BMRB Entry 25622

Name: Backbone 1H, 13C, and 15N chemical shift assignments for the thioredoxin-like fold of the single mutant D91R of dimeric KaiB from the Thermosynechococcus elongatus BP-1 cyanobacterial species
Published: 2015-07-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25622

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H, 13C, and 15N chemical shift assignments for the thioredoxin-like fold of the single mutant D91R of dimeric KaiB from the Thermosynechococcus elongatus BP-1 cyanobacterial species

Deposition date:

2015-05-16

Original release date:

2015-07-14

Authors:

Chang, Yonggang; Cohen, Susan; Phong, Connie; Myers, William; Kim, Yong-Ick; Tseng, Roger; Lin, Jenny; Zhang, Li; Boyd, Joseph; Lee, Yvonne; Kang, Shannon; Lee, David; Li, Sheng; Britt, R.; Rust, Michael; Golden, Susan; LiWang, Andy

Citation:

Citation: Chang, Yonggang; Cohen, Susan; Phong, Connie; Myers, William; Kim, Yong-Ick; Tseng, Roger; Lin, Jenny; Zhang, Li; Boyd, Joseph; Lee, Yvonne; Kang, Shannon; Lee, David; Li, Sheng; Britt, R.; Rust, Michael; Golden, Susan; LiWang, Andy. "A Protein Fold Switch Joins the Circadian Oscillator to Clock Output in Cyanobacteria" Science 349, 324-328 (2015).
PubMed: 26113641

Assembly members:

Assembly members:
FTBN94YYD91RF_fs, polymer, 110 residues, Formula weight is not available

Natural source:

Natural source: Common Name: cyanobacteria Taxonomy ID: 146786 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermosynechococcus elongatus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FTBN94YYD91RF_fs: DYKDDDDKMAPLRKTAVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIGLRL LADYKDDDDK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	244
15N chemical shifts	77
1H chemical shifts	77

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KaiB D91R mutant, chain 1	1
2	KaiB D91R mutant, chain 2	1

Entities:

Entity 1, KaiB D91R mutant, chain 1 110 residues - Formula weight is not available

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 25622

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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