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Structural basis for homodimerization of the Src-associated during mitosis, 68 kD protein (Sam68) Qua1 domain
Authors
Meyer, N., Tripsianes, K., Vincendeaux, M., Madl, T., Kateb, F., Brack-werner, R., Sattler, M.
Assembly
Sam68 Qua1 domain
Entity
1. Sam68 Qua1 domain (polymer, Thiol state: not present), 41 monomers, 4605.219 × 2 Da Detail

GAMEPENKYL PELMAEKDSL DPSFTHAMQL LTAEIEKIQK G


Total weight
9210.438 Da
Max. entity weight
4605.219 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
CYANA, ARIA
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 96.7 %, Completeness (bb): 96.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All96.7 % (466 of 482)98.4 % (250 of 254)94.1 % (176 of 187)97.6 % (40 of 41)
Backbone96.2 % (231 of 240)98.8 % (80 of 81)94.2 % (114 of 121)97.4 % (37 of 38)
Sidechain97.5 % (274 of 281)98.3 % (170 of 173)96.2 % (101 of 105)100.0 % (3 of 3)
Aromatic100.0 % (22 of 22)100.0 % (11 of 11)100.0 % (11 of 11)
Methyl100.0 % (40 of 40)100.0 % (20 of 20)100.0 % (20 of 20)

1. KH DOMAIN-CONTAINING,RNA-BINDING,SIGNAL TRANSDUCTION-ASSOCIATED PROTEIN 1

GAMEPENKYL PELMAEKDSL DPSFTHAMQL LTAEIEKIQK G

Sample #1

Solvent system 90% water, 10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 1 mM uniformly 15N, 13C labeled Sam68 Qua1


#NameIsotope labelingTypeConcentration
1sam68 Qua1[U-100% 13C; U-100% 15N]1 mM
2H2Onatural abundance90 %
3D2Onatural abundance10 %
4NaClnatural abundance100 mM
5potassium phosphatenatural abundance20 mM
Sample #2

Solvent system 90% water, 10% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 6.500, Details 1 mM uniformly 13C, 15N labled Qua1 aligned with Pf-1 filamentous Phages


#NameIsotope labelingTypeConcentration
6sam68 Qua1[U-100% 13C; U-100% 15N]1 mM
7H2Onatural abundance90 %
8D2Onatural abundance10 %
9NaClnatural abundance100 mM
10potassium phosphatenatural abundance20 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 2XA6, Strand ID: A, B Detail


Release date
2010-07-25
Citation
Structural basis for homodimerization of the Src-associated during mitosis, 68-kDa protein (Sam68) Qua1 domain
Meyer, N., Tripsianes, K., Vincendeau, M., Madl, T., Kateb, F., Brack-Werner, R., Sattler, M.
J. Biol. Chem. (2010), 285, 28893-28901, PubMed 20610388 , DOI 10.1074/jbc.M110.126185 ,
Related entities 1. Sam68 Qua1 domain, : 1 : 2 : 98 entities Detail
Interaction partners 1. Sam68 Qua1 domain, : 102 interactors Detail
Experiments performed 13 experiments Detail
nullKeywords Alternative splicing, Sam68, Qua1, STAR proteins, CD44, structural biology, NMR, homodimer, TRANSCRIPTION, CELL CYCLE;