BMRB Entry 50596

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50596

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution structure and conformational dynamics of a doublet acyl carrier protein from prodigiosin biosynthesis
Deposition date:
2020-11-27
Original release date:
2021-06-30
Authors:
Thongkawphueak, Thitapa; Winter, Ashley; Williams, Christopher; Maple, Hannah; Soontaranon, Siriwat; Kaewhan, Chonthicha; Campopiano, Dominic; Crump, Matthew; Wattana-Amorn, Pakorn
Citation:

Citation: Thongkawphueak, Thitapa; Winter, Ashley; Williams, Christopher; Maple, Hannah; Soontaranon, Siriwat; Kaewhan, Chonthicha; Campopiano, Dominic; Crump, Matthew; Wattana-Amorn, Pakorn. "Solution Structure and Conformational Dynamics of a Doublet Acyl Carrier Protein from Prodigiosin Biosynthesis."  Biochemistry 60, 219-230 (2021).
PubMed: 33416314

Assembly members:

Assembly members:
entity_1, polymer, 205 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Serratia sp. ATCC 39006   Taxonomy ID: 104623   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Serratia Serratia sp. ATCC 39006

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pPigHACP1ACP2-pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMNDVTTETYETLKQSVL HTFAQLTGYNVSELSLTSHL ENDLGVDSIALAEIAVSLSR QFQLNTPLLIQDINTIKDAL DGILQREFQLSEKVEPAAIA LSGDADLWLGNLVRQIFASH SGYDVNALALDAEIESDLGI DSVSVASAQGELFNTLQLNS ETIIANCNTLSALKQCLAAR LVQEKGQDWFELTRAPPPPP LRSGC

Data sets:
Data typeCount
13C chemical shifts850
15N chemical shifts224
1H chemical shifts1413

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ACP1ACP2 monomer1

Entities:

Entity 1, ACP1ACP2 monomer 205 residues - Formula weight is not available

1   GLYSERHISMETASNASPVALTHRTHRGLU
2   THRTYRGLUTHRLEULYSGLNSERVALLEU
3   HISTHRPHEALAGLNLEUTHRGLYTYRASN
4   VALSERGLULEUSERLEUTHRSERHISLEU
5   GLUASNASPLEUGLYVALASPSERILEALA
6   LEUALAGLUILEALAVALSERLEUSERARG
7   GLNPHEGLNLEUASNTHRPROLEULEUILE
8   GLNASPILEASNTHRILELYSASPALALEU
9   ASPGLYILELEUGLNARGGLUPHEGLNLEU
10   SERGLULYSVALGLUPROALAALAILEALA
11   LEUSERGLYASPALAASPLEUTRPLEUGLY
12   ASNLEUVALARGGLNILEPHEALASERHIS
13   SERGLYTYRASPVALASNALALEUALALEU
14   ASPALAGLUILEGLUSERASPLEUGLYILE
15   ASPSERVALSERVALALASERALAGLNGLY
16   GLULEUPHEASNTHRLEUGLNLEUASNSER
17   GLUTHRILEILEALAASNCYSASNTHRLEU
18   SERALALEULYSGLNCYSLEUALAALAARG
19   LEUVALGLNGLULYSGLYGLNASPTRPPHE
20   GLULEUTHRARGALAPROPROPROPROPRO
21   LEUARGSERGLYCYS

Samples:

sample_1: PigH ACP1-ACP2, [U-95% 13C; U-95% 15N], 360 uM

sample_2: PigH ACP1-ACP2, [U-99% 15N], 400 uM

sample_conditions_1: ionic strength: 0 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.4.2 - chemical shift assignment

NMRPipe - processing

TALOS-N - data analysis

ARIA2 v2.3 - structure solution

CNS v1.2 - structure solution

NMR spectrometers:

  • Varian VNMRS 600 MHz

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