BMRB Entry 11286
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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/BMR11286
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Title: Solution structure of the BSD domain of human Synapse associated protein 1
Deposition date: 2010-08-09 Original release date: 2011-08-18
Authors: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the BSD domain of human Synapse associated protein 1" . ., .-..
Assembly members:
BSD domain, polymer, 100 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):
BSD domain: GSSGSSGTNDEETIQQQILA
LSADKRNFLRDPPAGVQFNF
DFDQMYPVALVMLQEDELLS
KMRFALVPKLVKEEVFWRNY
FYRVSLIKQSAQLTSGPSSG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 440 |
15N chemical shifts | 99 |
1H chemical shifts | 685 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | BSD domain | 1 |
Entities:
Entity 1, BSD domain 100 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | THR | ASN | ASP | |
2 | GLU | GLU | THR | ILE | GLN | GLN | GLN | ILE | LEU | ALA | |
3 | LEU | SER | ALA | ASP | LYS | ARG | ASN | PHE | LEU | ARG | |
4 | ASP | PRO | PRO | ALA | GLY | VAL | GLN | PHE | ASN | PHE | |
5 | ASP | PHE | ASP | GLN | MET | TYR | PRO | VAL | ALA | LEU | |
6 | VAL | MET | LEU | GLN | GLU | ASP | GLU | LEU | LEU | SER | |
7 | LYS | MET | ARG | PHE | ALA | LEU | VAL | PRO | LYS | LEU | |
8 | VAL | LYS | GLU | GLU | VAL | PHE | TRP | ARG | ASN | TYR | |
9 | PHE | TYR | ARG | VAL | SER | LEU | ILE | LYS | GLN | SER | |
10 | ALA | GLN | LEU | THR | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: BSD domain, [U-13C; U-15N], 1.03 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 15N-separated NOESY | sample_1 | isotropic | condition_1 |
3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20031121, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B. A. - data analysis
Kujira v0.921, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
PDB | |
DBJ | BAB55087 BAD96576 BAG37229 BAG58299 BAG64741 |
EMBL | CAH18697 CAH90135 |
GB | AAH14657 AAK69273 AAK81893 ACE87132 AIC57513 |
REF | NP_001125031 NP_116185 XP_001097183 XP_002762707 XP_003819572 |
SP | Q96A49 |
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