BMRB Entry 11311
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11311
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
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: 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:
FAS1 domain, polymer, 146 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):
FAS1 domain: GSSGSSGMGTVMDVLKGDNR
FSMLVAAIQSAGLTETLNRE
GVYTVFAPTNEAFRALPPRE
RSRLLGDAKELANILKYHIG
DEILVSGGIGALVRLKSLQG
DKLEVSLKNNVVSVNKEPVA
EPDIMATNGVVHVITNVLQP
SGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 608 |
| 15N chemical shifts | 142 |
| 1H chemical shifts | 988 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FAS1 domain | 1 |
Entities:
Entity 1, FAS1 domain 146 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | MET | GLY | THR | ||||
| 2 | VAL | MET | ASP | VAL | LEU | LYS | GLY | ASP | ASN | ARG | ||||
| 3 | PHE | SER | MET | LEU | VAL | ALA | ALA | ILE | GLN | SER | ||||
| 4 | ALA | GLY | LEU | THR | GLU | THR | LEU | ASN | ARG | GLU | ||||
| 5 | GLY | VAL | TYR | THR | VAL | PHE | ALA | PRO | THR | ASN | ||||
| 6 | GLU | ALA | PHE | ARG | ALA | LEU | PRO | PRO | ARG | GLU | ||||
| 7 | ARG | SER | ARG | LEU | LEU | GLY | ASP | ALA | LYS | GLU | ||||
| 8 | LEU | ALA | ASN | ILE | LEU | LYS | TYR | HIS | ILE | GLY | ||||
| 9 | ASP | GLU | ILE | LEU | VAL | SER | GLY | GLY | ILE | GLY | ||||
| 10 | ALA | LEU | VAL | ARG | LEU | LYS | SER | LEU | GLN | GLY | ||||
| 11 | ASP | LYS | LEU | GLU | VAL | SER | LEU | LYS | ASN | ASN | ||||
| 12 | VAL | VAL | SER | VAL | ASN | LYS | GLU | PRO | VAL | ALA | ||||
| 13 | GLU | PRO | ASP | ILE | MET | ALA | THR | ASN | GLY | VAL | ||||
| 14 | VAL | HIS | VAL | ILE | THR | ASN | VAL | LEU | GLN | PRO | ||||
| 15 | SER | GLY | PRO | SER | SER | GLY |
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:
| 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 v0.921, Kobayashi, N. - data analysis
CYANA v1.0.7, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts