Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18192

Title: Solution structure of Sgf73(59-102) zinc finger domain

Authors: Gao, Xiaojun; Koehler, Christian; Bonnet, Jacques; Devys, Didier; Kieffer, Bruno

Citation: Koehler, Christian; Gao, Xiaojun; Bonnet, Jacques; Devys, Didier; Kieffer, Bruno. "Insights into the role of SGF11 and SGF73 for the interaction between SAGA and nucleosomes"  Not known ., .-..

Assembly members:
sgf73, polymer, 44 residues, 9567.000 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts175
15N chemical shifts44
1H chemical shifts270
heteronuclear NOE values33
T1 relaxation values33
T2 relaxation values33

Additional metadata:

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


Entity Assembly IDEntity NameEntity ID


Entity 1, SGF73 44 residues - 9567.000 Da.


Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN


sample_1: sgf73, [U-98% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; TCEP 0.05 mM; D2O 10%; H2O 90%

sample_3: sgf73, [U-99% 13C; U-98% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 75 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_2: sgf73, [U-98% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; TCEP 0.05 mM; D2O 100%

sample_conditions_1: ionic strength: 0.175 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.115 M; pH: 7.0; pressure: 1 atm; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_2
3D CBCA(CO)NHsample_3isotropicsample_conditions_2
3D HNCOsample_3isotropicsample_conditions_2
3D HNCAsample_3isotropicsample_conditions_2
3D HNCACBsample_3isotropicsample_conditions_2
3D HCCH-TOCSYsample_3isotropicsample_conditions_2
3D HNCACOsample_3isotropicsample_conditions_2
3D HN(CO)CAsample_3isotropicsample_conditions_2
2D 1H-1H NOESYsample_3isotropicsample_conditions_2
2D 1H-15N HSQC R1 editedsample_3isotropicsample_conditions_2
2D 1H-15N HSQC R2 editedsample_3isotropicsample_conditions_2
2D 1H-15N heteronuclear NOEsample_3isotropicsample_conditions_2


TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 950 MHz

Related Database Links:

DBJ GAA23323
EMBL CAA96770 CAY79696
GB AHY79310 AJP38728 AJR76048 AJR76549 AJR77046
REF NP_011449
SP P53165
TPG DAA08036