BMRB Entry 11290
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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/BMR11290
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Title: Solution structure of the fibronectin type-III domain of human fibronectin type III domain containing protein 3
Deposition date: 2010-08-09 Original release date: 2011-08-18
Authors: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the fibronectin type-III domain of human fibronectin type III domain containing protein 3" . ., .-..
Assembly members:
Fibronectin type-III domain, polymer, 109 residues, Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
Fibronectin type-III domain: GSSGSSGPSMPASPVLTKAG
ITWLSLQWSKPSGTPSDEGI
SYILEMEEETSGYGFKPKYD
GEDLAYTVKNLRRSTKYKFK
VIAYNSEGKSNPSEVVEFTT
CPDSGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 437 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 668 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Fibronectin type-III domain | 1 |
Entities:
Entity 1, Fibronectin type-III domain 109 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | PRO | SER | MET | ||||
| 2 | PRO | ALA | SER | PRO | VAL | LEU | THR | LYS | ALA | GLY | ||||
| 3 | ILE | THR | TRP | LEU | SER | LEU | GLN | TRP | SER | LYS | ||||
| 4 | PRO | SER | GLY | THR | PRO | SER | ASP | GLU | GLY | ILE | ||||
| 5 | SER | TYR | ILE | LEU | GLU | MET | GLU | GLU | GLU | THR | ||||
| 6 | SER | GLY | TYR | GLY | PHE | LYS | PRO | LYS | TYR | ASP | ||||
| 7 | GLY | GLU | ASP | LEU | ALA | TYR | THR | VAL | LYS | ASN | ||||
| 8 | LEU | ARG | ARG | SER | THR | LYS | TYR | LYS | PHE | LYS | ||||
| 9 | VAL | ILE | ALA | TYR | ASN | SER | GLU | GLY | LYS | SER | ||||
| 10 | ASN | PRO | SER | GLU | VAL | VAL | GLU | PHE | THR | THR | ||||
| 11 | CYS | PRO | ASP | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: fn3 domain, [U-13C; U-15N], 1.06 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 v20031121, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B. A. - data analysis
Kujira v0.9295, Kobayashi, N. - data analysis
CYANA v1.0.8, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB |
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