BMRB Entry 11353

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11353
MolProbity Validation Chart

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Title:
Solution structure of PHD domain in inhibitor of growth protein 3 (ING3)
Deposition date:
2010-09-07
Original release date:
2011-09-07
Authors:
He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.
Citation:

Citation: He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.. "Solution structure of PHD domain in inhibitor of growth protein 3 (ING3)"  .

Assembly members:

Assembly members:
PHD domain, polymer, 70 residues, Formula weight is not available
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: cell free synthesis   Host organism: E. coli - cell free   Vector: P040705-02

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PHD domain: GSSGSSGYCICNQVSYGEMV GCDNQDCPIEWFHYGCVGLT EAPKGKWYCPQCTAAMKRRG SRHKSGPSSG

Data sets:
Data typeCount
13C chemical shifts265
15N chemical shifts64
1H chemical shifts399

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PHD domain1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, PHD domain 70 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTYRCYSILE
2   CYSASNGLNVALSERTYRGLYGLUMETVAL
3   GLYCYSASPASNGLNASPCYSPROILEGLU
4   TRPPHEHISTYRGLYCYSVALGLYLEUTHR
5   GLUALAPROLYSGLYLYSTRPTYRCYSPRO
6   GLNCYSTHRALAALAMETLYSARGARGGLY
7   SERARGHISLYSSERGLYPROSERSERGLY

Entity 2, ZINC ION no.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: PHD domain, [U-13C; U-15N], 0.8 mM; d-Tris-HCl 20 mM; NaCl 100 mM; ZnCl2 0.1 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio F. - processing

NMRView v5.0.4, Johnson B.A. - data analysis

Kujira v0.863, Kobayashi N. - data analysis

CYANA v2.0.17, Guntert P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 700 MHz

Related Database Links:

PDB
DBJ BAA90942 BAC38021 BAE43273 BAG57123 BAG73291
EMBL CAF90810 CAG31907 CAH90959 CAJ83008 CDQ78875
GB AAG12172 AAG23285 AAG23286 AAH05721 AAH18342
REF NP_001008672 NP_001025904 NP_001029279 NP_001080280 NP_001125551
SP Q498T3 Q5RBA1 Q5ZK36 Q66KD5 Q7ZX31
TPG DAA30453
AlphaFold Q498T3 Q5RBA1 Q5ZK36 Q66KD5 Q7ZX31

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