BMRB Entry 26552
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR26552
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Plasmodium falciparum Immune Mapped Protein 1 (PfIMP1) PubMed: 25947350
Deposition date: 2015-04-08 Original release date: 2016-01-06
Authors: Williams, Felix; Kerry, Louise
Citation: Benjamin, Stefi; Williams, Felix; Kerry, Louise; Matthews, Stephen. "NMR assignment of the immune mapped protein 1 (IMP1) homologue from Plasmodium falciparum" Biomol. NMR Assignments 9, 393-395 (2015).
Assembly members:
PfIMP1, polymer, 181 residues, Formula weight is not available
Natural source: Common Name: apicomplexans Taxonomy ID: 36329 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PfIMP1: MHHHHHHSSGVDLGTENLYF
QSMMSEEKGAYLVFDNASNG
TLFIVWKKEKVENALMFIKP
TKEVPEFKFVNRNGKNELIR
NLQSDKKLFYSGICQFVKEA
KDIKGKLTLLQHFDSSFPIK
VDLYFLKGSKVMPLNTGEPF
VVQDIDAMSVLPKGSSSLKV
KTMAKDMFVSRGNTEGASIS
F
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 693 |
| 15N chemical shifts | 145 |
| 1H chemical shifts | 1087 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PfIMP1 monomer | 1 |
Entities:
Entity 1, PfIMP1 monomer 181 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 2 | VAL | ASP | LEU | GLY | THR | GLU | ASN | LEU | TYR | PHE | ||||
| 3 | GLN | SER | MET | MET | SER | GLU | GLU | LYS | GLY | ALA | ||||
| 4 | TYR | LEU | VAL | PHE | ASP | ASN | ALA | SER | ASN | GLY | ||||
| 5 | THR | LEU | PHE | ILE | VAL | TRP | LYS | LYS | GLU | LYS | ||||
| 6 | VAL | GLU | ASN | ALA | LEU | MET | PHE | ILE | LYS | PRO | ||||
| 7 | THR | LYS | GLU | VAL | PRO | GLU | PHE | LYS | PHE | VAL | ||||
| 8 | ASN | ARG | ASN | GLY | LYS | ASN | GLU | LEU | ILE | ARG | ||||
| 9 | ASN | LEU | GLN | SER | ASP | LYS | LYS | LEU | PHE | TYR | ||||
| 10 | SER | GLY | ILE | CYS | GLN | PHE | VAL | LYS | GLU | ALA | ||||
| 11 | LYS | ASP | ILE | LYS | GLY | LYS | LEU | THR | LEU | LEU | ||||
| 12 | GLN | HIS | PHE | ASP | SER | SER | PHE | PRO | ILE | LYS | ||||
| 13 | VAL | ASP | LEU | TYR | PHE | LEU | LYS | GLY | SER | LYS | ||||
| 14 | VAL | MET | PRO | LEU | ASN | THR | GLY | GLU | PRO | PHE | ||||
| 15 | VAL | VAL | GLN | ASP | ILE | ASP | ALA | MET | SER | VAL | ||||
| 16 | LEU | PRO | LYS | GLY | SER | SER | SER | LEU | LYS | VAL | ||||
| 17 | LYS | THR | MET | ALA | LYS | ASP | MET | PHE | VAL | SER | ||||
| 18 | ARG | GLY | ASN | THR | GLU | GLY | ALA | SER | ILE | SER | ||||
| 19 | PHE |
Samples:
sample_1: PfIMP1, [U-100% 13C; U-100% 15N], 1.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 250 mM; pH: 7.5; pressure: 1 atm; temperature: 303 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
Related Database Links:
| NCBI | XP_001349200 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts