Protherm

11
NO. 11
***** Sequence and structural information***** -
PROTEIN Ribonuclease HI
SOURCE Escherichia coli
LENGTH 155
MOL-WEIGHT 17525.88
PIR_ID NRECH
SWISSPROT_ID RNH_ECOLI (P0A7Y4)
E.C.NUMBER EC 3.1.4.8
PMD.NO A920875
PDB_wild 2RN2
Homologous PDB Entries
PDB_mutant 1RBT
MUTATION K 95 G
MUTATED_CHAIN -
NO_MOLECULE 1
SEC.STR. Coil
ASA 137.0
***** Experimental condition ***** -
T -
pH 3.00
BUFFER_NAME glycine-HCl
BUFFER_CONC 10 mM
ION_NAME_1 -
ION_CONC_1 -
PROTEIN_CONC -
MEASURE CD
METHOD Thermal
***** Thermodynamic data ***** -
dG_H2O -
ddG_H2O -
dG -
ddG -
Tm 49.8
dTm 5.7
dHvH 102.4
dHcal -
m -
Cm -
dCp -
STATE -
REVERSIBILITY yes
ACTIVITY 120%
ACTIVITY_Km -
ACTIVITY_Kcat -
ACTIVITY_Kd -
***** Literature ***** -
KEY_WORDS structural stability; mutagenesis; free energy change;
thermostabilization; Escherichia coli ribonuclease HI
REFERENCE J BIOL CHEM 267, 22014-22017 (1992) PMID: 1331044
AUTHOR Kimura S., Kanaya S. & Nakamura H.
REMARKS T is the temperature (Tm) of wild type at which ddG was measured