BMRB Entry 16966

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16966

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Title:
Insights into protein-protein and enzyme-substrate interactions in modular polyketide synthases
Deposition date:
2010-06-01
Original release date:
2014-03-04
Authors:
Tran, Lucky; Broadhurst, Richard; Tosin, Manuela; Cavalli, Andrea; Weissman, Kira
Citation:

Citation: Tran, Lucky; Broadhurst, Richard; Tosin, Manuela; Cavalli, Andrea; Weissman, Kira. "Insights into protein-protein and enzyme-substrate interactions in modular polyketide synthases."  Chem. Biol. 17, 705-716 (2010).
PubMed: 20659683

Assembly members:

Assembly members:
DEBS_ACP6, polymer, 90 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: S. erythraea   Taxonomy ID: 1836   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Saccharopolyspora erythraea

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET38b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DEBS_ACP6: GPLGSAAPAREMTSQELLEF THSHVAAILGHSSPDAVGQD QPFTELGFDSLTAVGLRNQL QQATGLALPATLVFEHPTVR RLADHIGQQL

Data sets:
Data typeCount
13C chemical shifts243
15N chemical shifts79
1H chemical shifts388

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DEBS_ACP61

Entities:

Entity 1, DEBS_ACP6 90 residues - Formula weight is not available

1   GLYPROLEUGLYSERALAALAPROALAARG
2   GLUMETTHRSERGLNGLULEULEUGLUPHE
3   THRHISSERHISVALALAALAILELEUGLY
4   HISSERSERPROASPALAVALGLYGLNASP
5   GLNPROPHETHRGLULEUGLYPHEASPSER
6   LEUTHRALAVALGLYLEUARGASNGLNLEU
7   GLNGLNALATHRGLYLEUALALEUPROALA
8   THRLEUVALPHEGLUHISPROTHRVALARG
9   ARGLEUALAASPHISILEGLYGLNGLNLEU

Samples:

sample_1: DEBS_ACP6, [U-13C; U-15N], 1 mM; TSP 20 uM; sodium phosphate 50 mM; sodium chloride 150 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.2 M; pH: 8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_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 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

AZARA, Boucher - processing

ANALYSIS v1, CCPN - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

REF WP_009950406

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