Difference between revisions of "Part:BBa K2740015"
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<partinfo>BBa_K2740015 parameters</partinfo> | <partinfo>BBa_K2740015 parameters</partinfo> | ||
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| + | <h2>Parameter of Protein </h2> | ||
| + | <p align="left">Number of amino acids: 509</p> | ||
| + | <p align="left">Molecular weight: 56395.40</p> | ||
| + | <p align="left">Theoretical pI: 5.74</p> | ||
| + | <p align="left">Amino acid composition: <br /> | ||
| + | Ala (A) 48 9.4%<br /> | ||
| + | Arg (R) 26 5.1%<br /> | ||
| + | Asn (N) 16 3.1%<br /> | ||
| + | Asp (D) 27 5.3%<br /> | ||
| + | Cys (C) 9 1.8%<br /> | ||
| + | Gln (Q) 19 3.7%<br /> | ||
| + | Glu (E) 35 6.9%<br /> | ||
| + | Gly (G) 40 7.9%<br /> | ||
| + | His (H) 17 3.3%<br /> | ||
| + | Ile (I) 23 4.5%<br /> | ||
| + | Leu (L) 51 10.0%<br /> | ||
| + | Lys (K) 23 4.5%<br /> | ||
| + | Met (M) 19 3.7%<br /> | ||
| + | Phe (F) 24 4.7%<br /> | ||
| + | Pro (P) 26 5.1%<br /> | ||
| + | Ser (S) 29 5.7%<br /> | ||
| + | Thr (T) 28 5.5%<br /> | ||
| + | Trp (W) 2 0.4%<br /> | ||
| + | Tyr (Y) 19 3.7%<br /> | ||
| + | Val (V) 28 5.5%<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): 62<br /> | ||
| + | Total number of positively charged residues (Arg + Lys): 49</p> | ||
| + | <p align="left">Atomic composition:</p> | ||
| + | <p align="left">Carbon C 2506<br /> | ||
| + | Hydrogen H 3909<br /> | ||
| + | Nitrogen N 681<br /> | ||
| + | Oxygen O 745<br /> | ||
| + | Sulfur S 28</p> | ||
| + | <p align="left">Formula: C2506H3909N681O745S28<br /> | ||
| + | Total number of atoms: 7869</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 39810<br /> | ||
| + | Abs 0.1% (=1 g/l) 0.706, assuming all pairs of Cys residues form cystines</p> | ||
| + | <p align="left"> </p> | ||
| + | <p align="left">Ext. coefficient 39310<br /> | ||
| + | Abs 0.1% (=1 g/l) 0.697, 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 43.04<br /> | ||
| + | This classifies the protein as unstable.</p> | ||
| + | <p align="left"> </p> | ||
| + | <p align="left">Aliphatic index: 82.08</p> | ||
| + | <p align="left">Grand average of hydropathicity (GRAVY): -0.197</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> | ||
Revision as of 05:29, 4 October 2018
CR1 nifK
CR1 nifK encodes the subunit beta (NifK) of the molybdenum-iron protein. Together with NifD, they form a α2β2 heterotetramer.
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 856
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 1106
Illegal SapI.rc site found at 1489
Parameter of Protein
Number of amino acids: 509
Molecular weight: 56395.40
Theoretical pI: 5.74
Amino acid composition:
Ala (A) 48 9.4%
Arg (R) 26 5.1%
Asn (N) 16 3.1%
Asp (D) 27 5.3%
Cys (C) 9 1.8%
Gln (Q) 19 3.7%
Glu (E) 35 6.9%
Gly (G) 40 7.9%
His (H) 17 3.3%
Ile (I) 23 4.5%
Leu (L) 51 10.0%
Lys (K) 23 4.5%
Met (M) 19 3.7%
Phe (F) 24 4.7%
Pro (P) 26 5.1%
Ser (S) 29 5.7%
Thr (T) 28 5.5%
Trp (W) 2 0.4%
Tyr (Y) 19 3.7%
Val (V) 28 5.5%
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): 62
Total number of positively charged residues (Arg + Lys): 49
Atomic composition:
Carbon C 2506
Hydrogen H 3909
Nitrogen N 681
Oxygen O 745
Sulfur S 28
Formula: C2506H3909N681O745S28
Total number of atoms: 7869
Extinction coefficients:
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 39810
Abs 0.1% (=1 g/l) 0.706, assuming all pairs of Cys residues form cystines
Ext. coefficient 39310
Abs 0.1% (=1 g/l) 0.697, 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 43.04
This classifies the protein as unstable.
Aliphatic index: 82.08
Grand average of hydropathicity (GRAVY): -0.197
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.