BMRB Entry 19530
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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/BMR19530
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Title: Resonance assignment of RQC domain of human Bloom syndrome protein PubMed: 24435566
Deposition date: 2013-09-25 Original release date: 2014-04-16
Authors: Ko, Junsang; Ryu, Kyoung-Seok; Choi, Byong-Seok
Citation: Park, Chin-Ju; Ko, Junsang; Ryu, Kyoung-Seok; Choi, Byong-Seok. "Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein." J. Biomol. NMR 58, 141-147 (2014).
Assembly members:
BLM_RQC, polymer, 144 residues, 16089.5 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):
BLM_RQC: CKTKDYKTRDVTDDVKSIVR
FVQEHSSSQGMRNIKHVGPS
GRFTMNMLVDIFLGSKSAKI
QSGIFGKGSAYSRHNAERLF
KKLILDKILDEDLYINANDQ
AIAYVMLGNKAQTVLNGNLK
VDFMETENSSSVKKQKALVA
KVSQ
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 796 |
| 13C chemical shifts | 324 |
| 15N chemical shifts | 120 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BLM RQC | 1 |
Entities:
Entity 1, BLM RQC 144 residues - 16089.5 Da.
| 1 | CYS | LYS | THR | LYS | ASP | TYR | LYS | THR | ARG | ASP | ||||
| 2 | VAL | THR | ASP | ASP | VAL | LYS | SER | ILE | VAL | ARG | ||||
| 3 | PHE | VAL | GLN | GLU | HIS | SER | SER | SER | GLN | GLY | ||||
| 4 | MET | ARG | ASN | ILE | LYS | HIS | VAL | GLY | PRO | SER | ||||
| 5 | GLY | ARG | PHE | THR | MET | ASN | MET | LEU | VAL | ASP | ||||
| 6 | ILE | PHE | LEU | GLY | SER | LYS | SER | ALA | LYS | ILE | ||||
| 7 | GLN | SER | GLY | ILE | PHE | GLY | LYS | GLY | SER | ALA | ||||
| 8 | TYR | SER | ARG | HIS | ASN | ALA | GLU | ARG | LEU | PHE | ||||
| 9 | LYS | LYS | LEU | ILE | LEU | ASP | LYS | ILE | LEU | ASP | ||||
| 10 | GLU | ASP | LEU | TYR | ILE | ASN | ALA | ASN | ASP | GLN | ||||
| 11 | ALA | ILE | ALA | TYR | VAL | MET | LEU | GLY | ASN | LYS | ||||
| 12 | ALA | GLN | THR | VAL | LEU | ASN | GLY | ASN | LEU | LYS | ||||
| 13 | VAL | ASP | PHE | MET | GLU | THR | GLU | ASN | SER | SER | ||||
| 14 | SER | VAL | LYS | LYS | GLN | LYS | ALA | LEU | VAL | ALA | ||||
| 15 | LYS | VAL | SER | GLN |
Samples:
sample_1: BLM RQC, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%; DTT 1 mM; Tris 20 mM; Sodium Chloride 100 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 900 MHz
Related Database Links:
| GB | NP_000048 .1 AAA87850 AAH93622 AAI01568 AAI15031 AAI15033 |
| PDB | |
| DBJ | BAG36927 BAH12008 BAH13907 |
| REF | NP_000048 NP_001274175 NP_001274177 XP_001097543 XP_003268551 |
| SP | P54132 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts