BMRB Entry 11501

Name: solution structure of PARP14 WWE domain
Published: 2018-12-18

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11501

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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:

solution structure of PARP14 WWE domain

Deposition date:

2012-05-08

Original release date:

2018-12-18

Authors:

He, Fahu; Muto, Yutaka; Inoue, Makoto; Kigawa, Takanori; Shirouzu, Mikako; Terada, Takaho; Yokoyama, Shigeyuki

Citation:

Citation: He, Fahu; Tsuda, Kengo; Takahashi, Mari; Kuwasako, Kanako; Terada, Takano; Shirouzu, Mikako; Watanabe, Satoru; Kigawa, Takanori; Kobayashi, Naohiro; Guntert, Peter; Yokoyama, Shigeyuki; Muto, Yutaka. "Structural insight into the interaction of ADP-ribose with the PARP WWE domains." FEBS Lett. 586, 3858-3864 (2012).
PubMed: 23010590

Assembly members:

Assembly members:
PARP14, polymer, 99 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: E. coli - cell free Vector: P-00001

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PARP14: GSSGSSGKSIRLAKEKESQA DYISTYVEWQYIDKNITQCF DKMTNMKLEVAWKAKKKDTV VQIHNQDFTVDLSTNTATAP QGQTFTVQRLVKASGPSSG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	405
15N chemical shifts	99
1H chemical shifts	647

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PARP14	1

Entities:

Entity 1, PARP14 99 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

LYS

SER

ILE

2

ARG

LEU

ALA

LYS

GLU

LYS

GLU

SER

GLN

ALA

3

ASP

TYR

ILE

SER

THR

TYR

VAL

GLU

TRP

GLN

4

TYR

ILE

ASP

LYS

ASN

ILE

THR

GLN

CYS

PHE

5

ASP

LYS

MET

THR

ASN

MET

LYS

LEU

GLU

VAL

6

ALA

TRP

LYS

ALA

LYS

ASP

THR

VAL

7

VAL

GLN

ILE

HIS

ASN

GLN

ASP

PHE

THR

VAL

8

ASP

LEU

SER

THR

ASN

THR

ALA

THR

ALA

PRO

9

GLN

GLY

GLN

THR

PHE

THR

VAL

GLN

ARG

LEU

10

VAL

LYS

ALA

SER

GLY

PRO

SER

GLY

Samples:

sample_1: PARP14, [U-99% 13C; U-99% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment

Kujira, N. Kobayashi - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Bruker Avance 800 MHz

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