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 16998

Title: Solution NMR Structure of Transcription factor NF-E2 subunit's DNA binding domain from Homo sapiens, Northeast Structural Genomics Consortium

Deposition date: 2010-06-11 Original release date: 2010-07-09

Authors: Liu, Gaohua; Janjua, Haleema; Xiao, Rong; Ciccosanti, Colleen; Shastry, Ritu; Acton, Thomas; Everett, John; Montelione, Gaetano

Citation: Tong, Sai; Janjua, Haleema; Xiao, Rong; Ciccosanti, Colleen; Shastry, Ritu; Acton, T.; Everett, J.; Montelione, G.. "Solution NMR Structure of Transcription factor NF-E2 subunit's DNA binding domain from Homo sapiens, Northeast Structural Genomics Consortium"  To be published ., .-..

Assembly members:
HR4653B, polymer, 91 residues, 10567.291 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):
HR4653B: MGHHHHHHSHMAKPTARGEA GSRDERRALAMKIPFPTDKI VNLPVDDFNELLARYPLTES QLALVRDIRRRGKNKVAAQN YRKRKLETIVQ

Data sets:
Data typeCount
13C chemical shifts286
15N chemical shifts82
1H chemical shifts588

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR4653B1

Entities:

Entity 1, HR4653B 91 residues - 10567.291 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METALALYSPROTHRALAARGGLYGLUALA
3   GLYSERARGASPGLUARGARGALALEUALA
4   METLYSILEPROPHEPROTHRASPLYSILE
5   VALASNLEUPROVALASPASPPHEASNGLU
6   LEULEUALAARGTYRPROLEUTHRGLUSER
7   GLNLEUALALEUVALARGASPILEARGARG
8   ARGGLYLYSASNLYSVALALAALAGLNASN
9   TYRARGLYSARGLYSLEUGLUTHRILEVAL
10   GLN

Samples:

sample_NC: HR4653B, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 95%; D2O 5%

sample_nc5: HR4653B, [U-10% 13C; U-100% 15N], 1.1 mM; H2O 95%; D2O 5%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_nc5isotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
3D C(CO)NH TOCSYsample_NCisotropicsample_conditions_1
2D 1H-15N HSQC 22sample_NCisotropicsample_conditions_1
2D 1H-15N HSQC T1sample_NCisotropicsample_conditions_1
2D 1H-15N HSQC T2sample_NCisotropicsample_conditions_1
2D 1H-15N HSQC 1sample_nc5isotropicsample_conditions_1
2D 1H-15N HSQC 2sample_nc5isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_nc5isotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_conditions_1
3D HCCH-COSYsample_NCisotropicsample_conditions_1
HN NOE0sample_NCisotropicsample_conditions_1
HN NOE3sample_NCisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

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

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAF83244 BAF83253 BAG36023 BAG73448
EMBL CAG29280 CAH90396
GB AAA16118 AAA35612 AAB34115 AAH05044 AAP35952
REF NP_001014923 NP_001125194 NP_001129495 NP_001172081 NP_001181687
SP Q16621 Q5EAD3
TPG DAA30025

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