BMRB Entry 19607
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19607
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Title: The C-terminal domain of SRA1p has a fold more similar to PRP18 than to an RRM and does not directly bind to the SRA1 RNA STR7 region. PubMed: 24486611
Deposition date: 2013-11-10 Original release date: 2014-02-10
Authors: Bilinovich, Stephanie; Davis, Caroline; Morris, Daniel; Ray, Louis; Prokop, Jeremy; Buchan, Greg; Leeper, Thomas
Citation: Bilinovich, Stephanie; Davis, Caroline; Morris, Daniel; Ray, Louis; Prokop, Jeremy; Buchan, Gregory; Leeper, Thomas. "The C-Terminal Domain of SRA1p Has a Fold More Similar to PRP18 than to an RRM and Does Not Directly Bind to the SRA1 RNA STR7 Region." J. Mol. Biol. ., .-. (2014).
Assembly members:
SRA1p_C-terminal_domain, polymer, 131 residues, 14769.870 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SRA1p_C-terminal_domain: GSEAVMEDVLRPLEQALEDC
RGHTRKQVCDDISRRLALLQ
EQWAGGKLSIPVKKRMALLV
QELSSHRWDAADDIHRSLMV
DHVTEVSQWMVGVKRLIAEK
RSLFSEEAANEEKSAATAEK
NHTIPGFQQAS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 536 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 789 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C-terminal domain of SRA1p | 1 |
Entities:
Entity 1, C-terminal domain of SRA1p 131 residues - 14769.870 Da.
| 1 | GLY | SER | GLU | ALA | VAL | MET | GLU | ASP | VAL | LEU | ||||
| 2 | ARG | PRO | LEU | GLU | GLN | ALA | LEU | GLU | ASP | CYS | ||||
| 3 | ARG | GLY | HIS | THR | ARG | LYS | GLN | VAL | CYS | ASP | ||||
| 4 | ASP | ILE | SER | ARG | ARG | LEU | ALA | LEU | LEU | GLN | ||||
| 5 | GLU | GLN | TRP | ALA | GLY | GLY | LYS | LEU | SER | ILE | ||||
| 6 | PRO | VAL | LYS | LYS | ARG | MET | ALA | LEU | LEU | VAL | ||||
| 7 | GLN | GLU | LEU | SER | SER | HIS | ARG | TRP | ASP | ALA | ||||
| 8 | ALA | ASP | ASP | ILE | HIS | ARG | SER | LEU | MET | VAL | ||||
| 9 | ASP | HIS | VAL | THR | GLU | VAL | SER | GLN | TRP | MET | ||||
| 10 | VAL | GLY | VAL | LYS | ARG | LEU | ILE | ALA | GLU | LYS | ||||
| 11 | ARG | SER | LEU | PHE | SER | GLU | GLU | ALA | ALA | ASN | ||||
| 12 | GLU | GLU | LYS | SER | ALA | ALA | THR | ALA | GLU | LYS | ||||
| 13 | ASN | HIS | THR | ILE | PRO | GLY | PHE | GLN | GLN | ALA | ||||
| 14 | SER |
Samples:
sample_1: sodium phosphate 50 mM; DTT 2 mM; sodium chloride 50 mM; SRA1p C-terminal domain, [U-98% 13C; U-98% 15N], 0.6 mM; H2O 95%; D2O 5%
sample_2: sodium phosphate 50 mM; DTT 2 mM; sodium chloride 50 mM; SRA1p C-terminal domain, [U-98% 13C; U-98% 15N], 0.6 mM; D2O 100%
sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3d HNCAintra | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACBintra | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCDHE | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.3, Linge, O, . - refinement, structure solution
CCPN, CCPN - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 750 MHz
Related Database Links:
| UNP | Q9HD15.1 |
| PDB | |
| DBJ | BAG51445 BAJ20657 |
| EMBL | CAH93286 |
| GB | AAG02114 AAG02115 AAG02116 AAH40043 AAI52789 |
| REF | NP_001030312 NP_001240693 XP_001086694 XP_001137717 XP_002816012 |
| SP | Q9HD15 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts