BMRB Entry 18192
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18192
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of Sgf73(59-102) zinc finger domain
Deposition date: 2012-01-10 Original release date: 2012-03-23
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):
sgf73: NPNAQLIEDPLDKPIQYRVC
EKCGKPLALTAIVDHLENHC
AGAS
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
Data type | Count |
13C chemical shifts | 175 |
15N chemical shifts | 44 |
1H chemical shifts | 270 |
heteronuclear NOE values | 33 |
T1 relaxation values | 33 |
T2 relaxation values | 33 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SGF73 | 1 |
2 | ZINC ION | 2 |
Entities:
Entity 1, SGF73 44 residues - 9567.000 Da.
1 | ASN | PRO | ASN | ALA | GLN | LEU | ILE | GLU | ASP | PRO | ||||
2 | LEU | ASP | LYS | PRO | ILE | GLN | TYR | ARG | VAL | CYS | ||||
3 | GLU | LYS | CYS | GLY | LYS | PRO | LEU | ALA | LEU | THR | ||||
4 | ALA | ILE | VAL | ASP | HIS | LEU | GLU | ASN | HIS | CYS | ||||
5 | ALA | GLY | ALA | SER |
Entity 2, ZINC ION - Zn - 65.409 Da.
1 | ZN |
Samples:
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
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H COSY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_2 |
3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_2 |
3D HNCO | sample_3 | isotropic | sample_conditions_2 |
3D HNCA | sample_3 | isotropic | sample_conditions_2 |
3D HNCACB | sample_3 | isotropic | sample_conditions_2 |
3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_2 |
3D HNCACO | sample_3 | isotropic | sample_conditions_2 |
3D HN(CO)CA | sample_3 | isotropic | sample_conditions_2 |
2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_2 |
2D 1H-15N HSQC R1 edited | sample_3 | isotropic | sample_conditions_2 |
2D 1H-15N HSQC R2 edited | sample_3 | isotropic | sample_conditions_2 |
2D 1H-15N heteronuclear NOE | sample_3 | isotropic | sample_conditions_2 |
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
- Bruker Avance 950 MHz
Related Database Links:
PDB | |
DBJ | GAA23323 |
EMBL | CAA96770 CAY79696 |
GB | AHY79310 AJP38728 AJR76048 AJR76549 AJR77046 |
REF | NP_011449 |
SP | P53165 |
TPG | DAA08036 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts