BMRB Entry 51747
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51747
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Title: Backbone Assignment of the S519N variant of SASH1 Pigmentation Associated Disordered Region (SPIDER) PubMed: 37155029
Deposition date: 2022-12-19 Original release date: 2023-04-21
Authors: Clements, Christopher; Shellman, Yiqun; Vogeli, Beat; Henen, Morkos
Citation: Clements, Christopher; Shellman, Yiqun; Vogeli, Beat; Henen, Morkos. "Solution NMR backbone assignment of the SASH1 SLy proteins associated disordered region (SPIDER)" Biomol. NMR Assign. 17, 151-157 (2023).
Assembly members:
entity_1, polymer, 169 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: recombinant technology Host organism: Escherichia coli Vector: Pet28 a (+)
Entity Sequences (FASTA):
entity_1: GLGSLSHGRTCSFGGFDLTN
RSLHVGSNNSDPMGKEGDFV
YKEVIKSPTASRISLGKKVK
SVKETMRKRMSKKYSSSVSE
QDSGLDGMPGSPPPSQPDPE
HLDKPKLKAGGSVESLRSSL
SGQNSMSGQTVSTTDSSTSN
RESVKSEDGDDEEPPYRGPF
CGRARVHTD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 460 |
| 15N chemical shifts | 153 |
| 1H chemical shifts | 153 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SPIDER-SASH1 | 1 |
Entities:
Entity 1, SPIDER-SASH1 169 residues - Formula weight is not available
SASH1 396-564 (Linker: 396-400, SPIDER: 401-553 & SH3: 554-564)
| 1 | GLY | LEU | GLY | SER | LEU | SER | HIS | GLY | ARG | THR | ||||
| 2 | CYS | SER | PHE | GLY | GLY | PHE | ASP | LEU | THR | ASN | ||||
| 3 | ARG | SER | LEU | HIS | VAL | GLY | SER | ASN | ASN | SER | ||||
| 4 | ASP | PRO | MET | GLY | LYS | GLU | GLY | ASP | PHE | VAL | ||||
| 5 | TYR | LYS | GLU | VAL | ILE | LYS | SER | PRO | THR | ALA | ||||
| 6 | SER | ARG | ILE | SER | LEU | GLY | LYS | LYS | VAL | LYS | ||||
| 7 | SER | VAL | LYS | GLU | THR | MET | ARG | LYS | ARG | MET | ||||
| 8 | SER | LYS | LYS | TYR | SER | SER | SER | VAL | SER | GLU | ||||
| 9 | GLN | ASP | SER | GLY | LEU | ASP | GLY | MET | PRO | GLY | ||||
| 10 | SER | PRO | PRO | PRO | SER | GLN | PRO | ASP | PRO | GLU | ||||
| 11 | HIS | LEU | ASP | LYS | PRO | LYS | LEU | LYS | ALA | GLY | ||||
| 12 | GLY | SER | VAL | GLU | SER | LEU | ARG | SER | SER | LEU | ||||
| 13 | SER | GLY | GLN | ASN | SER | MET | SER | GLY | GLN | THR | ||||
| 14 | VAL | SER | THR | THR | ASP | SER | SER | THR | SER | ASN | ||||
| 15 | ARG | GLU | SER | VAL | LYS | SER | GLU | ASP | GLY | ASP | ||||
| 16 | ASP | GLU | GLU | PRO | PRO | TYR | ARG | GLY | PRO | PHE | ||||
| 17 | CYS | GLY | ARG | ALA | ARG | VAL | HIS | THR | ASP |
Samples:
sample_1: SPIDER-SASH1, [U-100% 13C; U-100% 15N; U-80% 2H], 802 uM; NaCl 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 278 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNN | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.5.1 - chemical shift assignment, data analysis
TOPSPIN v4.1.4 - collection, data analysis
NMRFAM-SPARKY v1.470 - data analysis
NMRPipe - data analysis, processing
NMR spectrometers:
- Bruker AVANCE NEO 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts