CNRS Nantes University US2B US2B
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***  hng  ***

CA distance fluctuations for 24012217345632109

---  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
LEU 112 0.28 GLY 5 -1.07 SER 71
SER 167 0.32 ILE 6 -1.01 SER 71
SER 167 0.51 ARG 7 -1.05 SER 71
SER 167 0.64 ALA 8 -0.98 SER 71
SER 167 0.80 ALA 9 -1.04 SER 71
SER 167 1.03 THR 10 -0.99 SER 71
SER 167 1.03 SER 11 -1.07 THR 46
SER 167 1.23 GLN 12 -1.12 ASP 48
PHE 170 1.03 GLU 13 -1.19 SER 71
ASN 168 0.77 ILE 14 -1.10 THR 46
ASN 168 0.87 ASN 15 -1.37 THR 46
PHE 170 1.03 GLU 16 -1.28 LEU 49
ALA 139 0.68 LEU 17 -1.03 LEU 49
ALA 139 0.65 THR 18 -1.05 LEU 49
ALA 139 0.90 TYR 19 -1.34 LEU 49
ALA 139 0.79 TYR 20 -1.04 LEU 49
ALA 139 0.60 THR 21 -0.86 LEU 49
ALA 139 0.57 THR 22 -0.94 LEU 49
TYR 76 0.60 LEU 23 -0.81 LEU 49
PRO 101 0.61 SER 24 -0.61 LEU 49
PRO 101 0.63 ALA 25 -0.54 LEU 49
PRO 101 0.73 ASN 26 -0.47 LEU 49
PRO 101 0.88 SER 27 -0.45 ILE 51
PRO 101 0.87 TYR 28 -0.56 THR 62
PRO 101 0.91 CYS 29 -0.37 ASP 61
PRO 101 1.07 ARG 30 -0.34 LEU 58
PRO 101 1.01 THR 31 -0.41 ASN 15
PRO 101 0.99 VAL 32 -0.44 ASN 15
PRO 101 1.17 ILE 33 -0.33 ILE 51
PRO 101 1.28 PRO 34 -0.29 ASN 15
PRO 101 1.11 GLY 35 -0.39 ASN 15
PRO 101 1.06 ALA 36 -0.44 ASN 15
PRO 101 0.90 THR 37 -0.61 ASN 15
PRO 101 0.76 TRP 38 -0.76 ASN 15
PRO 101 0.79 ASP 39 -0.63 ASN 15
PRO 101 0.74 CYS 40 -0.58 ASN 15
GLN 132 0.67 ILE 41 -0.74 GLY 262
TYR 133 0.73 HIS 42 -0.85 GLY 262
GLN 132 0.75 CYS 43 -0.83 ASN 15
GLN 132 0.98 ASP 44 -0.83 SER 11
TYR 76 1.17 ALA 45 -1.01 SER 11
GLN 129 1.15 THR 46 -1.37 ASN 15
GLN 132 0.85 GLU 47 -1.12 ASN 15
GLN 132 0.93 ASP 48 -1.24 ASN 15
GLN 132 0.97 LEU 49 -1.34 TYR 19
ARG 160 0.97 LYS 50 -0.92 TYR 19
ARG 160 0.92 ILE 51 -0.70 TYR 19
ARG 160 0.98 ILE 52 -0.45 TYR 19
PRO 101 1.01 LYS 53 -0.43 LEU 92
PRO 101 1.19 THR 54 -0.40 LEU 92
PRO 101 1.43 TRP 55 -0.45 LEU 92
PRO 101 1.62 SER 56 -0.51 GLU 121
PRO 101 1.69 THR 57 -0.57 TRP 88
PRO 101 1.62 LEU 58 -0.63 SER 84
VAL 102 1.60 ILE 59 -0.80 SER 84
VAL 102 1.72 TYR 60 -0.94 SER 84
PRO 101 1.85 ASP 61 -0.77 SER 83
PRO 101 1.57 THR 62 -0.80 SER 82
PRO 101 1.40 ASN 63 -0.52 TYR 28
PRO 101 1.12 ALA 64 -0.64 LEU 122
PRO 101 0.94 MET 65 -0.51 LEU 92
ASP 156 0.85 VAL 66 -0.50 LEU 92
ARG 160 0.97 ALA 67 -0.53 TYR 19
