BMRB Entry 50022

Name: The WW1 domain enhances auto-inhibition in Smurf ubiquitin ligases
Published: 2020-09-21

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50022

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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:

The WW1 domain enhances auto-inhibition in Smurf ubiquitin ligases

Deposition date:

2019-09-23

Original release date:

2020-09-21

Authors:

Wiesner, Silke; Ruetalo, Natalia

Citation:

Citation: Ruetalo, Natalia; Anders, Samira; Stollmaier, Carsten; Jaeckl, Magnus; Schuetz-Stoffregen, Mira; Stefan, Nadine; Wolf, Christine; Wiesner, Silke. "The WW1 Domain Enhances Autoinhibition in Smurf Ubiquitin Ligases" J. Mol. Biol. 431, 4834-4847 (2019).
PubMed: 31628949

Assembly members:

Assembly members:
C2WW1, polymer, 191 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: pETM-41

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C2WW1: GAMGPVKLRLTVLCAKNLVK KDFFRLPDPFAKVVVDGSGQ CHSTDTVKNTLDPKWNQHYD LYIGKSDSVTISVWNHKKIH KKQGAGFLGCVRLLSNAINR LKDTGYQRLDLCKLGPNDND TVRGQIVVSLQSRDRIGTGG QVVDASRLFDNDLPDGWEER RTASGRIQYLNHITRTTQWE RPTRPASEYSS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	382
15N chemical shifts	166
1H chemical shifts	159

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C2WW1	1

Entities:

Entity 1, C2WW1 191 residues - Formula weight is not available

1

GLY

ALA

MET

GLY

PRO

VAL

LYS

LEU

ARG

LEU

2

THR

VAL

LEU

CYS

ALA

LYS

ASN

LEU

VAL

LYS

3

LYS

ASP

PHE

ARG

LEU

PRO

ASP

PRO

PHE

4

ALA

LYS

VAL

ASP

GLY

SER

GLY

GLN

5

CYS

HIS

SER

THR

ASP

THR

VAL

LYS

ASN

THR

6

LEU

ASP

PRO

LYS

TRP

ASN

GLN

HIS

TYR

ASP

7

LEU

TYR

ILE

GLY

LYS

SER

ASP

SER

VAL

THR

8

ILE

SER

VAL

TRP

ASN

HIS

LYS

ILE

HIS

9

LYS

GLN

GLY

ALA

GLY

PHE

LEU

GLY

CYS

10

VAL

ARG

LEU

SER

ASN

ALA

ILE

ASN

ARG

11

LEU

LYS

ASP

THR

GLY

TYR

GLN

ARG

LEU

ASP

12

LEU

CYS

LYS

LEU

GLY

PRO

ASN

ASP

ASN

ASP

13

THR

VAL

ARG

GLY

GLN

ILE

VAL

SER

LEU

14

GLN

SER

ARG

ASP

ARG

ILE

GLY

THR

GLY

15

GLN

VAL

ASP

ALA

SER

ARG

LEU

PHE

ASP

16

ASN

ASP

LEU

PRO

ASP

GLY

TRP

GLU

ARG

17

ARG

THR

ALA

SER

GLY

ARG

ILE

GLN

TYR

LEU

18

ASN

HIS

ILE

THR

ARG

THR

GLN

TRP

GLU

19

ARG

PRO

THR

ARG

PRO

ALA

SER

GLU

TYR

SER

20

SER

Samples:

sample_1: C2WW1, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.5 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

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