BMRB Entry 17062
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17062
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Title: Solution Structure of Human Plasminogen Kringle 3 PubMed: 20617841
Deposition date: 2010-07-15 Original release date: 2010-08-19
Authors: Christen, Martin; Frank, Pascal; Schaller, Johann; Llinas, Miguel
Citation: Christen, Martin; Frank, Pascal; Schaller, Johann; Llinas, Miguel. "Human plasminogen kringle 3: solution structure, functional insights, phylogenetic landscape" Biochemistry 49, 7131-7150 (2010).
Assembly members:
hPgn_rK3, polymer, 83 residues, 9505.4 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):
hPgn_rK3: TYQCLKGTGENYRGNVAVTV
SGHTCQHWSAQTPHTHNRTP
ENFPSKNLDENYCRNPDGKR
APWCHTTNSQVRWEYCKIPS
CDS
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 186 |
| 1H chemical shifts | 603 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hPgn_rK3 | 1 |
Entities:
Entity 1, hPgn_rK3 83 residues - 9505.4 Da.
Residues -3 to -1 and 81 to 82 are outside of the kringle domain proper. Sequence follows standard kringle amino acid numbering convention
| 1 | THR | TYR | GLN | CYS | LEU | LYS | GLY | THR | GLY | GLU | ||||
| 2 | ASN | TYR | ARG | GLY | ASN | VAL | ALA | VAL | THR | VAL | ||||
| 3 | SER | GLY | HIS | THR | CYS | GLN | HIS | TRP | SER | ALA | ||||
| 4 | GLN | THR | PRO | HIS | THR | HIS | ASN | ARG | THR | PRO | ||||
| 5 | GLU | ASN | PHE | PRO | SER | LYS | ASN | LEU | ASP | GLU | ||||
| 6 | ASN | TYR | CYS | ARG | ASN | PRO | ASP | GLY | LYS | ARG | ||||
| 7 | ALA | PRO | TRP | CYS | HIS | THR | THR | ASN | SER | GLN | ||||
| 8 | VAL | ARG | TRP | GLU | TYR | CYS | LYS | ILE | PRO | SER | ||||
| 9 | CYS | ASP | SER |
Samples:
sample_1: hPgn_rK3, [U-97% 15N], 1.0 mM; H2O 90%; D2O 90%; sodium azide 0.02%
Structure_determination: ionic strength: 0 M; pH*: 5.7; pressure: 1 atm; temperature: 273 K
Titrations: ionic strength: 0 M; pH*: 7.0; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | Structure_determination |
| 3D 1H-15N TOCSY | sample_1 | isotropic | Structure_determination |
| 3D 1H-15N NOESY | sample_1 | isotropic | Structure_determination |
| 3D HNHA | sample_1 | isotropic | Structure_determination |
| 3D HNHB | sample_1 | isotropic | Structure_determination |
| 2D 1H-1H COSY | sample_1 | isotropic | Structure_determination |
| 2D 1H-1H TOCSY | sample_1 | isotropic | Structure_determination |
| 2D 1H-1H NOESY | sample_1 | isotropic | Structure_determination |
| 2D 1H-15N HSQC | sample_1 | isotropic | Titrations |
Software:
xwinnmr v2.6, Bruker Biospin - collection
FELIX v98, Accelrys Software Inc. - processing
CcpNMR v1.0, CCPN - chemical shift assignment, data analysis, peak picking
ARIA v2.2, Linge, O, . - refinement, structure solution
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts