BMRB Entry 18012
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18012
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Title: Solution structure of N-terminal domain of human TIG3 PubMed: 22290676
Deposition date: 2011-10-21 Original release date: 2012-02-10
Authors: Wang, Lei; Yu, Wenyu; Xia, Bin
Citation: Wang, Lei; Yu, Wenyu; Ren, Xiaobai; Lin, Jian; Jin, Changwen; Xia, Bin. "1H, 13C, and 15N resonance assignments of the N-terminal domain of human TIG3." Biomol. NMR Assignments 6, 201-203 (2012).
Assembly members:
entity, polymer, 125 residues, 14050.996 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MASPHQEPKPGDLIEIFRLG
YEHWALYIGDGYVIHLAPPS
EYPGAGSSSVFSVLSNSAEV
KRERLEDVVGGCCYRVNNSL
DHEYQPRPVEVIISSAKEMV
GQKMKYSIVSRNCEHFVTQL
RYGKS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 452 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 729 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | N-terminal domain of human TIG3 | 1 |
Entities:
Entity 1, N-terminal domain of human TIG3 125 residues - 14050.996 Da.
This is the N-terminal domain of human tumor suppressor protein
| 1 | MET | ALA | SER | PRO | HIS | GLN | GLU | PRO | LYS | PRO | ||||
| 2 | GLY | ASP | LEU | ILE | GLU | ILE | PHE | ARG | LEU | GLY | ||||
| 3 | TYR | GLU | HIS | TRP | ALA | LEU | TYR | ILE | GLY | ASP | ||||
| 4 | GLY | TYR | VAL | ILE | HIS | LEU | ALA | PRO | PRO | SER | ||||
| 5 | GLU | TYR | PRO | GLY | ALA | GLY | SER | SER | SER | VAL | ||||
| 6 | PHE | SER | VAL | LEU | SER | ASN | SER | ALA | GLU | VAL | ||||
| 7 | LYS | ARG | GLU | ARG | LEU | GLU | ASP | VAL | VAL | GLY | ||||
| 8 | GLY | CYS | CYS | TYR | ARG | VAL | ASN | ASN | SER | LEU | ||||
| 9 | ASP | HIS | GLU | TYR | GLN | PRO | ARG | PRO | VAL | GLU | ||||
| 10 | VAL | ILE | ILE | SER | SER | ALA | LYS | GLU | MET | VAL | ||||
| 11 | GLY | GLN | LYS | MET | LYS | TYR | SER | ILE | VAL | SER | ||||
| 12 | ARG | ASN | CYS | GLU | HIS | PHE | VAL | THR | GLN | LEU | ||||
| 13 | ARG | TYR | GLY | LYS | SER |
Samples:
sample_1: TIG3N protein, [U-13C; U-15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 20 mM; urea 2 M; H2O 95%; D2O, [U-2H], 5%; DSS 0.01%
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER v9.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
DYANA v3.0, Guntert, Braun and Wuthrich - structure solution
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.0, Johnson, One Moon Scientific - peak picking
ProcheckNMR, Laskowski and MacArthur - geometry optimization
SANE, Duggan, Legge, Dyson & Wright - chemical shift assignment
TOPSPIN v3.0, Bruker Biospin - collection
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 25448 2545 |
| PDB | |
| DBJ | BAB08109 BAG35046 BAG56873 BAH22446 |
| GB | AAC84000 AAF02294 AAH09678 ABM82370 ABM85548 |
| REF | NP_004576 XP_003828577 XP_004051454 XP_508513 |
| SP | Q9UL19 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts