BMRB Entry 15348
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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/BMR15348
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Title: Solution structure of the Bright/ARID domain from the human JARID1C protein. PubMed: 19636912
Deposition date: 2007-06-29 Original release date: 2007-12-10
Authors: Koehler, Christian; Bishop, Shurene; Dowler, Elizabeth; Diehl, Annette; Schmieder, Peter; Leidert, Martina; Sundstrom, Michael; Arrowsmith, Cheryl; Wiegelt, Johan; Edwards, Aled; Oschkinat, Hartmut; Ball, Linda
Citation: Koehler, Christian; Bishop, Shurene; Dowler, Elizabeth; Schmieder, Peter; Diehl, Anne; Oschkinat, Hartmut; Ball, Linda. "Backbone and sidechain 1H, 13C and 15N resonance assignments of the Bright/ARID domain from the human JARID1C (SMCX) protein" Biomol. NMR Assignments 2, 9-11 (2008).
Assembly members:
JARID1C, polymer, 117 residues, Formula weight is not available
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):
JARID1C: SMNELEAQTRVKLNYLDQIA
KFWEIQGSSLKIPNVERRIL
DLYSLSKIVVEEGGYEAICK
DRRWARVAQRLNYPPGKNIG
SLLRSHYERIVYPYEMYQSG
ANLVCNTRPFDNEEKDK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 432 |
15N chemical shifts | 124 |
1H chemical shifts | 828 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Bright/ARID domain | 1 |
Entities:
Entity 1, Bright/ARID domain 117 residues - Formula weight is not available
residues 1-2 are from the affinity tag
1 | SER | MET | ASN | GLU | LEU | GLU | ALA | GLN | THR | ARG | ||||
2 | VAL | LYS | LEU | ASN | TYR | LEU | ASP | GLN | ILE | ALA | ||||
3 | LYS | PHE | TRP | GLU | ILE | GLN | GLY | SER | SER | LEU | ||||
4 | LYS | ILE | PRO | ASN | VAL | GLU | ARG | ARG | ILE | LEU | ||||
5 | ASP | LEU | TYR | SER | LEU | SER | LYS | ILE | VAL | VAL | ||||
6 | GLU | GLU | GLY | GLY | TYR | GLU | ALA | ILE | CYS | LYS | ||||
7 | ASP | ARG | ARG | TRP | ALA | ARG | VAL | ALA | GLN | ARG | ||||
8 | LEU | ASN | TYR | PRO | PRO | GLY | LYS | ASN | ILE | GLY | ||||
9 | SER | LEU | LEU | ARG | SER | HIS | TYR | GLU | ARG | ILE | ||||
10 | VAL | TYR | PRO | TYR | GLU | MET | TYR | GLN | SER | GLY | ||||
11 | ALA | ASN | LEU | VAL | CYS | ASN | THR | ARG | PRO | PHE | ||||
12 | ASP | ASN | GLU | GLU | LYS | ASP | LYS |
Samples:
sample_1: JARID1C, [U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; DTT 5 mM
sample_2: JARID1C, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; DTT 5 mM
sample_3: JARID1C, [U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; DTT 5 mM
sample_4: JARID1C, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; DTT 5 mM
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 297 K
sample_conditions_2: pH*: 6.0; pressure: 1 atm; temperature: 297 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCCO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
(H)CC(CO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_2 | 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:
xwinnmr v2.6 and 3.1, Bruker Biospin - collection, processing
SPARKY v3.10, Goddard - chemical shift assignment, data analysis, peak picking
CYANA v2,0, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH v2.14, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - reffnement in explicit water, structure solution
TALOS, Cornilescu, Delaglio and Bax - dihedral angle estimation
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DMX 750 MHz
Related Database Links:
SWS | P41229 |
GB | NP_004178 GI:11321605 AAA61302 AAC48698 AAD53049 AAF36510 AAH26777 |
PDB | |
DBJ | BAB25462 BAE33367 BAE34464 BAG65494 BAK62496 |
EMBL | CAA82759 CAH91220 |
REF | NP_001041497 NP_001090902 NP_001125719 NP_001140174 NP_001269551 |
SP | A1YVX4 P41229 P41230 Q38JA7 |
TPG | DAA12808 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts