12 | |
NO. | 12 |
***** 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 | 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 | 6.8 |
dHvH | 90.4 |
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 |
RELATED_ENTRIES | 5,6,7,8,9,10,11,13,14,15,16,2143,2144,2145,2146,2147,2148,13174,13175,13176,13177,13178,13179,13180,13181,13182,13183,13939,13940,13941,13942,13943,13944 |