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Averaged NMR model of switch ARC, a double mutant of ARC repressor
Authors
Cordes, M.H.J., Walsh, N.P., McKnight, C.J., Sauer, R.T.
Assembly
ARC repressor
Entity
1. ARC repressor (polymer, Thiol state: not present), 64 monomers, 7686.672 Da Detail

MKGMSKMPQF LNRWPREVLD LVRKVAEENG RSVNSEIYQR VMESFKKEGR IGAHHHHHHK NQHE


Formula weight
7686.672 Da
Source organism
Salmonella virus P22
Exptl. method
NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 89.1 %, Completeness: 84.3 %, Completeness (bb): 87.0 % Detail

Polymer type: polypeptide(L)

Total1H15N
All84.3 % (415 of 492)84.1 % (355 of 422)85.7 % (60 of 70)
Backbone87.0 % (167 of 192)86.9 % (113 of 130)87.1 % (54 of 62)
Sidechain82.7 % (248 of 300)82.9 % (242 of 292)75.0 % (6 of 8)
Aromatic60.0 % (21 of 35)58.8 % (20 of 34)100.0 % (1 of 1)
Methyl95.5 % (21 of 22)95.5 % (21 of 22)

1. ARC Repressor

MKGMSKMPQF LNRWPREVLD LVRKVAEENG RSVNSEIYQR VMESFKKEGR IGAHHHHHHK NQHE

Sample
#NameIsotope labelingTypeConcentration
1ARC Repressor0.0 ~ 0.0 mM

Protein Blocks Logo
Calculated from 1 models in PDB: 1QTG, Strand ID: A, B Detail


Release date
2000-06-15
Citation
Evolution of a protein fold in vitro
Cordes, M.H.J., Walsh, N.P., McKnight, C.J., Sauer, R.T.
Science (1999), 284, 325-328, PubMed 10195898 , DOI: ,
Related entities 1. ARC repressor, : 1 : 1 : 13 entities Detail
nullKeywords beta sheet, right-handed helix, structural change