BMRB Entry 51507

Name: Human PPARg2 AF-1 domain
Published: 2024-07-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51507

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGETLGDSPIDPESDSFTDT LSANISQEMTMVDTEMPFWP TNFGISSVDLSVMEDHSHSF DIKPFTTVDFSSISTPHYED IPFTRTDPVVADYKYDLKLQ EYQSAIKVEPASPPYYSEKT QLYNKPHEEPSNSLM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	498
15N chemical shifts	128
1H chemical shifts	115

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPARg AF-1	1

Entities:

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

1

MET

GLY

GLU

THR

LEU

GLY

ASP

SER

PRO

ILE

2

ASP

PRO

GLU

SER

ASP

SER

PHE

THR

ASP

THR

3

LEU

SER

ALA

ASN

ILE

SER

GLN

GLU

MET

THR

4

MET

VAL

ASP

THR

GLU

MET

PRO

PHE

TRP

PRO

5

THR

ASN

PHE

GLY

ILE

SER

VAL

ASP

LEU

6

SER

VAL

MET

GLU

ASP

HIS

SER

HIS

SER

PHE

7

ASP

ILE

LYS

PRO

PHE

THR

VAL

ASP

PHE

8

SER

ILE

SER

THR

PRO

HIS

TYR

GLU

ASP

9

ILE

PRO

PHE

THR

ARG

THR

ASP

PRO

VAL

10

ALA

ASP

TYR

LYS

TYR

ASP

LEU

LYS

LEU

GLN

11

GLU

TYR

GLN

SER

ALA

ILE

LYS

VAL

GLU

PRO

12

ALA

SER

PRO

TYR

SER

GLU

LYS

THR

13

GLN

LEU

TYR

ASN

LYS

PRO

HIS

GLU

PRO

14

SER

ASN

SER

LEU

MET

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:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_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