Difference between revisions of "Part:BBa K1796006"

(Parametre of Protein)
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==Parametre of Protein==
+
==Parameter of Protein==
<p> Number of amino acids: 294 </p>
+
<p> Number of amino acids: 288 </p>
 
<p> </p>
 
<p> </p>
<p> Molecular weight: 32136.5 </p>
+
<p> Molecular weight: 31494.9 </p>
 
<p> </p>
 
<p> </p>
<p> Theoretical pI: 4.79 </p>
+
<p> Theoretical pI: 4.78 </p>
 
<p> </p>
 
<p> </p>
<p> Amino acid composition:  </p>
+
<p> Amino acid composition: </p>
 
<p> </p>
 
<p> </p>
<p> Ala (A)  26      8.8% </p>
+
<p> Ala (A)  26      9.0% </p>
 
<p> </p>
 
<p> </p>
<p> Arg (R)  13      4.4% </p>
+
<p> Arg (R)  13      4.5% </p>
 
<p> </p>
 
<p> </p>
<p> Asn (N)  16       5.4% </p>
+
<p> Asn (N)  15       5.2% </p>
 
<p> </p>
 
<p> </p>
<p> Asp (D)  14      4.8% </p>
+
<p> Asp (D)  14      4.9% </p>
 
<p> </p>
 
<p> </p>
<p> Cys (C)  6      2.0% </p>
+
<p> Cys (C)  6      2.1% </p>
 
<p> </p>
 
<p> </p>
<p> Gln (Q)  13      4.4% </p>
+
<p> Gln (Q)  13      4.5% </p>
 
<p> </p>
 
<p> </p>
<p> Glu (E)  29       9.9% </p>
+
<p> Glu (E)  28       9.7% </p>
 
<p> </p>
 
<p> </p>
<p> Gly (G)  30      10.2% </p>
+
<p> Gly (G)  28      9.7% </p>
 
<p> </p>
 
<p> </p>
<p> His (H)  5       1.7% </p>
+
<p> His (H)  4       1.4% </p>
 
<p> </p>
 
<p> </p>
<p> Ile (I)  22      7.5% </p>
+
<p> Ile (I)  22      7.6% </p>
 
<p> </p>
 
<p> </p>
<p> Leu (L)  27      9.2% </p>
+
<p> Leu (L)  27      9.4% </p>
 
<p> </p>
 
<p> </p>
<p> Lys (K)  14      4.8% </p>
+
<p> Lys (K)  14      4.9% </p>
 
<p> </p>
 
<p> </p>
<p> Met (M)  11      3.7% </p>
+
<p> Met (M)  11      3.8% </p>
 
<p> </p>
 
<p> </p>
<p> Phe (F)  9       3.1% </p>
+
<p> Phe (F)  8       2.8% </p>
 
<p> </p>
 
<p> </p>
<p> Pro (P)  8      2.7% </p>
+
<p> Pro (P)  8      2.8% </p>
 
<p> </p>
 
<p> </p>
 
<p> Ser (S)  9      3.1% </p>
 
<p> Ser (S)  9      3.1% </p>
 
<p> </p>
 
<p> </p>
<p> Thr (T)  17      5.8% </p>
+
<p> Thr (T)  17      5.9% </p>
 
<p> </p>
 
<p> </p>
 
<p> Trp (W)  0      0.0% </p>
 
<p> Trp (W)  0      0.0% </p>
 
<p> </p>
 
<p> </p>
<p> Tyr (Y)  8      2.7% </p>
+
<p> Tyr (Y)  8      2.8% </p>
 
<p> </p>
 
<p> </p>
<p> Val (V)  17      5.8% </p>
+
<p> Val (V)  17      5.9% </p>
 
<p> </p>
 
<p> </p>
 
<p> Pyl (O)  0      0.0% </p>
 
<p> Pyl (O)  0      0.0% </p>
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<p> (X)  0          0.0% </p>
 
<p> (X)  0          0.0% </p>
 
<p> </p>
 
<p> </p>
<p> Total number of negatively charged residues (Asp + Glu): 43 </p>
+
<p> Total number of negatively charged residues (Asp + Glu): 42 </p>
 
<p> Total number of positively charged residues (Arg + Lys): 27 </p>
 
<p> Total number of positively charged residues (Arg + Lys): 27 </p>
 
<p> </p>
 
<p> </p>
<p> Atomic composition:Carbon      C              1400 </p>
+
<p> Atomic composition:Carbon      C              1372 </p>
<p> Hydrogen    H        2248 </p>
+
<p> Hydrogen    H        2213 </p>
<p> Nitrogen    N          386 </p>
+
<p> Nitrogen    N          377 </p>
<p> Oxygen      O          444 </p>
+
<p> Oxygen      O          435 </p>
 
<p> Sulfur      S          17 </p>
 
<p> Sulfur      S          17 </p>
 
<p> </p>
 
<p> </p>
<p> Formula: C1400H2248N386O444S17Total number of atoms: 4495 </p>
+
<p> Formula: C1372H2213N377O435S17Total number of atoms: 4414 </p>
 
<p> </p>
 
<p> </p>
 
<p> Extinction coefficients:This protein does not contain any Trp residues. Experience shows that </p>
 
<p> Extinction coefficients:This protein does not contain any Trp residues. Experience shows that </p>
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<p> </p>
 
<p> </p>
 
<p> Ext. coefficient    12295 </p>
 
<p> Ext. coefficient    12295 </p>
<p> Abs 0.1% (=1 g/l)  0.383, assuming all pairs of Cys residues form cystines </p>
+
<p> Abs 0.1% (=1 g/l)  0.390, assuming all pairs of Cys residues form cystines </p>
 
<p> </p>
 
<p> </p>
 
<p> </p>
 
<p> </p>
 
<p> Ext. coefficient    11920 </p>
 
<p> Ext. coefficient    11920 </p>
<p> Abs 0.1% (=1 g/l)  0.371, assuming all Cys residues are reduced </p>
+
<p> Abs 0.1% (=1 g/l)  0.378, assuming all Cys residues are reduced </p>
 
<p> </p>
 
<p> </p>
<p> Estimated half-life:The N-terminal of the sequence considered is H (His). </p>
+
<p> Estimated half-life:The N-terminal of the sequence considered is M (Met). </p>
 
<p> </p>
 
<p> </p>
<p> The estimated half-life is: 3.5 hours (mammalian reticulocytes, in vitro). </p>
+
<p> The estimated half-life is: 30 hours (mammalian reticulocytes, in vitro). </p>
<p>                             10 min (yeast, in vivo). </p>
+
<p>                             >20 hours (yeast, in vivo). </p>
 
<p>                             >10 hours (Escherichia coli, in vivo). </p>
 
<p>                             >10 hours (Escherichia coli, in vivo). </p>
 
<p> </p>
 
<p> </p>
 
<p> </p>
 
<p> </p>
<p> Instability index:The instability index (II) is computed to be 38.27 </p>
+
<p> Instability index:The instability index (II) is computed to be 39.05 </p>
 
<p> This classifies the protein as stable. </p>
 
<p> This classifies the protein as stable. </p>
 
<p> </p>
 
<p> </p>
 
<p> </p>
 
<p> </p>
 
<p> </p>
 
<p> </p>
<p> Aliphatic index: 90.61 </p>
+
<p> Aliphatic index: 92.50 </p>
 
<p> </p>
 
<p> </p>
<p> Grand average of hydropathicity (GRAVY): -0.185 </p>
+
<p> Grand average of hydropathicity (GRAVY): -0.161 </p>

Revision as of 01:24, 19 September 2015

Dinitrogenase reductase(nifH)

The nifH encoding dinitrogenase reductase(also called Fe protein) is an important gene in nitrogen fixation. The protein is a homodimer bridged by an intersubunit [4Fe-4S] cluster that serves as the obligate electron donor to the MoFe protein. Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Parameter of Protein

Number of amino acids: 288

Molecular weight: 31494.9

Theoretical pI: 4.78

Amino acid composition:聽

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: C1372H2213N377O435S17Total 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