BMRB Entry 26943

Name: mini monomeric TGF-b2
Published: 2017-04-26

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26943

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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:

mini monomeric TGF-b2

Deposition date:

2016-11-15

Original release date:

2017-04-26

Authors:

Hinck, Andrew

Citation:

Citation: Kim, Sun-Kyung; Myers, Lindsey; Hinck, Cynthia; Can, Kristin; Thirangala, Avi; Iskra, Brian; Brothers, Molly; Vonberg, Machell; Leal, Belinda; Richter, Blair; Kodak, Ravindra; Taylor, Alex; Du, Shoucheng; Barnes, Christopher; Calero, Guillermo; Hart, Peter; Hart, Matthew; Demeler, Borries; Hinck, Andrew. "An engineered TGF-beta monomer that functions as a dominant negative to block TGF-beta signaling" J. Biol. Chem. 292, 7173-7188 (2017).
PubMed: 28228478

Assembly members:

Assembly members:
mmTGF-b2, polymer, 93 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: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mmTGF-b2: MALDAAYCFRNVQDNCCLRP LYIDFKRDCGWKWIHEPKGY NANFCAGACPYRNSKSPSCV SQDLEPLTILYYIGKTPKIE QLSNMIVKSCKCS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	272
15N chemical shifts	86
1H chemical shifts	86

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mmTGF-b2	1

Entities:

Entity 1, mmTGF-b2 93 residues - Formula weight is not available

1

MET

ALA

LEU

ASP

ALA

TYR

CYS

PHE

ARG

2

ASN

VAL

GLN

ASP

ASN

CYS

LEU

ARG

PRO

3

LEU

TYR

ILE

ASP

PHE

LYS

ARG

ASP

CYS

GLY

4

TRP

LYS

TRP

ILE

HIS

GLU

PRO

LYS

GLY

TYR

5

ASN

ALA

ASN

PHE

CYS

ALA

GLY

ALA

CYS

PRO

6

TYR

ARG

ASN

SER

LYS

SER

PRO

SER

CYS

VAL

7

SER

GLN

ASP

LEU

GLU

PRO

LEU

THR

ILE

LEU

8

TYR

ILE

GLY

LYS

THR

PRO

LYS

ILE

GLU

9

GLN

LEU

SER

ASN

MET

ILE

VAL

LYS

SER

CYS

10

LYS

CYS

SER

Samples:

sample_1: mmTGF-b2, [U-99% 13C; U-99% 15N], 0.2 ± 0.02 mM; D2O, [U-99% 2H], 5 ± 0.2 %; H2O 95 ± 2 %; dibasic sodium phosphate 10 ± 1 mM; CHAPS 10 ± 1 mM

sample_conditions_1: ionic strength: 0.06 M; pH: 4.7; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY vNMRFAM-SPARKY, Goddard - chemical shift assignment

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 800 MHz

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