BMRB Entry 17542

Name: Structure of the first domain of human Smurf1 in complex with a doubly phosphorylated human Smad1 derived peptide.
Published: 2011-06-23

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PDB ID: 2lb0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17542
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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 the first domain of human Smurf1 in complex with a doubly phosphorylated human Smad1 derived peptide.

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:

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).
PubMed: 21685363

Assembly members:

Assembly members:
human Smurf1, polymer, 36 residues, 3878.262 Da.
doubly phosphorylated human Smad1 derived peptide, polymer, 10 residues, 1181.993 Da.

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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human Smurf1: GAMELPEGYEQRTTVQGQVY FLHTQTGVSTWHDPRI
doubly phosphorylated human Smad1 derived peptide: TSXDPGXPFQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	49
15N chemical shifts	19
1H chemical shifts	227

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	human Smurf1	1
2	doubly phosphorylated human Smad1 derived peptide	2

Entities:

Entity 1, human Smurf1 36 residues - 3878.262 Da.

1

GLY

ALA

MET

GLU

LEU

PRO

GLU

GLY

TYR

GLU

2

GLN

ARG

THR

VAL

GLN

GLY

GLN

VAL

TYR

3

PHE

LEU

HIS

THR

GLN

THR

GLY

VAL

SER

THR

4

TRP

HIS

ASP

PRO

ARG

ILE

Entity 2, doubly phosphorylated human Smad1 derived peptide 10 residues - 1181.993 Da.

1

THR

SER

SEP

ASP

PRO

GLY

SEP

PRO

PHE

GLN

Samples:

H: Smurf1 1 mM; Smad1 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N: Smurf1, [U-100% 15N], 1 mM; Smad1 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N13C: Smurf1, [U-100% 13C; U-100% 15N], 1 mM; Smad1 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

BMRB	17541
PDB	2LAZ 2LB0
DBJ	BAB13451 BAB29770 BAE32623 BAG11347
GB	AAC62434 AAF08298 AAH29097 AAH59201 AAI36805
REF	NP_001001943 NP_001033716 NP_001103068 NP_001186776 NP_001244560
SP	Q9CUN6 Q9HCE7
TPG	DAA15146
AlphaFold	Q9CUN6 Q9HCE7 Q9UFT8