAVVTVPAYFNDSQRQATKD AGTIAGLNVLRIINEPTAAA IAYGLDKKVGAERNVLIFDL GGGTFDVSILTIEDGIFEVK STAGDTHLGGEDFDNRMVNH FIAEFKRKHKKDISENKRAV RRLRTACERAKRTLSSSTQA SIEIDSLYEGIDFYTSITRA RFEELNADLFRGTLDPVEKA LRDAKLDKSQIHDIVLVGGS TRIPKIQKLLQDFFNGKELN KSINPDEAVAYGAAVQAAIL SGDKSE

Data sets:
Data typeCount
13C chemical shifts1211
15N chemical shifts341
1H chemical shifts804

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protein1
2ADP2

Entities:

Entity 1, Protein 386 residues - 42456 Da.

1   METSERLYSGLYPROALAVALGLYILEASP
2   LEUGLYTHRTHRTYRSERCYSVALGLYVAL
3   PHEGLNHISGLYLYSVALGLUILEILEALA
4   ASNASPGLNGLYASNARGTHRTHRPROSER
5   TYRVALALAPHETHRASPTHRGLUARGLEU
6   ILEGLYASPALAALALYSASNGLNVALALA
7   METASNPROTHRASNTHRVALPHEASPALA
8   LYSARGLEUILEGLYARGARGPHEASPASP
9   ALAVALVALGLNSERASPMETLYSHISTRP
10   PROPHEMETVALVALASNASPALAGLYARG
11   PROLYSVALGLNVALGLUTYRLYSGLYGLU
12   THRLYSSERPHETYRPROGLUGLUVALSER
13   SERMETVALLEUTHRLYSMETLYSGLUILE
14   ALAGLUALATYRLEUGLYLYSTHRVALTHR
15   ASNALAVALVALTHRVALPROALATYRPHE
16   ASNASPSERGLNARGGLNALATHRLYSASP
17   ALAGLYTHRILEALAGLYLEUASNVALLEU
18   ARGILEILEASNGLUPROTHRALAALAALA
19   ILEALATYRGLYLEUASPLYSLYSVALGLY
20   ALAGLUARGASNVALLEUILEPHEASPLEU
21   GLYGLYGLYTHRPHEASPVALSERILELEU
22   THRILEGLUASPGLYILEPHEGLUVALLYS
23   SERTHRALAGLYASPTHRHISLEUGLYGLY
24   GLUASPPHEASPASNARGMETVALASNHIS
25   PHEILEALAGLUPHELYSARGLYSHISLYS
26   LYSASPILESERGLUASNLYSARGALAVAL
27   ARGARGLEUARGTHRALACYSGLUARGALA
28   LYSARGTHRLEUSERSERSERTHRGLNALA
29   SERILEGLUILEASPSERLEUTYRGLUGLY
30   ILEASPPHETYRTHRSERILETHRARGALA
31   ARGPHEGLUGLULEUASNALAASPLEUPHE
32   ARGGLYTHRLEUASPPROVALGLULYSALA
33   LEUARGASPALALYSLEUASPLYSSERGLN
34   ILEHISASPILEVALLEUVALGLYGLYSER
35   THRARGILEPROLYSILEGLNLYSLEULEU
36   GLNASPPHEPHEASNGLYLYSGLULEUASN
37   LYSSERILEASNPROASPGLUALAVALALA
38   TYRGLYALAALAVALGLNALAALAILELEU
39   SERGLYASPLYSSERGLU

Entity 2, ADP - C10 H15 N5 O10 P2 - 427.201 Da.

1   ADP

Samples:

sample_1: HSC70-NBD, [U-13C; U-15N; U-2H], 250 ± 25 uM; ADP 5 ± 0.1 mM; potassium chloride 10 ± 0.1 mM; TRIS 25 ± 0.1 mM; potassium phosphate 20 ± 0.1 mM; sodium azide 0.02 ± 0.001 %; DTT 2 ± 0.1 mM

sample_2: HSC70-NBD, [U-13C; U-15N; U-2H, 13CH ILVAMY], 160 uM; ADP 5 mM; potassium chloride 10 mM; TRIS 25 mM; potassium phosphate 10 mM; sodium azide 0.02%; DTT 2 mM; PMSF 0.1%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 303 K

sample_conditions_2: pH: 7.2; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC TROSYsample_1isotropicsample_conditions_1
3D HNCA TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CA TROSYsample_1isotropicsample_conditions_1
3D HNCO TROSYsample_1isotropicsample_conditions_1
3D HN(CA)CO TROSYsample_1isotropicsample_conditions_1
3D HNCACB TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CACB TROSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC TROSYsample_2isotropicsample_conditions_2
3D HNCA TROSYsample_2isotropicsample_conditions_2
3D HN(CO)CA TROSYsample_2isotropicsample_conditions_2
3D HNCACB TROSYsample_2isotropicsample_conditions_2
3D HNCO TROSYsample_2isotropicsample_conditions_2
3D HN(CA)CO TROSYsample_2isotropicsample_conditions_2
3D HnCANHsample_2isotropicsample_conditions_2
3D hNCANHsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
3D H-NH NOESY-TROSYsample_2isotropicsample_conditions_2
3D C-NH HMQC-NOESY-TROSYsample_2isotropicsample_conditions_2
3D H-CH HMQC-NOESY-HSQCsample_2isotropicsample_conditions_2
3D C-CH HMQC-NOESY-HSQCsample_2isotropicsample_conditions_2

Software:

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

SPARKY, Goddard - data analysis, peak picking

EZ-ASSIGN v4.1, University of Michigan - chemical shift assignment

NOE-Calculations, Erik Zuiderweg - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UniProtKB P11142

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