BMRB Entry 5238
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5238
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Title: 1H and 15N chemical shift assignments for the heparin-binding domain of vascular endothelial growth factor PubMed: 9634701
Deposition date: 2001-12-18 Original release date: 2002-02-08
Authors: Fairbrother, Wayne; Champe, Mark; Christinger, Hans; Keyt, Bruce; Starovasnik, Melissa
Citation: Fairbrother, Wayne; Champe, Mark; Christinger, Hans; Keyt, Bruce; Starovasnik, Melissa. "Solution structure of the heparin-binding domain of vascular endothelial growth factor" Structure 6, 637-649 (1998).
Assembly members:
vascular endothelial growth factor, polymer, 55 residues, 6477 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):
vascular endothelial growth factor: ARQENPCGPCSERRKHLFVQ
DPQTCKCSCKNTDSRCKARQ
LELNERTCRCDKPRR
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 55 |
| 1H chemical shifts | 359 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | VEGF heparin-binding domain | 1 |
Entities:
Entity 1, VEGF heparin-binding domain 55 residues - 6477 Da.
| 1 | ALA | ARG | GLN | GLU | ASN | PRO | CYS | GLY | PRO | CYS | ||||
| 2 | SER | GLU | ARG | ARG | LYS | HIS | LEU | PHE | VAL | GLN | ||||
| 3 | ASP | PRO | GLN | THR | CYS | LYS | CYS | SER | CYS | LYS | ||||
| 4 | ASN | THR | ASP | SER | ARG | CYS | LYS | ALA | ARG | GLN | ||||
| 5 | LEU | GLU | LEU | ASN | GLU | ARG | THR | CYS | ARG | CYS | ||||
| 6 | ASP | LYS | PRO | ARG | ARG |
Samples:
sample_1: vascular endothelial growth factor 1.0 mM
sample_2: vascular endothelial growth factor, [U-15N], 2.0 mM
condition_1: pH: 5.5; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2QF-COSY | not available | not available | not available |
| 2Q | not available | not available | not available |
| TOCSY | not available | not available | not available |
| NOESY | not available | not available | not available |
| 1H-15N HSQC | not available | not available | not available |
| 1H-15N TOCSY-HSQC | not available | not available | not available |
| 1H-15N NOESY-HSQC | not available | not available | not available |
| 1H-15N ROESY-HSQC | not available | not available | not available |
| HNHA | not available | not available | not available |
| HNHB | not available | not available | not available |
Software:
FELIX - analysis, processing
NMR spectrometers:
- Bruker AMX 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAA78418 BAB20890 BAB68520 |
| EMBL | CAA09179 CAA44447 CAA57143 CAB82426 CAC19512 |
| GenBank | AAA30502 AAA30804 AAA35789 AAA36804 AAA36807 |
| PRF | 2105202A |
| REF | NP_001003175 NP_001009854 NP_001020537 NP_001020538 NP_001020539 |
| SWISS-PROT | P15691 P15692 P26617 P49151 Q9GKR0 |
Download simulated HSQC data in one of the following formats:
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