BMRB Entry 19229
Click here to enlarge.
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/BMR19229
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: PHD Domain from Human SHPRH PubMed: 23907177
Deposition date: 2013-05-07 Original release date: 2013-08-12
Authors: Machado, Luciana; Pustovalova, Yulia; Pozhidaeva, Alexandra; Almeida, Fabio; Bezsonova, Irina; Korzhnev, Dmitry
Citation: Machado, Luciana; Pustovalova, Yulia; Kile, Andrew; Pozhidaeva, Alexandra; Cimprich, Karlene; Almeida, Fabio; Bezsonova, Irina; Korzhnev, Dmitry. "PHD domain from human SHPRH." J. Biomol. NMR 56, 393-399 (2013).
Assembly members:
SHPRH, polymer, 73 residues, 7776.120 Da.
ZINC ION, 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):
SHPRH: GSPNSRVDFNTSDYRFECIC
GELDQIDRKPRVQCLKCHLW
QHAKCVNYDEKNLKIKPFYC
PHCLVAMEPVSTR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 285 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 467 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SHPRH | 1 |
| 2 | ZINC ION_1 | 2 |
| 3 | ZINC ION_2 | 2 |
Entities:
Entity 1, SHPRH 73 residues - 7776.120 Da.
| 1 | GLY | SER | PRO | ASN | SER | ARG | VAL | ASP | PHE | ASN | ||||
| 2 | THR | SER | ASP | TYR | ARG | PHE | GLU | CYS | ILE | CYS | ||||
| 3 | GLY | GLU | LEU | ASP | GLN | ILE | ASP | ARG | LYS | PRO | ||||
| 4 | ARG | VAL | GLN | CYS | LEU | LYS | CYS | HIS | LEU | TRP | ||||
| 5 | GLN | HIS | ALA | LYS | CYS | VAL | ASN | TYR | ASP | GLU | ||||
| 6 | LYS | ASN | LEU | LYS | ILE | LYS | PRO | PHE | TYR | CYS | ||||
| 7 | PRO | HIS | CYS | LEU | VAL | ALA | MET | GLU | PRO | VAL | ||||
| 8 | SER | THR | ARG |
Entity 2, ZINC ION_1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: HEPES, [U-100% 13C; U-100% 15N], 50 mM; sodium chloride 150 mM; ZINC ION 0.05 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 293 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 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 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 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.8, Keller and Wuthrich - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS v2.2, Cornilescu, Delaglio and Bax - prediction of backbone torsion angles
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
ABACUS v2.5, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization
Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis
CNS v2.5, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization
NMR spectrometers:
- Varian Avance 500 MHz
- Varian 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