BMRB Entry 27626

Title:
1H, 13C, and 15N Chemical Shift Assignments for the SAH domain from mouse myosin 7a
Deposition date:
2018-09-25
Original release date:
2019-01-02
Authors:
Batchelor, Matthew; Peckham, Michelle
Citation:

Citation: Batchelor, Matthew; Wolny, Marcin; Baker, Emily; Paci, Emanuele; Kalverda, Arnout; Peckham, Michelle. "Dynamic ion pair behavior stabilizes single alpha-helices in proteins"  J. Biol. Chem. 294, 3219-3234 (2019).
PubMed: 30593502

Assembly members:

Assembly members:
M7A_SAH, polymer, 80 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: pET28a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts391
15N chemical shifts83
1H chemical shifts552

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1M7A SAH, 11
2M7A SAH, 21

Entities:

Entity 1, M7A SAH, 1 80 residues - Formula weight is not available

1   SERARGLEUARGVALGLUTYRGLNARGARG
2   LEUGLUALAGLUARGMETARGLEUALAGLU
3   GLUGLULYSLEUARGLYSGLUMETSERALA
4   LYSLYSALALYSGLUGLUALAGLUARGLYS
5   HISGLNGLUARGLEUALAGLNLEUALAARG
6   GLUASPALAGLUARGGLULEULYSGLULYS
7   GLUGLUALAARGARGLYSLYSGLULEULEU
8   GLUGLNMETGLULYSALAARGHISGLUTRP

Samples:

sample_1: M7A SAH, [U-100% 13C; U-100% 15N], 0.4 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 23.4 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D (HC)CO(CCO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

Analysis, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Ascend AEON 950 MHz
  • Bruker Avance 750 MHz
  • 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