BMRB Entry 27221

Name: Backbone 1H, 13C and 15N Chemical Shift Assignments for residues 421-470 of human PABPC1
Published: 2018-03-08

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27221

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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 1H, 13C and 15N Chemical Shift Assignments for residues 421-470 of human PABPC1

Deposition date:

2017-08-16

Original release date:

2018-03-08

Authors:

Imai, Shunsuke; Sawazaki, Ryoichi; Yokogawa, Mariko; Shimada, Ichio; Osawa, Masanori

Citation:

Citation: Sawazaki, Ryoichi; Imai, Shunsuke; Yokogawa, Mariko; Hosoda, Nao; Hoshino, Shin-ichi; Mio, Muneyo; Mio, Kazuhiro; Shimada, Ichio; Osawa, Masanori. "Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail" Sci. Rep. 8, 1455-1455 (2018).
PubMed: 29362417

Assembly members:

Assembly members:
Residues_421-470_of_human_PABPC1, polymer, 55 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-42b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Residues_421-470_of_human_PABPC1: GPLGSAYYPPSQIAQLRPSP RWTAQGARPHPFQNMPGAIR PAAPRPPFSTMRPAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	114
15N chemical shifts	41
1H chemical shifts	41

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Residues 421-470 of PABPC1	1

Entities:

Entity 1, Residues 421-470 of PABPC1 55 residues - Formula weight is not available

Residues 1-5 are cloning artifacts.

1

GLY

PRO

LEU

GLY

SER

ALA

TYR

PRO

2

SER

GLN

ILE

ALA

GLN

LEU

ARG

PRO

SER

PRO

3

ARG

TRP

THR

ALA

GLN

GLY

ALA

ARG

PRO

HIS

4

PRO

PHE

GLN

ASN

MET

PRO

GLY

ALA

ILE

ARG

5

PRO

ALA

PRO

ARG

PRO

PHE

SER

THR

6

MET

ARG

PRO

ALA

SER

Samples:

sample_1: Residues 421-470 of PABPC1, [U-13C; U-15N], 290 uM; sodium phosphate 26 mM; sodium chloride 100 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
15N-edited TOCSY HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

xwinnmr vver 3.6, Bruker Biospin - processing

CARA vver 1.5.1, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz

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