BMRB Entry 15701

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15701
MolProbity Validation Chart

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Title:
solution struture of human C-terminal domain of pirh2/Northeast Structural Genomics Consortium (NESG) target HT2C
Deposition date:
2008-03-31
Original release date:
2008-04-07
Authors:
Lemak, Alexander; Sheng, Yi; Karra, Murthy; Srisailam, Sampath; Laister, Rob; Duan, Shili; Arrowsmith, Cheryl
Citation:

Citation: Sheng, Yi; Laister, Rob; Lemak, Alexander; Wu, Bin; Tai, Elizabeth; Duan, 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:

Assembly members:
human_C-termal_doamin_of_pirh2, polymer, 79 residues, 5240.008 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21 (DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human_C-termal_doamin_of_pirh2: GSHMMHSALDMTRYWRQLDD EVAQTPMPSEYQNMTVDILC NDCNGRSTVQFHILGMKCKI CESYNTAQAGGRRISLDQQ

Data typeCount
13C chemical shifts308
15N chemical shifts72
1H chemical shifts497

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZINC ION2

Entities:

Entity 1, entity_1 79 residues - 5240.008 Da.

1   GLYSERHISMETMETHISSERALALEUASP
2   METTHRARGTYRTRPARGGLNLEUASPASP
3   GLUVALALAGLNTHRPROMETPROSERGLU
4   TYRGLNASNMETTHRVALASPILELEUCYS
5   ASNASPCYSASNGLYARGSERTHRVALGLN
6   PHEHISILELEUGLYMETLYSCYSLYSILE
7   CYSGLUSERTYRASNTHRALAGLNALAGLY
8   GLYARGARGILESERLEUASPGLNGLN

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_2: human C-termal doamin of pirh2, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; potassium chloride 150 mM; ZnCl2 10 uM; DTT 0.8 mM

sample_1: human C-termal doamin of pirh2, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; potassium chloride 150 mM; ZnCl2 10 uM; DTT 0.8 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C-Aromatic NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct, Huang, Tejero, Powers and Montelione - Validation

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAD92309 BAG52375 BAI46763
GB AAH15464 AAH47393 AAK96896 AAL09356 AAL76101
REF NP_001009922 NP_001090959 NP_001248474 NP_001265465 NP_001265466
SP Q96PM5
AlphaFold Q96PM5

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks