BMRB Entry 51128

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51128

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Title:
1H, 13C, and 15N resonance assignment of mouse lipocalin-type prostaglandin D synthase/PGJ2 complex.
Deposition date:
2021-10-06
Original release date:
2022-05-05
Authors:
Shimamoto, Shigeru; Nakahata, Yuta; Hidaka, Yuji
Citation:

Citation: Shimamoto, Shigeru; Nakahata, Yuta; Hidaka, Yuji; Yoshida, Takuya; Ohkubo, Tadayasu. "NMR resonance assignments of mouse lipocalin-type prostaglandin D synthase/prostaglandin J 2 complex"  Biomol. NMR Assignments 16, 225-229 (2022).
PubMed: 35445291

Assembly members:

Assembly members:
entity_1, polymer, 165 residues, Formula weight is not available
entity_PGJ, non-polymer, 423.394 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QGHDTVQPNFQQDKFLGRWY SAGLASNSSWFREKKAVLYM CKTVVAPSTEGGLNLTSTFL RKNQCETKIMVLQPAGAPGH YTYSSPHSGSIHSVSVVEAN YDEYALLFSRGTKGPGQDFR MATLYSRTQTLKDELKEKFT TFSKAQGLTEEDIVFLPQPD KCIQE

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts135
1H chemical shifts804

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1polypeptide1
2ligand2

Entities:

Entity 1, polypeptide 165 residues - Formula weight is not available

1   GLNGLYHISASPTHRVALGLNPROASNPHE
2   GLNGLNASPLYSPHELEUGLYARGTRPTYR
3   SERALAGLYLEUALASERASNSERSERTRP
4   PHEARGGLULYSLYSALAVALLEUTYRMET
5   CYSLYSTHRVALVALALAPROSERTHRGLU
6   GLYGLYLEUASNLEUTHRSERTHRPHELEU
7   ARGLYSASNGLNCYSGLUTHRLYSILEMET
8   VALLEUGLNPROALAGLYALAPROGLYHIS
9   TYRTHRTYRSERSERPROHISSERGLYSER
10   ILEHISSERVALSERVALVALGLUALAASN
11   TYRASPGLUTYRALALEULEUPHESERARG
12   GLYTHRLYSGLYPROGLYGLNASPPHEARG
13   METALATHRLEUTYRSERARGTHRGLNTHR
14   LEULYSASPGLULEULYSGLULYSPHETHR
15   THRPHESERLYSALAGLNGLYLEUTHRGLU
16   GLUASPILEVALPHELEUPROGLNPROASP
17   LYSCYSILEGLNGLU

Entity 2, ligand - C22 H18 F N3 O5 - 423.394 Da.

1   PGJ

Samples:

sample_1: mouse lipocalin-type prostaglandin D synthase, [U-99% 15N], 0.25 mM; 15-Deoxy-D12,14-Prostaglandin J2 0.25 mM; sodium phosphate buffer 50 mM

sample_2: mouse lipocalin-type prostaglandin D synthase, [U-99% 13C; U-99% 15N], 0.25 mM; 15-Deoxy-D12,14-Prostaglandin J2 0.25 mM; sodium phosphate buffer 50 mM

sample_3: mouse lipocalin-type prostaglandin D synthase, [U-99% 13C; U-99% 15N], 0.25 mM; 15-Deoxy-D12,14-Prostaglandin J2 0.25 mM; sodium phosphate buffer 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_2isotropicsample_conditions_1
3D 13C-separated NOESYsample_3isotropicsample_conditions_1

Software:

NMRPipe - chemical shift assignment

NMRViewJ - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

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