BMRB Entry 11358
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11358
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Title: Assigned chemical shifts of the zf-CW domain with H3 peptide PubMed: 20826339
Deposition date: 2010-09-07 Original release date: 2011-01-04
Authors: He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.
Citation: He, Fahu; Umehara, Takashi; Saito, Kohei; Harada, Takushi; Watanabe, Satoru; Yabuki, Takashi; Kigawa, Takanori; Takahashi, Mari; Kuwasako, Kanako; Tsuda, Kengo; Matsuda, Takayoshi; Aoki, Masaaki; Seki, Eiko; Kobayashi, Naohiro; Guntert, Peter; Yokoyama, Shigeyuki; Muto, Yutaka. "Structural insight into the zinc finger CW domain as a histone modification reader." Structure 18, 1127-1139 (2010).
Assembly members:
zf-CW domain, polymer, 69 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.
H3 peptide, polymer, 20 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: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
zf-CW domain: GSSGSSGEISGFGQCLVWVQ
CSFPNCGKWRRLCGNIDPSV
LPDNWSCDQNTDVQYNRCDI
PEETWTGLE
H3 peptide: ARTKQTARKSTGGKAPRKQL
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 56 |
| 1H chemical shifts | 56 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | zf-CW domain | 1 |
| 2 | ZINC ION | 2 |
| 3 | H3 peptide | 3 |
Entities:
Entity 1, zf-CW domain 69 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | GLU | ILE | SER | ||||
| 2 | GLY | PHE | GLY | GLN | CYS | LEU | VAL | TRP | VAL | GLN | ||||
| 3 | CYS | SER | PHE | PRO | ASN | CYS | GLY | LYS | TRP | ARG | ||||
| 4 | ARG | LEU | CYS | GLY | ASN | ILE | ASP | PRO | SER | VAL | ||||
| 5 | LEU | PRO | ASP | ASN | TRP | SER | CYS | ASP | GLN | ASN | ||||
| 6 | THR | ASP | VAL | GLN | TYR | ASN | ARG | CYS | ASP | ILE | ||||
| 7 | PRO | GLU | GLU | THR | TRP | THR | GLY | LEU | GLU |
Entity 2, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Entity 3, H3 peptide 20 residues - Formula weight is not available
| 1 | ALA | ARG | THR | LYS | GLN | THR | ALA | ARG | LYS | SER | |
| 2 | THR | GLY | GLY | LYS | ALA | PRO | ARG | LYS | GLN | LEU |
Samples:
sample_1: zf-CW domain mM; H3 peptide 300 uM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 50 uM; IDA 1 mM; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20031121, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.9819, Kobayashi, N. - data analysis
CYANA v2.1, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| BMRB | 11115 11359 11360 11361 11362 16694 16878 18385 |
| PDB | |
| DBJ | BAA91424 BAC04028 BAG62414 BAG63489 BAA20144 BAA21441 BAA31218 BAA81840 BAA81841 |
| EMBL | CAB66669 CAA17819 CAA23780 CAA24375 CAA24647 CAA24952 |
| GB | AAH02725 AIC60275 EAW76538 EAW76539 EAW76540 AAA19824 AAA29441 AAA29965 AAA30003 AAA30026 |
| REF | NP_001244937 NP_060454 XP_002803268 XP_003318693 XP_003318694 NP_001005101 NP_001005464 NP_001013074 NP_001013721 NP_001014411 |
| SP | Q9H0M4 A1CP80 A1D240 A2QRR5 A2XHJ3 A2Y533 |
| PIR | A56580 A56618 A56654 I37460 I48113 |
| PRF | 0710252A 0806228A 1202262D 1202289A 1303352A |
| TPE | CBF88887 |
| TPG | DAA07131 DAA10514 DAA16173 DAA16175 DAA16178 |
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