BMRB Entry 16325

Name: Chemical shift assignments of the second domain of the listeria protein Lin2157, Northeast Structural Genomics Consortium target Lkr136b
Published: 2009-06-11

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PDB ID: 2kjk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16325
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:

Chemical shift assignments of the second domain of the listeria protein Lin2157, Northeast Structural Genomics Consortium target Lkr136b

Deposition date:

2009-05-29

Original release date:

2009-06-11

Authors:

Wang, Xu; Hamilton, Keith; Xiao, Rong; Lee, Dan; Ciccosanti, Colleen; Nair, R.; Rost, B.; Acton, T.; Swapna, G.; Everett, John; Montelione, Gaetano; Prestegard, James

Citation:

Citation: Wang, Xu; Montelione, Gaetano; Prestegard, James. "Solution Structure of Lkr136b" .

Assembly members:

Assembly members:
lkr136b, polymer, 100 residues, 11058 Da.

Natural source:

Natural source: Common Name: Listeria innocua Taxonomy ID: 1642 Superkingdom: Bacteria Kingdom: Firmicutes Genus/species: Listeria innocua

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET121

Entity Sequences (FASTA):

Entity Sequences (FASTA):
lkr136b: MVKVTYDGVYVLSVKEDVPA AGILHAGDLITEIDGQSFKS SQEFIDYIHSKKVGDTVKIK YKHGNKNEEASIKLTAIDKK GTPGIGITLVDDLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1

Data type	Count
13C chemical shifts	395
15N chemical shifts	92
1H chemical shifts	520
residual dipolar couplings	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	lkr136b	1

Entities:

Entity 1, lkr136b 100 residues - 11058 Da.

residues L93 to H100 are part of a His tag

1	MET	VAL	LYS	VAL	THR	TYR	ASP	GLY	VAL	TYR
2	VAL	LEU	SER	VAL	LYS	GLU	ASP	VAL	PRO	ALA
3	ALA	GLY	ILE	LEU	HIS	ALA	GLY	ASP	LEU	ILE
4	THR	GLU	ILE	ASP	GLY	GLN	SER	PHE	LYS	SER
5	SER	GLN	GLU	PHE	ILE	ASP	TYR	ILE	HIS	SER
6	LYS	LYS	VAL	GLY	ASP	THR	VAL	LYS	ILE	LYS
7	TYR	LYS	HIS	GLY	ASN	LYS	ASN	GLU	GLU	ALA
8	SER	ILE	LYS	LEU	THR	ALA	ILE	ASP	LYS	LYS
9	GLY	THR	PRO	GLY	ILE	GLY	ILE	THR	LEU	VAL
10	ASP	ASP	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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	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 HSQC/TROSY	sample_1	isotropic	sample_conditions_1
2D HSQC/TROSY	sample_2	anisotropic	sample_conditions_1

PDB	2KJK
EMBL	CAC97387
GB	EFR93256 EHN62540 KJR55152 KJR55498
REF	WP_003767762 WP_003769606 WP_010991039 WP_033532865

BMRB Entry 16325

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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