BMRB Entry 50526

Name: Assigned chemical shifts for PABPC1 RRM1 and BTG2(APRO)
Published: 2021-06-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50526

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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:

Assigned chemical shifts for PABPC1 RRM1 and BTG2(APRO)

Deposition date:

2020-10-21

Original release date:

2021-06-30

Authors:

Ripin, Nina; Allain, Frederic

Citation:

Citation: Amine, Hamza; Ripin, Nina; Sharma, Sahil; Stoecklin, Georg; Allain, Frederic; Seraphin, Bertrand; Mauxion, Fabienne. "A conserved motif in human BTG1 and BTG2 proteins mediates interaction with the poly(A) binding protein PABPC1 to stimulate mRNA deadenylation." RNA Biol. ., 1-16 (2021).
PubMed: 34060423

Assembly members:

Assembly members:
entity_1, polymer, 101 residues, Formula weight is not available
entity_2, polymer, 128 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: pET-GB1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMNPSAPSYPMASLYVGDL HPDVTEAMLYEKFSPAGPIL SIRVCRDMITRRSLGYAYVN FQQPADAERALDTMNFDVIK GKPVRIMWSQRDPSLRKSGV G
entity_2: GAMSHGKGTDMLPEIAAAVG FLSSLLRTRGCVSEQRLKVF SGALQEALTEHYKHHWFPEK PSKGSGYRCIRINHKMDPII SRVASQIGLSQPQLHQLLPS ELTLWVDPYEVSYRIGEDGS ICVLYEEA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	505
15N chemical shifts	181
1H chemical shifts	180

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PABPC1 RRM1	1
2	BTG2(APRO)	2

Entities:

Entity 1, PABPC1 RRM1 101 residues - Formula weight is not available

1

GLY

ALA

MET

ASN

PRO

SER

ALA

PRO

SER

TYR

2

PRO

MET

ALA

SER

LEU

TYR

VAL

GLY

ASP

LEU

3

HIS

PRO

ASP

VAL

THR

GLU

ALA

MET

LEU

TYR

4

GLU

LYS

PHE

SER

PRO

ALA

GLY

PRO

ILE

LEU

5

SER

ILE

ARG

VAL

CYS

ARG

ASP

MET

ILE

THR

6

ARG

SER

LEU

GLY

TYR

ALA

TYR

VAL

ASN

7

PHE

GLN

PRO

ALA

ASP

ALA

GLU

ARG

ALA

8

LEU

ASP

THR

MET

ASN

PHE

ASP

VAL

ILE

LYS

9

GLY

LYS

PRO

VAL

ARG

ILE

MET

TRP

SER

GLN

10

ARG

ASP

PRO

SER

LEU

ARG

LYS

SER

GLY

VAL

11

GLY

Entity 2, BTG2(APRO) 128 residues - Formula weight is not available

1

GLY

ALA

MET

SER

HIS

GLY

LYS

GLY

THR

ASP

2

MET

LEU

PRO

GLU

ILE

ALA

VAL

GLY

3

PHE

LEU

SER

LEU

ARG

THR

ARG

GLY

4

CYS

VAL

SER

GLU

GLN

ARG

LEU

LYS

VAL

PHE

5

SER

GLY

ALA

LEU

GLN

GLU

ALA

LEU

THR

GLU

6

HIS

TYR

LYS

HIS

TRP

PHE

PRO

GLU

LYS

7

PRO

SER

LYS

GLY

SER

GLY

TYR

ARG

CYS

ILE

8

ARG

ILE

ASN

HIS

LYS

MET

ASP

PRO

ILE

9

SER

ARG

VAL

ALA

SER

GLN

ILE

GLY

LEU

SER

10

GLN

PRO

GLN

LEU

HIS

GLN

LEU

PRO

SER

11

GLU

LEU

THR

LEU

TRP

VAL

ASP

PRO

TYR

GLU

12

VAL

SER

TYR

ARG

ILE

GLY

GLU

ASP

GLY

SER

13

ILE

CYS

VAL

LEU

TYR

GLU

ALA

Samples:

sample_1: PABPC1 RRM1, [U-99% 13C; U-99% 15N], 750 uM

sample_2: BTG2(APRO), [U-99% 13C; U-99% 15N], 600 uM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
3D CBCACONH	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HNCACO	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2

Software:

TOPSPIN Bruker Biospin - collection

SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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