BMRB Entry 15192
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15192
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Title: NMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen alphaC-Domain Fragment PubMed: 17590019
Deposition date: 2007-03-20 Original release date: 2007-09-12
Authors: Burton, Robert; Tsurupa, Galina; Roy, Hantgan; Nico, Tjandra; Leonid, Medved
Citation: Burton, Robert; Tsurupa, Galina; Hantgan, Roy; Tjandra, Nico; Medved, Leonid. "NMR solution structure, stability, and interaction of the recombinant bovine fibrinogen alphaC-domain fragment." Biochemistry 46, 8550-8560 (2007).
Assembly members:
subunit 1, polymer, 79 residues, 8975.755 Da.
Natural source: Common Name: not available Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
subunit 1: MIDNEKVTSGHTTTTRRSCS
KVITKTVTNADGRTETTKEV
VKSEDGSDCGDADFDWHHTF
PSRGNLDDFFHRDKDDFFT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 148 |
| 15N chemical shifts | 74 |
| 1H chemical shifts | 181 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
Entities:
Entity 1, subunit 1 79 residues - 8975.755 Da.
| 1 | MET | ILE | ASP | ASN | GLU | LYS | VAL | THR | SER | GLY | ||||
| 2 | HIS | THR | THR | THR | THR | ARG | ARG | SER | CYS | SER | ||||
| 3 | LYS | VAL | ILE | THR | LYS | THR | VAL | THR | ASN | ALA | ||||
| 4 | ASP | GLY | ARG | THR | GLU | THR | THR | LYS | GLU | VAL | ||||
| 5 | VAL | LYS | SER | GLU | ASP | GLY | SER | ASP | CYS | GLY | ||||
| 6 | ASP | ALA | ASP | PHE | ASP | TRP | HIS | HIS | THR | PHE | ||||
| 7 | PRO | SER | ARG | GLY | ASN | LEU | ASP | ASP | PHE | PHE | ||||
| 8 | HIS | ARG | ASP | LYS | ASP | ASP | PHE | PHE | THR |
Samples:
sample_1: entity_1, [U-99% 13C; U-99% 15N], 150 uM; KPO4 10 mM; NaCl 150 mM; D20 10%
sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 282 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker DMX 600 MHz
Related Database Links:
| PDB | |
| GB | AAC67562 AAI02565 AAI42073 |
| REF | NP_001028798 XP_005217494 |
| SP | P02672 |
| TPG | DAA20930 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts