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***  LYASE (OXO-ACID) 04-MAR-94 1CRM  ***

CA distance fluctuations for 260221185340572269

---  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
GLU 133 0.19 TRP 5 -0.42 GLY 63
GLN 249 0.19 GLY 6 -0.52 HIS 64
PRO 247 0.35 TYR 7 -0.39 MET 241
PRO 247 0.38 ASP 8 -0.49 MET 241
GLN 249 0.52 ASP 9 -0.42 PRO 240
PRO 250 0.38 LYS 10 -0.48 SER 231
GLN 249 0.27 ASN 11 -0.43 SER 231
GLN 249 0.37 GLY 12 -0.37 MET 241
GLN 249 0.40 PRO 13 -0.30 ASN 244
PRO 250 0.44 GLU 14 -0.34 SER 99
PRO 250 0.32 GLN 15 -0.31 SER 99
LEU 203 0.25 TRP 16 -0.27 VAL 233
SER 43 0.29 SER 17 -0.26 VAL 233
SER 43 0.26 LYS 18 -0.32 VAL 233
LYS 137 0.26 LEU 19 -0.35 VAL 233
LYS 137 0.31 TYR 20 -0.29 VAL 233
SER 43 0.30 PRO 21 -0.27 VAL 233
PRO 83 0.34 ILE 22 -0.24 VAL 233
SER 43 0.29 ALA 23 -0.23 VAL 62
SER 43 0.34 ASN 24 -0.23 PRO 247
SER 43 0.38 GLY 25 -0.19 VAL 62
SER 43 0.44 ASN 26 -0.29 SER 136
SER 43 0.39 ASN 27 -0.33 ALA 138
ASP 9 0.33 GLN 28 -0.16 SER 136
ASP 9 0.32 SER 29 -0.17 ALA 138
ASP 9 0.31 PRO 30 -0.15 ALA 138
ASP 9 0.38 VAL 31 -0.28 ALA 138
ASP 9 0.38 ASP 32 -0.27 ALA 138
ASP 9 0.32 ILE 33 -0.33 ALA 138
ASP 9 0.34 LYS 34 -0.35 ALA 138
ASP 9 0.28 THR 35 -0.32 ASP 139
ASP 9 0.30 SER 36 -0.36 ALA 138
ASP 9 0.35 GLU 37 -0.42 ASP 139
ASP 9 0.33 THR 38 -0.41 ASP 139
ASP 9 0.32 LYS 39 -0.41 LYS 127
ARG 254 0.28 HIS 40 -0.36 PRO 83
ARG 254 0.43 ASP 41 -0.46 SER 85
ASN 26 0.36 THR 42 -0.39 SER 85
ASN 26 0.44 SER 43 -0.46 SER 85
ASN 26 0.38 LEU 44 -0.35 SER 85
PRO 195 0.34 LYS 45 -0.25 SER 182
PRO 195 0.26 PRO 46 -0.28 SER 182
PRO 195 0.20 ILE 47 -0.29 SER 182
SER 187 0.17 SER 48 -0.30 SER 182
SER 187 0.32 VAL 49 -0.28 SER 48
SER 187 0.35 SER 50 -0.25 TYR 51
SER 187 0.29 TYR 51 -0.25 SER 50
SER 187 0.25 ASN 52 -0.20 GLY 81
LYS 156 0.20 PRO 53 -0.20 GLY 81
LYS 156 0.18 ALA 54 -0.22 GLY 235
LYS 156 0.17 THR 55 -0.21 GLY 235
LYS 156 0.18 ALA 56 -0.22 LYS 172
LEU 157 0.17 LYS 57 -0.24 GLY 235
VAL 160 0.17 GLU 58 -0.28 LYS 172
SER 130 0.14 ILE 59 -0.24 GLY 6
SER 130 0.14 ILE 60 -0.30 GLY 6
ALA 132 0.15 ASN 61 -0.34 GLY 6
ALA 132 0.21 VAL 62 -0.41 GLY 6
ALA 132 0.23 GLY 63 -0.48 GLY 6
ALA 132 0.24 HIS 64 -0.52 GLY 6
ALA 132 0.23 SER 65 -0.40 GLY 6
