BMRB Entry 11361
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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/BMR11361
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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).
PubMed: 20826339
Assembly members:
zf-CW domain, polymer, 69 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.
H4 trimethyl K20 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 Vector: P060116-12
Entity Sequences (FASTA):
zf-CW domain: GSSGSSGEISGFGQCLVWVQ
CSFPNCGKWRRLCGNIDPSV
LPDNWSCDQNTDVQYNRCDI
PEETWTGLE
H4 trimethyl K20 peptide: SGRGKGGKGLGKGGAKRHRX
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 57 |
| 1H chemical shifts | 57 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | zf-CW domain | 1 |
| 2 | ZINC ION | 2 |
| 3 | H4 trimethyl K20 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, H4 trimethyl K20 peptide 20 residues - Formula weight is not available
| 1 | SER | GLY | ARG | GLY | LYS | GLY | GLY | LYS | GLY | LEU | |
| 2 | GLY | LYS | GLY | GLY | ALA | LYS | ARG | HIS | ARG | M3L |
Samples:
sample_1: zf-CW domain mM; H4 trimethyl K20 peptide mM; 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 11358 11359 11360 11362 |
| PDB | |
| DBJ | BAA91424 BAC04028 BAG62414 BAG63489 BAA19208 BAA21442 BAA85120 BAB08365 BAB09507 |
| EMBL | CAB66669 CAA17818 CAA24130 CAA24373 CAA24645 CAA24924 |
| GB | AAH02725 AIC60275 EAW76538 EAW76539 EAW76540 AAA20820 AAA20821 AAA30002 AAA30024 AAA30054 |
| REF | NP_001244937 NP_060454 XP_002803268 XP_003318693 XP_003318694 NP_001016869 NP_001029249 NP_001032932 NP_001032934 NP_001044729 |
| SP | Q9H0M4 P02309 P04915 P08436 P09322 P0CG89 |
| PIR | D56618 S11312 S21367 S68537 |
| PRF | 0901261A 0912198A 1202262E 1314298A 1707275C |
| TPE | CBF86829 CBF88885 |
| TPG | DAA07130 DAA10515 DAA13862 DAA16108 DAA16158 |
| AlphaFold | Q9H0M4 P02309 P04915 P08436 P09322 P0CG89 |
Download HSQC peak lists in one of the following formats:
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SPARKY: Backbone
or all simulated peaks