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