Difference between revisions of "Part:BBa K2740013"
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<partinfo>BBa_K2740013 parameters</partinfo> | <partinfo>BBa_K2740013 parameters</partinfo> | ||
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+ | <h2>Parameter of Protein </h2> | ||
+ | <p align="left">Number of amino acids: 288</p> | ||
+ | <p align="left">Molecular weight: 31494.95</p> | ||
+ | <p align="left">Theoretical pI: 4.78</p> | ||
+ | <p align="left">Amino acid composition: <br /> | ||
+ | Ala (A) 26 9.0%<br /> | ||
+ | Arg (R) 13 4.5%<br /> | ||
+ | Asn (N) 15 5.2%<br /> | ||
+ | Asp (D) 14 4.9%<br /> | ||
+ | Cys (C) 6 2.1%<br /> | ||
+ | Gln (Q) 13 4.5%<br /> | ||
+ | Glu (E) 28 9.7%<br /> | ||
+ | Gly (G) 28 9.7%<br /> | ||
+ | His (H) 4 1.4%<br /> | ||
+ | Ile (I) 22 7.6%<br /> | ||
+ | Leu (L) 27 9.4%<br /> | ||
+ | Lys (K) 14 4.9%<br /> | ||
+ | Met (M) 11 3.8%<br /> | ||
+ | Phe (F) 8 2.8%<br /> | ||
+ | Pro (P) 8 2.8%<br /> | ||
+ | Ser (S) 9 3.1%<br /> | ||
+ | Thr (T) 17 5.9%<br /> | ||
+ | Trp (W) 0 0.0%<br /> | ||
+ | Tyr (Y) 8 2.8%<br /> | ||
+ | Val (V) 17 5.9%<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): 42<br /> | ||
+ | Total number of positively charged residues (Arg + Lys): 27</p> | ||
+ | <p align="left">Atomic composition:</p> | ||
+ | <p align="left">Carbon C 1372<br /> | ||
+ | Hydrogen H 2213<br /> | ||
+ | Nitrogen N 377<br /> | ||
+ | Oxygen O 435<br /> | ||
+ | Sulfur S 17</p> | ||
+ | <p align="left">Formula: C1372H2213N377O435S17<br /> | ||
+ | Total number of atoms: 4414</p> | ||
+ | <p align="left">Extinction coefficients:</p> | ||
+ | <p align="left">This protein does not contain any Trp residues. Experience shows that<br /> | ||
+ | this could result in more than 10% error in the computed extinction coefficient.</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 12295<br /> | ||
+ | Abs 0.1% (=1 g/l) 0.390, assuming all pairs of Cys residues form cystines</p> | ||
+ | <p align="left"> </p> | ||
+ | <p align="left">Ext. coefficient 11920<br /> | ||
+ | Abs 0.1% (=1 g/l) 0.378, 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 39.05<br /> | ||
+ | This classifies the protein as stable.</p> | ||
+ | <p align="left"> </p> | ||
+ | <p align="left">Aliphatic index: 92.50</p> | ||
+ | <p align="left">Grand average of hydropathicity (GRAVY): -0.161</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 05:22, 4 October 2018
CR1 nifH
CR1 nifH encodes nitrogenase reductase NifH, which is an electron donor to the molybdenum-iron (MoFe) protein, contributing to the electron transport in the nitrogen fixation system.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Unknown
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 718
Parameter of Protein
Number of amino acids: 288
Molecular weight: 31494.95
Theoretical pI: 4.78
Amino acid composition:
Ala (A) 26 9.0%
Arg (R) 13 4.5%
Asn (N) 15 5.2%
Asp (D) 14 4.9%
Cys (C) 6 2.1%
Gln (Q) 13 4.5%
Glu (E) 28 9.7%
Gly (G) 28 9.7%
His (H) 4 1.4%
Ile (I) 22 7.6%
Leu (L) 27 9.4%
Lys (K) 14 4.9%
Met (M) 11 3.8%
Phe (F) 8 2.8%
Pro (P) 8 2.8%
Ser (S) 9 3.1%
Thr (T) 17 5.9%
Trp (W) 0 0.0%
Tyr (Y) 8 2.8%
Val (V) 17 5.9%
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): 42
Total number of positively charged residues (Arg + Lys): 27
Atomic composition:
Carbon C 1372
Hydrogen H 2213
Nitrogen N 377
Oxygen O 435
Sulfur S 17
Formula: C1372H2213N377O435S17
Total number of atoms: 4414
Extinction coefficients:
This protein does not contain any Trp residues. Experience shows that
this could result in more than 10% error in the computed extinction coefficient.
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 12295
Abs 0.1% (=1 g/l) 0.390, assuming all pairs of Cys residues form cystines
Ext. coefficient 11920
Abs 0.1% (=1 g/l) 0.378, 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 39.05
This classifies the protein as stable.
Aliphatic index: 92.50
Grand average of hydropathicity (GRAVY): -0.161
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.