BMRB Entry 11311

Title:
Solution structure of the FAS1 domain of human transforming growth factor-beta induced protein IG-H3
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Yoneyama, M.; Tomizawa, T.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tomizawa, T.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the FAS1 domain of human transforming growth factor-beta induced protein IG-H3"  .

Assembly members:

Assembly members:
FAS1 domain, polymer, 146 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: cell free synthesis   Host organism: E. coli - cell free   Vector: P040524-06

Data sets:
Data typeCount
13C chemical shifts608
15N chemical shifts142
1H chemical shifts988

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FAS1 domain1

Entities:

Entity 1, FAS1 domain 146 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETGLYTHR
2   VALMETASPVALLEULYSGLYASPASNARG
3   PHESERMETLEUVALALAALAILEGLNSER
4   ALAGLYLEUTHRGLUTHRLEUASNARGGLU
5   GLYVALTYRTHRVALPHEALAPROTHRASN
6   GLUALAPHEARGALALEUPROPROARGGLU
7   ARGSERARGLEULEUGLYASPALALYSGLU
8   LEUALAASNILELEULYSTYRHISILEGLY
9   ASPGLUILELEUVALSERGLYGLYILEGLY
10   ALALEUVALARGLEULYSSERLEUGLNGLY
11   ASPLYSLEUGLUVALSERLEULYSASNASN
12   VALVALSERVALASNLYSGLUPROVALALA
13   GLUPROASPILEMETALATHRASNGLYVAL
14   VALHISVALILETHRASNVALLEUGLNPRO
15   SERGLYPROSERSERGLY

Samples:

sample_1: FAS1 domain, [U-13C; U-15N], 0.39 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.921, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 18466 18467 25425
PDB
GB AAC24944

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