BMRB Entry 25449
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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/BMR25449
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Title: Solution structure of RNA recognition motif of a cyclophilin33 - like protein from Plasmodium falciparum
Deposition date: 2015-01-22 Original release date: 2016-01-25
Authors: Ganguly, Akshay Kumar; Bhavesh, Neel Sarovar
Citation: Ganguly, Akshay Kumar; Bhavesh, Neel Sarovar. "Solution structure of RNA recognition motif of a cyclophilin33 - like protein from Plasmodium falciparum" Not known ., .-..
Assembly members:
RRM, polymer, 89 residues, 10149.340 Da.
Natural source: Common Name: Malaria 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):
RRM: GSHMSDNNATDILFVGGIDE
TIDEKSLYDIFSSFGDIRNI
EVPLNMTTKKNRGFAFVEYV
EVDDAKHALYNMNNFELNGK
RIHVNYSKT
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 366 |
15N chemical shifts | 97 |
1H chemical shifts | 535 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RRM | 1 |
Entities:
Entity 1, RRM 89 residues - 10149.340 Da.
Residues G,S and H at the N-terminus are part of a non-native affinity tag from the vector pET28a and have been renumbered to -2,-1 and 0.
1 | GLY | SER | HIS | MET | SER | ASP | ASN | ASN | ALA | THR | ||||
2 | ASP | ILE | LEU | PHE | VAL | GLY | GLY | ILE | ASP | GLU | ||||
3 | THR | ILE | ASP | GLU | LYS | SER | LEU | TYR | ASP | ILE | ||||
4 | PHE | SER | SER | PHE | GLY | ASP | ILE | ARG | ASN | ILE | ||||
5 | GLU | VAL | PRO | LEU | ASN | MET | THR | THR | LYS | LYS | ||||
6 | ASN | ARG | GLY | PHE | ALA | PHE | VAL | GLU | TYR | VAL | ||||
7 | GLU | VAL | ASP | ASP | ALA | LYS | HIS | ALA | LEU | TYR | ||||
8 | ASN | MET | ASN | ASN | PHE | GLU | LEU | ASN | GLY | LYS | ||||
9 | ARG | ILE | HIS | VAL | ASN | TYR | SER | LYS | THR |
Samples:
sample_1: RRM, [U-100% 13C; U-100% 15N], 0.5 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DSS 50 uM; D2O 10%; H2O 90%
sample_2: RRM, [U-100% 13C; U-100% 15N], 0.5 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DSS 50 uM; D2O 100%
sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)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 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 700 MHz
Related Database Links:
NCBI | XP_002809024.1 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts