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BMRB Entry 25514

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25514
MolProbity Validation Chart

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Title: Solution Structure of the phosphorylated J-domain of Human Cysteine String Protein (CSP)   PubMed: 27452402

Deposition date: 2015-03-04 Original release date: 2016-07-11

Authors: Patel, Pryank; Lian, Lu-Yun; Morgan, Alan; Burgoyne, Robert

Citation: Patel, Pryank; Prescott, Gerald; Burgoyne, Robert; Lian, Lu-Yun; Morgan, Alan. "Phosphorylation of Cysteine String Protein Triggers a Major Conformational Switch"  Structure 24, 1380-1386 (2016).

Assembly members:
Phosphorylated_DnaJ_domain_of_cysteine-string_protein, polymer, 105 residues, 11984.308 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):
Phosphorylated_DnaJ_domain_of_cysteine-string_protein: MRSPGMADQRQRSLXTSGES LYHVLGLDKNATSDDIKKSY RKLALKYHPDKNPDNPEAAD KFKEINNAHAILTDATKRNI YDKYGSLGLYVAEQFGEENV NTYFV

Data sets:
Data typeCount
13C chemical shifts400
15N chemical shifts106
1H chemical shifts649

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Phosphorylated_DnaJ_domain_of_cysteine-string_protein1

Entities:

Entity 1, Phosphorylated_DnaJ_domain_of_cysteine-string_protein 105 residues - 11984.308 Da.

1   METARGSERPROGLYMETALAASPGLNARG
2   GLNARGSERLEUSEPTHRSERGLYGLUSER
3   LEUTYRHISVALLEUGLYLEUASPLYSASN
4   ALATHRSERASPASPILELYSLYSSERTYR
5   ARGLYSLEUALALEULYSTYRHISPROASP
6   LYSASNPROASPASNPROGLUALAALAASP
7   LYSPHELYSGLUILEASNASNALAHISALA
8   ILELEUTHRASPALATHRLYSARGASNILE
9   TYRASPLYSTYRGLYSERLEUGLYLEUTYR
10   VALALAGLUGLNPHEGLYGLUGLUASNVAL
11   ASNTHRTYRPHEVAL

Samples:

sample_1: Phosphorylated DnaJ domain of cysteine-string protein, [U-13C; U-15N], 0.5 mM; MES 20 mM; sodium chloride 150 mM; DTT 1 mM; MgCl2 10 mM; EDTA 0.5 mM; PKA 0.73 nM; ATP 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN_Analysis, CCPN - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

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