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CA distance fluctuations for 240228060428927675

---  normal mode 8  ---

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
ALA 54 0.16 GLN 1 -0.28 THR 28
TYR 3 0.18 VAL 2 -0.26 PRO 225
ALA 54 0.19 TYR 3 -0.16 TRP 29
TYR 56 0.24 ASN 4 -0.15 PRO 31
TYR 56 0.18 ILE 5 -0.13 PRO 31
THR 16 0.21 THR 6 -0.12 ARG 219
PRO 228 0.23 TRP 7 -0.09 LEU 161
PRO 228 0.33 GLU 8 -0.07 LEU 161
PRO 228 0.34 VAL 9 -0.05 THR 195
PRO 228 0.44 THR 10 -0.05 GLU 15
PRO 228 0.46 ASN 11 -0.07 SER 116
PRO 228 0.50 GLY 12 -0.12 SER 116
PRO 228 0.59 ASP 13 -0.10 ALA 54
PRO 228 0.58 ARG 14 -0.06 SER 116
PRO 228 0.60 GLU 15 -0.07 SER 69
PRO 228 0.50 THR 16 -0.07 LEU 161
PRO 228 0.42 VAL 17 -0.08 LEU 161
PRO 228 0.30 TRP 18 -0.10 LEU 161
PRO 228 0.24 ALA 19 -0.10 LEU 161
SER 58 0.19 ILE 20 -0.15 LEU 161
TYR 56 0.24 SER 21 -0.17 LEU 161
SER 57 0.20 GLY 22 -0.21 ASN 160
SER 57 0.20 ASN 23 -0.25 GLY 224
SER 57 0.16 HIS 24 -0.28 GLY 224
SER 57 0.13 PRO 25 -0.26 GLN 1
ALA 73 0.11 LEU 26 -0.16 LYS 147
SER 72 0.11 TRP 27 -0.19 GLN 1
SER 72 0.13 THR 28 -0.28 GLN 1
SER 72 0.14 TRP 29 -0.23 VAL 2
SER 69 0.14 TRP 30 -0.26 GLN 182
SER 69 0.16 PRO 31 -0.22 HIS 24
SER 69 0.15 VAL 32 -0.23 ASP 158
LYS 174 0.15 LEU 33 -0.15 GLY 22
LYS 174 0.18 THR 34 -0.13 GLY 22
PRO 228 0.20 PRO 35 -0.09 LEU 161
PRO 228 0.21 ASP 36 -0.07 LEU 161
PRO 228 0.25 LEU 37 -0.04 TYR 56
PRO 228 0.30 CYS 38 -0.07 ASP 129
PRO 228 0.34 MET 39 -0.06 GLN 165
PRO 228 0.37 LEU 40 -0.05 GLY 115
PRO 228 0.40 ALA 41 -0.10 PRO 128
PRO 228 0.45 LEU 42 -0.10 PRO 128
PRO 228 0.52 SER 43 -0.13 PRO 128
PRO 228 0.49 GLY 44 -0.18 PRO 128
PRO 228 0.46 PRO 45 -0.23 ASP 129
PRO 228 0.45 PRO 46 -0.23 ASP 129
PRO 228 0.38 HIS 47 -0.21 ASP 129
PRO 228 0.37 TRP 48 -0.15 ASP 129
PRO 228 0.39 GLY 49 -0.17 ASP 129
PRO 228 0.43 LEU 50 -0.14 ASP 129
PRO 228 0.50 GLU 51 -0.17 ASP 129
PRO 228 0.52 TYR 52 -0.14 ASP 129
PRO 228 0.49 GLN 53 -0.13 SER 69
PRO 228 0.54 ALA 54 -0.13 SER 69
PRO 228 0.50 PRO 55 -0.11 SER 69
PRO 228 0.42 TYR 56 -0.13 SER 69
PRO 228 0.41 SER 57 -0.15 SER 69
PRO 228 0.34 SER 58 -0.17 SER 69
PRO 228 0.30 PRO 59 -0.13 SER 69
PRO 228 0.33 PRO 60 -0.15 SER 69
PRO 228 0.30 GLY 61 -0.14 ASP 129
PRO 228 0.27 PRO 62 -0.12 ASP 129
PRO 228 0.22 PRO 63 -0.12 SER 69
PRO 228 0.17 CYS 64 -0.09 ASP 129
PRO 228 0.14 CYS 65 -0.08 ASP 129
ASN 160 0.09 SER 66 -0.06 ASP 129
ASN 160 0.12 GLY 67 -0.09 THR 92
GLN 165 0.16 SER 68 -0.12 SER 58
PRO 31 0.16 SER 69 -0.17 SER 58
PRO 31 0.14 GLY 70 -0.10 SER 58
PRO 31 0.13 SER 71 -0.08 PRO 62
PRO 228 0.18 SER 72 -0.09 ASP 129
PRO 228 0.22 ALA 73 -0.11 ASP 129
PRO 228 0.26 GLY 74 -0.13 ASP 129
PRO 228 0.21 CYS 75 -0.11 ASP 129
PRO 228 0.21 SER 76 -0.11 ASP 129
PRO 228 0.18 ARG 77 -0.09 ASP 129
PRO 228 0.19 ASP 78 -0.10 ARG 208
PRO 228 0.16 CYS 79 -0.08 ASP 129
PRO 228 0.12 ASP 80 -0.06 ASP 129
PRO 228 0.15 GLU 81 -0.08 SER 206
PRO 228 0.14 PRO 82 -0.08 SER 206
PRO 228 0.17 LEU 83 -0.08 SER 206
PRO 228 0.17 THR 84 -0.12 SER 206
PRO 228 0.22 SER 85 -0.17 SER 206
PRO 228 0.24 LEU 86 -0.14 SER 206
PRO 228 0.27 THR 87 -0.12 ARG 208
PRO 228 0.25 PRO 88 -0.09 ASP 129
PRO 228 0.29 ARG 89 -0.12 ASP 129
PRO 228 0.31 CYS 90 -0.11 ASP 129
PRO 228 0.33 ASN 91 -0.14 ASP 129
PRO 228 0.28 THR 92 -0.12 ASP 129
PRO 228 0.22 ALA 93 -0.09 ASP 129
PRO 228 0.20 TRP 94 -0.09 ASP 129
PRO 228 0.24 ASN 95 -0.10 ASP 129
PRO 228 0.21 ARG 96 -0.08 ASP 129
PRO 228 0.15 LEU 97 -0.05 ASP 129
PRO 228 0.18 LYS 98 -0.06 VAL 32
PRO 228 0.20 LEU 99 -0.07 VAL 32
PRO 228 0.14 ASP 100 -0.09 HIS 24
PRO 228 0.12 GLN 101 -0.11 HIS 24
PRO 228 0.16 VAL 102 -0.11 VAL 32
PRO 228 0.14 THR 103 -0.14 VAL 32
VAL 167 0.11 HIS 104 -0.16 VAL 32
VAL 167 0.09 LYS 105 -0.15 HIS 24
THR 163 0.09 SER 106 -0.18 HIS 24
PRO 228 0.11 SER 107 -0.15 TRP 30
PRO 228 0.15 GLU 108 -0.13 TRP 30
PRO 228 0.15 GLY 109 -0.14 VAL 32
PRO 228 0.19 PHE 110 -0.13 TRP 30
PRO 228 0.20 TYR 111 -0.15 TRP 30
PRO 228 0.24 VAL 112 -0.13 TRP 30
PRO 228 0.28 CYS 113 -0.11 TRP 30
PRO 228 0.31 PRO 114 -0.09 GLY 44
PRO 228 0.39 GLY 115 -0.13 GLY 44
PRO 228 0.42 SER 116 -0.12 GLY 44
PRO 228 0.35 HIS 117 -0.09 GLY 44
PRO 228 0.32 ARG 118 -0.09 GLY 44
PRO 228 0.30 PRO 119 -0.10 PRO 45
PRO 228 0.32 ARG 120 -0.11 PRO 45
PRO 228 0.31 GLU 121 -0.10 PRO 45
PRO 228 0.37 ALA 122 -0.13 PRO 45
PRO 228 0.36 LYS 123 -0.12 PRO 46
PRO 228 0.35 SER 124 -0.13 PRO 46
PRO 228 0.35 CYS 125 -0.12 PRO 46
PRO 228 0.41 GLY 126 -0.15 PRO 46
PRO 228 0.47 GLY 127 -0.16 PRO 45
PRO 228 0.48 PRO 128 -0.22 PRO 45
PRO 228 0.47 ASP 129 -0.23 PRO 46
PRO 228 0.40 SER 130 -0.17 HIS 47
PRO 228 0.39 PHE 131 -0.15 PRO 45
PRO 228 0.37 TYR 132 -0.12 PRO 45
PRO 228 0.32 CYS 133 -0.11 HIS 47
PRO 228 0.34 ALA 134 -0.13 HIS 47
PRO 228 0.29 SER 135 -0.10 SER 85
PRO 228 0.23 TRP 136 -0.11 THR 184
PRO 228 0.22 GLY 137 -0.12 ASN 185
PRO 228 0.26 CYS 138 -0.11 THR 184
PRO 228 0.23 GLU 139 -0.12 TRP 30
PRO 228 0.18 THR 140 -0.17 THR 184
PRO 228 0.15 THR 141 -0.19 TRP 30
PRO 228 0.15 GLY 142 -0.18 TRP 30
THR 162 0.15 ARG 143 -0.21 VAL 32
THR 162 0.12 VAL 144 -0.18 TRP 30
THR 162 0.13 TYR 145 -0.20 TRP 30
THR 162 0.12 TRP 146 -0.20 THR 28
THR 162 0.15 LYS 147 -0.22 TRP 30
THR 162 0.13 PRO 148 -0.20 THR 184
THR 162 0.16 SER 149 -0.22 THR 184
THR 162 0.15 SER 150 -0.17 GLN 1
LEU 161 0.15 SER 151 -0.18 GLN 1
PRO 228 0.15 TRP 152 -0.14 GLN 1
PRO 228 0.19 ASP 153 -0.12 GLN 1
