BMRB Entry 19438
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19438
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Title: tgam
Deposition date: 2013-08-19 Original release date: 2014-09-02
Authors: Yang, Yinshan; Montet de Guillen, Karine; Roumestand, Christian
Citation: Yang, Yinshan; Montet de Guillen, Karine; Roumestand, Christian. "NMR structure of Tgam" Not known ., .-..
Assembly members:
Tgam, polymer, 148 residues, 16758.439 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):
Tgam: MKYDVVIIPESFHRFDKHNM
EHICPPMVIGDRSYDIAMEI
VNGVDRVIKASFNASVEELE
GEDCDVLYRKYTLEKEGKKG
IVHVKLRKITENCPPVDGNR
CSVLEFERDIECIVKAIEEC
LAKGELNSKLEGKPIPNPLL
GLDSTRTG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 417 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 295 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Tgam | 1 |
Entities:
Entity 1, Tgam 148 residues - 16758.439 Da.
| 1 | MET | LYS | TYR | ASP | VAL | VAL | ILE | ILE | PRO | GLU | ||||
| 2 | SER | PHE | HIS | ARG | PHE | ASP | LYS | HIS | ASN | MET | ||||
| 3 | GLU | HIS | ILE | CYS | PRO | PRO | MET | VAL | ILE | GLY | ||||
| 4 | ASP | ARG | SER | TYR | ASP | ILE | ALA | MET | GLU | ILE | ||||
| 5 | VAL | ASN | GLY | VAL | ASP | ARG | VAL | ILE | LYS | ALA | ||||
| 6 | SER | PHE | ASN | ALA | SER | VAL | GLU | GLU | LEU | GLU | ||||
| 7 | GLY | GLU | ASP | CYS | ASP | VAL | LEU | TYR | ARG | LYS | ||||
| 8 | TYR | THR | LEU | GLU | LYS | GLU | GLY | LYS | LYS | GLY | ||||
| 9 | ILE | VAL | HIS | VAL | LYS | LEU | ARG | LYS | ILE | THR | ||||
| 10 | GLU | ASN | CYS | PRO | PRO | VAL | ASP | GLY | ASN | ARG | ||||
| 11 | CYS | SER | VAL | LEU | GLU | PHE | GLU | ARG | ASP | ILE | ||||
| 12 | GLU | CYS | ILE | VAL | LYS | ALA | ILE | GLU | GLU | CYS | ||||
| 13 | LEU | ALA | LYS | GLY | GLU | LEU | ASN | SER | LYS | LEU | ||||
| 14 | GLU | GLY | LYS | PRO | ILE | PRO | ASN | PRO | LEU | LEU | ||||
| 15 | GLY | LEU | ASP | SER | THR | ARG | THR | GLY |
Samples:
sample_1: H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.60; pressure: 1 atm; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts