BMRB Entry 6459

Name: Chemical Shift Assignment for Itch E3 WW3 domain
Published: 2005-09-22

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PDB ID: 1yiu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6459
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Chemical Shift Assignment for Itch E3 WW3 domain

Deposition date:

2005-01-14

Original release date:

2005-09-22

Authors:

Shaw, Alison; Martin-Malpartida, Pau; Morales, Begonya; Yraola, Francesc; Royo, Miriam; Macias, Maria

Citation:

Citation: Shaw, Alison; Martin-Malpartida, Pau; Morales, Begonya; Yraola, Francesc; Royo, Miriam; Macias, Maria. "Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain" Proteins 60, 558-560 (2005).
PubMed: 15971201

Assembly members:

Assembly members:
WW 3 domain, polymer, 37 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WW 3 domain: GAMGPLPPGWEKRTDSNGRV YFVNHNTRITQWEDPRS

Data sets:

assigned_chemical_shifts
- Carbon
- Nitrogen

Data type	Count
13C chemical shifts	118
15N chemical shifts	42
1H chemical shifts	386

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WW 3 domain	1

Entities:

Entity 1, WW 3 domain 37 residues - Formula weight is not available

1

GLY

ALA

MET

GLY

PRO

LEU

PRO

GLY

TRP

2

GLU

LYS

ARG

THR

ASP

SER

ASN

GLY

ARG

VAL

3

TYR

PHE

VAL

ASN

HIS

ASN

THR

ARG

ILE

THR

4

GLN

TRP

GLU

ASP

PRO

ARG

SER

Samples:

unlabeled: WW 3 domain 1 mM; NaCl 100 mM; Na2HPO4 50 mM

15N_labeled: WW 3 domain, [U-15N], 1 mM; NaCl 100 mM; Na2HPO4 50 mM

13C_15N_labeled: WW 3 domain, [U-13C; U-15N], 1 mM; NaCl 100 mM; Na2HPO4 50 mM

conditions_1: pH: 6.0; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N-HSQC	15N_labeled	not available	conditions_1
CBCA(CO)NH	13C_15N_labeled	not available	conditions_1
CBCANH	13C_15N_labeled	not available	conditions_1
15N_edited_TOCSY	15N_labeled	not available	conditions_1
15N_edited_NOESY	15N_labeled	not available	conditions_1
13C_edited_NOESY	13C_15N_labeled	not available	conditions_1
13C_edited_TOCSY	13C_15N_labeled	not available	conditions_1
(H)CC(CO)NH	13C_15N_labeled	not available	conditions_1
H(CC)(CO)NH	13C_15N_labeled	not available	conditions_1

Software:

CNS, Bruenger AT - structure calculation

xwinnmr, Bruker Biospin - acquisition

XEASY, Bartels, C. - assignment

NMRPipe, Delaglio, F. - processing

ARIA, Nilges, M. - assignment

NMR spectrometers:

Bruker DRX 600 MHz
Bruker DRX 800 MHz