PRO 228 0.18 TYR 154 -0.14 THR 28
PRO 228 0.15 ILE 155 -0.19 TRP 30
LEU 161 0.13 THR 156 -0.22 TRP 30
PRO 228 0.13 VAL 157 -0.20 TRP 30
LEU 161 0.14 ASP 158 -0.23 VAL 32
VAL 169 0.12 ASN 159 -0.19 VAL 32
VAL 169 0.16 ASN 160 -0.21 GLY 22
SER 151 0.15 LEU 161 -0.21 GLY 22
SER 149 0.16 THR 162 -0.20 GLY 224
LYS 147 0.12 THR 163 -0.15 GLY 22
SER 149 0.13 SER 164 -0.18 GLY 224
SER 68 0.16 GLN 165 -0.19 GLY 224
SER 151 0.13 ALA 166 -0.12 GLY 224
SER 149 0.11 VAL 167 -0.09 GLY 224
ASN 160 0.13 GLN 168 -0.09 TYR 56
ASN 160 0.16 VAL 169 -0.11 TYR 56
PRO 228 0.13 CYS 170 -0.07 TYR 56
PRO 228 0.12 LYS 171 -0.06 ASP 129
ASN 160 0.13 ASP 172 -0.11 ASN 173
PRO 228 0.19 ASN 173 -0.12 SER 69
THR 34 0.18 LYS 174 -0.11 SER 58
PRO 228 0.19 TRP 175 -0.10 TYR 56
PRO 228 0.13 CYS 176 -0.10 ALA 166
PRO 228 0.15 ASN 177 -0.06 GLY 22
LYS 174 0.13 PRO 178 -0.10 GLY 22
PRO 228 0.13 LEU 179 -0.12 GLY 22
LYS 174 0.14 ALA 180 -0.22 VAL 32
LYS 174 0.13 ILE 181 -0.19 VAL 157
SER 68 0.14 GLN 182 -0.26 TRP 30
SER 69 0.13 PHE 183 -0.21 TRP 30
SER 68 0.14 THR 184 -0.22 SER 149
SER 69 0.14 ASN 185 -0.24 GLN 1
SER 68 0.12 ALA 186 -0.19 GLN 1
PRO 228 0.14 GLY 187 -0.15 GLN 1
SER 69 0.12 LYS 188 -0.21 GLN 1
SER 69 0.10 GLN 189 -0.19 GLN 1
PRO 228 0.18 VAL 190 -0.10 GLN 1
PRO 228 0.21 THR 191 -0.06 LYS 147
PRO 228 0.32 SER 192 -0.04 ARG 217
PRO 228 0.32 TRP 193 -0.04 ARG 217
PRO 228 0.42 THR 194 -0.05 ALA 19
PRO 228 0.50 THR 195 -0.07 ARG 217
PRO 228 0.43 GLY 196 -0.06 GLU 15
PRO 228 0.39 HIS 197 -0.06 ASP 13
PRO 228 0.39 TYR 198 -0.09 GLY 12
PRO 228 0.35 TRP 199 -0.09 GLY 44
PRO 228 0.35 GLY 200 -0.11 GLY 44
PRO 228 0.30 LEU 201 -0.10 TRP 30
PRO 228 0.29 ARG 202 -0.10 TRP 30
PRO 228 0.25 LEU 203 -0.10 TRP 30
PRO 228 0.22 TYR 204 -0.12 TRP 30
PRO 228 0.23 VAL 205 -0.14 SER 85
PRO 228 0.25 SER 206 -0.17 SER 85
PRO 228 0.27 GLY 207 -0.13 SER 85
PRO 228 0.31 ARG 208 -0.14 SER 85
PRO 228 0.29 ASP 209 -0.11 LEU 86
PRO 228 0.33 PRO 210 -0.11 THR 87
PRO 228 0.35 GLY 211 -0.09 ARG 89
PRO 228 0.40 LEU 212 -0.10 GLY 200
PRO 228 0.41 THR 213 -0.14 GLY 44
PRO 228 0.40 PHE 214 -0.07 GLY 44
PRO 228 0.40 GLY 215 -0.05 GLU 15
PRO 228 0.34 ILE 216 -0.06 GLY 196
PRO 228 0.37 ARG 217 -0.07 THR 195
PRO 228 0.32 LEU 218 -0.05 LEU 161
GLN 221 0.39 ARG 219 -0.12 THR 6
GLN 221 0.33 TYR 220 -0.08 LEU 161
GLU 15 0.39 GLN 221 -0.10 TYR 3
GLU 15 0.33 ASN 222 -0.10 ASN 23
ALA 54 0.32 LEU 223 -0.22 ASN 23
ALA 54 0.34 GLY 224 -0.28 HIS 24
ALA 54 0.35 PRO 225 -0.26 VAL 2
GLU 15 0.39 ARG 226 -0.19 VAL 2
GLU 15 0.52 VAL 227 -0.13 VAL 2
GLU 15 0.60 PRO 228 -0.11 GLY 224

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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.