BMRB Entry 18504
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18504
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Title: pfsub2 solution NMR structure PubMed: 23011838
Deposition date: 2012-06-06 Original release date: 2012-10-01
Authors: HE, Yanan; CHEN, Yihong; RUAN, Biao; O'BROCHTA, David; BRYAN, Philip; ORBAN, John
Citation: He, Yanan; Chen, Yihong; Oganesyan, Natalia; Ruan, Biao; Bryan, David; Orban, Philip. "Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum." Proteins 80, 2810-2817 (2012).
Assembly members:
pfsub2, polymer, 149 residues, 10570.397 Da.
Natural source: Common Name: Malaria parasite P. falciparum Taxonomy ID: 5833 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
pfsub2: TSNKKILLNVDKLVDQYLLN
LKNNHTSKQELILVLKGELD
LHSKNMKNVINNAKKNLEKY
FKEHFKEFDKISYDISTPIN
FLCIFIPTLFDMNNMDLLKQ
ALLILHNDLHEYVENWSFSS
TYHTYEADYIKEQDSVYDRS
PKKKYIKAS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 471 |
| 15N chemical shifts | 118 |
| 1H chemical shifts | 562 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | pfsub2 | 1 |
Entities:
Entity 1, pfsub2 149 residues - 10570.397 Da.
| 1 | THR | SER | ASN | LYS | LYS | ILE | LEU | LEU | ASN | VAL | ||||
| 2 | ASP | LYS | LEU | VAL | ASP | GLN | TYR | LEU | LEU | ASN | ||||
| 3 | LEU | LYS | ASN | ASN | HIS | THR | SER | LYS | GLN | GLU | ||||
| 4 | LEU | ILE | LEU | VAL | LEU | LYS | GLY | GLU | LEU | ASP | ||||
| 5 | LEU | HIS | SER | LYS | ASN | MET | LYS | ASN | VAL | ILE | ||||
| 6 | ASN | ASN | ALA | LYS | LYS | ASN | LEU | GLU | LYS | TYR | ||||
| 7 | PHE | LYS | GLU | HIS | PHE | LYS | GLU | PHE | ASP | LYS | ||||
| 8 | ILE | SER | TYR | ASP | ILE | SER | THR | PRO | ILE | ASN | ||||
| 9 | PHE | LEU | CYS | ILE | PHE | ILE | PRO | THR | LEU | PHE | ||||
| 10 | ASP | MET | ASN | ASN | MET | ASP | LEU | LEU | LYS | GLN | ||||
| 11 | ALA | LEU | LEU | ILE | LEU | HIS | ASN | ASP | LEU | HIS | ||||
| 12 | GLU | TYR | VAL | GLU | ASN | TRP | SER | PHE | SER | SER | ||||
| 13 | THR | TYR | HIS | THR | TYR | GLU | ALA | ASP | TYR | ILE | ||||
| 14 | LYS | GLU | GLN | ASP | SER | VAL | TYR | ASP | ARG | SER | ||||
| 15 | PRO | LYS | LYS | LYS | TYR | ILE | LYS | ALA | SER |
Samples:
sample_1: pfsub2, [U-13C; U-15N], 0.3 – 0.4 mM; potassium phosphate 100 mM; sodium azide 10 mM; D2O 5%; H2O 95%
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.21, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| EMBL | CAB37326 CAB43592 CDO65172 |
| GB | AAN35964 AAY33847 ETW15317 ETW30319 ETW35903 |
| REF | XP_001348051 XP_012763770 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts