BMRB Entry 11127
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11127
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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: 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:
fibronectin type III (fn3) domain, polymer, 121 residues, Formula weight is not available
Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryotase Kingdom: Metazoaouse Genus/species: Mus musculususe
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: P040719-11
Entity Sequences (FASTA):
fibronectin type III (fn3) domain: GSSGSSGSQPDHGRLSPPEA
PDRPTISTASETSVYVTWIP
RGNGGFPIQSFRVEYKKLKK
VGDWILATSAIPPSRLSVEI
TGLEKGISYKFRVRALNMLG
ESEPSAPSRPYVVSGSGPSS
G
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 506 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 787 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | fibronectin type III (fn3) domain | 1 |
Entities:
Entity 1, fibronectin type III (fn3) domain 121 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | SER | GLN | PRO | ||||
| 2 | ASP | HIS | GLY | ARG | LEU | SER | PRO | PRO | GLU | ALA | ||||
| 3 | PRO | ASP | ARG | PRO | THR | ILE | SER | THR | ALA | SER | ||||
| 4 | GLU | THR | SER | VAL | TYR | VAL | THR | TRP | ILE | PRO | ||||
| 5 | ARG | GLY | ASN | GLY | GLY | PHE | PRO | ILE | GLN | SER | ||||
| 6 | PHE | ARG | VAL | GLU | TYR | LYS | LYS | LEU | LYS | LYS | ||||
| 7 | VAL | GLY | ASP | TRP | ILE | LEU | ALA | THR | SER | ALA | ||||
| 8 | ILE | PRO | PRO | SER | ARG | LEU | SER | VAL | GLU | ILE | ||||
| 9 | THR | GLY | LEU | GLU | LYS | GLY | ILE | SER | TYR | LYS | ||||
| 10 | PHE | ARG | VAL | ARG | ALA | LEU | ASN | MET | LEU | GLY | ||||
| 11 | GLU | SER | GLU | PRO | SER | ALA | PRO | SER | ARG | PRO | ||||
| 12 | TYR | VAL | VAL | SER | GLY | SER | GLY | PRO | SER | SER | ||||
| 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_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 |
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