BMRB Entry 18971

Name: Structure and dynamics of a human Nedd4 WW domain-ENaC complex
Published: 2013-06-04

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PDB ID: 2m3o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18971
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Structure and dynamics of a human Nedd4 WW domain-ENaC complex

Deposition date:

2013-01-23

Original release date:

2013-06-04

Authors:

Bobby, Romel; Medini, Karima; Neudecker, Philipp; Lee, Verne; MacDonald, Fiona; Brimble, Margaret; Lott, J. Shaun; Dingley, Andrew

Citation:

Citation: Bobby, Romel; Medini, Karima; Neudecker, Philipp; Lee, Tet Verne; Brimble, Margaret; McDonald, Fiona; Lott, J. Shaun; Dingley, Andrew. "Structure and dynamics of human Nedd4-1 WW3 in complex with the ENaC PY motif." Biochim. Biophys. Acta 1834, 1632-1641 (2013).
PubMed: 23665454

Assembly members:

Assembly members:
Nedd4_WW3*_domain, polymer, 43 residues, 4971.661 Da.
alpha_ENaC_PY_peptide, polymer, 11 residues, 1058.196 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET42

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nedd4_WW3*_domain: GSMEQGFLPKGWEVRHAPNG RPFFIDHNTKTTTWEDPRLK IPA
alpha_ENaC_PY_peptide: TAPPPAYATLG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2
heteronucl_NOEs
heteronucl_T1_relaxation
heteronucl_T2_relaxation
order_parameters
- order_parameter_list_1

Data type	Count
13C chemical shifts	219
15N chemical shifts	60
1H chemical shifts	361
heteronuclear NOE values	102
order parameters	34
T1 relaxation values	102
T2 relaxation values	102

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Nedd4_WW3*_domain	1
2	alpha_ENaC_PY_peptide	2

Entities:

Entity 1, Nedd4_WW3*_domain 43 residues - 4971.661 Da.

Residues G416-E419 in NMR structure represent non-native residues from the expression vector

1

GLY

SER

MET

GLU

GLN

GLY

PHE

LEU

PRO

LYS

2

GLY

TRP

GLU

VAL

ARG

HIS

ALA

PRO

ASN

GLY

3

ARG

PRO

PHE

ILE

ASP

HIS

ASN

THR

LYS

4

THR

TRP

GLU

ASP

PRO

ARG

LEU

LYS

5

ILE

PRO

ALA

Entity 2, alpha_ENaC_PY_peptide 11 residues - 1058.196 Da.

1

THR

ALA

PRO

ALA

TYR

ALA

THR

LEU

2

GLY

Samples:

sample_1: Nedd4 WW3* domain, [U-99% 13C; U-99% 15N], 1.1 mM; alpha ENaC PY peptide 2.2 mM; sodium phosphate 20 mM; sodium azide 0.1%; TSP 1 mM; H2O 93%; D2O 7%

sample_2: Nedd4 WW3* domain 3.0 mM; alpha ENaC PY peptide, [U-99% 13C; U-99% 15N], 1.5 mM; sodium phosphate 20 mM; sodium azide 0.1%; TSP 1.0 mM; H2O 93%; D2O 7%

sample_3: Nedd4 WW3* domain, [U-99% 15N], 1.61 mM; alpha ENaC PY peptide 4.38 mM; sodium phosphate 20 mM; sodium azide 0.1%; TSP 1 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
2D C(CO)NH	sample_2	isotropic	sample_conditions_1
2D HNCO	sample_2	isotropic	sample_conditions_1
2D HNCACB	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 15N/13C-EDITED NOESY	sample_2	isotropic	sample_conditions_1
2D 13C-edited/filtered NOESY	sample_2	isotropic	sample_conditions_1
2D long-range HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N R2 relaxation	sample_3	isotropic	sample_conditions_1
2D 1H-15N R1 relaxation	sample_3	isotropic	sample_conditions_1
2D 1H-15N heteronuclear NOE	sample_3	isotropic	sample_conditions_1
2D 1H-15N R1rho relaxation	sample_3	isotropic	sample_conditions_1
2D 1H-15N R1 relaxation	sample_3	isotropic	sample_conditions_1
2D 1H-15N heteronuclear NOE	sample_3	isotropic	sample_conditions_1
2D 1H-15N R1rho relaxation	sample_3	isotropic	sample_conditions_1
2D 1H-15N R1 relaxation	sample_3	isotropic	sample_conditions_1
2D 1H-15N heteronuclear NOE	sample_3	isotropic	sample_conditions_1
3D HCAN	sample_1	isotropic	sample_conditions_1
2D HCAN	sample_2	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
2D HBCBCACONHAN	sample_2	isotropic	sample_conditions_1
2D HBCBCACONHACA	sample_2	isotropic	sample_conditions_1
2D 15N CPMG dispersion	sample_3	isotropic	sample_conditions_1
2D 15N CPMG dispersion	sample_3	isotropic	sample_conditions_1

NCBI	4734
BMRB	16574 16575
PDB	2KPZ 2KQ0 2M3O 4N7F
REF	XP_010008470 XP_011758823 XP_012325247
UNP	P37088
AlphaFold	Q9UM64

BMRB Entry 18971

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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