Search

Determination of the Three-Dimensional Solution Structure of the C-Terminal Domain of CellobiohydrolOCe I from Trichodermi reesi. A Study using NMR and Hybrid distance Geometry-Dynamical Simulated Annealing.
Authors
Kraulis, P.J., Clore, G.MARIUS., Nilges, M., Jones, A., Petterson, G., Knowles, J., Gronenborn, A.M.
Assembly
cellobiohydrolase
Entity
1. cellobiohydrolase (polymer), 36 monomers, 3745.115 Da Detail

TQSHYGQCGG IGYSGPTVCA SGTTCQVLNP YYSQCL


Formula weight
3745.115 Da
Source organism
Trichoderma reesei QM6a
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 99.5 %, Completeness (bb): 98.7 % Detail

Polymer type: polypeptide(L)

Total1H
All99.5 % (189 of 190)99.5 % (189 of 190)
Backbone98.7 % (75 of 76)98.7 % (75 of 76)
Sidechain100.0 % (114 of 114)100.0 % (114 of 114)
Aromatic100.0 % (18 of 18)100.0 % (18 of 18)
Methyl100.0 % (15 of 15)100.0 % (15 of 15)

1. cellobiohydrolase

TQSHYGQCGG IGYSGPTVCA SGTTCQVLNP YYSQCL

Sample

Temperature 288 K, pH 3.9



Release date
1995-07-30
Citation
Determination of the Three-Dimensional Solution Structure of the C-Terminal Domain of CellobiohydrolOCe I from Trichodermi reesi. A Study using NMR and Hybrid distance Geometry-Dynamical Simulated Annealing
Kraulis, P.J., Clore, G.MARIUS., Nilges, M., Jones, A., Petterson, G., Knowles, J., Gronenborn, A.M.
Biochemistry (1989), 28, 7241-7257, DOI:
Related entities 1. cellobiohydrolase, : 1 : 10 : 1 : 9 : 100 entities Detail
Experiments performed 1 experiments Detail
Chemical shift validation 3 contents Detail