BMRB Entry 26807

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26807

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
The DNA-binding domain of the human Egr-1 in the free state
Deposition date:
2016-05-25
Original release date:
2016-06-29
Authors:
Iwahara, Junji
Citation:

Citation: Esadze, Alexandre; Chen, Chuanying; Zandarashvili, Levani; Roy, Sourav; Pettitt, B. Montgomery; Iwahara, Junji. "Changes in conformational dynamics of basic side chains upon protein-DNA association"  Nucleic Acids Res. 44, 6961-6970 (2016).
PubMed: 27288446

Assembly members:

Assembly members:
The_Egr-1_zinc-finger_protein, polymer, 90 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET49b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
The_Egr-1_zinc-finger_protein: PERPYACPVESCDRRFSRSD ELTRHIRIHTGQKPFQCRIC MRNFSRSDHLTTHIRTHTGE KPFACDICGRKFARSDERKR HTKIHLRQKD

Data sets:
Data typeCount
13C chemical shifts368
15N chemical shifts110
1H chemical shifts549

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1The DNA-binding domain of the human Egr-1 protein1
2Zinc ion 12
3Zinc ion 22
4Zinc ion 32

Entities:

Entity 1, The DNA-binding domain of the human Egr-1 protein 90 residues - Formula weight is not available

1   PROGLUARGPROTYRALACYSPROVALGLU
2   SERCYSASPARGARGPHESERARGSERASP
3   GLULEUTHRARGHISILEARGILEHISTHR
4   GLYGLNLYSPROPHEGLNCYSARGILECYS
5   METARGASNPHESERARGSERASPHISLEU
6   THRTHRHISILEARGTHRHISTHRGLYGLU
7   LYSPROPHEALACYSASPILECYSGLYARG
8   LYSPHEALAARGSERASPGLUARGLYSARG
9   HISTHRLYSILEHISLEUARGGLNLYSASP

Entity 2, Zinc ion 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: The DNA-binding domain of the human Egr-1 protein, [U-99% 13C; U-99% 15N], 1 mM; Zinc ion 1 1 mM; Zinc ion 1 1 mM; Zinc ion 3 1 mM; potassium succinate, [U-99% 2H], 20 mM; potassium chloride 20 mM; Zinc chloride 0.1 mM

sample_conditions_1: ionic strength: 0.040 M; pH: 5.8; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D (H2C)N(CC)H-TOCSYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz

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