BMRB Entry 11362

Title:
Assigned chemical shifts of the zf-CW domain in zinc finger CW-type PWWP domain protein 1
Deposition date:
2010-09-07
Original release date:
2011-01-04
Authors:
He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.
Citation:

Citation: He, Fahu; Umehara, Takashi; Saito, Kohei; Harada, Takushi; Watanabe, Satoru; Yabuki, Takashi; Kigawa, Takanori; Takahashi, Mari; Kuwasako, Kanako; Tsuda, Kengo; Matsuda, Takayoshi; Aoki, Masaaki; Seki, Eiko; Kobayashi, Naohiro; Guntert, Peter; Yokoyama, Shigeyuki; Muto, Yutaka. "Structural insight into the zinc finger CW domain as a histone modification reader."  Structure 18, 1127-1139 (2010).
PubMed: 20826339

Assembly members:

Assembly members:
zf-CW domain, polymer, 69 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: P060116-12

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts273
15N chemical shifts71
1H chemical shifts429

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zf-CW domain1
2ZINC ION2

Entities:

Entity 1, zf-CW domain 69 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUILESER
2   GLYPHEGLYGLNCYSLEUVALTRPVALGLN
3   CYSSERPHEPROASNCYSGLYLYSTRPARG
4   ARGLEUCYSGLYASNILEASPPROSERVAL
5   LEUPROASPASNTRPSERCYSASPGLNASN
6   THRASPVALGLNTYRASNARGCYSASPILE
7   PROGLUGLUTHRTRPTHRGLYLEUGLU

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zf-CW domain mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 50 uM; IDA 1 mM; 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 v0.9819, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 11115 11358 11359 11360 11361
PDB
DBJ BAA91424 BAC04028 BAG62414 BAG63489
EMBL CAB66669
GB AAH02725 AIC60275 EAW76538 EAW76539 EAW76540
REF NP_001244937 NP_060454 XP_002803268 XP_003318693 XP_003318694
SP Q9H0M4
AlphaFold Q9H0M4

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