BMRB Entry 11347

Title:
Solution structure of the PHD domain in PHD finger protein 21A
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 the PHD domain in PHD finger protein 21A"  .

Assembly members:

Assembly members:
PHD domain, polymer, 56 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: P061030-12

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts224
15N chemical shifts50
1H chemical shifts347

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 56 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYHISGLUASP
2   PHECYSSERVALCYSARGLYSSERGLYGLN
3   LEULEUMETCYSASPTHRCYSSERARGVAL
4   TYRHISLEUASPCYSLEUASPPROPROLEU
5   LYSTHRILEPROLYSGLYMETTRPILECYS
6   PROARGCYSGLNASPGLN

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

1   ZN

Samples:

sample_1: PHD domain, [U-13C; U-15N], 1.0 mM; d-Tris-HCl 20 mM; NaCl 100 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 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9820, Kobayashi, N. - data analysis

CYANA v2.1, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB14492 BAB21787 BAC29735 BAC65327 BAC98234
EMBL CAH10542 CDQ58507
GB AAF64262 AAH15714 AAH19181 AAM09095 ABZ92334
REF NP_001095272 NP_001103160 NP_001103161 NP_001186576 NP_001193126
SP Q6ZPK0 Q96BD5
TPG DAA21793 DAA21794
AlphaFold Q6ZPK0 Q96BD5

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