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CA distance fluctuations for 2402120130382434456

---  normal mode 10  ---

This matrix displays the maximum distance fluctuations between all pairs of CA atoms and between the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Distance increases are plotted in blue and decreases in red for the strongest 10% of the residue pair distance changes. Every pixel corresponds to a single residue. Grey lines are drawn every 10 residues, yellow lines every 100 residues (counting from the upper left corner).

The following table indicates for every residue the two corresponding residues with the strongest CA distance fluctuations.

[HELP on distance fluctuations]

GD ok
largest increasereflargest decrease
ASP 79 0.90 MET 1 -1.18 ASP 27
VAL 78 0.79 ILE 2 -1.27 ASP 27
VAL 78 0.60 SER 3 -1.51 ASP 27
LEU 54 0.82 LEU 4 -1.33 ASP 27
LEU 54 1.09 ILE 5 -1.61 LEU 24
THR 35 1.55 ALA 6 -1.75 LEU 24
LEU 54 1.72 ALA 7 -1.26 TRP 22
LEU 54 1.63 LEU 8 -1.15 TRP 22
PHE 31 1.68 ALA 9 -0.76 PRO 21
TRP 30 1.67 VAL 10 -0.66 PRO 21
ASN 34 1.54 ASP 11 -0.65 TRP 22
ASN 34 1.66 ARG 12 -0.98 TRP 22
LEU 54 1.44 VAL 13 -1.01 TRP 22
LEU 54 1.59 ILE 14 -1.42 TRP 22
LEU 54 1.31 GLY 15 -1.11 TRP 22
PRO 55 1.26 PRO 21 -1.05 VAL 119
PRO 55 0.92 TRP 22 -1.52 GLY 97
PRO 55 0.84 ASN 23 -1.55 GLY 96
PRO 55 1.03 LEU 24 -1.75 ALA 6
PRO 55 0.94 PRO 25 -1.55 THR 46
HIS 149 1.39 ALA 26 -1.11 SER 49
PRO 55 1.37 ASP 27 -1.51 SER 3
PRO 55 1.34 LEU 28 -1.53 ILE 94
TYR 151 1.83 ALA 29 -1.27 ILE 50
VAL 10 1.67 TRP 30 -1.12 PRO 89
ALA 9 1.68 PHE 31 -1.39 PRO 89
HIS 114 1.67 LYS 32 -1.01 ILE 50
TYR 128 1.46 ARG 33 -0.63 ILE 50
TYR 128 1.70 ASN 34 -0.87 PRO 89
ALA 7 1.59 THR 35 -1.03 PRO 89
GLU 154 1.63 LEU 36 -0.55 ILE 50
PHE 153 1.74 ASP 37 -0.47 PRO 89
ILE 155 1.51 LYS 38 -0.48 PHE 31
ILE 155 0.98 PRO 39 -0.65 LEU 28
TYR 111 0.87 VAL 40 -0.97 LEU 28
TYR 111 0.44 ILE 41 -1.07 LEU 28
GLY 67 0.57 MET 42 -1.15 PRO 25
GLY 67 0.45 GLY 43 -1.30 ASN 23
GLY 67 0.49 ARG 44 -1.19 ASN 23
GLY 67 0.59 HIS 45 -1.40 PRO 25
THR 68 0.74 THR 46 -1.55 PRO 25
GLY 67 0.92 TRP 47 -1.17 PRO 25
GLY 67 0.89 GLU 48 -1.22 GLN 146
THR 68 0.81 SER 49 -1.44 GLN 146
THR 68 1.02 ILE 50 -1.27 ALA 29
GLY 67 1.21 GLY 51 -0.87 GLN 146
THR 68 1.22 ARG 52 -0.30 ALA 145
ALA 7 1.18 PRO 53 -0.16 ALA 145
ALA 7 1.72 LEU 54 -0.12 LEU 36
ILE 115 1.76 PRO 55 -0.23 VAL 72
CYS 152 1.53 GLY 56 -0.32 PRO 89
PHE 153 1.39 ARG 57 -0.34 ILE 50
PHE 153 1.04 LYS 58 -0.31 ILE 50
PHE 153 0.77 ASN 59 -0.58 PRO 25
PHE 137 0.54 ILE 60 -0.74 ASN 23
GLY 67 0.40 ILE 61 -0.91 ASN 23
ILE 91 0.39 LEU 62 -1.05 ASN 23
MET 1 0.37 SER 63 -1.05 ASN 23
PRO 89 0.34 SER 64 -1.04 ASN 23
GLU 48 0.36 GLN 65 -0.82 ASN 23
GLU 48 0.83 PRO 66 -0.70 GLU 80
GLY 51 1.21 GLY 67 -0.51 GLU 80
ARG 52 1.22 THR 68 -0.33 GLU 80
ARG 52 0.83 ASP 69 -0.48 GLU 80
GLU 139 0.76 ASP 70 -0.43 GLU 80
GLU 139 0.94 ARG 71 -0.23 GLU 80
GLU 139 0.74 VAL 72 -0.35 ASN 23
GLU 139 0.55 THR 73 -0.59 ASN 23
GLU 139 0.41 TRP 74 -0.70 ASN 23
ALA 84 0.51 VAL 75 -0.82 ASN 23
PRO 89 0.53 LYS 76 -0.88 ASN 23
PRO 89 0.66 SER 77 -0.93 TRP 22
ILE 91 0.91 VAL 78 -0.89 TRP 22
PRO 89 1.10 ASP 79 -0.74 TRP 22
PRO 89 0.79 GLU 80 -0.76 ASN 23
ILE 91 0.70 ALA 81 -0.84 ASN 23
PRO 89 0.83 ILE 82 -0.81 ASP 132
PRO 89 0.69 ALA 83 -0.81 ASP 132
VAL 75 0.51 ALA 84 -0.71 ASP 132
PHE 137 0.59 CYS 85 -0.88 LYS 106
PHE 137 0.62 GLY 86 -0.92 ASP 132
ARG 71 0.49 ASP 87 -1.64 ASP 132
PHE 137 0.96 VAL 88 -0.79 LYS 106
ASP 79 1.10 PRO 89 -1.39 PHE 31
ASP 79 0.94 GLU 90 -1.39 PHE 31
VAL 78 0.91 ILE 91 -1.22 ASP 27
VAL 78 0.67 MET 92 -1.46 LEU 28
LEU 54 0.67 VAL 93 -1.37 LEU 28
LEU 54 0.92 ILE 94 -1.53 LEU 28
LEU 54 0.89 GLY 95 -1.47 ASN 23
LEU 54 0.78 GLY 96 -1.55 ASN 23
LEU 54 0.86 GLY 97 -1.52 TRP 22
LEU 54 0.62 ARG 98 -1.26 TRP 22
LEU 54 0.57 VAL 99 -1.29 ASN 23
LEU 54 0.76 TYR 100 -1.34 TRP 22
ASN 34 0.68 GLU 101 -1.24 TRP 22
LEU 54 0.53 GLN 102 -1.15 TRP 22
ILE 2 0.59 PHE 103 -1.07 TRP 22
LEU 54 0.58 LEU 104 -1.14 LEU 24
LEU 54 0.45 PRO 105 -1.09 ASP 87
MET 1 0.33 LYS 106 -1.01 ASP 87
LEU 54 0.44 ALA 107 -1.07 ASP 27
LEU 54 0.49 GLN 108 -1.03 ASP 27
LEU 54 0.70 LYS 109 -1.08 ASP 27
LEU 54 0.92 LEU 110 -1.21 LEU 24
LYS 38 1.39 TYR 111 -1.20 LEU 24
THR 35 1.58 LEU 112 -1.21 LEU 24
LEU 36 1.62 THR 113 -0.88 LEU 24
LYS 32 1.67 HIS 114 -0.73 TRP 22
PRO 55 1.76 ILE 115 -0.52 TRP 22
PRO 55 1.70 ASP 116 -0.49 PRO 21
PRO 55 1.70 ALA 117 -0.55 PRO 21
PRO 55 1.47 GLU 118 -0.73 PRO 21
PRO 55 1.33 VAL 119 -1.05 PRO 21
PRO 55 1.15 GLU 120 -0.74 SER 64
LEU 54 1.13 GLY 121 -0.84 SER 64
LEU 54 1.03 ASP 122 -1.02 SER 64
LEU 54 1.15 THR 123 -1.09 TRP 22
ASN 34 1.32 HIS 124 -1.13 TRP 22
ASN 34 1.36 PHE 125 -1.27 TRP 22
ASN 34 1.28 PRO 126 -1.13 TRP 22
ASN 34 1.64 ASP 127 -0.76 TRP 22
ASN 34 1.70 TYR 128 -0.76 ASP 87
ARG 33 1.41 GLU 129 -1.14 ASP 87
ARG 33 1.42 PRO 130 -0.85 ASP 87
ARG 33 1.02 ASP 131 -1.26 ASP 87
ARG 33 1.06 ASP 132 -1.64 ASP 87
ARG 33 1.38 TRP 133 -1.03 ASP 87
ARG 33 1.23 GLU 134 -0.65 PRO 105
LEU 36 1.11 SER 135 -0.73 ASP 127
ASP 37 1.19 VAL 136 -0.51 TRP 22
ASP 37 1.31 PHE 137 -0.45 TRP 22
ASP 37 1.32 SER 138 -0.55 ASP 11
ASP 37 1.34 GLU 139 -0.34 ASP 11
GLY 56 1.30 PHE 140 -0.39 ASP 116
GLY 56 1.38 HIS 141 -0.26 HIS 45
PRO 55 1.33 ASP 142 -0.48 HIS 45
PRO 55 1.22 ALA 143 -0.78 HIS 45
PRO 130 0.91 ASP 144 -1.09 SER 49
PRO 130 0.75 ALA 145 -1.32 SER 49
PRO 55 0.71 GLN 146 -1.44 SER 49
PRO 55 0.99 ASN 147 -1.17 ILE 5
PRO 55 1.04 SER 148 -1.19 HIS 45
PRO 55 1.49 HIS 149 -0.74 HIS 45
PRO 55 1.55 SER 150 -0.47 HIS 45
ALA 29 1.83 TYR 151 -0.39 HIS 45
GLY 56 1.53 CYS 152 -0.40 TRP 22
ASP 37 1.74 PHE 153 -0.50 TRP 22
LEU 36 1.63 GLU 154 -0.68 TRP 22
LYS 38 1.51 ILE 155 -0.75 LEU 24
LEU 36 1.22 LEU 156 -0.82 TRP 22
ARG 33 0.88 GLU 157 -0.84 LEU 24
ARG 33 0.89 ARG 158 -0.95 ASP 87

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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.