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Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form
Authors
Stott, K.M.
Assembly
E2plipD4 dimer
Entity
1. E2plipD4 dimer (polymer, Thiol state: not present), 85 monomers, 8878.252 × 2 Da Detail

MVKEVNVPDI VEVTEVMVKV GDKVAAEQSL ITVEGDKASM EVPAPFAGVV KELKVNVGDK VKTGSLIMIF EVEGAAPAAA PAKQE


Total weight
17756.504 Da
Max. entity weight
8878.252 Da
Source organism
Escherichia coli
Exptl. method
solution NMR
Refine. method
DGSA-distance geometry simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 88.2 %, Completeness: 81.0 %, Completeness (bb): 87.3 % Detail

Polymer type: polypeptide(L)

Total1H15N
All81.0 % (460 of 568)80.2 % (388 of 484)85.7 % (72 of 84)
Backbone87.3 % (219 of 251)86.5 % (148 of 171)88.7 % (71 of 80)
Sidechain76.0 % (241 of 317)76.7 % (240 of 313)25.0 % (1 of 4)
Aromatic100.0 % (10 of 10)100.0 % (10 of 10)
Methyl88.7 % (55 of 62)88.7 % (55 of 62)

1. E2plipD4

MVKEVNVPDI VEVTEVMVKV GDKVAAEQSL ITVEGDKASM EVPAPFAGVV KELKVNVGDK VKTGSLIMIF EVEGAAPAAA PAKQE

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0


#NameIsotope labelingTypeConcentration
1E2plipD4[U-15N]1 mM
2sodium phosphatenatural abundance20 mM
3TSPnatural abundance40 uM
4H2Onatural abundance90 %
5D2Onatural abundance10 %

Protein Blocks Logo
Calculated from 20 models in PDB: 2K7V, Strand ID: A, B Detail


Release date
2009-09-02
Citation
A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure
Stott, K.M., Yusof, A.M., Perham, R.N., Jones, D.D.
Structure (2009), 17, 1117-1127, PubMed 19679089 , DOI 10.1016/j.str.2009.07.001 ,
Related entities 1. E2plipD4 dimer, : 1 : 76 entities Detail
Interaction partners 1. E2plipD4 dimer, : 100 interactors Detail
Experiments performed 6 experiments Detail
NMR combined restraints 4 contents Detail
Keywords Misfolded dimer