BMRB Entry 30007

Title:
Solution structure of the apo state of the acyl carrier protein from the MLSA2 subunit 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:
entity_1, polymer, 95 residues, 10237.473 Da.

Natural source:

Natural source:   Common Name: Mycobacterium ulcerans   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)   Vector: pET28

Data sets:
Data typeCount
13C chemical shifts348
15N chemical shifts93
1H chemical shifts542

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

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

Samples:

sample_1: entity_1 mM; 333-trimethylsilylpropionate, sodium salt 0.1 ± .05 mM; sodium phosphate 150 ± 25 mM

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-TOCSY-HSQCsample_1isotropicsample_conditions_1
3D 15N-NOESY-HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 13C-NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

Analysis, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 800 MHz

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