Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15333
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Sheng, Yi; Laister, Rob; Lemak, Alexander; Wu, Bin; Tai, Elizabeth; Duran, Shili; Lukin, Jonathan; Sunnerhagen, Maria; Srisailam, Sampath; Karra, Murthy; Benchimol, Sam; Arrowsmith, Cheryl. "Molecular basis of Pirh2-mediated p53 ubiquitylation" Nat. Struct. Mol. Biol. 15, 1334-1342 (2008).
PubMed: 19043414
Assembly members:
Pirh2_RING_domain, polymer, 52 residues, 6007.025 Da.
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 Vector: pGEX
Entity Sequences (FASTA):
Pirh2_RING_domain: ENVSQQNCPICLEDIHTSRV
VAHVLPCGHLLHRTCYEEML
KEGYRCPLCMHS
Data type | Count |
13C chemical shifts | 215 |
15N chemical shifts | 49 |
1H chemical shifts | 345 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Pirh2 RING domain | 1 |
2 | ZINC ION, 1 | 2 |
3 | ZINC ION, 2 | 2 |
Entity 1, Pirh2 RING domain 52 residues - 6007.025 Da.
1 | GLU | ASN | VAL | SER | GLN | GLN | ASN | CYS | PRO | ILE | ||||
2 | CYS | LEU | GLU | ASP | ILE | HIS | THR | SER | ARG | VAL | ||||
3 | VAL | ALA | HIS | VAL | LEU | PRO | CYS | GLY | HIS | LEU | ||||
4 | LEU | HIS | ARG | THR | CYS | TYR | GLU | GLU | MET | LEU | ||||
5 | LYS | GLU | GLY | TYR | ARG | CYS | PRO | LEU | CYS | MET | ||||
6 | HIS | SER |
Entity 2, ZINC ION, 1 - Zn - 65.409 Da.
1 | ZN |
sample_2: Pirh2 RING domain, [U-13C; U-15N], 0.7 mM; sodium phosphate 25 mM; potassium chloride 150 mM; ZnCl2 10 uM; DTT, [U-99% 2H], 2 mM; D2O 10%
sample_1: Pirh2 RING domain, [U-13C; U-15N], 0.7 mM; sodium phosphate 25 mM; potassium chloride 150 mM; ZnCl2 10 uM; DTT, [U-99% 2H], 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 300 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C_aromatic NOESY | sample_2 | isotropic | sample_conditions_1 |
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PDB | |
DBJ | BAB31179 BAB31236 BAC37254 BAD92309 BAG52375 |
GB | AAH23138 AAH47393 AAH57143 AAH83739 AAK96896 |
REF | NP_001007619 NP_001248474 NP_001258726 NP_001265465 NP_001265467 |
SP | Q96PM5 Q9CR50 |
AlphaFold | Q96PM5 Q9CR50 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks