BMRB Entry 5933
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5933
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Title: Sequence-specific backbone and sidechain resonance assignments of the Ste50 binding domain of the MAPKKK Ste11 PubMed: 15544813
Deposition date: 2003-09-05 Original release date: 2005-03-01
Authors: Bhattacharjya, Surajit; Xu, Ping; Shaykhutdinov, Rustem; Gingras, Richard; Ni, Feng
Citation: Bhattacharjya, Surajit; Xu, Ping; Gingras, R.; Shaykhutdinov, R.; Wu, C.; Whiteway, M.; Ni, Feng. "Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex" J. Mol. Biol. 344, 1071-1087 (2004).
Assembly members:
SAM domain of Ste11, polymer, 68 residues, Formula weight is not available
Natural source: Common Name: Budding yeast Taxonomy ID: 4932 Superkingdom: Eucaryote Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SAM domain of Ste11: DEKTNDLPFVQLFLEEIGCT
QYLDSFIQCNLVTEEEIKYL
DKDILIALGVNKIGDRLKIL
RKSKSFQR
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 474 |
| 13C chemical shifts | 299 |
| 15N chemical shifts | 72 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ste11 SAM, chain 1 | 1 |
| 2 | Ste11 SAM, chain 2 | 1 |
Entities:
Entity 1, Ste11 SAM, chain 1 68 residues - Formula weight is not available
| 1 | ASP | GLU | LYS | THR | ASN | ASP | LEU | PRO | PHE | VAL | ||||
| 2 | GLN | LEU | PHE | LEU | GLU | GLU | ILE | GLY | CYS | THR | ||||
| 3 | GLN | TYR | LEU | ASP | SER | PHE | ILE | GLN | CYS | ASN | ||||
| 4 | LEU | VAL | THR | GLU | GLU | GLU | ILE | LYS | TYR | LEU | ||||
| 5 | ASP | LYS | ASP | ILE | LEU | ILE | ALA | LEU | GLY | VAL | ||||
| 6 | ASN | LYS | ILE | GLY | ASP | ARG | LEU | LYS | ILE | LEU | ||||
| 7 | ARG | LYS | SER | LYS | SER | PHE | GLN | ARG |
Samples:
sample_1: SAM domain of Ste11, [U-15N], 0.8 mM; K-phosphate buffer 10 mM; NaCl 300 mM
sample_2: SAM domain of Ste11, [U-15N; U-13C], 0.8 mM; K-phosphate buffer 10 mM; NaCl 300 mM
sample_conditions_set_1: pH: 5.8; temperature: 288 K; ionic strength: 0.01 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D (1H-15N) HSQC | not available | not available | not available |
| 2D (1H-1H) NOESY | not available | not available | not available |
| 3D (1H-15N) NOESY-HSQC | not available | not available | not available |
| 3D (1H-15N) TOCSY-HSQC | not available | not available | not available |
| 3D HNCA | not available | not available | not available |
| 3D HN(CO)CA | not available | not available | not available |
| 3D CBCA(CO)NH | not available | not available | not available |
| 3D HNCO | not available | not available | not available |
| 3D HBHA(C0)NH | not available | not available | not available |
| 3D (H)CCH-COSY | not available | not available | not available |
| 3D (1H-13C) NOESY-HSQC | not available | not available | not available |
Software:
NMR-PIPE - FID transformations
NMR-View - spectral analysis
NMR spectrometers:
- Bruker DRX 800 MHz
Related Database Links:
| PDB | |
| DBJ | GAA25223 |
| EMBL | CAA37522 CAY81586 |
| GB | AAB67571 AHY78717 EDN59268 EDZ70440 EEU06456 |
| REF | NP_013466 |
| SP | A7A1P0 B5VNQ3 P23561 |
| TPG | DAA09666 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts