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Backbone 1H, 15N, and 13C Chemical Shifts of Myosin VI Medial Tail Domain
Authors
Barnes, C., Shen, Y., Ying, J., Takagi, Y., Torchia, D.A., Sellers, J.R., Bax, A.
Assembly
MT Domain
Entity
1. MT Domain (polymer, Thiol state: not present), 68 monomers, 8914.736 Da Detail

KQQEEEAERL RRIQEEMEKE RKRREEDEQR RRKEEEERRM KLEMEAKRKQ EEEERKKRED DEKRIQAE


Formula weight
8914.736 Da
Source organism
Sus scrofa
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.5 %, Completeness: 31.1 %, Completeness (bb): 64.2 % Detail

Polymer type: polypeptide(D)

Total1H13C15N
All31.1 % (275 of 883)16.5 % (82 of 497)40.4 % (126 of 312)90.5 % (67 of 74)
Backbone64.2 % (262 of 408)52.2 % (71 of 136)60.8 % (124 of 204)98.5 % (67 of 68)
Sidechain13.4 % (73 of 543) 3.0 % (11 of 361)35.2 % (62 of 176) 0.0 % (0 of 6)
Methyl13.6 % (3 of 22) 0.0 % (0 of 11)27.3 % (3 of 11)

1. MT Domain

KQQEEEAERL RRIQEEMEKE RKRREEDEQR RRKEEEERRM KLEMEAKRKQ EEEERKKRED DEKRIQAE

Sample #1

Solvent system 92% H2O/8% D2O, Pressure 1 atm, Temperature 273 K, pH 6.3, Details pH = 6.3, 20 C


#NameIsotope labelingTypeConcentration
1sodium phosphatenatural abundance20 mM
2EDTAnatural abundance2 mM
3MT Domain[U-13C; U-15N; U-2H]1 mM
Sample #2

Solvent system 92% H2O/8% D2O, Pressure 1 atm, Temperature 273 K, pH 6.3


#NameIsotope labelingTypeConcentration
4sodium phosphatenatural abundance20 mM
5EDTAnatural abundance2 mM
6MT Domain[U-100% 2H; U-100% 15N]1 mM

Release date
2019-03-13
Citation
Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy
Barnes, C., Shen, Y., Ying, J., Takagi, Y., Torchia, D.A., Sellers, J.R., Bax, A.
J. Am. Chem. Soc. (2019), 141, 9004-9017, PubMed 31117653 , DOI 10.1021/jacs.9b03116 ,
Related entities 1. MT Domain, : 1 : 2 : 2 : 1 : 31 entities Detail
Interaction partners 1. MT Domain, : 2 interactors Detail
Experiments performed 2 experiments Detail
Chemical shift validation 3 contents Detail