BMRB Entry 30006

Title:
Solution structure of an octanoyl- loaded acyl carrier protein domain from module MLSA2 of the mycolactone polyketide synthase
Deposition date:
2016-01-28
Original release date:
2016-03-14
Authors:
Vance, S.; Tkachenko, O.; Thomas, B.; Bassuni, M.; Hong, H.; Nietlispach, D.; Broadhurst, R.
Citation:

Citation: Vance, S.; Tkachenko, O.; Thomas, B.; Bassuni, M.; Hong, H.; Nietlispach, D.; Broadhurst, R.. "Sticky swinging arm dynamics: studies of an acyl carrier protein domain from the mycolactone polyketide synthase"  Biochem. J. 473, 1097-1110 (2016).
PubMed: 26920023

Assembly members:

Assembly members:
Type I modular polyketide synthase, polymer, 95 residues, 10237.473 Da.
S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] octanethioate, non-polymer, 484.544 Da.

Natural source:

Natural source:   Common Name: high GC Gram+   Taxonomy ID: 1809   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium ulcerans

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts315
15N chemical shifts92
1H chemical shifts675

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
266S2

Entities:

Entity 1, entity_1 95 residues - 10237.473 Da.

1   GLYSERHISMETARGLEUASNGLYLEUSER
2   PROGLNGLNGLNGLNGLNTHRLEUALATHR
3   LEUVALALAALAALATHRALATHRVALLEU
4   GLYHISHISTHRPROGLUSERILESERPRO
5   ALATHRALAPHELYSASPLEUGLYILEASP
6   SERLEUTHRALALEUGLULEUARGASNTHR
7   LEUTHRHISASNTHRGLYLEUASPLEUPRO
8   PROTHRLEUILEPHEASPHISPROTHRPRO
9   HISALALEUTHRGLNHISLEUHISTHRARG
10   LEUTHRGLNSERHIS

Entity 2, 66S - C19 H37 N2 O8 P S - 484.544 Da.

1   66S

Samples:

sample_1: 3,3,3-trimethylsilylpropionate, sodium salt 0.1 ± .05 mM; sodium phosphate 150 ± 25 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D [1H,15N]-HSQCsample_1isotropicsample_conditions_1
3D 15N-HSQC-TOCSYsample_1isotropicsample_conditions_1
3D 15N-HSQC-NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 13C-HSQC-NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - structure calculation

Analysis, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX500 500 MHz
  • Bruker DRX800 800 MHz

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