BMRB Entry 25549

Name: 1H, 13C, 15N backbone chemical shift assignments of mouse BMAL2 transactivation domain
Published: 2015-04-27

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25549

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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:

1H, 13C, 15N backbone chemical shift assignments of mouse BMAL2 transactivation domain

Deposition date:

2015-03-23

Original release date:

2015-04-27

Authors:

Lee, Hsiau-Wei; Gustafson, Chelsea; Parsley, Nicole; Partch, Carrie

Citation:

Citation: Xu, Haiyan; Guftafson, Chelsea; Sammons, Patrick; Khan, Sanjoy; Parsley, Nicole; Ramanathan, Chidambaram; Lee, Hsiau-Wei; Liu, Andrew; Partch, Carrie. "Cryptochrome 1 regulates the circadian clock through dynamic interactions with the BMAL1 C terminus" Nat. Struct. Mol. Biol. 22, 476-484 (2015).
PubMed: 25961797

Assembly members:

Assembly members:
mBMAL2-TAD, polymer, 46 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mBMAL2-TAD: AMDPEFLGFDVLCDSDSIDM AAFMNYLEAEGGLGDPGDFS DIQWAL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	84
15N chemical shifts	41
1H chemical shifts	41

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mBMAL2-TAD	1

Entities:

Entity 1, mBMAL2-TAD 46 residues - Formula weight is not available

1

ALA

MET

ASP

PRO

GLU

PHE

LEU

GLY

PHE

ASP

2

VAL

LEU

CYS

ASP

SER

ASP

SER

ILE

ASP

MET

3

ALA

PHE

MET

ASN

TYR

LEU

GLU

ALA

GLU

4

GLY

LEU

GLY

ASP

PRO

GLY

ASP

PHE

SER

5

ASP

ILE

GLN

TRP

ALA

LEU

Samples:

sample_1: mBMAL2-TAD, [U-100% 13C; U-100% 15N], 0.3 mM; MES 10 mM; NaCl 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

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