BMRB Entry 18735

Name: Solution NMR Structure of the DNA-Binding Domain of Human NF-E2-Related Factor 2, Northeast Structural Genomics Consortium (NESG) Target HR3520O
Published: 2012-11-21

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PDB ID: 2lz1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18735
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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:

Assembly members:
HR3520O, polymer, 90 residues, 10667.535 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: pET15_NESG

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	358
15N chemical shifts	86
1H chemical shifts	589

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR3520O	1

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	MET	GLY	HIS	HIS	HIS	HIS	HIS	HIS	SER	HIS
2	MET	LYS	HIS	SER	SER	ARG	LEU	GLU	ALA	HIS
3	LEU	THR	ARG	ASP	GLU	LEU	ARG	ALA	LYS	ALA
4	LEU	HIS	ILE	PRO	PHE	PRO	VAL	GLU	LYS	ILE
5	ILE	ASN	LEU	PRO	VAL	VAL	ASP	PHE	ASN	GLU
6	MET	MET	SER	LYS	GLU	GLN	PHE	ASN	GLU	ALA
7	GLN	LEU	ALA	LEU	ILE	ARG	ASP	ILE	ARG	ARG
8	ARG	GLY	LYS	ASN	LYS	VAL	ALA	ALA	GLN	ASN
9	CYS	ARG	LYS	ARG	LYS	LEU	GLU	ASN	ILE	VAL

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D (H)CCH-TOCSY aliphatic	NC	isotropic	sample_conditions_1
3D (H)CCH-COSY aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC methyl	NC5	isotropic	sample_conditions_1
1D 15N T1	NC	isotropic	sample_conditions_1
1D 15N T2	NC	isotropic	sample_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

UNP	Q16236
PDB	2LZ1
REF	XP_002712351 XP_008257007 XP_008257008
AlphaFold	Q96F71

1	MET	GLY	HIS	HIS	HIS	HIS	HIS	HIS	SER	HIS
2	MET	LYS	HIS	SER	SER	ARG	LEU	GLU	ALA	HIS
3	LEU	THR	ARG	ASP	GLU	LEU	ARG	ALA	LYS	ALA
4	LEU	HIS	ILE	PRO	PHE	PRO	VAL	GLU	LYS	ILE
5	ILE	ASN	LEU	PRO	VAL	VAL	ASP	PHE	ASN	GLU
6	MET	MET	SER	LYS	GLU	GLN	PHE	ASN	GLU	ALA
7	GLN	LEU	ALA	LEU	ILE	ARG	ASP	ILE	ARG	ARG
8	ARG	GLY	LYS	ASN	LYS	VAL	ALA	ALA	GLN	ASN
9	CYS	ARG	LYS	ARG	LYS	LEU	GLU	ASN	ILE	VAL

1	MET	GLY	HIS	HIS	HIS	HIS	HIS	HIS	SER	HIS
2	MET	LYS	HIS	SER	SER	ARG	LEU	GLU	ALA	HIS
3	LEU	THR	ARG	ASP	GLU	LEU	ARG	ALA	LYS	ALA
4	LEU	HIS	ILE	PRO	PHE	PRO	VAL	GLU	LYS	ILE
5	ILE	ASN	LEU	PRO	VAL	VAL	ASP	PHE	ASN	GLU
6	MET	MET	SER	LYS	GLU	GLN	PHE	ASN	GLU	ALA
7	GLN	LEU	ALA	LEU	ILE	ARG	ASP	ILE	ARG	ARG
8	ARG	GLY	LYS	ASN	LYS	VAL	ALA	ALA	GLN	ASN
9	CYS	ARG	LYS	ARG	LYS	LEU	GLU	ASN	ILE	VAL