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NMR structure of the C-terminal domain of pUL89
Authors
Couvreux, A., Hantz, S., Marquant, R., Champier, G., Alain, S., Morellet, N., Bouaziz, S.
Assembly
pUL89
Entity
1. pUL89 (polymer, Thiol state: not present), 68 monomers, 7907.834 Da Detail

DQNHIEQPFY LMGRDKALAV EQFISRFNSG YIKASQELVS YTIKLSHDPI EYLLEQIQNL HRVTLAEG


Formula weight
7907.834 Da
Exptl. method
solution NMR
Refine. method
distance geometry, simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 90.3 %, Completeness (bb): 97.1 % Detail

Polymer type: polypeptide(L)

Total1H
All90.3 % (389 of 431)90.3 % (389 of 431)
Backbone97.1 % (133 of 137)97.1 % (133 of 137)
Sidechain87.1 % (256 of 294)87.1 % (256 of 294)
Aromatic91.9 % (34 of 37)91.9 % (34 of 37)
Methyl80.0 % (32 of 40)80.0 % (32 of 40)

1. pUL89-Cter

DQNHIEQPFY LMGRDKALAV EQFISRFNSG YIKASQELVS YTIKLSHDPI EYLLEQIQNL HRVTLAEG

Sample

Solvent system 50% H2O / 50% acetonitril (v/v), Pressure 1 atm, Temperature 283 K, pH 3.2, Details 15N and 13C labelled amino acids L578, V587, V606, L620, L621 have been incorporated during chemical synthesis


#NameIsotope labelingTypeConcentration
1pUL89-Cternatural abundance0.8 mM
2H2Onatural abundance50 %
3acetonitrilnatural abundance50 %

Protein Blocks Logo
Calculated from 10 models in PDB: 2KN8, Strand ID: A Detail


Release date
2012-08-02
Citation
Identification of the interaction domain of the small terminase subunit pUL89 with the large subunit pUL56 of human cytomegalovirus
Thoma, C., Borst, E., Messerle, M., Rieger, M., Hwang, J., Bogner, E.
Biochemistry (2006), 45, 8855-8863, PubMed 16846228 , DOI 10.1021/bi0600796 ,
Related entities 1. pUL89, : 1 : 4 : 15 entities Detail
Experiments performed 6 experiments Detail
nullKeywords HCMV, NMR, pUL89, Terminase