BMRB Entry 5185
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5185
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Title: 1H, 13C, and 15N resonance assignment of the vascular endothelial growth factor receptor-binding domain in complex with a receptor-blocking peptide PubMed: 11883783
Deposition date: 2001-10-19 Original release date: 2002-05-07
Authors: Pan, Borlan; Fairbrother, Wayne
Citation: Pan, Borlan; Fairbrother, Wayne. "Letter to the Editor: 1H, 13C, and 15N Resonance Assignment of the Vascular Endothelial Growth Factor Receptor-binding Domain in Complex with a Receptor-blocking Peptide" J. Biomol. NMR 22, 189-190 (2002).
Assembly members:
vascular endothelial growth factor, polymer, 99 residues, 11625.4 Da.
v107 peptide, polymer, 19 residues, 2343.0 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
vascular endothelial growth factor: HHEVVKFMDVYQRSYCHPIE
TLVDIFQEYPDEIEYIFKPS
CVPLMRCGGCCNDEGLECVP
TEESNITMQIMRIKPHQGQH
IGEMSFLQHNKCECRPKKD
v107 peptide: GGNECDIARMWEWECFERL
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 693 |
| 13C chemical shifts | 444 |
| 15N chemical shifts | 97 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | VEGF subunit 1 | 1 |
| 2 | VEGF subunit 2 | 1 |
| 3 | v107 subunit 1 | 2 |
| 4 | v107 subunit 2 | 2 |
Entities:
Entity 1, VEGF subunit 1 99 residues - 11625.4 Da.
| 1 | HIS | HIS | GLU | VAL | VAL | LYS | PHE | MET | ASP | VAL | ||||
| 2 | TYR | GLN | ARG | SER | TYR | CYS | HIS | PRO | ILE | GLU | ||||
| 3 | THR | LEU | VAL | ASP | ILE | PHE | GLN | GLU | TYR | PRO | ||||
| 4 | ASP | GLU | ILE | GLU | TYR | ILE | PHE | LYS | PRO | SER | ||||
| 5 | CYS | VAL | PRO | LEU | MET | ARG | CYS | GLY | GLY | CYS | ||||
| 6 | CYS | ASN | ASP | GLU | GLY | LEU | GLU | CYS | VAL | PRO | ||||
| 7 | THR | GLU | GLU | SER | ASN | ILE | THR | MET | GLN | ILE | ||||
| 8 | MET | ARG | ILE | LYS | PRO | HIS | GLN | GLY | GLN | HIS | ||||
| 9 | ILE | GLY | GLU | MET | SER | PHE | LEU | GLN | HIS | ASN | ||||
| 10 | LYS | CYS | GLU | CYS | ARG | PRO | LYS | LYS | ASP |
Entity 2, v107 subunit 1 19 residues - 2343.0 Da.
| 1 | GLY | GLY | ASN | GLU | CYS | ASP | ILE | ALA | ARG | MET | ||||
| 2 | TRP | GLU | TRP | GLU | CYS | PHE | GLU | ARG | LEU |
Samples:
Sample_1: vascular endothelial growth factor, [U-98% 13C; U-98% 15N], 2.0 mM; v107 peptide 2.25 mM; H2O 90%; D2O 10%
Sample_2: vascular endothelial growth factor, [U-98% 13C; U-98% 15N], 2.0 mM; v107 peptide 2.25 mM; D2O 100%
Cond_1: pH: 7.0; temperature: 318 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|
Software:
No software information available
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts