BMRB Entry 16398

Name: 1H, 13C and 15N Chemical Shift Assignment for the Psb27 Protein of Synechocystis PCC 6803
Published: 2009-11-16

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16398

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: 1H, 13C and 15N Chemical Shift Assignment for the Psb27 Protein of Synechocystis PCC 6803 PubMed: 19789994

Deposition date: 2009-07-08 Original release date: 2009-11-16

Authors: Cormann, Kai; Nowaczyk, Marc; Ikeuchi, Masahiko; Roegner, Matthias; Stoll, Raphael

Citation: Cormann, Kai; Ikeuchi, Masahiko; Rogner, Matthias; Nowaczyk, Marc; Stoll, Raphael. "Sequence-specific (1)H, (13)C, and (15)N backbone assignment of Psb27 from Synechocystis PCC 6803." Biomol NMR Assign 3, 247-249 (2009).

Assembly members:
Psb27, polymer, 110 residues, Formula weight is not available

Natural source: Common Name: Synechocystis sp. PCC 6803 Taxonomy ID: 1148 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis sp. PCC 6803

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

Entity Sequences (FASTA):
Psb27: CDSGTGLTGNYSQDTLTVIA TLREAIDLPQDAPNRQEVQD TARGQINDYISRYRRKGDAG GLKSFTTMQTALNSLAGYYT SYGARPIPEKLKKRLQLEFT QAERSIERGV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	379
15N chemical shifts	121
1H chemical shifts	614

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Psb27	1

Entities:

Entity 1, Psb27 110 residues - Formula weight is not available

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

Samples:

sample_1: Psb27, [U-15N], 1.0 mM; H2O 90%; D2O 10%; sodium phosphate buffer, pH 6.5 20 mM

sample_2: Psb27, [U-13C; U-15N], 0.9 mM; H2O 90%; D2O 10%; sodium phosphate buffer, pH 6.5 20 mM

sample_conditions_1: ionic strength: 40 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Bruker DRX 600 MHz

PDB	2KMF 2KND
DBJ	BAA11640 BAA18462 BAK50636 BAL29634 BAL32803
GB	AGF52149 ALJ68102
REF	WP_041425825
SP	P74367

Biological Magnetic Resonance Data Bank