BMRB

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 18191

Title: Solution structure of Sgf11(63-99) 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:
sgf11, polymer, 38 residues, 8599.688 Da.
ZN, 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):
sgf11: GKQQESSQYIHCENCGRDVS ANRLAAHLQRCLSRGARR

Data sets:
Data typeCount
13C chemical shifts144
15N chemical shifts45
1H chemical shifts232
heteronuclear NOE values36
T1 relaxation values36
T2 relaxation values36

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SGF111
2ZINC ION2

Entities:

Entity 1, SGF11 38 residues - 8599.688 Da.

1   GLYLYSGLNGLNGLUSERSERGLNTYRILE
2   HISCYSGLUASNCYSGLYARGASPVALSER
3   ALAASNARGLEUALAALAHISLEUGLNARG
4   CYSLEUSERARGGLYALAARGARG

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: sgf11, [U-99% 13C; U-98% 15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 75 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_conditions: ionic strength: 0.115 M; pH: 7.0; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions
2D 1H-1H COSYsample_1isotropicsample_conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions
3D HNCOsample_1isotropicsample_conditions
3D HNCAsample_1isotropicsample_conditions
3D HNCACBsample_1isotropicsample_conditions
3D HN(CO)CAsample_1isotropicsample_conditions
3D HCCH-TOCSYsample_1isotropicsample_conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions
3D HNCACOsample_1isotropicsample_conditions
2D 1H-15N HSQC R1 editedsample_1isotropicsample_conditions
2D 1H-15N HSQC R2 editedsample_1isotropicsample_conditions
2D 1H-15N heteronuclear NOEsample_1isotropicsample_conditions

Software:

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

Related Database Links:

PDB
DBJ GAA26924
EMBL CAY86913
GB AAB68174 AAS56656 AHY78128 AJP42096 AJV91186
REF NP_015278
SP A6ZWK1 B3LL20 Q03067
TPG DAA11383