BMRB Entry 15783
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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/BMR15783
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Title: acidic fibroblast growth factor solution structure in the FGF-1-C2A binary complex: key component in the fibroblast growthfactor non-classical pathway PubMed: 19723500
Deposition date: 2008-05-28 Original release date: 2009-10-12
Authors: Mohan, Sepuru; Yu, Chin
Citation: Anbazhagan, Veerappan; Wang, Han-Min; Lu, Ching-Song; Yu, Chin. "A residue-level investigation of the equilibrium unfolding of the C2A domain of synaptotagmin 1." Arch. Biochem. Biophys. 490, 158-162 (2009).
Assembly members:
FGF-1, polymer, 133 residues, 15118.163 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo spiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FGF-1: YKKPKLLYCSNGGHFLRILP
DGTVDGTRDRSDQHIQLQLS
AESVGEVYIKSTETGQYLAM
DTDGLLYGSQTPNEECLFLE
RLEENHYNTYISKKHAEKNW
FVGLKKNGSCKRGPRTHYGQ
KAILFLPLPVSSD
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 694 |
| 15N chemical shifts | 132 |
| 13C chemical shifts | 364 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FGF-1 | 1 |
Entities:
Entity 1, FGF-1 133 residues - 15118.163 Da.
| 1 | TYR | LYS | LYS | PRO | LYS | LEU | LEU | TYR | CYS | SER | ||||
| 2 | ASN | GLY | GLY | HIS | PHE | LEU | ARG | ILE | LEU | PRO | ||||
| 3 | ASP | GLY | THR | VAL | ASP | GLY | THR | ARG | ASP | ARG | ||||
| 4 | SER | ASP | GLN | HIS | ILE | GLN | LEU | GLN | LEU | SER | ||||
| 5 | ALA | GLU | SER | VAL | GLY | GLU | VAL | TYR | ILE | LYS | ||||
| 6 | SER | THR | GLU | THR | GLY | GLN | TYR | LEU | ALA | MET | ||||
| 7 | ASP | THR | ASP | GLY | LEU | LEU | TYR | GLY | SER | GLN | ||||
| 8 | THR | PRO | ASN | GLU | GLU | CYS | LEU | PHE | LEU | GLU | ||||
| 9 | ARG | LEU | GLU | GLU | ASN | HIS | TYR | ASN | THR | TYR | ||||
| 10 | ILE | SER | LYS | LYS | HIS | ALA | GLU | LYS | ASN | TRP | ||||
| 11 | PHE | VAL | GLY | LEU | LYS | LYS | ASN | GLY | SER | CYS | ||||
| 12 | LYS | ARG | GLY | PRO | ARG | THR | HIS | TYR | GLY | GLN | ||||
| 13 | LYS | ALA | ILE | LEU | PHE | LEU | PRO | LEU | PRO | VAL | ||||
| 14 | SER | SER | ASP |
Samples:
sample: FGF-1 1.0 mM; Phosphate buffer 25 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_15N-separated_NOESY | sample | isotropic | sample_conditions_1 |
Software:
ARIA v1.2, Linge, O, . - structure solution
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AV600 600 MHz
- Bruker AV800 800 MHz
Related Database Links:
| BMRB | 15960 16493 16494 16502 17464 17674 |
| PDB | |
| DBJ | BAC29035 BAF82451 BAG35227 BAI46827 |
| EMBL | CAA32448 CAA36206 CAA42869 CAA46661 CAI29610 |
| GB | AAA37618 AAA52446 AAA52638 AAA79245 AAB29057 |
| PRF | 1605206A |
| REF | NP_000791 NP_001127073 NP_001138364 NP_001138406 NP_001138407 |
| SP | P05230 P20002 P34004 P61148 P61149 |
Download simulated HSQC data in one of the following formats:
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