BMRB Entry 16766
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16766
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Title: Solution Structure of the human BLM HRDC domain PubMed: 20639533
Deposition date: 2010-03-04 Original release date: 2010-09-08
Authors: Kim, Young Mee; Choi, Byong-Seok
Citation: Kim, Young Mee; Choi, Byong-Seok. "Structure and function of the regulatory HRDC domain from human Bloom syndrome protein." Nucleic Acids Res. 38, 7764-7777 (2010).
Assembly members:
BLM HRDC domain, polymer, 85 residues, 9595.003 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 HRDC domain: QREEMVKKCLGELTEVCKSL
GKVFGVHYFNIFNTVTLKKL
AESLSSDPEVLLQIDGVTED
KLEKYGAEVISVLQKYSEWT
SPAED
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 373 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 624 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BLM HRDC domain | 1 |
Entities:
Entity 1, BLM HRDC domain 85 residues - 9595.003 Da.
| 1 | GLN | ARG | GLU | GLU | MET | VAL | LYS | LYS | CYS | LEU | ||||
| 2 | GLY | GLU | LEU | THR | GLU | VAL | CYS | LYS | SER | LEU | ||||
| 3 | GLY | LYS | VAL | PHE | GLY | VAL | HIS | TYR | PHE | ASN | ||||
| 4 | ILE | PHE | ASN | THR | VAL | THR | LEU | LYS | LYS | LEU | ||||
| 5 | ALA | GLU | SER | LEU | SER | SER | ASP | PRO | GLU | VAL | ||||
| 6 | LEU | LEU | GLN | ILE | ASP | GLY | VAL | THR | GLU | ASP | ||||
| 7 | LYS | LEU | GLU | LYS | TYR | GLY | ALA | GLU | VAL | ILE | ||||
| 8 | SER | VAL | LEU | GLN | LYS | TYR | SER | GLU | TRP | THR | ||||
| 9 | SER | PRO | ALA | GLU | ASP |
Samples:
sample_1: BLM HRDC domain, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; DTT 1 mM; HEPES 20 mM; sodium chloride 100 mM; sodium azide 0.02%
sample_2: BLM HRDC domain, [U-99% 13C; U-99% 15N], 1 mM; D2O 100%; DTT 1 mM; HEPES 20 mM; sodium chloride 100 mM; sodium azide 0.02%
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 11252 |
| PDB | |
| DBJ | BAG36927 BAH12008 BAH13907 |
| GB | AAA87850 AAH93622 AAI01568 AAI15031 AAI15033 |
| REF | NP_000048 NP_001274175 NP_001274176 NP_001274177 XP_001097543 |
| SP | P54132 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts