BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11352

Title: Solution structure of PHD domain in inhibitor of growth family, member 1-like

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: He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.. "Solution structure of PHD domain in inhibitor of growth family, member 1-like"  .

Assembly members:
PHD domain, polymer, 71 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P030408-27

Entity Sequences (FASTA):
PHD domain: GSSGSSGEFAIDPNEPTYCL CNQVSYGEMIGCDNEQCPIE WFHFSCVSLTYKPKGKWYCP KCRGDSGPSSG

Data sets:
Data typeCount
13C chemical shifts293
15N chemical shifts66
1H chemical shifts427

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

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

Entities:

Entity 1, PHD domain 71 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUPHEALA
2   ILEASPPROASNGLUPROTHRTYRCYSLEU
3   CYSASNGLNVALSERTYRGLYGLUMETILE
4   GLYCYSASPASNGLUGLNCYSPROILEGLU
5   TRPPHEHISPHESERCYSVALSERLEUTHR
6   TYRLYSPROLYSGLYLYSTRPTYRCYSPRO
7   LYSCYSARGGLYASPSERGLYPROSERSER
8   GLY

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: 293 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, 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 800 MHz

Related Database Links:

PDB
GB ERE88163
REF XP_004657164 XP_006099431 XP_006772779 XP_008150109 XP_014320366

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