BMRB Entry 17396
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17396
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Title: 1H, 13C, and 15N Chemical Shift Assignments for FCS domain from human polyhomeotic homolog 1 PubMed: 21351738
Deposition date: 2011-01-06 Original release date: 2011-05-19
Authors: Ilangovan, Udayar; Kim, Chongwoo
Citation: Wang, Renjing; Ilangovan, Udayar; Leal, Belinda; Robinson, Angela; Amann, Barbara; Tong, Corey; Berg, Jeremy; Hinck, Andrew; Kim, Chongwoo. "Identification of Nucleic Acid Binding Residues in the FCS Domain of the Polycomb Group Protein Polyhomeotic." Biochemistry 50, 4998-5007 (2011).
Assembly members:
FCS_domain_of_hPh1, polymer, 49 residues, Formula weight is not available
ZN, non-polymer, 65.409 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):
FCS_domain_of_hPh1: GTRGVDSPSAELDKKANLLK
CEYCGKYAPAEQFRGSKRFC
SMTCAKRYN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 198 |
| 15N chemical shifts | 46 |
| 1H chemical shifts | 306 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Zn bound FCS domain of hPh1 | 1 |
| 2 | zinc ion | 2 |
Entities:
Entity 1, Zn bound FCS domain of hPh1 49 residues - Formula weight is not available
| 1 | GLY | THR | ARG | GLY | VAL | ASP | SER | PRO | SER | ALA | ||||
| 2 | GLU | LEU | ASP | LYS | LYS | ALA | ASN | LEU | LEU | LYS | ||||
| 3 | CYS | GLU | TYR | CYS | GLY | LYS | TYR | ALA | PRO | ALA | ||||
| 4 | GLU | GLN | PHE | ARG | GLY | SER | LYS | ARG | PHE | CYS | ||||
| 5 | SER | MET | THR | CYS | ALA | LYS | ARG | TYR | ASN |
Entity 2, zinc ion - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: Zn bound FCS domain of hPh1, [U-100% 15N], 1.5 mM; H2O 95%; D2O 5%
sample_2: Zn bound FCS domain of hPh1, [U-95% 13C; U-95% 15N], 1.5 mM; H2O 95%; D2O 5%
sample_3: Zn bound FCS domain of hPh1, [U-10% 13C; U-99% 15N], 1.5 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.050 M; pH: 6.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts