Protherm

16
NO. 16
***** Sequence and structural information***** -
PROTEIN Ribonuclease HI
SOURCE Escherichia coli
LENGTH 155
MOL-WEIGHT 17582.93
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 1RBU
MUTATION K 95 N
MUTATED_CHAIN -
NO_MOLECULE 1
SEC.STR. Turn
ASA 137.0
***** Experimental condition ***** -
T -
pH 5.50
BUFFER_NAME Sodium acetate
BUFFER_CONC 20 mM
ION_NAME_1 -
ION_CONC_1 -
PROTEIN_CONC -
MEASURE CD
METHOD Thermal
***** Thermodynamic data ***** -
dG_H2O -
ddG_H2O -
dG -
ddG -
Tm 52.0
dTm 3.2
dHvH 90.0
dHcal -
m -
Cm -
dCp -
STATE -
REVERSIBILITY yes
ACTIVITY 90%
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