BMRB Entry 27148

Name: Backbone and side chain chemical shift assignments of wild-type PACT-D3.
Published: 2019-04-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27148

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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:

Backbone and side chain chemical shift assignments of wild-type PACT-D3.

Deposition date:

2017-06-19

Original release date:

2019-04-15

Authors:

Heyam, Alex

Citation:

Citation: Heyam, Alex; Coupland, Claire; Degut, Clement; Haley, Ruth; Baxter, Nicola; Jakob, Leonhard; Aguiar, Pedro; Meister, Gunter; Williamson, Michael; Lagos, Dimitris; Plevin, Michael. "Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins." Nucleic Acids Res. 45, 12577-12584 (2017).
PubMed: 29045748

Assembly members:

Assembly members:
PACT-D3_wt, polymer, 79 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: pETFPP_2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PACT-D3_wt: GPAMTDYIQLLSEIAKEQGF NITYLDIDELSANGQYQCLA ELSTSPITVCHGSGISCGNA QSDAAHNALQYLKIIAERK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	584
15N chemical shifts	155
1H chemical shifts	893

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PACT-D3 state_A	1
2	PACT-D3 state_B	1

Entities:

Entity 1, PACT-D3 state_A 79 residues - Formula weight is not available

The first four residues (GPAM) are non-native, and remain after cleavage of an affinity tag. This is followed by PACT residues 239-313.

1

GLY

PRO

ALA

MET

THR

ASP

TYR

ILE

GLN

LEU

2

LEU

SER

GLU

ILE

ALA

LYS

GLU

GLN

GLY

PHE

3

ASN

ILE

THR

TYR

LEU

ASP

ILE

ASP

GLU

LEU

4

SER

ALA

ASN

GLY

GLN

TYR

GLN

CYS

LEU

ALA

5

GLU

LEU

SER

THR

SER

PRO

ILE

THR

VAL

CYS

6

HIS

GLY

SER

GLY

ILE

SER

CYS

GLY

ASN

ALA

7

GLN

SER

ASP

ALA

HIS

ASN

ALA

LEU

GLN

8

TYR

LEU

LYS

ILE

ALA

GLU

ARG

LYS

Samples:

backbone_assignment: PACT-D3_wt, [U-13C; U-15N], 1.3 mM; sodium chloride 50 mM; MES 20 mM; TCEP 10 mM; DSS 50 uM

sidechain_assignment: PACT-D3_wt, [U-13C; U-15N], 2.4 mM; sodium chloride 50 mM; MES 20 mM; TCEP 10 mM; DSS 50 uM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N SOFAST-HMQC	backbone_assignment	isotropic	sample_conditions_1
HNCACB	backbone_assignment	isotropic	sample_conditions_1
CBCACONH	backbone_assignment	isotropic	sample_conditions_1
HNCO	sidechain_assignment	isotropic	sample_conditions_1
CC(CO)NH-TOCSY	sidechain_assignment	isotropic	sample_conditions_1
HCCH-TOCSY	sidechain_assignment	isotropic	sample_conditions_1
1H-13C HSQC	sidechain_assignment	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0-3.5, Bruker Biospin - collection, processing

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz
Bruker Avance 800 MHz

UNP	O75569
AlphaFold	Q8NDK4