BMRB Entry 17544

Name: Structure of the second domain of human Nedd4L in complex with a doubly phosphorylated human Smad3 derived peptide.
Published: 2011-06-23

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PDB ID: 2lb2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17544
MolProbity Validation Chart

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

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Title: Structure of the second domain of human Nedd4L in complex with a doubly phosphorylated human Smad3 derived peptide. PubMed: 21685363

Deposition date: 2011-03-22 Original release date: 2011-06-23

Authors: Macias, Maria; Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan

Citation: Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan; Macias, Maria. "A Smad action turnover switch operated by WW domain readers of a phosphoserine code." Genes Dev. 25, 1275-1288 (2011).

Assembly members:
second domain of human Nedd4L, polymer, 35 residues, 4184.715 Da.
doubly phosphorylated human Smad3, polymer, 12 residues, 1341.284 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

Entity Sequences (FASTA):
second domain of human Nedd4L: GLPSGWEERKDAKGRTYYVN HNNRTTTWTRPIMQL
doubly phosphorylated human Smad3: EXPPPGYLSEDG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	98
15N chemical shifts	33
1H chemical shifts	313

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Nedd4L	1
2	Smad3	2

Entities:

Entity 1, Nedd4L 35 residues - 4184.715 Da.

1

GLY

LEU

PRO

SER

GLY

TRP

GLU

ARG

LYS

2

ASP

ALA

LYS

GLY

ARG

THR

TYR

VAL

ASN

3

HIS

ASN

ARG

THR

TRP

THR

ARG

4

PRO

ILE

MET

GLN

LEU

Entity 2, Smad3 12 residues - 1341.284 Da.

1

GLU

TPO

PRO

GLY

TYR

LEU

SER

GLU

2

ASP

GLY

Samples:

H: Nedd4L 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N: Nedd4L, [U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N13C: Nedd4L, [U-100% 13C; U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.420 M; pH: 7; pressure: 1 atm; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	H	isotropic	sample_conditions_1
2D 1H-1H TOCSY	H	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N13C	isotropic	sample_conditions_1
3D HNCACB	15N13C	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N	isotropic	sample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

XEASY, Bartels et al. - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker DRX 600 MHz

Biological Magnetic Resonance Data Bank