ALA 132 0.21 PHE 66 -0.30 GLY 6
ALA 132 0.20 HIS 67 -0.26 GLY 6
SER 130 0.17 VAL 68 -0.21 GLY 6
SER 130 0.18 ASN 69 -0.20 LYS 172
SER 130 0.16 PHE 70 -0.20 GLU 234
LYS 156 0.15 GLU 71 -0.23 GLY 235
SER 187 0.14 ASP 72 -0.19 THR 255
SER 187 0.15 ASN 73 -0.21 GLY 235
SER 187 0.18 GLN 74 -0.21 SER 43
SER 187 0.20 ASP 75 -0.24 SER 43
SER 187 0.24 ARG 76 -0.23 SER 43
SER 187 0.25 SER 77 -0.21 SER 43
SER 187 0.23 VAL 78 -0.24 SER 43
SER 187 0.22 LEU 79 -0.21 VAL 78
ILE 22 0.19 LYS 80 -0.38 GLY 81
ASN 26 0.24 GLY 81 -0.38 LYS 80
PRO 195 0.32 GLY 82 -0.24 SER 182
PRO 195 0.38 PRO 83 -0.41 ASP 41
GLU 205 0.32 PHE 84 -0.35 ASP 41
ASP 139 0.36 SER 85 -0.46 SER 43
ASP 139 0.25 ASP 86 -0.36 ASP 41
ILE 22 0.15 SER 87 -0.33 PHE 84
SER 187 0.15 TYR 88 -0.24 LYS 39
SER 187 0.17 ARG 89 -0.22 ASP 41
SER 187 0.17 LEU 90 -0.18 SER 43
SER 130 0.18 PHE 91 -0.17 PRO 195
PHE 93 0.18 GLN 92 -0.17 LEU 198
GLN 92 0.18 PHE 93 -0.15 GLY 6
ALA 132 0.18 HIS 94 -0.19 GLY 6
ALA 132 0.18 PHE 95 -0.18 GLY 6
ALA 132 0.17 HIS 96 -0.20 PRO 13
SER 105 0.24 TRP 97 -0.22 PRO 13
VAL 112 0.28 GLY 98 -0.29 GLU 14
ALA 238 0.34 SER 99 -0.34 GLU 14
ALA 238 0.32 THR 100 -0.33 GLU 14
VAL 112 0.28 ASN 101 -0.29 GLU 14
VAL 112 0.39 GLU 102 -0.26 GLU 14
VAL 112 0.37 HIS 103 -0.26 GLU 14
ALA 238 0.25 GLY 104 -0.25 GLU 14
TRP 97 0.24 SER 105 -0.13 GLU 14
VAL 239 0.20 GLU 106 -0.14 ASN 24
ASP 9 0.25 HIS 107 -0.16 ALA 138
ASP 9 0.27 THR 108 -0.17 ALA 138
LYS 113 0.28 VAL 109 -0.22 ALA 138
GLU 102 0.33 ASP 110 -0.27 ALA 138
ASP 9 0.34 GLY 111 -0.23 ALA 138
GLU 102 0.39 VAL 112 -0.18 ALA 138
VAL 112 0.33 LYS 113 -0.16 ASN 24
SER 115 0.27 TYR 114 -0.13 GLU 14
TYR 114 0.27 SER 115 -0.21 GLU 14
TYR 114 0.17 ALA 116 -0.19 PRO 13
TYR 114 0.13 GLU 117 -0.11 PRO 13
ALA 132 0.13 LEU 118 -0.12 GLY 6
ALA 132 0.13 HIS 119 -0.08 ILE 210
ALA 121 0.13 VAL 120 -0.13 PHE 93
VAL 120 0.13 ALA 121 -0.17 THR 208
SER 187 0.13 HIS 122 -0.20 THR 255
SER 187 0.12 TRP 123 -0.28 THR 255
TYR 20 0.16 ASN 124 -0.36 THR 255
SER 187 0.13 SER 125 -0.31 THR 255
TYR 20 0.16 ALA 126 -0.36 THR 255
TYR 20 0.19 LYS 127 -0.45 THR 255
TYR 20 0.18 TYR 128 -0.38 THR 255
GLY 63 0.15 SER 129 -0.33 THR 255
HIS 67 0.19 SER 130 -0.28 ARG 254
SER 65 0.17 LEU 131 -0.27 ARG 254