ARG 160 1.18 ARG 68 -0.53 TYR 19
GLN 129 1.16 GLY 69 -1.17 GLU 16
ASP 128 1.31 ASP 70 -0.99 GLU 16
GLN 132 1.15 SER 71 -1.19 GLU 13
GLN 132 0.95 GLU 72 -1.37 PRO 194
TYR 133 1.11 LYS 73 -0.59 PRO 194
ALA 45 1.11 THR 74 -0.53 SER 167
ALA 45 1.04 ILE 75 -0.53 LEU 92
ALA 45 1.17 TYR 76 -0.56 LEU 92
ALA 45 0.80 ILE 77 -0.64 LEU 92
PRO 101 0.70 VAL 78 -0.54 LEU 92
PRO 101 0.88 PHE 79 -0.66 LEU 122
PRO 101 0.99 ARG 80 -0.52 LEU 122
PRO 101 0.90 GLY 81 -0.61 SER 114
PRO 101 0.90 SER 82 -1.09 SER 114
PRO 101 0.99 SER 83 -0.86 TYR 60
PRO 101 0.78 SER 84 -1.01 SER 114
PRO 101 0.65 ILE 85 -1.03 SER 114
LEU 267 0.64 ARG 86 -1.01 ASP 113
LEU 255 0.51 ASN 87 -1.33 ASP 113
VAL 254 0.67 TRP 88 -1.57 SER 114
VAL 254 0.94 ILE 89 -1.52 GLY 110
LEU 255 0.66 ALA 90 -1.46 GLY 110
PHE 251 0.60 ASP 91 -1.36 LEU 112
PRO 250 0.82 LEU 92 -1.76 LEU 112
SER 83 0.73 THR 93 -1.51 PHE 213
ASP 61 0.70 PHE 94 -1.06 GLN 159
ASP 61 0.74 VAL 95 -1.10 GLN 159
PRO 209 0.96 PRO 96 -1.40 GLN 159
PHE 213 0.85 VAL 97 -1.55 ASP 156
TYR 60 1.10 SER 98 -1.73 GLN 159
TYR 60 1.43 TYR 99 -1.59 GLU 161
TYR 60 1.59 PRO 100 -1.42 GLU 161
ASP 61 1.85 PRO 101 -0.93 GLU 161
TYR 60 1.72 VAL 102 -0.78 GLU 161
ASP 113 1.67 SER 103 -0.73 GLU 161
ASP 113 1.34 GLY 104 -0.73 GLN 159
TYR 60 0.99 THR 105 -1.34 GLN 159
TYR 60 0.97 LYS 106 -1.50 GLN 159
TYR 60 0.80 VAL 107 -1.40 GLN 159
PRO 209 0.89 HIS 108 -1.39 ASP 156
TYR 99 1.38 LYS 109 -1.30 ASP 91
PRO 101 1.33 GLY 110 -1.52 ILE 89
VAL 102 1.11 PHE 111 -1.28 LEU 92
VAL 102 1.20 LEU 112 -1.76 LEU 92
SER 103 1.67 ASP 113 -1.54 TRP 88
VAL 102 1.71 SER 114 -1.57 TRP 88
VAL 102 1.33 TYR 115 -1.28 TRP 88
SER 103 1.35 GLY 116 -1.27 ASP 91
VAL 102 1.49 GLU 117 -1.09 TRP 88
VAL 102 1.27 VAL 118 -1.03 LEU 92
VAL 102 1.02 GLN 119 -1.26 LEU 92
SER 103 0.91 ASN 120 -1.17 LEU 92
VAL 102 0.88 GLU 121 -1.04 LEU 92
GLN 159 0.91 LEU 122 -1.03 LEU 92
GLN 159 1.27 VAL 123 -1.27 LEU 92
GLN 159 1.06 ALA 124 -1.15 LEU 92
ARG 160 1.18 THR 125 -0.94 LEU 92
ARG 160 1.35 VAL 126 -0.96 LEU 92
ARG 160 1.82 LEU 127 -1.11 LEU 92
ARG 160 1.32 ASP 128 -0.95 LEU 92
ASP 70 1.20 GLN 129 -0.74 LEU 92
GLU 162 1.22 PHE 130 -0.90 ASN 168
ASP 70 1.25 LYS 131 -0.95 VAL 97
ASP 70 1.22 GLN 132 -0.71 VAL 97
LYS 73 1.11 TYR 133 -0.61 VAL 97
GLU 162 1.02 PRO 134 -0.91 ASN 168
GLY 163 0.82 SER 135 -0.74 SER 167
ALA 45 0.81 TYR 136 -0.52 LEU 92
GLN 12 0.92 LYS 137 -0.83 PHE 130
GLU 16 0.86 VAL 138 -0.81 PHE 130
GLU 16 0.98 ALA 139 -0.63 VAL 126
GLU 16 0.72 VAL 140 -0.72 LEU 92
CYS 153 0.52 THR 141 -0.58 LEU 49
PRO 101 0.61 GLY 142 -0.51 LEU 49
PRO 101 0.60 HIS 143 -0.53 LEU 49
PRO 101 0.63 SER 144 -0.53 SER 114
PRO 101 0.82 LEU 145 -0.69 ILE 89
PRO 101 0.80 GLY 146 -0.68 VAL 123
VAL 102 0.60 GLY 147 -0.57 LEU 92
VAL 102 0.69 ALA 148 -0.85 ILE 89
VAL 102 0.92 THR 149 -1.01 LEU 92
VAL 102 0.64 ALA 150 -0.85 LEU 92
THR 191 0.88 LEU 151 -0.97 LEU 92
THR 191 1.12 LEU 152 -1.30 LEU 92
THR 191 0.82 CYS 153 -1.26 LEU 92
THR 191 0.81 ALA 154 -1.04 LEU 92
THR 191 1.02 LEU 155 -1.33 VAL 107
LEU 122 0.85 ASP 156 -1.55 VAL 97
ILE 75 1.03 LEU 157 -1.44 VAL 97
ALA 45 0.67 TYR 158 -1.38 VAL 97
VAL 123 1.27 GLN 159 -1.73 SER 98
LEU 127 1.82 ARG 160 -1.54 SER 98
LEU 127 1.30 GLU 161 -1.59 TYR 99
PHE 130 1.22 GLU 162 -1.21 VAL 97
ALA 45 0.83 GLY 163 -1.14 PRO 100
GLN 12 0.85 LEU 164 -1.12 VAL 97
GLN 12 0.83 SER 165 -1.09 TYR 99
GLN 12 0.92 SER 166 -0.83 GLU 72
GLN 12 1.23 SER 167 -0.85 PRO 134
GLN 12 1.21 ASN 168 -0.91 PRO 134
GLN 12 0.99 LEU 169 -0.79 VAL 97
GLN 12 1.04 PHE 170 -0.83 GLU 72
GLU 13 0.80 LEU 171 -0.77 GLU 72
GLU 13 0.63 TYR 172 -0.84 GLU 72
GLU 13 0.42 THR 173 -0.64 GLU 72
PRO 101 0.40 GLN 174 -0.65 LEU 49
PRO 101 0.42 GLY 175 -0.55 LEU 49
PRO 101 0.45 GLN 176 -0.51 GLU 72
PRO 101 0.41 PRO 177 -0.61 LEU 155
THR 241 0.41 ARG 178 -0.74 LEU 155
TYR 60 0.51 VAL 179 -1.04 LEU 155
LEU 112 0.71 GLY 180 -1.03 GLN 159
LEU 112 0.64 ASN 181 -0.99 PHE 94
LEU 112 0.67 PRO 182 -0.83 THR 93
LEU 112 0.87 ALA 183 -0.83 GLN 159
LEU 112 1.15 PHE 184 -0.98 GLN 159
LEU 112 0.90 ALA 185 -0.75 GLU 72
LEU 112 0.88 ASN 186 -0.76 GLU 72
GLY 116 1.15 TYR 187 -0.69 GLU 72
LEU 152 1.05 VAL 188 -0.80 GLU 72
LEU 152 0.82 VAL 189 -0.92 GLU 72
GLY 116 1.08 SER 190 -0.80 GLU 72
LEU 152 1.12 THR 191 -0.77 GLU 72
LEU 152 0.73 GLY 192 -1.09 GLU 72
ALA 154 0.76 ILE 193 -1.07 GLU 72
GLU 13 0.75 PRO 194 -1.37 GLU 72
GLU 13 0.65 TYR 195 -1.12 GLU 72
GLU 13 0.60 ARG 196 -1.10 GLU 72
GLU 13 0.38 ARG 197 -0.86 GLU 72
GLU 13 0.32 THR 198 -0.77 SER 71
PRO 101 0.26 VAL 199 -0.66 SER 71
PRO 101 0.28 ASN 200 -0.63 LEU 49
LEU 92 0.32 GLU 201 -0.59 SER 71
LEU 92 0.47 ARG 202 -0.52 SER 71
LEU 92 0.39 ASP 203 -0.49 LEU 49
