BMRB Entry 11125

Title:
Solution structure of the 6th fibronectin type III domain from human fibronectin type III domain containing protein 3
Deposition date:
2010-03-31
Original release date:
2011-04-01
Authors:
Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation:

Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the 6th fibronectin type III domain from human fibronectin type III domain containing protein 3"  .

Assembly members:

Assembly members:
fibronectin type III (fn3) domain, polymer, 106 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: P040705-15

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts404
15N chemical shifts96
1H chemical shifts637

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1fibronectin type III (fn3) domain1

Entities:

Entity 1, fibronectin type III (fn3) domain 106 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROASPGLN
2   CYSLYSPROPROGLNVALTHRCYSARGSER
3   ALATHRCYSALAGLNVALASNTRPGLUVAL
4   PROLEUSERASNGLYTHRASPVALTHRGLU
5   TYRARGLEUGLUTRPGLYGLYVALGLUGLY
6   SERMETGLNILECYSTYRCYSGLYPROGLY
7   LEUSERTYRGLUILELYSGLYLEUSERPRO
8   ALATHRTHRTYRTYRCYSARGVALGLNALA
9   LEUSERVALVALGLYALAGLYPROPHESER
10   GLUVALVALALACYSVALTHRPROPROSER
11   SERGLYPROSERSERGLY

Samples:

sample_1: fn3 domain, [U-13C; U-15N], 0.66 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 220 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9295, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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