BMRB Entry 26943

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

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts86
1H chemical shifts86

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1mmTGF-b21

Entities:

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

1   METALALEUASPALAALATYRCYSPHEARG
2   ASNVALGLNASPASNCYSCYSLEUARGPRO
3   LEUTYRILEASPPHELYSARGASPCYSGLY
4   TRPLYSTRPILEHISGLUPROLYSGLYTYR
5   ASNALAASNPHECYSALAGLYALACYSPRO
6   TYRARGASNSERLYSSERPROSERCYSVAL
7   SERGLNASPLEUGLUPROLEUTHRILELEU
8   TYRTYRILEGLYLYSTHRPROLYSILEGLU
9   GLNLEUSERASNMETILEVALLYSSERCYS
10   LYSCYSSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_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