BMRB Entry 16251

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PDB ID: 2khq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16251
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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 a phage integrase SSP1947 fragment 59-159 from Staphylococcus saprophyticus, Northeast Structural Genomics Consortium Target SyR103B

Deposition date:

2009-04-10

Original release date:

2009-06-23

Authors:

Eletsky, Alexander; Mills, Jeffrey; Hua, Jia; Belote, Rachel; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, G; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Mills, Jeffrey; Hua, Jia; Belote, Rachel; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, G; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of a phage integrase SSP1947 fragment 59-159 from Staphylococcus saprophyticus" Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
syr103b_protein, polymer, 110 residues, 13529.361 Da.

Natural source:

Natural source: Common Name: Staphyloccus saprophyticus Taxonomy ID: 29385 Superkingdom: Bacteria Kingdom: not available Genus/species: staphylococcus saprophyticus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
syr103b_protein: MITFADYFYQWYEVNKLPHV SESTKRHYESAYKHIKDHFR HKLLKDIKRTEYQKFLNEYG LTHSYETIRKLNSYIRNAFD DAIHEGYVIKNPTYKAELHA SVLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	480
15N chemical shifts	118
1H chemical shifts	781

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	syr103b	1

Entities:

Entity 1, syr103b 110 residues - 13529.361 Da.

Residues 2-102 correspond to the 59-159 fragment of the native protein. Residues 103-110 represent a non-native affinity tag, and residue 1 is a result of a new transcription initiation site

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

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
2D 1H-13C CT-HSQC aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC	isotropic	sample_conditions_1
3D 1H-15N,13C NOESY	NC	isotropic	sample_conditions_1
3D 1H-13C NOESY	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
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
3D HCCH-COSY aliphatic	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY aliphatic	NC	isotropic	sample_conditions_1
3D HCCH-COSY aromatic	NC	isotropic	sample_conditions_1
2D 1H-15N LR-HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl	NC5	isotropic	sample_conditions_1
2D MEXICO	NC	isotropic	sample_conditions_1
2D CLEANEX	NC	isotropic	sample_conditions_1

PDB	2KHQ
DBJ	BAE19092
REF	WP_011303617 WP_019469479

BMRB Entry 16251

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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