BMRB Entry 4396
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4396
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Duggan, Brendan; Dyson, H.; Wright, Peter. "Inherent flexibility in a potent inhibitor of blood coagulation, recombinant
nematode anticoagulant protein c2" Eur. J. Biochem. 265, 539-548 (1999).
PubMed: 10504384
Assembly members:
Nematode Anticoagulant Protein c2, polymer, 85 residues, 9643 Da.
Natural source: Common Name: dog hookworm Taxonomy ID: 29170 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Ancylostoma caninum
Experimental source: Production method: recombinant technology Host organism: Pichia pastoris Vector: pYAM7SP8
Entity Sequences (FASTA):
Nematode Anticoagulant Protein c2: KATMQCGENEKYDSCGSKEC
DKKCKYDGVEEEDDEEPNVP
CLVRVCHQDCVCEEGFYRNK
DDKCVSAEDCELDNMDFIYP
GTRNP
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 22 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 511 |
| coupling constants | 76 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NAPc2 | 1 |
Entities:
Entity 1, NAPc2 85 residues - 9643 Da.
| 1 | LYS | ALA | THR | MET | GLN | CYS | GLY | GLU | ASN | GLU | ||||
| 2 | LYS | TYR | ASP | SER | CYS | GLY | SER | LYS | GLU | CYS | ||||
| 3 | ASP | LYS | LYS | CYS | LYS | TYR | ASP | GLY | VAL | GLU | ||||
| 4 | GLU | GLU | ASP | ASP | GLU | GLU | PRO | ASN | VAL | PRO | ||||
| 5 | CYS | LEU | VAL | ARG | VAL | CYS | HIS | GLN | ASP | CYS | ||||
| 6 | VAL | CYS | GLU | GLU | GLY | PHE | TYR | ARG | ASN | LYS | ||||
| 7 | ASP | ASP | LYS | CYS | VAL | SER | ALA | GLU | ASP | CYS | ||||
| 8 | GLU | LEU | ASP | ASN | MET | ASP | PHE | ILE | TYR | PRO | ||||
| 9 | GLY | THR | ARG | ASN | PRO |
Samples:
sample_1: Nematode Anticoagulant Protein c2, [U-55% 15N], 2.0 mM; sodium chloride 50 mM; DSS 20 uM
sample_cond_1: ionic strength: 0.05 M; pH: 4.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| NOESY | sample_1 | not available | sample_cond_1 |
| DQ-COSY | sample_1 | not available | sample_cond_1 |
| 15N HSQC | sample_1 | not available | sample_cond_1 |
| 15N NOESY-HSQC | sample_1 | not available | sample_cond_1 |
| 15N TOCSY-HSQC | sample_1 | not available | sample_cond_1 |
| 15N HSQC-NOESY-HSQ | sample_1 | not available | sample_cond_1 |
| HNHA | sample_1 | not available | sample_cond_1 |
| 13C HSQC | sample_1 | not available | sample_cond_1 |
| 15N {1H} NOE | sample_1 | not available | sample_cond_1 |
Software:
Felix v95 and 97 - data processing and analysis
Dyana v1.5 - molecular dynamics
Amber v5.1 - molecular dynamics
Procheck-NMR v3.4.4 - structure analysis
SANE v1 - In-house software: automated NOESY assignment and restraint generation
NMR spectrometers:
- Bruker AMX 500 MHz
- Bruker AMX 600 MHz
- Bruker DMX 750 MHz
- Bruker DMX 500 MHz
- Bruker DMX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks