BMRB Entry 25280

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25280

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Title:
1H, 13C, and 15N chemical shift assignments of mouse BMAL1 transactivation domain
Deposition date:
2014-10-10
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:
mBMAL1-TAD, polymer, 54 residues, 5624.217 Da.

Natural source:

Natural source:   Common Name: house 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):
mBMAL1-TAD: AMDPEFIGIDMIDNDQGSSS PSNDEAAMAVIMSLLEADAG LGGPVDFSDLPWPL

Data sets:
Data typeCount
13C chemical shifts200
15N chemical shifts49
1H chemical shifts309

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1mouse BMAL1 transactivation domain1

Entities:

Entity 1, mouse BMAL1 transactivation domain 54 residues - 5624.217 Da.

1   ALAMETASPPROGLUPHEILEGLYILEASP
2   METILEASPASNASPGLNGLYSERSERSER
3   PROSERASNASPGLUALAALAMETALAVAL
4   ILEMETSERLEULEUGLUALAASPALAGLY
5   LEUGLYGLYPROVALASPPHESERASPLEU
6   PROTRPPROLEU

Samples:

sample_1: mBMAL1-TAD, [U-100% 13C; U-100% 15N], 0.3 mM; D2O, [U-2H], 10%; H2O 90%; sodium chloride 50 mM; MES 10 mM

sample_2: mBMAL1-TAD, [U-100% 15N], 0.6 mM; D2O, [U-2H], 10%; H2O 90%; sodium chloride 50 mM; MES 10 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

Sparky, Goddard - chemical shift assignment

NMRView, Johnson, One Moon Scientific - data analysis

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

PSVS, Bhattacharya and Montelione - 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