Difference between revisions of "Part:BBa K2740016"
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<partinfo>BBa_K2740016 parameters</partinfo> | <partinfo>BBa_K2740016 parameters</partinfo> | ||
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| + | <h2>Parameter of Protein </h2> | ||
| + | <p align="left">Number of amino acids: 453</p> | ||
| + | <p align="left">Molecular weight: 49636.54</p> | ||
| + | <p align="left">Theoretical pI: 6.00</p> | ||
| + | <p align="left">Amino acid composition: <br /> | ||
| + | Ala (A) 39 8.6%<br /> | ||
| + | Arg (R) 29 6.4%<br /> | ||
| + | Asn (N) 11 2.4%<br /> | ||
| + | Asp (D) 19 4.2%<br /> | ||
| + | Cys (C) 7 1.5%<br /> | ||
| + | Gln (Q) 16 3.5%<br /> | ||
| + | Glu (E) 37 8.2%<br /> | ||
| + | Gly (G) 45 9.9%<br /> | ||
| + | His (H) 10 2.2%<br /> | ||
| + | Ile (I) 30 6.6%<br /> | ||
| + | Leu (L) 38 8.4%<br /> | ||
| + | Lys (K) 21 4.6%<br /> | ||
| + | Met (M) 11 2.4%<br /> | ||
| + | Phe (F) 12 2.6%<br /> | ||
| + | Pro (P) 21 4.6%<br /> | ||
| + | Ser (S) 32 7.1%<br /> | ||
| + | Thr (T) 24 5.3%<br /> | ||
| + | Trp (W) 6 1.3%<br /> | ||
| + | Tyr (Y) 15 3.3%<br /> | ||
| + | Val (V) 30 6.6%<br /> | ||
| + | Pyl (O) 0 0.0%<br /> | ||
| + | Sec (U) 0 0.0%</p> | ||
| + | <p align="left"> (B) 0 0.0%<br /> | ||
| + | (Z) 0 0.0%<br /> | ||
| + | (X) 0 0.0%</p> | ||
| + | <p align="left"> </p> | ||
| + | <p align="left">Total number of negatively charged residues (Asp + Glu): 56<br /> | ||
| + | Total number of positively charged residues (Arg + Lys): 50</p> | ||
| + | <p align="left">Atomic composition:</p> | ||
| + | <p align="left">Carbon C 2192<br /> | ||
| + | Hydrogen H 3480<br /> | ||
| + | Nitrogen N 614<br /> | ||
| + | Oxygen O 664<br /> | ||
| + | Sulfur S 18</p> | ||
| + | <p align="left">Formula: C2192H3480N614O664S18<br /> | ||
| + | Total number of atoms: 6968</p> | ||
| + | <p align="left">Extinction coefficients:</p> | ||
| + | <p align="left">Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.</p> | ||
| + | <p align="left">Ext. coefficient 55725<br /> | ||
| + | Abs 0.1% (=1 g/l) 1.123, assuming all pairs of Cys residues form cystines</p> | ||
| + | <p align="left"> </p> | ||
| + | <p align="left">Ext. coefficient 55350<br /> | ||
| + | Abs 0.1% (=1 g/l) 1.115, assuming all Cys residues are reduced</p> | ||
| + | <p align="left">Estimated half-life:</p> | ||
| + | <p align="left">The N-terminal of the sequence considered is M (Met).</p> | ||
| + | <p align="left">The estimated half-life is: 30 hours (mammalian reticulocytes, in vitro).<br /> | ||
| + | >20 hours (yeast, in vivo).<br /> | ||
| + | >10 hours (Escherichia coli, in vivo).</p> | ||
| + | <p align="left"> </p> | ||
| + | <p align="left">Instability index:</p> | ||
| + | <p align="left">The instability index (II) is computed to be 40.63<br /> | ||
| + | This classifies the protein as unstable.</p> | ||
| + | <p align="left"> </p> | ||
| + | <p align="left">Aliphatic index: 86.36</p> | ||
| + | <p align="left">Grand average of hydropathicity (GRAVY): -0.234</p> | ||
| + | <div> | ||
| + | <h2>Design Notes</h2> | ||
| + | </div> | ||
| + | <p align="left">Nitrogenase is a complex enzyme system consisting of nine protein components. Additionally, to maintain stoichiometry of these protein components is an essential requirement for nitrogenase biosynthesis and activity. However, there is only one copy of each structure gene present in the nif gene cluster. Therefore, cloning each of these nif genes and setting as independent part can facilitate the regulation of balancing expression ratios from the transcription and/or translation level(s) when they are heterogeneously expressed in non-diazotrophic hosts.</p> | ||
Latest revision as of 10:15, 8 October 2018
CR1 nifE
CR1 nifE encodes the cofactor NifE for the maturation of functional molybdenum-iron protein.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 6
Illegal AgeI site found at 379 - 1000COMPATIBLE WITH RFC[1000]
Parameter of Protein
Number of amino acids: 453
Molecular weight: 49636.54
Theoretical pI: 6.00
Amino acid composition:
Ala (A) 39 8.6%
Arg (R) 29 6.4%
Asn (N) 11 2.4%
Asp (D) 19 4.2%
Cys (C) 7 1.5%
Gln (Q) 16 3.5%
Glu (E) 37 8.2%
Gly (G) 45 9.9%
His (H) 10 2.2%
Ile (I) 30 6.6%
Leu (L) 38 8.4%
Lys (K) 21 4.6%
Met (M) 11 2.4%
Phe (F) 12 2.6%
Pro (P) 21 4.6%
Ser (S) 32 7.1%
Thr (T) 24 5.3%
Trp (W) 6 1.3%
Tyr (Y) 15 3.3%
Val (V) 30 6.6%
Pyl (O) 0 0.0%
Sec (U) 0 0.0%
(B) 0 0.0%
(Z) 0 0.0%
(X) 0 0.0%
Total number of negatively charged residues (Asp + Glu): 56
Total number of positively charged residues (Arg + Lys): 50
Atomic composition:
Carbon C 2192
Hydrogen H 3480
Nitrogen N 614
Oxygen O 664
Sulfur S 18
Formula: C2192H3480N614O664S18
Total number of atoms: 6968
Extinction coefficients:
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 55725
Abs 0.1% (=1 g/l) 1.123, assuming all pairs of Cys residues form cystines
Ext. coefficient 55350
Abs 0.1% (=1 g/l) 1.115, assuming all Cys residues are reduced
Estimated half-life:
The N-terminal of the sequence considered is M (Met).
The estimated half-life is: 30 hours (mammalian reticulocytes, in vitro).
>20 hours (yeast, in vivo).
>10 hours (Escherichia coli, in vivo).
Instability index:
The instability index (II) is computed to be 40.63
This classifies the protein as unstable.
Aliphatic index: 86.36
Grand average of hydropathicity (GRAVY): -0.234
Design Notes
Nitrogenase is a complex enzyme system consisting of nine protein components. Additionally, to maintain stoichiometry of these protein components is an essential requirement for nitrogenase biosynthesis and activity. However, there is only one copy of each structure gene present in the nif gene cluster. Therefore, cloning each of these nif genes and setting as independent part can facilitate the regulation of balancing expression ratios from the transcription and/or translation level(s) when they are heterogeneously expressed in non-diazotrophic hosts.