BMRB Entry 30858

Name: Structure of Nedd4L WW3 domain
Published: 2021-07-15

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PDB ID: 7lp5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30858
MolProbity Validation Chart

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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: Structure of Nedd4L WW3 domain PubMed: 34284061

Deposition date: 2021-02-11 Original release date: 2021-07-15

Authors: Alam, S.; Alian, A.; Thompson, T.; Rheinemann, L.; Sundquist, W.

Citation: Rheinemann, Lara; Thompson, Tuscan; Mercenne, Gaelle; Paine, Elliott; Peterson, Francis; Volkman, Brian; Alam, Steven; Alian, Akram; Sundquist, Wesley. "Interactions between AMOT PPxY motifs and NEDD4L WW domains function in HIV-1 release" J. Biol. Chem. 297, 100975-100975 (2021).

Assembly members:
entity_1, polymer, 68 residues, 7756.744 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
entity_1: MQNNEELPTYEEAKVGGGGG SKVTQSFLPPGWEMRIAPNG RPFFIDHNTKTTTWEDPRLK FPVHMRSK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	276
15N chemical shifts	66
1H chemical shifts	444

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 68 residues - 7756.744 Da.

1

MET

GLN

ASN

GLU

LEU

PRO

THR

TYR

2

GLU

ALA

LYS

VAL

GLY

3

SER

LYS

VAL

THR

GLN

SER

PHE

LEU

PRO

4

GLY

TRP

GLU

MET

ARG

ILE

ALA

PRO

ASN

GLY

5

ARG

PRO

PHE

ILE

ASP

HIS

ASN

THR

LYS

6

THR

TRP

GLU

ASP

PRO

ARG

LEU

LYS

7

PHE

PRO

VAL

HIS

MET

ARG

SER

LYS

Samples:

sample_1: Angiomotin,E3 ubiquitin-protein ligase NEDD4-like fusion, [U-100% 13C; U-100% 15N], mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_2: Angiomotin,E3 ubiquitin-protein ligase NEDD4-like fusion, [U-100% 15N], mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

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

Felix v2007, Accelrys Software Inc. - data analysis

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 900 MHz
Varian INOVA 800 MHz

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