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Solution structure of SelM from Mus musculus
Authors
Ferguson, A.D., Labunskyy, V.M., Fomenko, D.E., Arac, D., Chelliah, Y., Amezcua, C.A., Rizo, J., Gladyshev, V.N., Deisenhofer, J.
Assembly
Selenoprotein M
Entity
1. Selenoprotein M (polymer), 129 monomers, 15038.79 Da Detail

MTNYRPDWNR LRGLARGRVE TCGGCQLNRL KEVKAFVTED IQLYHNLVMK HLPGADPELV LLSRNYQELE RIPLSQMTRD EINALVQELG FYRKSAPEAQ VPPEYLWAPA KPPEEASEHD DLEHHHHHH


Formula weight
15038.79 Da
Entity Connection
disulfide 1 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1disulfidesing1:CYS22:SG1:CYS25:SG

Source organism
Mus musculus
Exptl. method
NMR
Refine. method
Distance geometry
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.1 %, Completeness: 90.8 %, Completeness (bb): 89.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All90.8 % (1394 of 1536)91.0 % (735 of 808)90.1 % (536 of 595)92.5 % (123 of 133)
Backbone89.9 % (678 of 754)90.2 % (229 of 254)89.2 % (340 of 381)91.6 % (109 of 119)
Sidechain91.7 % (830 of 905)91.3 % (506 of 554)92.0 % (310 of 337)100.0 % (14 of 14)
Aromatic76.7 % (92 of 120)76.7 % (46 of 60)75.9 % (44 of 58)100.0 % (2 of 2)
Methyl97.7 % (127 of 130)95.4 % (62 of 65)100.0 % (65 of 65)

1. Selenoprotein M

MTNYRPDWNR LRGLARGRVE TCGGCQLNRL KEVKAFVTED IQLYHNLVMK HLPGADPELV LLSRNYQELE RIPLSQMTRD EINALVQELG FYRKSAPEAQ VPPEYLWAPA KPPEEASEHD DLEHHHHHH

Sample

Pressure 1 atm, Temperature 298 K, pH 6


#NameIsotope labelingTypeConcentration
1Selenoprotein M[U-15N; U-13C]1 mM
2phosphate buffer50 mM
3H2O90 %
4D2O10 %

LACS Plot; CA
Referencing offset: -0.12 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.12 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: -0.02 ppm, Outliers: 3 Detail
LACS Plot; CO
Referencing offset: 0.23 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2A2P, Strand ID: A Detail


Release date
2005-12-27
Citation
NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family
Ferguson, A.D., Labunskyy, V.M., Fomenko, D.E., Arac, D., Chelliah, Y., Amezcua, C.A., Rizo, J., Gladyshev, V.N., Deisenhofer, J.
J. Biol. Chem. (2006), 281, 3536-3543, PubMed 16319061 , DOI 10.1074/jbc.M511386200 ,
Related entities 1. Selenoprotein M, : 1 : 1 : 6 entities Detail
Experiments performed 4 experiments Detail
nullKeywords Selenoprotein, Redox enzyme