BMRB Entry 15785
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15785
MolProbity Validation Chart
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Title: C2A domain of synaptototagmin I 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:
C2A, polymer, 128 residues, 14784.028 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):
C2A: EKLGKLQYSLDYDFQNNQLL
VGIIQAAELPALDMGGTSDP
YVKVFLLPDKKKKFETKVHR
KTLNPVFNEQFTFKVPYSEL
GGKTLVMAVYDFDRFSKHDI
IGEFKVPMNTVDFGHVTEEW
RDLQSAEK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 531 |
| 15N chemical shifts | 134 |
| 1H chemical shifts | 870 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C2A | 1 |
Entities:
Entity 1, C2A 128 residues - 14784.028 Da.
| 1 | GLU | LYS | LEU | GLY | LYS | LEU | GLN | TYR | SER | LEU | ||||
| 2 | ASP | TYR | ASP | PHE | GLN | ASN | ASN | GLN | LEU | LEU | ||||
| 3 | VAL | GLY | ILE | ILE | GLN | ALA | ALA | GLU | LEU | PRO | ||||
| 4 | ALA | LEU | ASP | MET | GLY | GLY | THR | SER | ASP | PRO | ||||
| 5 | TYR | VAL | LYS | VAL | PHE | LEU | LEU | PRO | ASP | LYS | ||||
| 6 | LYS | LYS | LYS | PHE | GLU | THR | LYS | VAL | HIS | ARG | ||||
| 7 | LYS | THR | LEU | ASN | PRO | VAL | PHE | ASN | GLU | GLN | ||||
| 8 | PHE | THR | PHE | LYS | VAL | PRO | TYR | SER | GLU | LEU | ||||
| 9 | GLY | GLY | LYS | THR | LEU | VAL | MET | ALA | VAL | TYR | ||||
| 10 | ASP | PHE | ASP | ARG | PHE | SER | LYS | HIS | ASP | ILE | ||||
| 11 | ILE | GLY | GLU | PHE | LYS | VAL | PRO | MET | ASN | THR | ||||
| 12 | VAL | ASP | PHE | GLY | HIS | VAL | THR | GLU | GLU | TRP | ||||
| 13 | ARG | ASP | LEU | GLN | SER | ALA | GLU | LYS |
Samples:
sample_1: C2A, [U-100% 13C; U-100% 15N], 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_1 | isotropic | sample_conditions_1 |
| 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker AV600 600 MHz
- Bruker AV800 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts