BMRB Entry 17880
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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/BMR17880
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Title: 1H, 13C, and 15N Chemical Shift Assignments for a yeast protein PubMed: 22488857
Deposition date: 2011-08-23 Original release date: 2012-04-23
Authors: Wang, Tao
Citation: Wang, Tao; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming. "Solution structure of SWI1 AT-rich interaction domain from Saccharomyces cerevisiae and its nonspecific binding to DNA." Proteins 80, 1911-1917 (2012).
Assembly members:
yeast_protein, polymer, 125 residues, Formula weight is not available
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
yeast_protein: MQSLNPALQEKISTELNNKQ
YELFMKSLIENCKKRNMPLQ
SIPEIGNRKINLFYLYMLVQ
KFGGADQVTRTQQWSMVAQR
LQISDYQQLESIYFRILLPY
ERHMISQEGIKETQAKRLEH
HHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 303 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 485 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | yeast_protein | 1 |
Entities:
Entity 1, yeast_protein 125 residues - Formula weight is not available
| 1 | MET | GLN | SER | LEU | ASN | PRO | ALA | LEU | GLN | GLU | ||||
| 2 | LYS | ILE | SER | THR | GLU | LEU | ASN | ASN | LYS | GLN | ||||
| 3 | TYR | GLU | LEU | PHE | MET | LYS | SER | LEU | ILE | GLU | ||||
| 4 | ASN | CYS | LYS | LYS | ARG | ASN | MET | PRO | LEU | GLN | ||||
| 5 | SER | ILE | PRO | GLU | ILE | GLY | ASN | ARG | LYS | ILE | ||||
| 6 | ASN | LEU | PHE | TYR | LEU | TYR | MET | LEU | VAL | GLN | ||||
| 7 | LYS | PHE | GLY | GLY | ALA | ASP | GLN | VAL | THR | ARG | ||||
| 8 | THR | GLN | GLN | TRP | SER | MET | VAL | ALA | GLN | ARG | ||||
| 9 | LEU | GLN | ILE | SER | ASP | TYR | GLN | GLN | LEU | GLU | ||||
| 10 | SER | ILE | TYR | PHE | ARG | ILE | LEU | LEU | PRO | TYR | ||||
| 11 | GLU | ARG | HIS | MET | ILE | SER | GLN | GLU | GLY | ILE | ||||
| 12 | LYS | GLU | THR | GLN | ALA | LYS | ARG | LEU | GLU | HIS | ||||
| 13 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: yeast protein, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 100 mM; sodium phosphate 2 mM; EDTA 1.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker DMX 500 MHz
Related Database Links:
| PDB | |
| DBJ | GAA26956 |
| EMBL | CAA31013 CAY86943 |
| GB | AAB68089 AHY78155 AJP42124 AJV91214 AJV91652 |
| REF | NP_015309 |
| SP | P09547 |
| TPG | DAA11412 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts