BMRB Entry 10264
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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/BMR10264
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Title: The solution structure of the VHS domain of human Signal transducing adaptor molecule 2
Deposition date: 2008-12-03 Original release date: 2010-03-11
Authors: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "The solution structure of the VHS domain of human Signal transducing adaptor molecule 2" .
Assembly members:
VHS domain, polymer, 163 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 Vector: P040607-06
Entity Sequences (FASTA):
VHS domain: GSSGSSGMPLFTANPFEQDV
EKATNEYNTTEDWSLIMDIC
DKVGSTPNGAKDCLKAIMKR
VNHKVPHVALQALTLLGACV
ANCGKIFHLEVCSRDFATEV
RAVIKNKAHPKVCEKLKSLM
VEWSEEFQKDPQFSLISATI
KSMKEEGITFPPAGSQTSGP
SSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 703 |
| 15N chemical shifts | 162 |
| 1H chemical shifts | 1054 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | VHS domain | 1 |
Entities:
Entity 1, VHS domain 163 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | MET | PRO | LEU | ||||
| 2 | PHE | THR | ALA | ASN | PRO | PHE | GLU | GLN | ASP | VAL | ||||
| 3 | GLU | LYS | ALA | THR | ASN | GLU | TYR | ASN | THR | THR | ||||
| 4 | GLU | ASP | TRP | SER | LEU | ILE | MET | ASP | ILE | CYS | ||||
| 5 | ASP | LYS | VAL | GLY | SER | THR | PRO | ASN | GLY | ALA | ||||
| 6 | LYS | ASP | CYS | LEU | LYS | ALA | ILE | MET | LYS | ARG | ||||
| 7 | VAL | ASN | HIS | LYS | VAL | PRO | HIS | VAL | ALA | LEU | ||||
| 8 | GLN | ALA | LEU | THR | LEU | LEU | GLY | ALA | CYS | VAL | ||||
| 9 | ALA | ASN | CYS | GLY | LYS | ILE | PHE | HIS | LEU | GLU | ||||
| 10 | VAL | CYS | SER | ARG | ASP | PHE | ALA | THR | GLU | VAL | ||||
| 11 | ARG | ALA | VAL | ILE | LYS | ASN | LYS | ALA | HIS | PRO | ||||
| 12 | LYS | VAL | CYS | GLU | LYS | LEU | LYS | SER | LEU | MET | ||||
| 13 | VAL | GLU | TRP | SER | GLU | GLU | PHE | GLN | LYS | ASP | ||||
| 14 | PRO | GLN | PHE | SER | LEU | ILE | SER | ALA | THR | ILE | ||||
| 15 | LYS | SER | MET | LYS | GLU | GLU | GLY | ILE | THR | PHE | ||||
| 16 | PRO | PRO | ALA | GLY | SER | GLN | THR | SER | GLY | PRO | ||||
| 17 | SER | SER | GLY |
Samples:
sample_1: VHS domain, [U-13C; U-15N], 1.5 mM; d-Tris HCl 20 mM; NaCl 100 mM; d-DTT 5 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 v20031121, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.926, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 900 MHz
Related Database Links:
| BMRB | 18185 |
| PDB | |
| DBJ | BAF84954 BAF85536 BAG72771 BAK62690 |
| EMBL | CAB63735 CAL38297 |
| GB | AAC63963 AAC63964 AAH28740 AAH83912 AAI12605 |
| REF | NP_001012085 NP_001069574 NP_001267210 NP_005834 XP_002749486 |
| SP | O75886 Q5XHY7 |
| TPG | DAA32691 |
| AlphaFold | O75886 Q5XHY7 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts