BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 30636

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30636
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Structural Basis for Client Recognition and Activity of Hsp40 Chaperones   PubMed: 31604242

Deposition date: 2019-07-10 Original release date: 2019-09-11

Authors: Jiang, Y.; Rossi, P.; Kalodimos, C.

Citation: Jiang, Y.; Rossi, P.; Kalodimos, C.. "Structural basis for client recognition and activity of Hsp40 chaperones"  Science 365, 1313-1319 (2019).

Assembly members:
entity_1, polymer, 90 residues, 9176.394 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: MDDVIDADYKPADGSGGSGG SGGSQDLYATLDVPAPIAVV GGKVRAMTLEGPVEVAVPPR TQAGRKLRLKGKGFPGPAGR GDLYLEVRIT

Data sets:
Data typeCount
13C chemical shifts352
15N chemical shifts80
1H chemical shifts538

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 90 residues - 9176.394 Da.

1   METASPASPVALILEASPALAASPTYRLYS
2   PROALAASPGLYSERGLYGLYSERGLYGLY
3   SERGLYGLYSERGLNASPLEUTYRALATHR
4   LEUASPVALPROALAPROILEALAVALVAL
5   GLYGLYLYSVALARGALAMETTHRLEUGLU
6   GLYPROVALGLUVALALAVALPROPROARG
7   THRGLNALAGLYARGLYSLEUARGLEULYS
8   GLYLYSGLYPHEPROGLYPROALAGLYARG
9   GLYASPLEUTYRLEUGLUVALARGILETHR

Samples:

sample_1: DnaK-ctail-CBD2, [U-100% 13C; U-100% 15N], 1 mM; potassium chloride 75 mM; potassium phosphate 20 mM; sodium azide 0.04%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D CaroCH-noesysample_1isotropicsample_conditions_1
3D CCH-noesysample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

Sparky, Goddard - peak picking

TopSpin, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

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

PSVS, Bhattacharya and Montelione - geometry optimization

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz

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