BMRB Entry 19906
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19906
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Title: Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide PubMed: 24985319
Deposition date: 2014-04-10 Original release date: 2014-09-22
Authors: Suh, Jeong-Yong; Yu, Tae-Kyung
Citation: Yu, T.K.; Shin, S.A.; Kim, E.H.; Kim, S.; Ryu, K.S.; Cheong, H.; Ahn, H.C.; Jon, S.; Suh, Jeong-Yong. "An Unusual Protein-Protein Interaction through Coupled Unfolding and Binding" Angew. Chem. Int. Ed. Engl. 53, 9784-9787 (2014).
Assembly members:
EDB, polymer, 93 residues, Formula weight is not available
APT, polymer, 26 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
Entity Sequences (FASTA):
EDB: GSEVPQLTDLSFVDITDSSI
GLRWTPLNSSTIIGYRITVV
AAGEGIPIFEDFVDSSVGYY
TVTGLEPGIDYDISVITLIN
GGESAPTTLTQQT
APT: SSSPIQGSWTWENGKWTWKG
IIRLEQ
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 681 |
| 13C chemical shifts | 328 |
| 15N chemical shifts | 104 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EDB | 1 |
| 2 | APT | 2 |
Entities:
Entity 1, EDB 93 residues - Formula weight is not available
| 1 | GLY | SER | GLU | VAL | PRO | GLN | LEU | THR | ASP | LEU | ||||
| 2 | SER | PHE | VAL | ASP | ILE | THR | ASP | SER | SER | ILE | ||||
| 3 | GLY | LEU | ARG | TRP | THR | PRO | LEU | ASN | SER | SER | ||||
| 4 | THR | ILE | ILE | GLY | TYR | ARG | ILE | THR | VAL | VAL | ||||
| 5 | ALA | ALA | GLY | GLU | GLY | ILE | PRO | ILE | PHE | GLU | ||||
| 6 | ASP | PHE | VAL | ASP | SER | SER | VAL | GLY | TYR | TYR | ||||
| 7 | THR | VAL | THR | GLY | LEU | GLU | PRO | GLY | ILE | ASP | ||||
| 8 | TYR | ASP | ILE | SER | VAL | ILE | THR | LEU | ILE | ASN | ||||
| 9 | GLY | GLY | GLU | SER | ALA | PRO | THR | THR | LEU | THR | ||||
| 10 | GLN | GLN | THR |
Entity 2, APT 26 residues - Formula weight is not available
| 1 | SER | SER | SER | PRO | ILE | GLN | GLY | SER | TRP | THR | ||||
| 2 | TRP | GLU | ASN | GLY | LYS | TRP | THR | TRP | LYS | GLY | ||||
| 3 | ILE | ILE | ARG | LEU | GLU | GLN |
Samples:
sample_1: EDB, [U-100% 13C; U-100% 15N], 0.3 mM; APT, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%
sample_conditions_1: temperature: 273 K; pH: 6; pressure: 1 atm; ionic strength: 20 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR_NIH, Garrett, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, refinement
NMR spectrometers:
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts