BMRB Entry 15528
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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/BMR15528
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Title: Solution structure of the protease-resistent domain of Xenopus ePABP2 PubMed: 18824697
Deposition date: 2007-10-16 Original release date: 2007-10-19
Authors: Song, J.; Markley, J.
Citation: Song, Jikui; McGivern, Jered; Nichols, Karl; Markley, John; Sheets, Michael. "Structural basis for RNA recognition by a type II poly(A)-binding protein" Proc. Natl. Acad. Sci. U.S.A. 105, 15317-15322 (2008).
Assembly members:
ePABP2-trp, polymer, 124 residues, Formula weight is not available
Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus Laevis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ePABP2-trp: AIAPCMQTTHSKMTAGAYTE
GPPQPLSAEEKKEIDKRSVY
VGNVDYGSTAQDLEAHFSSC
GSINRITILCDKFSGHPKGY
AYIEFAERNSVDAAVAMDET
VFRGRTIKVLPKRTNMPGIS
STDR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 460 |
| 15N chemical shifts | 124 |
| 1H chemical shifts | 715 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protease-resistent domain, chain 1 | 1 |
| 2 | protease-resistent domain, chain 2 | 1 |
Entities:
Entity 1, protease-resistent domain, chain 1 124 residues - Formula weight is not available
| 1 | ALA | ILE | ALA | PRO | CYS | MET | GLN | THR | THR | HIS | ||||
| 2 | SER | LYS | MET | THR | ALA | GLY | ALA | TYR | THR | GLU | ||||
| 3 | GLY | PRO | PRO | GLN | PRO | LEU | SER | ALA | GLU | GLU | ||||
| 4 | LYS | LYS | GLU | ILE | ASP | LYS | ARG | SER | VAL | TYR | ||||
| 5 | VAL | GLY | ASN | VAL | ASP | TYR | GLY | SER | THR | ALA | ||||
| 6 | GLN | ASP | LEU | GLU | ALA | HIS | PHE | SER | SER | CYS | ||||
| 7 | GLY | SER | ILE | ASN | ARG | ILE | THR | ILE | LEU | CYS | ||||
| 8 | ASP | LYS | PHE | SER | GLY | HIS | PRO | LYS | GLY | TYR | ||||
| 9 | ALA | TYR | ILE | GLU | PHE | ALA | GLU | ARG | ASN | SER | ||||
| 10 | VAL | ASP | ALA | ALA | VAL | ALA | MET | ASP | GLU | THR | ||||
| 11 | VAL | PHE | ARG | GLY | ARG | THR | ILE | LYS | VAL | LEU | ||||
| 12 | PRO | LYS | ARG | THR | ASN | MET | PRO | GLY | ILE | SER | ||||
| 13 | SER | THR | ASP | ARG |
Samples:
sample_1: ePABP2-trp, [U-100% 13C; U-100% 15N], 1 mM; NaCl 100 mM; NaAc 10 mM
sample_2: ePABP2-trp, [U-100% 13C; U-100% 15N], 0.5 mM; ePABP2-trp 0.5 mM; NaCl 100 mM; NaAc 10 mM
sample_3: ePABP2-trp, [U-100% 15N], 0.5 mM; PEG 5%; NaCl 100 mM; NaAc 10 mM
sample_conditions_1: ionic strength: 100 mM; pH: 5.0; pressure: 1 atm; temperature: 308 K
sample_conditions_2: ionic strength: 100 mM; pH: 5.0; pressure: 1 atm; temperature: 302 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H,15N-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 1H,13C-HSQC | sample_1 | isotropic | sample_conditions_1 |
| HNCACB | sample_1 | isotropic | sample_conditions_1 |
| HCCONH | sample_1 | isotropic | sample_conditions_1 |
| CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| CCONH | sample_1 | isotropic | sample_conditions_1 |
| HCCHTOCSY | sample_1 | isotropic | sample_conditions_1 |
| HBACONH | sample_1 | isotropic | sample_conditions_1 |
| 13C-EDITED 1H,1H-NOESY (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 15N-EDITED 1H,1H-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 13C,15N filtered, 13C EDITED 1H,1H-NOESY | sample_2 | isotropic | sample_conditions_1 |
| 15N IPAP HSQC | sample_3 | anisotropic | sample_conditions_2 |
| 13C-EDITED 1H,1H-NOESY (arom) | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.17.0, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement
xwinnmr v3.5, Bruker - collection
NMRPipe v97.027.12.56, Delagio,F. et al. - processing
SPARKY v3.113, Goddard,T.D. and Kneller,D.G. - data analysis
GARANT v2.1, Bartels,C. et al - data analysis
CYANA v2.1, Guntert,P. et al - structural calculation
NMR spectrometers:
- Bruker DMX 750 MHz
- Varian INOVA 600 MHz
- Varian INOVA 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts