BMRB Entry 51507

Title:
Human PPARg2 AF-1 domain
Deposition date:
2022-06-29
Original release date:
2024-07-05
Authors:
Mosure, Sarah
Citation:

Citation: Mosure, Sarah; Munoz-Tello, Paola; Kuo, Kuang-Ting; MacTavish, Brian; Yu, Xiaoyu; Scholl, Daniel; Williams, Christopher; Strutzenberg, Timothy; Bass, Jared; Brust, Richard; Deniz, Ashok; Griffin, Patrick; Kojetin, Douglas. "Structural basis of interdomain communication in PPARy"  bioRxiv ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 135 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET46

Data sets:
Data typeCount
13C chemical shifts498
15N chemical shifts128
1H chemical shifts115

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PPARg AF-11

Entities:

Entity 1, PPARg AF-1 135 residues - Formula weight is not available

1   METGLYGLUTHRLEUGLYASPSERPROILE
2   ASPPROGLUSERASPSERPHETHRASPTHR
3   LEUSERALAASNILESERGLNGLUMETTHR
4   METVALASPTHRGLUMETPROPHETRPPRO
5   THRASNPHEGLYILESERSERVALASPLEU
6   SERVALMETGLUASPHISSERHISSERPHE
7   ASPILELYSPROPHETHRTHRVALASPPHE
8   SERSERILESERTHRPROHISTYRGLUASP
9   ILEPROPHETHRARGTHRASPPROVALVAL
10   ALAASPTYRLYSTYRASPLEULYSLEUGLN
11   GLUTYRGLNSERALAILELYSVALGLUPRO
12   ALASERPROPROTYRTYRSERGLULYSTHR
13   GLNLEUTYRASNLYSPROHISGLUGLUPRO
14   SERASNSERLEUMET

Samples:

sample_1: PPARg AF-1, [U-100% 13C; U-100% 15N], 300 uM; potassium phosphate 50 mM; potassium chloride 20 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRFx - processing

NMRViewJ - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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