BMRB Entry 50738

Name: Smad2 interdomain linker
Published: 2021-09-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50738

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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:

Smad2 interdomain linker

Deposition date:

2021-01-27

Original release date:

2021-09-14

Authors:

Gomes, Tiago

Citation:

Citation: Gomes, Tiago; Martin-Malpartida, Pau; Ruiz, Lidia; Aragona, Eric; Cordeiro, Tiago; Macias, Maria. "Conformational landscape of multidomain SMAD proteins" Comp. Struc. Biotech. J. 19, 5210-5224 (2021).
PubMed: 34630939

Assembly members:

Assembly members:
entity_1, polymer, 107 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: PETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAHHHHHHSSGLEVLFQGPL PPVLVPRHTEILTELPPLDD YTHSIPENTNFPAGIEPQSN YIPETPPPGYISEDGETSDQ QLNQSMDTGSPAELSPTTLS PVNHSLD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	144
15N chemical shifts	65
1H chemical shifts	65

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Smad2linker	1

Entities:

Entity 1, Smad2linker 107 residues - Formula weight is not available

1

MET

ALA

HIS

SER

2

GLY

LEU

GLU

VAL

LEU

PHE

GLN

GLY

PRO

LEU

3

PRO

VAL

LEU

VAL

PRO

ARG

HIS

THR

GLU

4

ILE

LEU

THR

GLU

LEU

PRO

LEU

ASP

5

TYR

THR

HIS

SER

ILE

PRO

GLU

ASN

THR

ASN

6

PHE

PRO

ALA

GLY

ILE

GLU

PRO

GLN

SER

ASN

7

TYR

ILE

PRO

GLU

THR

PRO

GLY

TYR

8

ILE

SER

GLU

ASP

GLY

GLU

THR

SER

ASP

GLN

9

GLN

LEU

ASN

GLN

SER

MET

ASP

THR

GLY

SER

10

PRO

ALA

GLU

LEU

SER

PRO

THR

LEU

SER

11

PRO

VAL

ASN

HIS

SER

LEU

ASP

Samples:

sample_1: s4linker, [U-100% 13C; U-100% 15N], 400 uM

sample_conditions_1: ionic strength: 0.15 M; pH: 7; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
HNCACONH	sample_1	isotropic	sample_conditions_1
HNCANH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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