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NMR Study of Sso7d Mutant (F31A) Minimized Average Structure
Authors
CONSONNI, R., SANTOMO, L., ZETTA, L.
Assembly
SSO7D
Entity
1. SSO7D (polymer, Thiol state: not present), 62 monomers, 6943.006 Da Detail

ATVKFKYKGE EKQVDISKIK KVWRVGKMIS ATYDEGGGKT GRGAVSEKDA PKELLQMLEK QK


Formula weight
6943.006 Da
Source organism
Saccharolobus solfataricus
Exptl. method
NMR
Refine. method
SIMULATED ANNEALING
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 66.8 %, Completeness (bb): 97.7 % Detail

Polymer type: polypeptide(L)

Total1H
All66.8 % (267 of 400)66.8 % (267 of 400)
Backbone97.7 % (127 of 130)97.7 % (127 of 130)
Sidechain51.9 % (140 of 270)51.9 % (140 of 270)
Aromatic63.2 % (12 of 19)63.2 % (12 of 19)
Methyl75.9 % (22 of 29)75.9 % (22 of 29)

1. SSO7D

ATVKFKYKGE EKQVDISKIK KVWRVGKMIS ATYDEGGGKT GRGAVSEKDA PKELLQMLEK QK

Sample

Temperature 300 (±0.1) K


#NameIsotope labelingTypeConcentration
1SSO7D2.0 mM

Protein Blocks Logo
Calculated from 1 models in PDB: 1B4O, Strand ID: A Detail


Release date
2001-01-13
Citation
A single-point mutation in the extreme heat- and pressure-resistant sso7d protein from sulfolobus solfataricus leads to a major rearrangement of the hydrophobic core
Consonni, R., Santomo, L., Fusi, P., Tortora, P., Zetta, L.
Biochemistry (1999), 38, 12709-12717, PubMed 10504241 , DOI: ,
Related entities 1. SSO7D, : 1 : 6 : 59 entities Detail
Experiments performed 3 experiments Detail
nullKeywords RNASE and DNA-Binding Protein, Thermostable Ribonuclease, 3D-Structure, NMR, Sulfolobus Solfataricus