BMRB Entry 18167

Name: Solution Structure of Cyanobacterial PsbP (CyanoP) from Synechocystis sp. PCC 6803
Published: 2012-03-23

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PDB ID: 2lnj
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/BMR18167
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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 Cyanobacterial PsbP (CyanoP) from Synechocystis sp. PCC 6803

Deposition date:

2011-12-28

Original release date:

2012-03-23

Authors:

Jackson, Simon; Hinds, Mark; Eaton-Rye, Julian

Citation:

Citation: Jackson, Simon; Hinds, Mark; Eaton-Rye, Julian. "Solution structure of CyanoP from Synechocystis sp. PCC 6803: new insights on the structural basis for functional specialization amongst PsbP family proteins." Biochim. Biophys. Acta 1817, 1331-1338 (2012).
PubMed: 22414666

Assembly members:

Assembly members:
entity, polymer, 170 residues, 18744.742 Da.

Natural source:

Natural source: Common Name: Synechocystis sp. Taxonomy ID: 1143 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis sp.

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P-3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPLGSCGGVGIASLQRYSDT KDGYEFLYPNGWIGVDVKGA SPGVDVVFRDLIERDENLSV IISEIPSDKTLTDLGTATDV GYRFMKTVNDASQGDRQAEL INAEARDEDGQVYYTLEYRV LVGDNVERHDLASVTTNRGK LITFDLSTAEDRWDTVKSLF DTVASSFHVY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	647
15N chemical shifts	177
1H chemical shifts	1112

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PsbP	1

Entities:

Entity 1, PsbP 170 residues - 18744.742 Da.

There are 5 N-terminal vector derived residues (GPLGS). The sequence represents the enzymatically processed PsbP.

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

Samples:

sample_1: PsbP, [U-100% 15N], 0.4 mM; TCEP 5 mM; sodium phosphate 25 mM; sodium chloride 10 mM; H2O 95%; D2O 5%

sample_2: PsbP, [U-100% 13C; U-100% 15N], 0.4 mM; TCEP 5 mM; sodium phosphate 25 mM; sodium chloride 10 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.7; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2, Bruker Biospin - collection, processing

ANALYSIS, CCPN - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

PDB	2LNJ
DBJ	BAA18019 BAK50191 BAL29190 BAL32359 BAL35528
GB	AGF51707 ALJ67700
REF	WP_010872644

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

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