BMRB Entry 30628

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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/BMR30628
MolProbity Validation Chart

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Title:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Deposition date:
2019-07-08
Original release date:
2019-09-11
Authors:
Jiang, Y.; Rossi, P.; Kalodimos, C.
Citation:

Citation: Jiang, Y.; Rossi, P.; Kalodimos, C.. "Structural basis for client recognition and activity of Hsp40 chaperones"  Science 365, 1313-1319 (2019).
PubMed: 31604242

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, 9256.687 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MLPLLFTPVTKGSGGSGGSG GSGRDLRAELPLTLEEAFHG GERVVEVAGRRVSVRIPPGV REGSVIRVPGMGGQGNPPGD LLLVVRLLPH

Data sets:
Data typeCount
13C chemical shifts337
15N chemical shifts77
1H chemical shifts525

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 - 9256.687 Da.

1   METLEUPROLEULEUPHETHRPROVALTHR
2   LYSGLYSERGLYGLYSERGLYGLYSERGLY
3   GLYSERGLYARGASPLEUARGALAGLULEU
4   PROLEUTHRLEUGLUGLUALAPHEHISGLY
5   GLYGLUARGVALVALGLUVALALAGLYARG
6   ARGVALSERVALARGILEPROPROGLYVAL
7   ARGGLUGLYSERVALILEARGVALPROGLY
8   METGLYGLYGLNGLYASNPROPROGLYASP
9   LEULEULEUVALVALARGLEULEUPROHIS

Samples:

sample_1: L11-K20_CBD1, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 20 mM; potassium chloride 75 mM; sodium azide 0.04%

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

Experiments:

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TopSpin v4.0, Bruker Biospin - collection

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

PSVS, Bhattacharya and Montelione - processing

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz

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