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Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker
Authors
Murphy, J.M., Hansen, D., Wiesner, S., Muhandiram, D., Borg, M., Smith, M.J., Sicheri, F., Kay, L.E., Forman-Kay, J.D., Pawson, T.
Assembly
CA150 FF1+linker
Entity
1. CA150 FF1+linker (polymer, Thiol state: not present), 71 monomers, 8559.810 Da Detail

GAMGSLEARM KQFKDMLLER GVSAFSTWEK ELHKIVFDPR YLLLNPKERK QVFDQYVKTR AEEERREKKN K


Formula weight
8559.81 Da
Source organism
Mus musculus
Exptl. method
solution NMR
Refine. method
simulated annealing, distance geometry
Data set
assigned_chemical_shifts
Chem. Shift Complete1
Sequence coverage: 98.6 %, Completeness: 77.6 %, Completeness (bb): 71.3 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All77.6 % (702 of 905)86.8 % (421 of 485)76.8 % (265 of 345)21.3 % (16 of 75)
Backbone71.3 % (301 of 422)95.8 % (137 of 143)70.5 % (148 of 210)23.2 % (16 of 69)
Sidechain85.1 % (469 of 551)83.0 % (284 of 342)91.1 % (185 of 203) 0.0 % (0 of 6)
Aromatic75.0 % (54 of 72)86.1 % (31 of 36)65.7 % (23 of 35) 0.0 % (0 of 1)
Methyl98.3 % (59 of 60)96.7 % (29 of 30)100.0 % (30 of 30)

1. CA150 FF1+linker

GAMGSLEARM KQFKDMLLER GVSAFSTWEK ELHKIVFDPR YLLLNPKERK QVFDQYVKTR AEEERREKKN K

Sample

Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 285 K, pH 6.5, Details 3D data collected for protein at 1-1.7mM in PBS pH 6.5


#NameIsotope labelingTypeConcentration
1CA150_FF1+linker[U-99% 13C; U-99% 15N]1.0 ~ 1.7 mM
2H20natural abundance95 %
3D20natural abundance5 %

Chem. Shift Complete2
Sequence coverage: 98.6 %, Completeness: 68.1 %, Completeness (bb): 63.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All68.1 % (1232 of 1810)85.8 % (832 of 970)45.2 % (312 of 690)58.7 % (88 of 150)
Backbone63.9 % (539 of 844)94.8 % (271 of 286)44.3 % (186 of 420)59.4 % (82 of 138)
Sidechain69.3 % (764 of 1102)80.8 % (553 of 684)50.5 % (205 of 406)50.0 % (6 of 12)
Aromatic56.3 % (81 of 144)79.2 % (57 of 72)32.9 % (23 of 70)50.0 % (1 of 2)
Methyl74.2 % (89 of 120)98.3 % (59 of 60)50.0 % (30 of 60)

1. CA150 FF1+linker

GAMGSLEARM KQFKDMLLER GVSAFSTWEK ELHKIVFDPR YLLLNPKERK QVFDQYVKTR AEEERREKKN K

Sample

Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 285 K, pH 6.5, Details 3D data collected for protein at 1-1.7mM in PBS pH 6.5


#NameIsotope labelingTypeConcentration
1CA150_FF1+linker[U-99% 13C; U-99% 15N]1.0 ~ 1.7 mM
2H20natural abundance95 %
3D20natural abundance5 %

Protein Blocks Logo
Calculated from 7 models in PDB: 2KIS, Strand ID: A Detail


Release date
2009-09-03
Citation
Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays
Murphy, J.M., Hansen, D., Wiesner, S., Muhandiram, D., Borg, M., Smith, M.J., Sicheri, F., Kay, L.E., Forman-Kay, J.D., Pawson, T.
J. Mol. Biol. (2009), 393, 409-424, PubMed 19715701 , DOI 10.1016/j.jmb.2009.08.049 ,
Related entities 1. CA150 FF1+linker, : 1 : 55 entities Detail
Interaction partners 1. CA150 FF1+linker, : 7 interactors Detail
Experiments performed 5 experiments Detail
nullKeywords extended helix, FF domain, interdomain dynamics, interdomain helix, linker peptide