BMRB Entry 16927

Name: Solution structure of SuR18C from Streptococcus thermophilus. Northeast Structural Genomics Consortium Target SuR18C
Published: 2012-02-22

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PDB ID: 2kxy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16927
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 structure of SuR18C from Streptococcus thermophilus. Northeast Structural Genomics Consortium Target SuR18C

Deposition date:

2010-05-13

Original release date:

2012-02-22

Authors:

Liu, Yizhou; Lee, Hsiau-Wei; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Everett, John; Montelione, Gaetano; Prestegard, James

Citation:

Citation: Liu, Yizhou; Lee, Hsiau-Wei; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Everett, John; Montelione, Gaetano; Prestegard, James. "Chemical shift assignment for SuR18C from Streptococcus thermophilus, Northeast Structural Genomics Consortium Target SuR18C" .

Assembly members:

Assembly members:
protein sur18c, polymer, 100 residues, 11015.632 Da.

Natural source:

Natural source: Common Name: Streptococcus thermophilus Taxonomy ID: 1308 Superkingdom: Eubacteria Kingdom: not available Genus/species: Streptococcus thermophilus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein sur18c: KISLRKLSKSVPVKLELTGD KASNVSSISYSFDRGHVTIV GSQEAMDKIDSITVPVDISQ VTEDTSKTLELKAEGVTVQP STVKVNLKVTQKLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	386
15N chemical shifts	96
1H chemical shifts	617

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein sur18c	1

Entities:

Entity 1, protein sur18c 100 residues - 11015.632 Da.

1	LYS	ILE	SER	LEU	ARG	LYS	LEU	SER	LYS	SER
2	VAL	PRO	VAL	LYS	LEU	GLU	LEU	THR	GLY	ASP
3	LYS	ALA	SER	ASN	VAL	SER	SER	ILE	SER	TYR
4	SER	PHE	ASP	ARG	GLY	HIS	VAL	THR	ILE	VAL
5	GLY	SER	GLN	GLU	ALA	MET	ASP	LYS	ILE	ASP
6	SER	ILE	THR	VAL	PRO	VAL	ASP	ILE	SER	GLN
7	VAL	THR	GLU	ASP	THR	SER	LYS	THR	LEU	GLU
8	LEU	LYS	ALA	GLU	GLY	VAL	THR	VAL	GLN	PRO
9	SER	THR	VAL	LYS	VAL	ASN	LEU	LYS	VAL	THR
10	GLN	LYS	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	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
2D J-mod NH	sample_1	isotropic	sample_conditions_1
2D J-mod NCO	sample_1	isotropic	sample_conditions_1
2D J-mod NH	sample_1	anisotropic	sample_conditions_1
2D J-mod NCO	sample_1	anisotropic	sample_conditions_1

PDB	2KXY
EMBL	CCC20158 CDA39160
GB	AAV60886 AAV62796 ABJ66419 ADQ63244 AFJ83617
REF	WP_002951082 WP_011226156

BMRB Entry 16927

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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