BMRB Entry 10316
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10316
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Title: Solution structure of the PH domain of TBC1 domain family member 2 protein from human
Deposition date: 2009-03-11 Original release date: 2010-03-11
Authors: Li, H.; Tochio, N.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.
Citation: Li, H.; Tochio, N.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of TBC1 domain family member 2 protein from human" . ., .-..
Assembly members:
PH domain, polymer, 119 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
Entity Sequences (FASTA):
PH domain: GSSGSSGKKLCGYLSKFGGK
GPIRGWKSRWFFYDERKCQL
YYSRTAQDANPLDSIDLSSA
VFDCKADAEEGIFEIKTPSR
VITLKAATKQAMLYWLQQLQ
MKRWEFHNSPPAPSGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 508 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 769 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PH domain | 1 |
Entities:
Entity 1, PH domain 119 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | LYS | LYS | LEU | ||||
| 2 | CYS | GLY | TYR | LEU | SER | LYS | PHE | GLY | GLY | LYS | ||||
| 3 | GLY | PRO | ILE | ARG | GLY | TRP | LYS | SER | ARG | TRP | ||||
| 4 | PHE | PHE | TYR | ASP | GLU | ARG | LYS | CYS | GLN | LEU | ||||
| 5 | TYR | TYR | SER | ARG | THR | ALA | GLN | ASP | ALA | ASN | ||||
| 6 | PRO | LEU | ASP | SER | ILE | ASP | LEU | SER | SER | ALA | ||||
| 7 | VAL | PHE | ASP | CYS | LYS | ALA | ASP | ALA | GLU | GLU | ||||
| 8 | GLY | ILE | PHE | GLU | ILE | LYS | THR | PRO | SER | ARG | ||||
| 9 | VAL | ILE | THR | LEU | LYS | ALA | ALA | THR | LYS | GLN | ||||
| 10 | ALA | MET | LEU | TYR | TRP | LEU | GLN | GLN | LEU | GLN | ||||
| 11 | MET | LYS | ARG | TRP | GLU | PHE | HIS | ASN | SER | PRO | ||||
| 12 | PRO | ALA | PRO | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: PH domain, [U-13C; U-15N], 1.31 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 13C-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v3.5, Bruker - collection
NMRPipe v20030801, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.932, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAD92958 BAG54761 BAH16625 |
| EMBL | CAH92074 |
| GB | AAK07684 AAL55877 EAW58882 EAW58883 EAW58884 |
| REF | NP_001254500 NP_060891 XP_001158356 XP_003260594 XP_003260595 |
| SP | Q9BYX2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
or all simulated shifts