HIS 64 0.24 ALA 132 -0.26 ARG 254
PRO 202 0.22 GLU 133 -0.33 ARG 254
TYR 20 0.21 ALA 134 -0.37 ARG 254
PRO 202 0.22 ALA 135 -0.30 ARG 254
TYR 20 0.29 SER 136 -0.36 ARG 254
TYR 20 0.31 LYS 137 -0.49 ARG 254
SER 85 0.35 ALA 138 -0.64 ARG 254
SER 85 0.36 ASP 139 -0.58 PRO 195
TYR 20 0.24 GLY 140 -0.40 PRO 195
TYR 20 0.18 LEU 141 -0.30 PRO 195
ILE 22 0.15 ALA 142 -0.24 THR 255
ASP 9 0.11 VAL 143 -0.16 ALA 121
ASP 9 0.09 ILE 144 -0.11 PHE 93
ASP 9 0.09 GLY 145 -0.07 ASP 139
TYR 51 0.10 VAL 146 -0.10 LEU 189
THR 35 0.15 LEU 147 -0.09 LEU 189
THR 35 0.17 MET 148 -0.14 GLU 14
THR 35 0.23 LYS 149 -0.16 GLU 14
ASP 110 0.23 VAL 150 -0.19 GLU 14
SER 36 0.22 GLY 151 -0.19 GLU 14
SER 36 0.18 GLU 152 -0.21 SER 187
PHE 176 0.17 ALA 153 -0.25 SER 187
ASN 178 0.18 ASN 154 -0.27 SER 187
ASN 178 0.20 PRO 155 -0.25 SER 187
PHE 179 0.22 LYS 156 -0.23 PRO 46
PHE 176 0.19 LEU 157 -0.21 PRO 46
PHE 176 0.19 GLN 158 -0.21 ASP 8
PHE 176 0.21 LYS 159 -0.21 PRO 46
PHE 176 0.18 VAL 160 -0.22 GLY 6
ALA 174 0.21 LEU 161 -0.25 ASP 8
ALA 174 0.24 ASP 162 -0.25 ASP 8
ALA 174 0.25 ALA 163 -0.24 LYS 10
GLN 222 0.18 LEU 164 -0.28 LYS 10
GLU 221 0.24 GLN 165 -0.29 LYS 10
GLU 221 0.18 ALA 166 -0.28 LYS 10
GLN 225 0.19 ILE 167 -0.30 LYS 10
SER 228 0.21 LYS 168 -0.34 LYS 10
SER 228 0.25 THR 169 -0.36 LYS 10
SER 228 0.11 LYS 170 -0.40 LYS 10
GLN 225 0.11 GLY 171 -0.35 GLU 234
GLN 225 0.15 LYS 172 -0.46 ARG 173
ALA 163 0.19 ARG 173 -0.46 LYS 172
ALA 163 0.25 ALA 174 -0.32 PRO 175
LYS 159 0.19 PRO 175 -0.32 ALA 174
LYS 159 0.21 PHE 176 -0.24 ALA 166
LYS 156 0.20 THR 177 -0.26 ALA 166
LYS 156 0.21 ASN 178 -0.22 ALA 166
LYS 156 0.22 PHE 179 -0.22 ALA 163
ILE 216 0.18 ASP 180 -0.27 SER 48
ILE 216 0.17 PRO 181 -0.23 SER 48
LEU 185 0.21 SER 182 -0.30 SER 48
ILE 216 0.18 THR 183 -0.28 PRO 46
ILE 216 0.23 LEU 184 -0.24 PRO 46
SER 182 0.21 LEU 185 -0.22 PRO 46
SER 50 0.18 PRO 186 -0.19 ASN 154
SER 50 0.35 SER 187 -0.27 ASN 154
VAL 49 0.24 SER 188 -0.18 ASN 154
VAL 49 0.14 LEU 189 -0.20 LYS 156
ASN 26 0.16 ASP 190 -0.16 PRO 83
ASN 26 0.16 PHE 191 -0.19 PRO 83
ASP 9 0.23 TRP 192 -0.25 ASP 139
LYS 45 0.23 THR 193 -0.34 ASP 139
ASN 27 0.32 TYR 194 -0.48 ASP 139
PRO 83 0.38 PRO 195 -0.63 ALA 138
PRO 83 0.30 GLY 196 -0.34 ALA 138