LEU 92 0.52 ILE 204 -0.44 SER 71
PRO 101 0.42 VAL 205 -0.44 LEU 155
PRO 96 0.32 PRO 206 -0.58 GLU 72
PRO 96 0.44 HIS 207 -0.66 THR 93
PRO 96 0.59 LEU 208 -0.74 THR 93
PRO 96 0.96 PRO 209 -0.96 THR 93
PRO 96 0.85 PRO 210 -0.98 THR 93
PRO 96 0.66 ALA 211 -0.96 THR 93
PRO 96 0.70 ALA 212 -1.06 THR 93
PRO 96 0.86 PHE 213 -1.51 THR 93
VAL 97 0.68 GLY 214 -1.22 THR 93
VAL 107 0.51 PHE 215 -1.09 THR 93
LEU 112 0.45 LEU 216 -0.84 THR 93
LEU 112 0.46 HIS 217 -0.79 GLU 72
LEU 112 0.58 ALA 218 -0.90 GLU 72
LEU 151 0.47 GLY 219 -1.04 GLU 72
LEU 151 0.35 SER 220 -1.07 GLU 72
THR 241 0.38 GLU 221 -0.97 SER 71
SER 167 0.37 TYR 222 -0.98 SER 71
SER 167 0.31 TRP 223 -0.83 SER 71
SER 167 0.39 ILE 224 -0.75 LEU 49
SER 167 0.36 THR 225 -0.67 SER 71
SER 167 0.46 ASP 226 -0.62 THR 46
LYS 137 0.53 ASN 227 -0.63 HIS 42
LYS 137 0.60 SER 228 -0.59 HIS 42
ASN 168 0.69 PRO 229 -0.64 THR 46
ASN 168 0.68 GLU 230 -0.76 THR 46
SER 167 0.61 THR 231 -0.76 THR 46
SER 167 0.55 VAL 232 -0.86 SER 71
SER 167 0.43 GLN 233 -0.94 SER 71
SER 167 0.43 VAL 234 -1.05 SER 71
LEU 112 0.28 CYS 235 -1.00 SER 71
LEU 112 0.32 THR 236 -1.13 SER 71
LEU 112 0.38 SER 237 -1.00 GLU 72
LEU 112 0.46 ASP 238 -1.05 GLU 72
LEU 112 0.50 LEU 239 -0.91 GLU 72
LEU 112 0.43 GLU 240 -0.83 GLU 72
LEU 112 0.43 THR 241 -0.75 GLU 72
PRO 96 0.38 SER 242 -0.70 SER 71
PRO 96 0.29 ASP 243 -0.80 SER 71
LEU 92 0.22 CYS 244 -0.80 SER 71
LEU 92 0.30 SER 245 -0.69 SER 71
LEU 92 0.40 ASN 246 -0.65 SER 71
LEU 92 0.44 SER 247 -0.66 SER 71
LEU 92 0.53 ILE 248 -0.58 SER 71
LEU 92 0.65 VAL 249 -0.61 THR 93
LEU 92 0.82 PRO 250 -0.65 THR 93
LEU 92 0.77 PHE 251 -0.50 THR 93
LEU 92 0.72 THR 252 -0.44 SER 71
ILE 89 0.74 SER 253 -0.40 LEU 49
ILE 89 0.94 VAL 254 -0.49 SER 114
ILE 89 0.77 LEU 255 -0.47 SER 114
ILE 89 0.52 ASP 256 -0.47 LEU 49
PRO 101 0.46 HIS 257 -0.47 SER 114
PRO 101 0.51 LEU 258 -0.49 SER 114
PRO 101 0.45 SER 259 -0.53 LEU 49
ALA 139 0.40 TYR 260 -0.67 LEU 49
LYS 137 0.47 PHE 261 -0.82 THR 46
LYS 137 0.44 GLY 262 -0.85 HIS 42
PRO 101 0.45 ILE 263 -0.73 HIS 42
ARG 86 0.53 ASN 264 -0.49 ILE 41
PRO 101 0.58 THR 265 -0.49 LEU 49
PRO 101 0.69 GLY 266 -0.56 SER 114
PRO 101 0.68 LEU 267 -0.63 ASP 61
PRO 101 0.70 CYS 268 -0.53 ASP 61

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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.