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Biological Magnetic Resonance Data Bank


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BMRB Entry 36077

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36077
MolProbity Validation Chart

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Title: Solution structure for human HSP70 substrate binding domain   PubMed: 29495458

Deposition date: 2017-04-26 Original release date: 2018-05-14

Authors: Hoshikawa, M.; Tochio, N.; Tate, S.

Citation: Umehara, Kohei; Hoshikawa, Miho; Tochio, Naoya; Tate, Shin-Ichi. "Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication"  Molecules 23, E528-E528 (2018).

Assembly members:
Heat shock 70 kDa protein 1A, polymer, 185 residues, 20323.885 Da.

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

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

Entity Sequences (FASTA):
Heat shock 70 kDa protein 1A: HMGDKSENVQDLLLLDVAPL SLGLETAGGVMTALIKRNST IPTKQTQIFTTYSDNQPGVL IQVYEGERAMTKDNNLLGRF ELSGIPPAPRGVPQIEVTFD IDANGILNVTATDKSTGKAN KITITNDKGRLSKEEIERMV QEAEKYKAEDEVQRERVSAK NALESYAFNMKSAVEDEGLK GKISE

Data sets:
Data typeCount
13C chemical shifts781
15N chemical shifts197
1H chemical shifts1136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 185 residues - 20323.885 Da.

1   HISMETGLYASPLYSSERGLUASNVALGLN
2   ASPLEULEULEULEUASPVALALAPROLEU
3   SERLEUGLYLEUGLUTHRALAGLYGLYVAL
4   METTHRALALEUILELYSARGASNSERTHR
5   ILEPROTHRLYSGLNTHRGLNILEPHETHR
6   THRTYRSERASPASNGLNPROGLYVALLEU
7   ILEGLNVALTYRGLUGLYGLUARGALAMET
8   THRLYSASPASNASNLEULEUGLYARGPHE
9   GLULEUSERGLYILEPROPROALAPROARG
10   GLYVALPROGLNILEGLUVALTHRPHEASP
11   ILEASPALAASNGLYILELEUASNVALTHR
12   ALATHRASPLYSSERTHRGLYLYSALAASN
13   LYSILETHRILETHRASNASPLYSGLYARG
14   LEUSERLYSGLUGLUILEGLUARGMETVAL
15   GLNGLUALAGLULYSTYRLYSALAGLUASP
16   GLUVALGLNARGGLUARGVALSERALALYS
17   ASNALALEUGLUSERTYRALAPHEASNMET
18   LYSSERALAVALGLUASPGLUGLYLEULYS
19   GLYLYSILESERGLU

Samples:

sample_1: human HSP70 substrate binding domain mM; DTT 10 mM; potassium chloride 50 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

magro, Kobayashi, N. - data analysis

NMR spectrometers:

  • Bruker AvanceII 700 MHz

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