Click here to enlarge.

PDB ID: 8zu6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36671
MolProbity Validation Chart

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

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

Please specify the pdb ID.

Name: Solution NMR Structure of PACT D3 Homodimer
Published: 2026-06-08

Title:

Solution NMR Structure of PACT D3 Homodimer

Deposition date:

2024-06-08

Original release date:

2026-06-08

Authors:

Zhao, L.; Ahmad, S.; Hur, S.; Chou, J.

Citation:

Citation: Ahmad, Sadeem; Zou, Tao; Hwang, Jihee; Zhao, Linlin; Wang, Xi; Davydenko, Anton; Buchumenski, Ilana; Zhuang, Patrick; Fishbein, Alyssa; Capcha-Rodriguez, Diego; Orgel, Aaron; Levanon, Erez; Myong, Sua; Chou, James; Meyerson, Matthew; Hur, Sun. "PACT prevents aberrant activation of PKR by endogenous dsRNA without sequestration." Nat. Commun. 16, 3325-3325 (2025).
PubMed: 40199855

Assembly members:

Assembly members:
Interferon-inducible double-stranded RNA-dependent protein kinase activator A, polymer, 188 residues, 10271.357 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Interferon-inducible double-stranded RNA-dependent protein kinase activator A: MAHHHHHHSAALEVLFQGPG YQDPDYIQLLSEIAKEQGFN ITYLDIDELSANGQYQCLAE LSTSPITVCHGSGISCGNAQ SDAAHNALQYLKII

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	194
15N chemical shifts	63
1H chemical shifts	63

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1_1	1
2	entity_1_2	1

Entities:

Entity 1, entity_1_1 188 residues - 10271.357 Da.

1

MET

ALA

HIS

SER

ALA

2

ALA

LEU

GLU

VAL

LEU

PHE

GLN

GLY

PRO

GLY

3

TYR

GLN

ASP

PRO

ASP

TYR

ILE

GLN

LEU

4

SER

GLU

ILE

ALA

LYS

GLU

GLN

GLY

PHE

ASN

5

ILE

THR

TYR

LEU

ASP

ILE

ASP

GLU

LEU

SER

6

ALA

ASN

GLY

GLN

TYR

GLN

CYS

LEU

ALA

GLU

7

LEU

SER

THR

SER

PRO

ILE

THR

VAL

CYS

HIS

8

GLY

SER

GLY

ILE

SER

CYS

GLY

ASN

ALA

GLN

9

SER

ASP

ALA

HIS

ASN

ALA

LEU

GLN

TYR

10

LEU

LYS

ILE

Samples:

sample_1: PACT D3, [U-13C; U-15N], 0.7 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: PACT D3, [U-15N], 0.7 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 Pa; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

XEASY, Bartels et al. - refinement

CcpNmr Analysis, CCPN - peak picking

NMR spectrometers:

Bruker AVANCE 600 MHz
Bruker AVANCE 900 MHz

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

BMRB Entry 36671