BMRB Entry 11127

Title:
Solution structure of the 2nd fibronectin type III domain from mouse biregional cell adhesion molecule-related/down-regulated oncogenes (Cdon) binding protein
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 2nd fibronectin type III domain from mouse biregional cell adhesion molecule-related/down-regulated oncogenes (Cdon) binding protein"  .

Assembly members:

Assembly members:
fibronectin type III (fn3) domain, polymer, 121 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryotase   Kingdom: Metazoaouse   Genus/species: Mus musculususe

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P040719-11

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts107
1H chemical shifts787

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 121 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYSERGLNPRO
2   ASPHISGLYARGLEUSERPROPROGLUALA
3   PROASPARGPROTHRILESERTHRALASER
4   GLUTHRSERVALTYRVALTHRTRPILEPRO
5   ARGGLYASNGLYGLYPHEPROILEGLNSER
6   PHEARGVALGLUTYRLYSLYSLEULYSLYS
7   VALGLYASPTRPILELEUALATHRSERALA
8   ILEPROPROSERARGLEUSERVALGLUILE
9   THRGLYLEUGLULYSGLYILESERTYRLYS
10   PHEARGVALARGALALEUASNMETLEUGLY
11   GLUSERGLUPROSERALAPROSERARGPRO
12   TYRVALVALSERGLYSERGLYPROSERSER
13   GLY

Samples:

sample_1: fn3 domain, [U-13C; U-15N], 1.43 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 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