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SMN Tudor Domain Structure and its Interaction with the Sm Proteins
Authors
Selenko, P., Sprangers, R., Stier, G., Buehler, D., Fischer, U., Sattler, M.
Assembly
SMN tudor domain
Entity
1. SMN tudor domain (polymer, Thiol state: all free), 91 monomers, 10048.91 Da Detail

GAMKKNTAAS LQQWKVGDKC SAIWSEDGCI YPATIASIDF KRETCVVVYT GYGNREEQNL SDLLSPICEV ANNIEQNAQE NENESQVSTD E


Formula weight
10048.91 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
mixed torsion and Cartesian angle dynamics simulated annealing protocol
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 70.3 %, Completeness: 58.7 %, Completeness (bb): 57.6 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All58.7 % (595 of 1013)61.3 % (322 of 525)54.0 % (207 of 383)62.9 % (66 of 105)
Backbone57.6 % (312 of 542)66.5 % (123 of 185)48.1 % (129 of 268)67.4 % (60 of 89)
Sidechain61.2 % (341 of 557)58.5 % (199 of 340)67.7 % (136 of 201)37.5 % (6 of 16)
Aromatic72.4 % (42 of 58)72.4 % (21 of 29)70.4 % (19 of 27)100.0 % (2 of 2)
Methyl64.4 % (58 of 90)64.4 % (29 of 45)64.4 % (29 of 45)

1. Survival of Motor Neurons protein

GAMKKNTAAS LQQWKVGDKC SAIWSEDGCI YPATIASIDF KRETCVVVYT GYGNREEQNL SDLLSPICEV ANNIEQNAQE NENESQVSTD E

Sample #1

Pressure 1 atm, Temperature 295 (±2) K, pH 6.3 (±0)


#NameIsotope labelingTypeConcentration
1Survival of Motor Neurons protein[U-100% 15N]1.0 mM
2sodium chloride20 mM
3phosphate buffer30 mM
4H2O95 %
5D2O5 %
Sample #2

Pressure 1 atm, Temperature 295 (±2) K, pH 6.3 (±0)


#NameIsotope labelingTypeConcentration
6Survival of Motor Neurons protein[U-100% 13C; U-100% 15N]1.0 mM
7sodium chloride20 mM
8phosphate buffer30 mM
9H2O95 %
10D2O5 %

LACS Plot; CA
Referencing offset: 0.16 ppm, Outliers: 4 Detail
LACS Plot; CB
Referencing offset: 0.16 ppm, Outliers: 4 Detail
LACS Plot; HA
Referencing offset: -0.09 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 10 models in PDB: 1G5V, Strand ID: A Detail


Release date
2001-05-02
Citation 1
SMN tudor domain structure and its interaction with the Sm proteins
Selenko, P., Sprangers, R., Stier, G., Buehler, D., Fischer, U., Sattler, M.
Nat. Struct. Biol. (2001), 8, 27-31, PubMed 11135666 , DOI 10.1038/83014 ,
Citation 2
NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , DOI 10.1007/bf00197809 ,
Citation 3
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
Bartels, C., Xia, T., Billeter, M., Guntert, P., Wuthrich, K.
J. Biomol. NMR (1995), 6, 1-10, PubMed , DOI:
Citation 4
Crystallography & NMR system: A new software suite for macromolecular structure determination
Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., Read, R.J., Rice, L.M., Simonson, T., Warren, G.L.
Acta Crystallogr. D. Biol. Crystallogr. (1998), 54, 905-921, PubMed 9757107 , DOI 10.1107/s0907444998003254 ,
Related entities 1. SMN tudor domain, : 1 : 16 entities Detail
Interaction partners 1. SMN tudor domain, : 161 interactors Detail
Experiments performed 9 experiments Detail
nullKeywords SMA, Sm interacting protein, SMN, splicing, software, spectrum analysis, Structure analysis, Structure calculation