Table 1.
Description of data in ProNAB with an example entry showing the binding affinity data of ‘Cysteine-tRNA ligase’ protein–RNA complex
| Description | Example |
|---|---|
| Entry id | 12197 |
| Protein Name | Cysteine–tRNA ligase |
| Synonyms | Cysteinyl–tRNA synthetase; CysRS |
| EC number | 6.1.1.16 |
| Protein Source | Escherichia coli (strain K12) |
| Sequence | MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVAFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVAMVDRMIAEMHKDFDALNILRPDMEPRATHHIAEIIELTEQLIAKGHAYVADNGDVMFDV… |
| Length | 461 |
| Mass (Da) | 52,202 |
| UniProt ID | P21888 |
| PROSITE ID | - |
| DisProt ID | - |
| PDB of Free Protein | 1LI5 |
| ASA of Free protein (Å2) | 29 |
| ProTherm Id | - |
| Mutation in protein | N351A |
| Nucleic acid Name | TRNA-cys |
| Nucleic acid Source | Synthetic |
| Type of Nuclei acid | RNA |
| Sequence | GGCGCGUUAACAAAGCGGUUAUGUAGCGGAUUGCAAAUCCGUCUAGUCCGGUUCGACUCCGGAAC…. |
| Mutation in Nucleic acid | G48C |
| Genbank ID | 56966181 |
| PDB Complex | 1U0B |
| NDB Complex | PR0135 |
| ASA of Complex (Å2) | 40 |
| Sec str | Coil |
| pH | 7.5 |
| Temperature (K) | 298 |
| Buffer | 20 mM Tris–Hcl |
| Ion name | 50 mM NaCl |
| Method | Fluorescence |
| K d wild (M) | 2.7 × 10–7 |
| K d mutant (M) | 8.16 × 10–6 |
| K a wild (M–1) | 4 × 106 |
| K a mutant (M–1) | 1 × 105 |
| ΔG wild (kcal/mol) | −8.96 |
| ΔG mutant (kcal/mol) | −6.94 |
| ΔΔG (kcal/mol) | 2.02 |
| ΔH wild (kcal/mol) | - |
| ΔH mutant (kcal/mol) | - |
| Stoichiometry | - |
| Reference | Nat Struct Mol Biol. 2004 Nov;11(11):1134–41. |
| Title | Shape-selective RNA recognition by cysteinyl-tRNA synthetase. |
| Authors | Hauenstein S, Zhang CM, Hou YM, Perona JJ |
| Keywords | CysRS; tRNA aminoacylation; elongation factor; |
| PubMed | 15489861 |
| DOI | http://dx.doi.org/10.1038/nsmb849 |
| Location of data | Table 2; Page No.: 1138 |
| Remarks | - |
| Related Entries | 12194; 12195; 12196 |