BMRB Entry 11358

Title:
Assigned chemical shifts of the zf-CW domain with H3 peptide
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.
H3 peptide, polymer, 20 residues, Formula weight is not available

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
15N chemical shifts56
1H chemical shifts56

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zf-CW domain1
2ZINC ION2
3H3 peptide3

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

Entity 3, H3 peptide 20 residues - Formula weight is not available

1   ALAARGTHRLYSGLNTHRALAARGLYSSER
2   THRGLYGLYLYSALAPROARGLYSGLNLEU

Samples:

sample_1: zf-CW domain mM; H3 peptide 300 uM; 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 11359 11360 11361 11362 16694 16878 18385
PDB
DBJ BAA91424 BAC04028 BAG62414 BAG63489 BAA20144 BAA21441 BAA31218 BAA81840 BAA81841
EMBL CAB66669 CAA17819 CAA23780 CAA24375 CAA24647 CAA24952
GB AAH02725 AIC60275 EAW76538 EAW76539 EAW76540 AAA19824 AAA29441 AAA29965 AAA30003 AAA30026
REF NP_001244937 NP_060454 XP_002803268 XP_003318693 XP_003318694 NP_001005101 NP_001005464 NP_001013074 NP_001013721 NP_001014411
SP Q9H0M4 A1CP80 A1D240 A2QRR5 A2XHJ3 A2Y533
PIR A56580 A56618 A56654 I37460 I48113
PRF 0710252A 0806228A 1202262D 1202289A 1303352A
TPE CBF88887
TPG DAA07131 DAA10514 DAA16173 DAA16175 DAA16178
AlphaFold Q9H0M4 A2XHJ3 A2QRR5 A1D240 A1CP80 A2Y533

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