BMRB Entry 11265
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11265
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Title: Solution Structure of the N-terminal Ras-binding Domain (RBD) in Human a-Raf Kinase
Deposition date: 2010-08-09 Original release date: 2011-08-18
Authors: Zhao, C.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation: Zhao, C.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the N-terminal Ras-binding Domain (RBD) in Human a-Raf Kinase" . ., .-..
Assembly members:
Ras-binding domain, polymer, 86 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):
Ras-binding domain: GSSGSSGGTVKVYLPNKQRT
VVTVRDGMSVYDSLDKALKV
RGLNQDCCVVYRLIKGRKTV
TAWDTAIAPLDGEELIVEVL
SGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 338 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 556 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ras-binding domain | 1 |
Entities:
Entity 1, Ras-binding domain 86 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | GLY | THR | VAL | ||||
| 2 | LYS | VAL | TYR | LEU | PRO | ASN | LYS | GLN | ARG | THR | ||||
| 3 | VAL | VAL | THR | VAL | ARG | ASP | GLY | MET | SER | VAL | ||||
| 4 | TYR | ASP | SER | LEU | ASP | LYS | ALA | LEU | LYS | VAL | ||||
| 5 | ARG | GLY | LEU | ASN | GLN | ASP | CYS | CYS | VAL | VAL | ||||
| 6 | TYR | ARG | LEU | ILE | LYS | GLY | ARG | LYS | THR | VAL | ||||
| 7 | THR | ALA | TRP | ASP | THR | ALA | ILE | ALA | PRO | LEU | ||||
| 8 | ASP | GLY | GLU | GLU | LEU | ILE | VAL | GLU | VAL | LEU | ||||
| 9 | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: Ras-binding domain, [U-13C; U-15N], 0.86 mM; d-Tris-HCl 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 296.0 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 v20020425, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B. A. - data analysis
Kujira v0.921, Kobayashi, N. - data analysis
CYANA v1.0.8, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA22379 BAB23522 BAB26674 BAB32131 BAC30217 |
| EMBL | CAA28476 CAA30023 |
| GB | AAA65219 AAB03517 AAB27592 AAH02466 AAH04757 |
| REF | NP_001014964 NP_001028835 NP_001153117 NP_001159362 NP_001243125 |
| SP | O19004 P04627 P10398 P14056 |
| TPG | DAA12857 |
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