BMRB Entry 17829
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17829
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Title: FVIII C2 Domain PubMed: 22392338
Deposition date: 2011-08-03 Original release date: 2012-03-01
Authors: Nuzzio, Kristin; Cullinan, David; Novakovic, Valerie; Boettcher, John; Rienstra, Chad; Gilbert, Gary; Baleja, James
Citation: Nuzzio, Kristin; Cullinan, David; Novakovic, Valerie; Boettcher, John; Rienstra, Chad; Gilbert, Gary; Baleja, James. "Backbone resonance assignments of the C2 domain of coagulation factor VIII." Biomol. NMR Assignments 7, 31-34 (2013).
Assembly members:
C2_Domain, polymer, 163 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
C2_Domain: GSHMCSMPLGMESKAISDAQ
ITASSYFTNMFATWSPSKAR
LHLQGRSNAWRPQVNNPKEW
LQVDFQKTMKVTGVTTQGVK
SLLTSMYVKEFLISSSQDGH
QWTLFFQNGKVKVFQGNQDS
FTPVVNSLDPPLLTRYLRIH
PQSWVHQIALRMEVLGCEAQ
DLY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 440 |
| 15N chemical shifts | 145 |
| 1H chemical shifts | 145 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C2_Domain | 1 |
Entities:
Entity 1, C2_Domain 163 residues - Formula weight is not available
| 1 | GLY | SER | HIS | MET | CYS | SER | MET | PRO | LEU | GLY | ||||
| 2 | MET | GLU | SER | LYS | ALA | ILE | SER | ASP | ALA | GLN | ||||
| 3 | ILE | THR | ALA | SER | SER | TYR | PHE | THR | ASN | MET | ||||
| 4 | PHE | ALA | THR | TRP | SER | PRO | SER | LYS | ALA | ARG | ||||
| 5 | LEU | HIS | LEU | GLN | GLY | ARG | SER | ASN | ALA | TRP | ||||
| 6 | ARG | PRO | GLN | VAL | ASN | ASN | PRO | LYS | GLU | TRP | ||||
| 7 | LEU | GLN | VAL | ASP | PHE | GLN | LYS | THR | MET | LYS | ||||
| 8 | VAL | THR | GLY | VAL | THR | THR | GLN | GLY | VAL | LYS | ||||
| 9 | SER | LEU | LEU | THR | SER | MET | TYR | VAL | LYS | GLU | ||||
| 10 | PHE | LEU | ILE | SER | SER | SER | GLN | ASP | GLY | HIS | ||||
| 11 | GLN | TRP | THR | LEU | PHE | PHE | GLN | ASN | GLY | LYS | ||||
| 12 | VAL | LYS | VAL | PHE | GLN | GLY | ASN | GLN | ASP | SER | ||||
| 13 | PHE | THR | PRO | VAL | VAL | ASN | SER | LEU | ASP | PRO | ||||
| 14 | PRO | LEU | LEU | THR | ARG | TYR | LEU | ARG | ILE | HIS | ||||
| 15 | PRO | GLN | SER | TRP | VAL | HIS | GLN | ILE | ALA | LEU | ||||
| 16 | ARG | MET | GLU | VAL | LEU | GLY | CYS | GLU | ALA | GLN | ||||
| 17 | ASP | LEU | TYR |
Samples:
sample_1: C2 Domain 0.8 mM; H2O 90%; D2O 10%; sodium chloride 50 mM; EDTA 50 uM; NaN3 0.01%; DSS 20 uM; imidazole 10 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker AMX 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts