BMRB Entry 18613
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18613
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Title: NMR solution structure of Eph receptor PubMed: 22277260
Deposition date: 2012-07-24 Original release date: 2013-07-22
Authors: Qin, Haina; Song, Jianxing
Citation: Qin, Haina; Lim, Liangzhong; Song, Jianxing. "Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations." BMC Biophys. 5, 2-2 (2012).
Assembly members:
entity, polymer, 183 residues, 20989.896 Da.
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
Entity Sequences (FASTA):
entity: GSNEVTLLDSRSVQGELGWI
ASPLEGGWEEVSIMDEKNTP
IRTYQVCNVMEPSQNNWLRT
DWITREGAQRVYIEIKFTLR
DCNSLPGVMGTCKETFNLYY
YESDNDKERFIRENQFVKID
TIAADESFTQVDIGDRIMKL
NTEIRDVGPLSKKGFYLAFQ
DVGACIALVSVRVFYKKAPL
TVR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 449 |
| 15N chemical shifts | 163 |
| 1H chemical shifts | 948 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Eph receptor | 1 |
Entities:
Entity 1, Eph receptor 183 residues - 20989.896 Da.
| 1 | GLY | SER | ASN | GLU | VAL | THR | LEU | LEU | ASP | SER | ||||
| 2 | ARG | SER | VAL | GLN | GLY | GLU | LEU | GLY | TRP | ILE | ||||
| 3 | ALA | SER | PRO | LEU | GLU | GLY | GLY | TRP | GLU | GLU | ||||
| 4 | VAL | SER | ILE | MET | ASP | GLU | LYS | ASN | THR | PRO | ||||
| 5 | ILE | ARG | THR | TYR | GLN | VAL | CYS | ASN | VAL | MET | ||||
| 6 | GLU | PRO | SER | GLN | ASN | ASN | TRP | LEU | ARG | THR | ||||
| 7 | ASP | TRP | ILE | THR | ARG | GLU | GLY | ALA | GLN | ARG | ||||
| 8 | VAL | TYR | ILE | GLU | ILE | LYS | PHE | THR | LEU | ARG | ||||
| 9 | ASP | CYS | ASN | SER | LEU | PRO | GLY | VAL | MET | GLY | ||||
| 10 | THR | CYS | LYS | GLU | THR | PHE | ASN | LEU | TYR | TYR | ||||
| 11 | TYR | GLU | SER | ASP | ASN | ASP | LYS | GLU | ARG | PHE | ||||
| 12 | ILE | ARG | GLU | ASN | GLN | PHE | VAL | LYS | ILE | ASP | ||||
| 13 | THR | ILE | ALA | ALA | ASP | GLU | SER | PHE | THR | GLN | ||||
| 14 | VAL | ASP | ILE | GLY | ASP | ARG | ILE | MET | LYS | LEU | ||||
| 15 | ASN | THR | GLU | ILE | ARG | ASP | VAL | GLY | PRO | LEU | ||||
| 16 | SER | LYS | LYS | GLY | PHE | TYR | LEU | ALA | PHE | GLN | ||||
| 17 | ASP | VAL | GLY | ALA | CYS | ILE | ALA | LEU | VAL | SER | ||||
| 18 | VAL | ARG | VAL | PHE | TYR | LYS | LYS | ALA | PRO | LEU | ||||
| 19 | THR | VAL | ARG |
Samples:
sample_1: protein, [U-99% 15N], 0.5 mM; potassium phosphate 10 mM; sodium azide 0.00002 mM; D2O 10 % v/v; H2O 100 % v/v; DTT 0 w/v
sample_conditions_1: ionic strength: 0.01 M; pH: 6.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Braun and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts