BMRB Entry 17212
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17212
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Title: 1H, 13C and 15N resonance assignment of Rap1 BRCT domain from Saccharomyces cerevisiae PubMed: 21187076
Deposition date: 2010-09-28 Original release date: 2011-03-30
Authors: Zhang, Wen; Zhang, Jiahai; Tu, Xiaoming
Citation: Zhang, Wen; Zhang, Jiahai; Zhang, Xuecheng; Xu, Chao; Tu, Xiaoming. "Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold." Biochem. Biophys. Res. Commun. 404, 1055-1059 (2011).
Assembly members:
Rap1_BRCT_domain, polymer, 106 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):
Rap1_BRCT_domain: MEKKEQVSGPPLSNMKFYLN
RDADAHDSLNDIDQLARLIR
ANGGEVLDSKPRESKENVFI
VSPYNHTNLPTVTPTYIKAC
CQSNSLLNMENYLVPYDNLE
HHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 344 |
15N chemical shifts | 89 |
1H chemical shifts | 487 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Rap1 BRCT domain | 1 |
Entities:
Entity 1, Rap1 BRCT domain 106 residues - Formula weight is not available
1 | MET | GLU | LYS | LYS | GLU | GLN | VAL | SER | GLY | PRO | ||||
2 | PRO | LEU | SER | ASN | MET | LYS | PHE | TYR | LEU | ASN | ||||
3 | ARG | ASP | ALA | ASP | ALA | HIS | ASP | SER | LEU | ASN | ||||
4 | ASP | ILE | ASP | GLN | LEU | ALA | ARG | LEU | ILE | ARG | ||||
5 | ALA | ASN | GLY | GLY | GLU | VAL | LEU | ASP | SER | LYS | ||||
6 | PRO | ARG | GLU | SER | LYS | GLU | ASN | VAL | PHE | ILE | ||||
7 | VAL | SER | PRO | TYR | ASN | HIS | THR | ASN | LEU | PRO | ||||
8 | THR | VAL | THR | PRO | THR | TYR | ILE | LYS | ALA | CYS | ||||
9 | CYS | GLN | SER | ASN | SER | LEU | LEU | ASN | MET | GLU | ||||
10 | ASN | TYR | LEU | VAL | PRO | TYR | ASP | ASN | LEU | GLU | ||||
11 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: sodium phosphate 20 mM; sodium chloride 100 mM; Rap1 BRCT domain 0.8 mM
sample_conditions_1: ionic strength: 0.12 M; pH: 6.5; pressure: 1 atm; temperature: 298 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 HNCO | 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 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, collection
NMR spectrometers:
- Bruker DMX 500 MHz
Related Database Links:
PDB | |
DBJ | GAA25889 |
EMBL | CAA55491 CAA96118 CAY82390 |
GB | AAA18404 AHY76889 AJP41127 AJT01564 AJT01934 |
REF | NP_014183 |
SP | P11938 |
TPG | DAA10340 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts