BMRB Entry 25623

Name: Backbone 1H, 13C, and 15N chemical shift assignments for the double mutant G89A,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/BMR25623

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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 double mutant G89A,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:
FTeKaiBN94YYGD, polymer, 102 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):
FTeKaiBN94YYGD: DYKDDDDKMAPLRKTAVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIALRL LA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	271
15N chemical shifts	85
1H chemical shifts	85

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KaiB G89A D91R mutant, chain 1	1
2	KaiB G89A D91R mutant, chain 2	1

Entities:

Entity 1, KaiB G89A D91R mutant, chain 1 102 residues - Formula weight is not available

1

ASP

TYR

LYS

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

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

ASP

LYS

ILE

LEU

ALA

THR

8

PRO

THR

LEU

ALA

LYS

VAL

LEU

PRO

9

VAL

ARG

ILE

GLY

ASP

LEU

SER

ASN

10

ARG

GLU

LYS

VAL

LEU

ILE

ALA

LEU

ARG

LEU

11

LEU

ALA

Samples:

sample_1: FTeKaiBN94YYGD, [U-99% 13C; U-98% 15N], 800 uM; Tris 20 mM; NaCl 50 mM; DSS 10 uM; NaNa3 0.02%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

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

SPARKY, Goddard - data analysis

Mars, Young-Sang Jung and Markus Zweckstetter - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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