BMRB Entry 25983
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25983
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Title: Solution NMR structure of ligand free sterol carrier protein 2 like 2 from Aedes aegypti PubMed: 27508310
Deposition date: 2016-03-07 Original release date: 2017-03-02
Authors: Singarapu, Kiran; Ummanni, Ramesh
Citation: Singarapu, Kiran; Ahuja, Ashish; Potula, Purushotam; Ummanni, Ramesh. "Solution Nuclear Magnetic Resonance Studies of Sterol Carrier Protein 2 Like 2 (SCP2L2) Reveal the Insecticide Specific Structural Characteristics of SCP2 Proteins in Aedes aegypti Mosquitoes" Biochemistry 55, 4919-4927 (2016).
Assembly members:
entity, polymer, 111 residues, 11940.874 Da.
Natural source: Common Name: mosquitos Taxonomy ID: 7159 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Aedes aegypti
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MSVETIIERIKARVGAVDPN
GPRKVLGVFQLNIKTASGVE
QWIVDLKQLKVDQGVFASPD
VTVTVGLEDMLAISGKTLTV
GDALKQGKIELSGDADLAAK
LAEVIHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 355 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 752 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 111 residues - 11940.874 Da.
| 1 | MET | SER | VAL | GLU | THR | ILE | ILE | GLU | ARG | ILE | ||||
| 2 | LYS | ALA | ARG | VAL | GLY | ALA | VAL | ASP | PRO | ASN | ||||
| 3 | GLY | PRO | ARG | LYS | VAL | LEU | GLY | VAL | PHE | GLN | ||||
| 4 | LEU | ASN | ILE | LYS | THR | ALA | SER | GLY | VAL | GLU | ||||
| 5 | GLN | TRP | ILE | VAL | ASP | LEU | LYS | GLN | LEU | LYS | ||||
| 6 | VAL | ASP | GLN | GLY | VAL | PHE | ALA | SER | PRO | ASP | ||||
| 7 | VAL | THR | VAL | THR | VAL | GLY | LEU | GLU | ASP | MET | ||||
| 8 | LEU | ALA | ILE | SER | GLY | LYS | THR | LEU | THR | VAL | ||||
| 9 | GLY | ASP | ALA | LEU | LYS | GLN | GLY | LYS | ILE | GLU | ||||
| 10 | LEU | SER | GLY | ASP | ALA | ASP | LEU | ALA | ALA | LYS | ||||
| 11 | LEU | ALA | GLU | VAL | ILE | HIS | HIS | HIS | HIS | HIS | ||||
| 12 | HIS |
Samples:
sample_1: entity, [U-100% 15N], 0.7 mM; H2O 90%; D2O, [U-2H], 10%
sample_2: entity, [U-100% 13C; U-100% 15N], 0.7 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol, Koradi, Billeter and Wuthrich - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PSVS, Bhattacharya and Montelione - geometry optimization
SPARKY, Goddard - data analysis
TALOS, Cornilescu, Delaglio and Bax - data analysis
TOPSPIN, Bruker Biospin - collection
XEASY, Bartels et al. - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts