BMRB Entry 11361

Title:
Assigned chemical shifts of the zf-CW domain with H4 trimethyl K20 peptide   PubMed: 20826339
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).

Assembly members:

Assembly members:
zf-CW domain, polymer, 69 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.
H4 trimethyl K20 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:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P060116-12

Experimental source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P060116-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
zf-CW domain: GSSGSSGEISGFGQCLVWVQ CSFPNCGKWRRLCGNIDPSV LPDNWSCDQNTDVQYNRCDI PEETWTGLE
H4 trimethyl K20 peptide: SGRGKGGKGLGKGGAKRHRX

Data sets:
Data typeCount
15N chemical shifts57
1H chemical shifts57

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zf-CW domain1
2ZINC ION2
3H4 trimethyl K20 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, H4 trimethyl K20 peptide 20 residues - Formula weight is not available

1   SERGLYARGGLYLYSGLYGLYLYSGLYLEU
2   GLYLYSGLYGLYALALYSARGHISARGM3L

Samples:

sample_1: zf-CW domain mM; H4 trimethyl K20 peptide 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 11362
PDB
DBJ BAA91424 BAC04028 BAG62414 BAG63489 BAA19208 BAA21442 BAA85120 BAB08365 BAB09507
EMBL CAB66669 CAA17818 CAA24130 CAA24373 CAA24645 CAA24924
GB AAH02725 AIC60275 EAW76538 EAW76539 EAW76540 AAA20820 AAA20821 AAA30002 AAA30024 AAA30054
REF NP_001244937 NP_060454 XP_002803268 XP_003318693 XP_003318694 NP_001016869 NP_001029249 NP_001032932 NP_001032934 NP_001044729
SP Q9H0M4 P02309 P04915 P08436 P09322 P0CG89
PIR D56618 S11312 S21367 S68537
PRF 0901261A 0912198A 1202262E 1314298A 1707275C
TPE CBF86829 CBF88885
TPG DAA07130 DAA10515 DAA13862 DAA16108 DAA16158
AlphaFold P02309

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