BMRB Entry 16794

Name: NMR Solution Structure of Q7A1E8 protein from Staphylococcus aureus: Northeast Structural Genomics Consortium target: ZR215
Published: 2012-08-03

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PDB ID: 2kvs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16794
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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:

NMR Solution Structure of Q7A1E8 protein from Staphylococcus aureus: Northeast Structural Genomics Consortium target: ZR215

Deposition date:

2010-03-28

Original release date:

2012-08-03

Authors:

Swapna, G.V.T.; Montelione, Alexander; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Rost, Burkhard; Everett, John; Montelione, Gaetano

Citation:

Citation: Swapna, G.V.T.; Montelione, Alexander; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Rost, Burkhard; Everett, John; Montelione, Gaetano. "NMR solution structure of Q7A1E8 protein from Staphylococcus aureus, Northeast Structural Genomics Consortium target: ZR215" .

Assembly members:

Assembly members:
ZR215, polymer, 80 residues, 9438.43 Da.

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Eubacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ZR215: MAGDPMTFYNFIMGFQNDNT PFGILAEHVSEDKAFPRLEE RHQVIRAYVMSNYTDHQLIE TTNRAISLYMANLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
coupling_constants
- coupling_constant_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	255
15N chemical shifts	79
1H chemical shifts	506

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ZR215	1

Entities:

Entity 1, ZR215 80 residues - 9438.43 Da.

Residues 1-5 represent the N-terminal tag and 73-80 represent the C-terminal hexa-His tag

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

BMRB Entry 16794

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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