PRO 83 0.26 SER 197 -0.15 VAL 31
ASP 9 0.19 LEU 198 -0.18 HIS 67
ASP 9 0.20 THR 199 -0.13 GLY 25
ALA 132 0.18 HIS 200 -0.19 VAL 62
GLU 133 0.20 PRO 201 -0.29 VAL 62
SER 136 0.28 PRO 202 -0.26 VAL 62
TRP 16 0.25 LEU 203 -0.22 VAL 62
SER 85 0.27 TYR 204 -0.20 ASN 27
PRO 83 0.34 GLU 205 -0.29 SER 136
SER 85 0.33 SER 206 -0.34 ARG 254
PRO 83 0.23 VAL 207 -0.31 PRO 195
PRO 83 0.30 THR 208 -0.31 ASP 139
ASP 9 0.19 TRP 209 -0.21 ASP 139
ASP 9 0.15 ILE 210 -0.14 ASP 139
ASP 9 0.15 ILE 211 -0.14 ASP 139
VAL 49 0.13 CYS 212 -0.12 PRO 83
THR 35 0.11 LYS 213 -0.13 PRO 83
PRO 186 0.16 GLU 214 -0.11 PRO 83
THR 35 0.19 SER 215 -0.13 SER 187
LEU 184 0.23 ILE 216 -0.23 SER 187
THR 35 0.17 SER 217 -0.24 SER 187
THR 35 0.16 VAL 218 -0.20 SER 187
ASP 110 0.18 SER 219 -0.20 GLU 14
GLY 235 0.22 SER 220 -0.24 GLU 14
GLN 165 0.24 GLU 221 -0.26 ASP 9
GLN 165 0.20 GLN 222 -0.25 ASP 8
VAL 112 0.21 LEU 223 -0.26 ASP 8
GLY 235 0.27 ALA 224 -0.31 ASP 8
GLU 234 0.25 GLN 225 -0.30 ASP 8
GLU 234 0.19 PHE 226 -0.31 ASP 8
GLU 234 0.26 ARG 227 -0.38 ASP 8
GLU 234 0.37 SER 228 -0.36 ASP 8
GLU 234 0.24 LEU 229 -0.34 ASP 8
GLU 234 0.26 LEU 230 -0.40 LYS 10
ALA 132 0.17 SER 231 -0.48 LYS 10
VAL 112 0.16 ASN 232 -0.47 LYS 10
SER 228 0.20 VAL 233 -0.43 LYS 10
SER 228 0.37 GLU 234 -0.35 GLY 171
SER 228 0.33 GLY 235 -0.30 ARG 173
THR 100 0.23 ASP 236 -0.32 LYS 10
SER 99 0.28 ASN 237 -0.26 LYS 168
SER 99 0.34 ALA 238 -0.32 LYS 168
HIS 243 0.28 VAL 239 -0.37 LYS 10
SER 99 0.28 PRO 240 -0.42 ASP 9
PRO 240 0.22 MET 241 -0.49 ASP 8
ALA 238 0.29 GLN 242 -0.44 ASP 8
VAL 239 0.28 HIS 243 -0.30 GLY 12
VAL 239 0.22 ASN 244 -0.30 PRO 13
VAL 239 0.22 ASN 245 -0.22 PRO 13
ASP 9 0.28 ARG 246 -0.19 ALA 23
ASP 9 0.49 PRO 247 -0.23 ASN 24
ASP 9 0.44 THR 248 -0.19 ASN 24
ASP 9 0.52 GLN 249 -0.17 GLY 111
ASP 9 0.51 PRO 250 -0.27 ALA 138
ASP 9 0.45 LEU 251 -0.42 ALA 138
ASP 9 0.42 LYS 252 -0.40 ALA 138
ASP 9 0.41 GLY 253 -0.51 ALA 138
THR 255 0.49 ARG 254 -0.64 ALA 138
ARG 254 0.49 THR 255 -0.57 ASP 139
ASP 9 0.34 VAL 256 -0.49 ASP 139
ARG 254 0.37 ARG 257 -0.39 ASP 139
ASP 9 0.24 ALA 258 -0.37 PRO 83
ASN 26 0.25 SER 259 -0.35 PRO 83
ASN 26 0.19 PHE 260 -0.25 PRO 83

If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: december 26th, 2025.