BMRB Entry 25638
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25638
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Title: NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1 PubMed: 26286320
Deposition date: 2015-05-26 Original release date: 2016-05-31
Authors: Mohanty, Biswaranjan; Silva, Ana; Mackay, Joel; Ryan, Daniel
Citation: Mohanty, Biswaranjan; Silva, Ana; Mackay, Joel; Ryan, Daniel. "1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1" Biomol. NMR Assign. 10, 31-34 (2016).
Assembly members:
entity, polymer, 108 residues, 12905.072 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):
entity: GPLGSLDQKTFSICKERMRP
VKAALKQLDRPEKGLSEREQ
LEHTRQCLIKIGDHITECLK
EYTNPEQIKQWRKNLWIFVS
KFTEFDARKLHKLYKHAIKK
RQESQQNS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 467 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 747 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 108 residues - 12905.072 Da.
| 1 | GLY | PRO | LEU | GLY | SER | LEU | ASP | GLN | LYS | THR | ||||
| 2 | PHE | SER | ILE | CYS | LYS | GLU | ARG | MET | ARG | PRO | ||||
| 3 | VAL | LYS | ALA | ALA | LEU | LYS | GLN | LEU | ASP | ARG | ||||
| 4 | PRO | GLU | LYS | GLY | LEU | SER | GLU | ARG | GLU | GLN | ||||
| 5 | LEU | GLU | HIS | THR | ARG | GLN | CYS | LEU | ILE | LYS | ||||
| 6 | ILE | GLY | ASP | HIS | ILE | THR | GLU | CYS | LEU | LYS | ||||
| 7 | GLU | TYR | THR | ASN | PRO | GLU | GLN | ILE | LYS | GLN | ||||
| 8 | TRP | ARG | LYS | ASN | LEU | TRP | ILE | PHE | VAL | SER | ||||
| 9 | LYS | PHE | THR | GLU | PHE | ASP | ALA | ARG | LYS | LEU | ||||
| 10 | HIS | LYS | LEU | TYR | LYS | HIS | ALA | ILE | LYS | LYS | ||||
| 11 | ARG | GLN | GLU | SER | GLN | GLN | ASN | SER |
Samples:
sample_1: CHD1-C, [U-98% 13C; U-98% 15N], 440 uM; Sodium phosphate 20 mM; NaCl 10 mM; DTT 1 mM; Sodium Azide 0.3%; DSS 0.3%; 1X protease inhibitor 0.1%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 10 mM; 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 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2, Bruker Biospin - data collection, processing
CARA v1.5.3, Keller and Wuthrich - chemical shift assignment, peak picking
UNIO v2.0.1, Herrmann and Wuthrich - NOE assignment, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation
OPALp v1.2, Koradi,Billeter and Guntert - Water refinement
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts