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 18735

Title: Solution NMR Structure of the DNA-Binding Domain of Human NF-E2-Related Factor 2, Northeast Structural Genomics Consortium (NESG) Target HR3520O

Deposition date: 2012-09-22 Original release date: 2012-11-21

Authors: Eletsky, Alexander; Pulavarti, Surya; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Pulavarti, Surya; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of the DNA-Binding Domain of Human NF-E2-Related Factor 2, Northeast Structural Genomics Consortium (NESG) Target HR3520O"  To be published ., .-..

Assembly members:
HR3520O, polymer, 90 residues, 10667.535 Da.

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

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

Entity Sequences (FASTA):
HR3520O: MGHHHHHHSHMKHSSRLEAH LTRDELRAKALHIPFPVEKI INLPVVDFNEMMSKEQFNEA QLALIRDIRRRGKNKVAAQN CRKRKLENIV

Data sets:
Data typeCount
13C chemical shifts358
15N chemical shifts86
1H chemical shifts589

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR3520O1

Entities:

Entity 1, HR3520O 90 residues - 10667.535 Da.

Residues 12-90 correspond to residues 445-523 of the native protein. Residues 1-11 represent a non-native affinity tag

1   METGLYHISHISHISHISHISHISSERHIS
2   METLYSHISSERSERARGLEUGLUALAHIS
3   LEUTHRARGASPGLULEUARGALALYSALA
4   LEUHISILEPROPHEPROVALGLULYSILE
5   ILEASNLEUPROVALVALASPPHEASNGLU
6   METMETSERLYSGLUGLNPHEASNGLUALA
7   GLNLEUALALEUILEARGASPILEARGARG
8   ARGGLYLYSASNLYSVALALAALAGLNASN
9   CYSARGLYSARGLYSLEUGLUASNILEVAL

Samples:

NC: HR3520O, [U-100% 13C; U-100% 15N], 0.5 mM; DSS 50 uM; sodium azide 0.02%; Arginine 50 mM; DTT 10 mM; ammonium acetate 50 mM

NC5: HR3520O, [5% 13C; U-100% 15N], 0.5 mM; DSS 50 uM; sodium azide 0.02%; Arginine 50 mM; DTT 10 mM; ammonium acetate 50 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D (H)CCH-TOCSY aliphaticNCisotropicsample_conditions_1
3D (H)CCH-COSY aliphaticNCisotropicsample_conditions_1
2D 1H-13C HSQC methylNC5isotropicsample_conditions_1
1D 15N T1NCisotropicsample_conditions_1
1D 15N T2NCisotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AS-DP v1.0, Huang, Tejero, Powers and Montelione - refinement

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

VNMRJ v2.2D, Varian - collection

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS v1.4, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

UNP Q16236
PDB
REF XP_002712351 XP_008257007 XP_008257008

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