BMRB Entry 34301

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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/BMR34301
MolProbity Validation Chart

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Title:
B1-type ACP domain from module 7 of MLSB
Deposition date:
2018-07-10
Original release date:
2019-03-14
Authors:
Moretto, Luisa; Heylen, Rachel; Holroyd, Natalie; Vance, Steven; Broadhurst, Richard
Citation:

Citation: Moretto, Luisa; Heylen, Rachel; Holroyd, Natalie; Vance, Steven; Broadhurst, Richard. "Modular type I polyketide synthase acyl carrier protein domains share a common N-terminally extended fold."  Sci. Rep. 9, 2325-2325 (2019).
PubMed: 30787330

Assembly members:

Assembly members:
Type I modular polyketide synthase, polymer, 102 residues, 10723.946 Da.

Natural source:

Natural source:   Common Name: Mycobacterium ulcerans Agy99   Taxonomy ID: 362242   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium Mycobacterium ulcerans

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Type I modular polyketide synthase: GAASAATDLAARLNGLSPQQ QQQTLATLVAAATATVLGHH TPESISPATAFKDLGIDSLT ALELRNTLTHNTGLDLPPTL IFDHPTPHALTQHLHTRLTQ SH

Data sets:
Data typeCount
13C chemical shifts396
15N chemical shifts94
1H chemical shifts611

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 102 residues - 10723.946 Da.

1   GLYALAALASERALAALATHRASPLEUALA
2   ALAARGLEUASNGLYLEUSERPROGLNGLN
3   GLNGLNGLNTHRLEUALATHRLEUVALALA
4   ALAALATHRALATHRVALLEUGLYHISHIS
5   THRPROGLUSERILESERPROALATHRALA
6   PHELYSASPLEUGLYILEASPSERLEUTHR
7   ALALEUGLULEUARGASNTHRLEUTHRHIS
8   ASNTHRGLYLEUASPLEUPROPROTHRLEU
9   ILEPHEASPHISPROTHRPROHISALALEU
10   THRGLNHISLEUHISTHRARGLEUTHRGLN
11   SERHIS

Samples:

sample_1: sodium choride, NA, 150 ± 10 mM; sodium phosphate, NA, 50 ± 5 mM; 15N_mH0ACPb, [U-15N], 0.8 ± 0.05 mM

sample_2: sodium phosphate, NA, 50 ± 5 mM; 13C15N_mH0ACPb, [U-13C; U-15N], 0.8 ± 0.05 mM; sodium chloride, NA, 150 ± 10 mM

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

sample_conditions_2: ionic strength: 150 mM; pH: 7.5 pD; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D 1H-13C NOESYsample_2isotropicsample_conditions_2

Software:

TOPSPIN, Bruker Biospin - collection

AZARA, Boucher - processing

Analysis, CCPN - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 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