BMRB Entry 19013
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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/BMR19013
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Title: Solution structure of the RRM domain of the hypothetical protein CAGL0M09691g from Candida glabrata
Deposition date: 2013-02-07 Original release date: 2013-03-06
Authors: Harris, R.; Hillerich, B.; Ahmed, M.; Bonanno, J.; Chamala, S.; Evans, B.; Lafleur, J.; Hammonds, J.; Washington, E.; Stead, M.; Love, J.; Attonito, J.; Seidel, R.; Chook, Y.; Rout, M.; Girvin, M.; Almo, S.; Harris, R.; Hillerich, B.; Ahmed, M.; Bonanno, J.; Chamala, S.; Evans, B.; Lafleur, J.; Washington, E.; Stead, M.; Love, J.; Attonito, J.; Patel, H.; Seidel, R.; Chook, Y.; Rout, M.; Girvin, M.; Almo, S.
Citation: Harris, R.; Hillerich, B.; Ahmed, M.; Bonanno, J.; Chamala, S.; Evans, B.; Lafleur, J.; Hammonds, J.; Washington, E.; Stead, M.; Love, J.; Attonito, J.; Patel, H.; Seidel, R.; Chook, Y.; Rout, M.; Girvin, M.; Almo, S.. "Solution structure of the RRM domain of the hypothetical protein CAGL0M09691g from Candida glabrata" To be published ., .-..
Assembly members:
RRM_domain_of_the_hypothetical_protein, polymer, 124 residues, 14227.990 Da.
Natural source: Common Name: ascomycetes Taxonomy ID: 5478 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Candida glabrata
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RRM_domain_of_the_hypothetical_protein: MSLGSESETGNAVVVFGYRE
AITKQILAYFAQFGEILEDL
ESELGDTETMRTPGYFFQQA
PNRRRISREHGRTWTKLTYA
NHSSYLRALREHGTIYCGAA
IGCVPYKHELISELSREGHH
HHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 532 |
15N chemical shifts | 131 |
1H chemical shifts | 816 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RRM domain of the hypothetical protein | 1 |
Entities:
Entity 1, RRM domain of the hypothetical protein 124 residues - 14227.990 Da.
expressed sequence start-stop 171-283 N-term cloning artifact: MSL C-term cloning artifact: EGHHHHHH
1 | MET | SER | LEU | GLY | SER | GLU | SER | GLU | THR | GLY | ||||
2 | ASN | ALA | VAL | VAL | VAL | PHE | GLY | TYR | ARG | GLU | ||||
3 | ALA | ILE | THR | LYS | GLN | ILE | LEU | ALA | TYR | PHE | ||||
4 | ALA | GLN | PHE | GLY | GLU | ILE | LEU | GLU | ASP | LEU | ||||
5 | GLU | SER | GLU | LEU | GLY | ASP | THR | GLU | THR | MET | ||||
6 | ARG | THR | PRO | GLY | TYR | PHE | PHE | GLN | GLN | ALA | ||||
7 | PRO | ASN | ARG | ARG | ARG | ILE | SER | ARG | GLU | HIS | ||||
8 | GLY | ARG | THR | TRP | THR | LYS | LEU | THR | TYR | ALA | ||||
9 | ASN | HIS | SER | SER | TYR | LEU | ARG | ALA | LEU | ARG | ||||
10 | GLU | HIS | GLY | THR | ILE | TYR | CYS | GLY | ALA | ALA | ||||
11 | ILE | GLY | CYS | VAL | PRO | TYR | LYS | HIS | GLU | LEU | ||||
12 | ILE | SER | GLU | LEU | SER | ARG | GLU | GLY | HIS | HIS | ||||
13 | HIS | HIS | HIS | HIS |
Samples:
sample_1: RRM domain of the hypothetical protein, [U-100% 13C; U-100% 15N], 1.0 mM; sodium acetate 10 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 0.5 mM; H2O 90%; D2O 10%
sample_2: RRM domain of the hypothetical protein, [U-100% 13C; U-100% 15N], 1.0 mM; sodium acetate 10 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 110 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
15N HSQC | sample_1 | isotropic | sample_conditions_1 |
15N NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
13C HSQC | sample_2 | isotropic | sample_conditions_1 |
aromatic 13C HSQC | sample_2 | isotropic | sample_conditions_1 |
13C NOESY-HSQC | sample_2 | isotropic | sample_conditions_1 |
13C aromatic NOESY-HSQC | sample_2 | isotropic | sample_conditions_1 |
HNCO | sample_1 | isotropic | sample_conditions_1 |
HNCACO | sample_1 | isotropic | sample_conditions_1 |
HNCA | sample_1 | isotropic | sample_conditions_1 |
HNCOCA | sample_1 | isotropic | sample_conditions_1 |
HNCACB | sample_1 | isotropic | sample_conditions_1 |
CBCACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.21, Brunger A. T. et.al. - refinement
VNMRJ v2.2D, Varian - collection
TOPSPIN v2.1, Bruker Biospin - collection
MDDNMR v2.2, (MDDNMR) Orekhov, Jaravine, Kazimierczuk - collection, processing
CCPN_Analysis v2.2, CCPN - data analysis
ARIA v2.3, Linge, O, . - data analysis
X-PLOR NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Varian Inova 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts