BMRB Entry 51080
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51080
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Baudin, Antoine; Moreno-Romero, Alma; Xu, Xiaoping; Selig, Emily; Penalva, Luiz; Libich, David. "Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes" Front. Mol. Biosci 8, 744707-744707 (2021).
PubMed: 34631798
Assembly members:
entity_1, polymer, 252 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: pAG8HA
Entity Sequences (FASTA):
entity_1: GEFSVDRPIIDRPIRGRGGL
GRGRGGRGRGMGRGDGFDSR
GKREFDRHSGSDRSSFSHYS
GLKHEDKRGGSGSHNWGTVK
DELTESPKYIQKQISYNYSD
LDQSNVTEETPEGEEHHPVA
DTENKENEVEEVKEEGPKEM
TLDEWKAIQNKDRAKVEFNI
RKPNEGADGQWKKGFVLHKS
KSEEAHAEDSVMDHHFRKPA
NDITSQLEINFGDLGRPGRG
GRGGRGGRGRGGRPNRGSRT
DKSSASAPDVDD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 619 |
| 15N chemical shifts | 179 |
| 1H chemical shifts | 179 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SERBP1 | 1 |
Entities:
Entity 1, SERBP1 252 residues - Formula weight is not available
| 1 | GLY | GLU | PHE | SER | VAL | ASP | ARG | PRO | ILE | ILE | ||||
| 2 | ASP | ARG | PRO | ILE | ARG | GLY | ARG | GLY | GLY | LEU | ||||
| 3 | GLY | ARG | GLY | ARG | GLY | GLY | ARG | GLY | ARG | GLY | ||||
| 4 | MET | GLY | ARG | GLY | ASP | GLY | PHE | ASP | SER | ARG | ||||
| 5 | GLY | LYS | ARG | GLU | PHE | ASP | ARG | HIS | SER | GLY | ||||
| 6 | SER | ASP | ARG | SER | SER | PHE | SER | HIS | TYR | SER | ||||
| 7 | GLY | LEU | LYS | HIS | GLU | ASP | LYS | ARG | GLY | GLY | ||||
| 8 | SER | GLY | SER | HIS | ASN | TRP | GLY | THR | VAL | LYS | ||||
| 9 | ASP | GLU | LEU | THR | GLU | SER | PRO | LYS | TYR | ILE | ||||
| 10 | GLN | LYS | GLN | ILE | SER | TYR | ASN | TYR | SER | ASP | ||||
| 11 | LEU | ASP | GLN | SER | ASN | VAL | THR | GLU | GLU | THR | ||||
| 12 | PRO | GLU | GLY | GLU | GLU | HIS | HIS | PRO | VAL | ALA | ||||
| 13 | ASP | THR | GLU | ASN | LYS | GLU | ASN | GLU | VAL | GLU | ||||
| 14 | GLU | VAL | LYS | GLU | GLU | GLY | PRO | LYS | GLU | MET | ||||
| 15 | THR | LEU | ASP | GLU | TRP | LYS | ALA | ILE | GLN | ASN | ||||
| 16 | LYS | ASP | ARG | ALA | LYS | VAL | GLU | PHE | ASN | ILE | ||||
| 17 | ARG | LYS | PRO | ASN | GLU | GLY | ALA | ASP | GLY | GLN | ||||
| 18 | TRP | LYS | LYS | GLY | PHE | VAL | LEU | HIS | LYS | SER | ||||
| 19 | LYS | SER | GLU | GLU | ALA | HIS | ALA | GLU | ASP | SER | ||||
| 20 | VAL | MET | ASP | HIS | HIS | PHE | ARG | LYS | PRO | ALA | ||||
| 21 | ASN | ASP | ILE | THR | SER | GLN | LEU | GLU | ILE | ASN | ||||
| 22 | PHE | GLY | ASP | LEU | GLY | ARG | PRO | GLY | ARG | GLY | ||||
| 23 | GLY | ARG | GLY | GLY | ARG | GLY | GLY | ARG | GLY | ARG | ||||
| 24 | GLY | GLY | ARG | PRO | ASN | ARG | GLY | SER | ARG | THR | ||||
| 25 | ASP | LYS | SER | SER | ALA | SER | ALA | PRO | ASP | VAL | ||||
| 26 | ASP | ASP |
Samples:
sample_1: SERBP1, [U-100% 13C; U-100% 15N], 300 uM
sample_conditions_1: ionic strength: 60 mM; pH: 6.9; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.5 - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks