BMRB Entry 25618

Name: Backbone 1H, 13C, and 15N chemical shift assignments for N-SasA, the N-terminal domain of SasA, from the Thermosynechococcus elongatus BP-1 cyanobacterial species
Published: 2015-07-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25618

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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 N-SasA, the N-terminal domain of SasA, from the Thermosynechococcus elongatus BP-1 cyanobacterial species

Deposition date:

2015-05-15

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:
FTeSasA16107P16AF, polymer, 108 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):
FTeSasA16107P16AF: DYKDDDDKALSLLLFVANRP GDEEETAAIQAHIQQLPSNF SFELKVVPIGEQPYLLEEYK LVATPALIKVRPEPRQTLAG RKLLQKVDYWWPRWQREVAL DYKDDDDK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	175
15N chemical shifts	79
1H chemical shifts	79

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-SasA	1

Entities:

Entity 1, N-SasA 108 residues - Formula weight is not available

1

ASP

TYR

LYS

ASP

LYS

ALA

LEU

2

SER

LEU

PHE

VAL

ALA

ASN

ARG

PRO

3

GLY

ASP

GLU

THR

ALA

ILE

GLN

4

ALA

HIS

ILE

GLN

LEU

PRO

SER

ASN

PHE

5

SER

PHE

GLU

LEU

LYS

VAL

PRO

ILE

GLY

6

GLU

GLN

PRO

TYR

LEU

GLU

TYR

LYS

7

LEU

VAL

ALA

THR

PRO

ALA

LEU

ILE

LYS

VAL

8

ARG

PRO

GLU

PRO

ARG

GLN

THR

LEU

ALA

GLY

9

ARG

LYS

LEU

GLN

LYS

VAL

ASP

TYR

TRP

10

TRP

PRO

ARG

TRP

GLN

ARG

GLU

VAL

ALA

LEU

11

ASP

TYR

LYS

ASP

LYS

Samples:

sample_1: N-SasA, [U-99% 13C; U-98% 15N], 450 uM; Protease Inhibitor Cocktail 450 uM; Tris 5 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

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