Difference between revisions of "Part:BBa K2740017"
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<partinfo>BBa_K2740017 parameters</partinfo> | <partinfo>BBa_K2740017 parameters</partinfo> | ||
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| + | <h2>Parameter of Protein </h2> | ||
| + | <p align="left">Number of amino acids: 435</p> | ||
| + | <p align="left">Molecular weight: 46939.70</p> | ||
| + | <p align="left">Theoretical pI: 6.18</p> | ||
| + | <p align="left">Amino acid composition: <br /> | ||
| + | Ala (A) 44 10.1%<br /> | ||
| + | Arg (R) 24 5.5%<br /> | ||
| + | Asn (N) 7 1.6%<br /> | ||
| + | Asp (D) 21 4.8%<br /> | ||
| + | Cys (C) 4 0.9%<br /> | ||
| + | Gln (Q) 13 3.0%<br /> | ||
| + | Glu (E) 26 6.0%<br /> | ||
| + | Gly (G) 38 8.7%<br /> | ||
| + | His (H) 14 3.2%<br /> | ||
| + | Ile (I) 20 4.6%<br /> | ||
| + | Leu (L) 52 12.0%<br /> | ||
| + | Lys (K) 17 3.9%<br /> | ||
| + | Met (M) 11 2.5%<br /> | ||
| + | Phe (F) 15 3.4%<br /> | ||
| + | Pro (P) 22 5.1%<br /> | ||
| + | Ser (S) 41 9.4%<br /> | ||
| + | Thr (T) 23 5.3%<br /> | ||
| + | Trp (W) 6 1.4%<br /> | ||
| + | Tyr (Y) 8 1.8%<br /> | ||
| + | Val (V) 29 6.7%<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): 47<br /> | ||
| + | Total number of positively charged residues (Arg + Lys): 41</p> | ||
| + | <p align="left">Atomic composition:</p> | ||
| + | <p align="left">Carbon C 2087<br /> | ||
| + | Hydrogen H 3318<br /> | ||
| + | Nitrogen N 578<br /> | ||
| + | Oxygen O 622<br /> | ||
| + | Sulfur S 15</p> | ||
| + | <p align="left">Formula: C2087H3318N578O622S15<br /> | ||
| + | Total number of atoms: 6620</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 45170<br /> | ||
| + | Abs 0.1% (=1 g/l) 0.962, assuming all pairs of Cys residues form cystines</p> | ||
| + | <p align="left"> </p> | ||
| + | <p align="left">Ext. coefficient 44920<br /> | ||
| + | Abs 0.1% (=1 g/l) 0.957, 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 L (Leu).</p> | ||
| + | <p align="left">The estimated half-life is: 5.5 hours (mammalian reticulocytes, in vitro).<br /> | ||
| + | 3 min (yeast, in vivo).<br /> | ||
| + | 2 min (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 38.18<br /> | ||
| + | This classifies the protein as stable.</p> | ||
| + | <p align="left"> </p> | ||
| + | <p align="left">Aliphatic index: 94.00</p> | ||
| + | <p align="left">Grand average of hydropathicity (GRAVY): -0.017</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 10:16, 8 October 2018
CR1 nifN
CR1 nifN encodes the cofactor NifN 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 525
- 1000COMPATIBLE WITH RFC[1000]
Parameter of Protein
Number of amino acids: 435
Molecular weight: 46939.70
Theoretical pI: 6.18
Amino acid composition:
Ala (A) 44 10.1%
Arg (R) 24 5.5%
Asn (N) 7 1.6%
Asp (D) 21 4.8%
Cys (C) 4 0.9%
Gln (Q) 13 3.0%
Glu (E) 26 6.0%
Gly (G) 38 8.7%
His (H) 14 3.2%
Ile (I) 20 4.6%
Leu (L) 52 12.0%
Lys (K) 17 3.9%
Met (M) 11 2.5%
Phe (F) 15 3.4%
Pro (P) 22 5.1%
Ser (S) 41 9.4%
Thr (T) 23 5.3%
Trp (W) 6 1.4%
Tyr (Y) 8 1.8%
Val (V) 29 6.7%
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): 47
Total number of positively charged residues (Arg + Lys): 41
Atomic composition:
Carbon C 2087
Hydrogen H 3318
Nitrogen N 578
Oxygen O 622
Sulfur S 15
Formula: C2087H3318N578O622S15
Total number of atoms: 6620
Extinction coefficients:
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 45170
Abs 0.1% (=1 g/l) 0.962, assuming all pairs of Cys residues form cystines
Ext. coefficient 44920
Abs 0.1% (=1 g/l) 0.957, assuming all Cys residues are reduced
Estimated half-life:
The N-terminal of the sequence considered is L (Leu).
The estimated half-life is: 5.5 hours (mammalian reticulocytes, in vitro).
3 min (yeast, in vivo).
2 min (Escherichia coli, in vivo).
Instability index:
The instability index (II) is computed to be 38.18
This classifies the protein as stable.
Aliphatic index: 94.00
Grand average of hydropathicity (GRAVY): -0.017
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.