BMRB Entry 16085

Title:
1H, 13C, 15N Chemical Shift Assignment for Saccharomyces cerevisiae Acyl Carrier Protein.
Deposition date:
2008-12-23
Original release date:
2009-04-16
Authors:
Perez, Daniel
Citation:

Citation: Perez, Daniel; Wider, Gerhard. "1H, 15N, 13C resonance assignment of the acyl carrier protein subunit of the Saccharomyces cerevisiae fatty acid synthase"  Biomol. NMR Assignments 3, 133-136 (2009).
PubMed: 19636964

Assembly members:

Assembly members:
Acyl_Carrier_Protein, polymer, 183 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts725
15N chemical shifts169
1H chemical shifts1181

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ACP single polypeptide chain1

Entities:

Entity 1, ACP single polypeptide chain 183 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   GLUASNLEUTYRPHEGLNSERASNALAGLU
3   ILEALAASPGLUPROVALLYSALASERLEU
4   LEULEUHISVALLEUVALALAHISLYSLEU
5   LYSLYSSERLEUASPSERILEPROMETSER
6   LYSTHRILELYSASPLEUVALGLYGLYLYS
7   SERTHRVALGLNASNGLUILELEUGLYASP
8   LEUGLYLYSGLUPHEGLYTHRTHRPROGLU
9   LYSPROGLUGLUTHRPROLEUGLUGLULEU
10   ALAGLUTHRPHEGLNASPTHRPHESERGLY
11   ALALEUGLYLYSGLNSERSERSERLEULEU
12   SERARGLEUILESERSERLYSMETPROGLY
13   GLYPHETHRILETHRVALALAARGLYSTYR
14   LEUGLNTHRARGTRPGLYLEUPROSERGLY
15   ARGGLNASPGLYVALLEULEUVALALALEU
16   SERASNGLUPROALAALAARGLEUGLYSER
17   GLUALAASPALALYSALAPHELEUASPSER
18   METALAGLNLYSTYRALASERILEVALGLY
19   VALASPLEU

Samples:

sample_1: Acyl Carrier Protein, [U-13C; U-15N], 1 mM; KH2PO4 : K2HPO4 (0.685 : 0.315) buffer 52 mM

sample_conditions_1: ionic strength: 0.052 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - data analysis

NMR spectrometers:

  • Bruker DRX 750 MHz

Related Database Links:

PDB
DBJ GAA26747
EMBL CAA54218 CAA64256 CAA97948 CAY86729
GB AAA34601 AHY77952 AJP41920 AJU23364 AJU24052
REF NP_015093
SP P19097
TPG DAA11205
AlphaFold P19097

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