BMRB Entry 34085

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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/BMR34085
MolProbity Validation Chart

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Title:
Bamb_5917 Acyl-Carrier Protein
Deposition date:
2017-01-09
Original release date:
2018-07-26
Authors:
Gallo, A.; Kosol, S.; Griffiths, D.; Masschelein, J.; Alkhalaf, L.; Smith, H.; Valentic, T.; Tsai, S.; Challis, G.; Lewandowski, J.
Citation:

Citation: Kosol, Simone; Gallo, Angelo; Griffiths, Daniel; Valentic, Timothy; Masschelein, Joleen; Jenner, Matthew; de Los Santos, Emmanuel; Manzi, Lucio; Sydor, Paulina; Rea, Dean; Zhou, Shanshan; Fulop, Vilmos; Oldham, Neil; Tsai, Shiou-Chuan; Challis, Gregory; Lewandowski, Jozef. "Structural basis for chain release from the enacyloxin polyketide synthase"  Nat. Chem. 11, 913-923 (2019).
PubMed: 31548674

Assembly members:

Assembly members:
Phosphopantetheine-binding protein, polymer, 107 residues, 11323.716 Da.

Natural source:

Natural source:   Common Name: b-proteobacteria   Taxonomy ID: 339670   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia ambifaria

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Phosphopantetheine-binding protein: GIDPFTGAAAGVSAAGIEPD LTAIWQALFALPAVGRHQDF FALGGDSQLGLRMLAQLRER HGVDLPLRCLYEAPTVARLA ETIVRLAAPAPSGDQDDASE YEEGVIR

Data sets:
Data typeCount
13C chemical shifts396
15N chemical shifts96
1H chemical shifts640

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 107 residues - 11323.716 Da.

1   GLYILEASPPROPHETHRGLYALAALAALA
2   GLYVALSERALAALAGLYILEGLUPROASP
3   LEUTHRALAILETRPGLNALALEUPHEALA
4   LEUPROALAVALGLYARGHISGLNASPPHE
5   PHEALALEUGLYGLYASPSERGLNLEUGLY
6   LEUARGMETLEUALAGLNLEUARGGLUARG
7   HISGLYVALASPLEUPROLEUARGCYSLEU
8   TYRGLUALAPROTHRVALALAARGLEUALA
9   GLUTHRILEVALARGLEUALAALAPROALA
10   PROSERGLYASPGLNASPASPALASERGLU
11   TYRGLUGLUGLYVALILEARG

Samples:

sample_1: 15N_PCP17, [U-99% 15N], 0.5 mM; D2O 10%; DSS 1%; H2O 90%; potassium phosphate 50 mM; sodium chloride 200 mM

sample_2: 13C,15N_PCP17, [U-13C; U-15N], 0.3 mM; D2O 10%; DSS 1%; H2O 90%; potassium phosphate 50 mM; sodium chloride 200 mM

sample_conditions_1: ionic strength: 250 mM; pH: 6.50; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

AMBER v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

ATNOS/CANDID vUNIO, Herrmann, Guntert and Wuthrich - peak picking

CARA v3, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v3.5pl6, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AvanceII 700 MHz

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