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 18546

Title: Solution structure of the tandem zinc finger domain of fission yeast Stc1   PubMed: 23613586

Deposition date: 2012-06-22 Original release date: 2013-05-06

Authors: He, Chao; Shi, Yun; Bayne, Elizabeth; Wu, Hui

Citation: He, Chao; Pillai, Sreerekha; Taglini, Francesca; Li, Fudong; Ruan, Ke; Zhang, Jiahai; Wu, Jihui; Shi, Yunyu; Bayne, Elizabeth. "Structural analysis of Stc1 provides insights into the coupling of RNAi and chromatin modification."  Proc. Natl. Acad. Sci. U.S.A. 110, E1879-E1888 (2013).

Assembly members:
entity_1, polymer, 97 residues, 11085.919 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: fission yeast   Taxonomy ID: 4896   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Schizosaccharomyces pombe

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
entity_1: HMGKNDNDALIMCMRCRKVK GIDSYSKTQWSKTFTFVRGR TVSVSDPKVICRTCQPKQHD SIWCTACQQTKGINEFSKAQ RHVLDPRCQICVHSQRN

Data sets:
Data typeCount
13C chemical shifts385
15N chemical shifts105
1H chemical shifts649

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1tandem zinc finger domain of Stc11
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, tandem zinc finger domain of Stc1 97 residues - 11085.919 Da.

1   HISMETGLYLYSASNASPASNASPALALEU
2   ILEMETCYSMETARGCYSARGLYSVALLYS
3   GLYILEASPSERTYRSERLYSTHRGLNTRP
4   SERLYSTHRPHETHRPHEVALARGGLYARG
5   THRVALSERVALSERASPPROLYSVALILE
6   CYSARGTHRCYSGLNPROLYSGLNHISASP
7   SERILETRPCYSTHRALACYSGLNGLNTHR
8   LYSGLYILEASNGLUPHESERLYSALAGLN
9   ARGHISVALLEUASPPROARGCYSGLNILE
10   CYSVALHISSERGLNARGASN

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: sodium chloride 200 mM; Bis-Tris 20 mM; entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; ZINC ION 1.6 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

Molmol, Koradi, Billeter and Wuthrich - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

UNP O94276
PDB
EMBL CAA21813
REF NP_596535
SP O94276
AlphaFold O94276 O94276

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