BMRB Entry 18115

Title:
Solution Structure of The C-terminal Domain (537-610) of Human Heat Shock Protein 70
Deposition date:
2011-12-01
Original release date:
2012-08-29
Authors:
Zhou, Chenjie; Gao, Xuechao; Wu, Meng; Hu, Hongyu
Citation:

Citation: Gao, Xuechao; Zhou, Chenjie; Zhou, Ziren; Wu, Meng; Cao, Chunyang; Hu, Hongyu. "The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation"  J. Biol. Chem. 287, 6044-6052 (2012).
PubMed: 22219199

Assembly members:

Assembly members:
entity, polymer, 75 residues, 8325.507 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-32M

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts310
15N chemical shifts79
1H chemical shifts484

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal Domain (537-610) of Human Heat Shock Protein 701

Entities:

Entity 1, C-terminal Domain (537-610) of Human Heat Shock Protein 70 75 residues - 8325.507 Da.

1   GLYSERALALYSASNALALEUGLUSERTYR
2   ALAPHEASNMETLYSSERALAVALGLUASP
3   GLUGLYLEULYSGLYLYSILESERGLUALA
4   ASPLYSLYSLYSVALLEUASPLYSCYSGLN
5   GLUVALILESERTRPLEUASPALAASNTHR
6   LEUALAGLULYSASPGLUPHEGLUHISLYS
7   ARGLYSGLULEUGLUGLNVALCYSASNPRO
8   ILEILESERGLYLEU

Samples:

sample_1: entity, [U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_3: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 100%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_3isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_3isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement, structure solution

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, peak picking

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAB63299 BAB63300 BAC79353 BAC79354 BAC79355
EMBL CAA50019 CAH23703 CAH91519 CAH92327 CAN13333
GB AAA03450 AAA03451 AAA52697 AAA63226 AAA63227
REF NP_001003067 NP_001125893 NP_001243852 NP_001254803 NP_001270918
SP P0DMV8 P0DMV9 P34930 Q27965 Q27975
TPG DAA16342 DAA16344
AlphaFold P0DMV9 Q27965 Q27975 P0DMV8 P34930

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