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

CA distance fluctuations for 260221185340572269

---  normal mode 9  ---

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
GLY 111 0.26 TRP 5 -0.71 ALA 132
GLY 111 0.28 GLY 6 -0.58 ALA 132
GLY 111 0.36 TYR 7 -0.60 SER 231
GLY 111 0.44 ASP 8 -0.89 ASN 237
GLY 111 0.70 ASP 9 -1.12 ASN 237
GLY 111 0.54 LYS 10 -1.05 ASP 236
GLY 111 0.38 ASN 11 -0.77 ASP 236
GLY 111 0.45 GLY 12 -0.67 ASN 237
GLY 111 0.42 PRO 13 -0.51 ASN 237
GLY 111 0.50 GLU 14 -0.60 ASN 237
GLY 111 0.42 GLN 15 -0.64 ASN 237
GLY 111 0.29 TRP 16 -0.53 ALA 132
PRO 250 0.30 SER 17 -0.44 ALA 132
GLY 111 0.27 LYS 18 -0.53 ALA 132
GLY 111 0.22 LEU 19 -0.64 ALA 132
PRO 21 0.16 TYR 20 -0.60 ALA 132
GLU 37 0.17 PRO 21 -0.37 ALA 132
ARG 173 0.15 ILE 22 -0.27 ALA 132
GLU 37 0.19 ALA 23 -0.32 ALA 132
GLU 37 0.24 ASN 24 -0.32 ASN 237
ALA 138 0.14 GLY 25 -0.24 ASN 237
ALA 138 0.22 ASN 26 -0.21 ASN 237
ALA 138 0.20 ASN 27 -0.17 ASN 237
ASP 9 0.17 GLN 28 -0.20 ASN 237
ASP 9 0.22 SER 29 -0.17 ASN 237
ASP 9 0.30 PRO 30 -0.15 ASN 237
ASP 9 0.39 VAL 31 -0.17 LYS 113
ASP 9 0.51 ASP 32 -0.18 GLY 253
ASP 9 0.46 ILE 33 -0.15 ARG 254
ASP 9 0.51 LYS 34 -0.16 SER 215
ASP 9 0.45 THR 35 -0.23 SER 215
ASP 9 0.48 SER 36 -0.20 SER 215
ASP 9 0.45 GLU 37 -0.14 SER 215
ASP 9 0.38 THR 38 -0.13 SER 215
ASP 9 0.32 LYS 39 -0.08 PRO 155
ASP 9 0.29 HIS 40 -0.07 SER 182
ASP 9 0.22 ASP 41 -0.11 SER 206
ASP 9 0.20 THR 42 -0.12 PRO 202
ASP 9 0.15 SER 43 -0.16 PRO 202
ASP 9 0.15 LEU 44 -0.16 PRO 202
ASP 9 0.13 LYS 45 -0.16 PRO 202
ASP 9 0.13 PRO 46 -0.15 PRO 202
PRO 186 0.14 ILE 47 -0.17 PRO 202
PRO 186 0.17 SER 48 -0.18 PRO 202
SER 217 0.15 VAL 49 -0.20 TRP 5
THR 183 0.17 SER 50 -0.22 TRP 5
THR 183 0.17 TYR 51 -0.24 TRP 5
LYS 156 0.16 ASN 52 -0.25 TRP 5
LYS 156 0.16 PRO 53 -0.22 TRP 5
ALA 132 0.15 ALA 54 -0.25 TRP 5
ALA 132 0.17 THR 55 -0.30 TRP 5
ALA 135 0.21 ALA 56 -0.27 TRP 5
ALA 132 0.27 LYS 57 -0.29 LYS 10
ALA 135 0.31 GLU 58 -0.31 LYS 10
ALA 135 0.30 ILE 59 -0.28 LYS 10
ALA 135 0.28 ILE 60 -0.35 LYS 10
TYR 204 0.22 ASN 61 -0.38 LYS 10
TYR 204 0.23 VAL 62 -0.45 GLY 6
PRO 202 0.13 GLY 63 -0.54 ASP 8
MET 241 0.10 HIS 64 -0.48 TYR 7
TYR 204 0.18 SER 65 -0.32 TYR 7
TYR 204 0.23 PHE 66 -0.28 ASP 8
ALA 135 0.26 HIS 67 -0.33 GLY 6
ALA 135 0.29 VAL 68 -0.27 GLY 6
ALA 135 0.32 ASN 69 -0.38 GLY 6
ALA 135 0.26 PHE 70 -0.35 TRP 5
ALA 132 0.19 GLU 71 -0.44 TRP 5
THR 55 0.15 ASP 72 -0.48 TRP 5
ALA 54 0.15 ASN 73 -0.49 TRP 5
THR 183 0.10 GLN 74 -0.42 TRP 5
THR 183 0.11 ASP 75 -0.36 TRP 5
LYS 156 0.13 ARG 76 -0.32 TRP 5
THR 183 0.14 SER 77 -0.30 TRP 5
THR 183 0.13 VAL 78 -0.29 TRP 5
SER 217 0.11 LEU 79 -0.25 TRP 5
PRO 186 0.12 LYS 80 -0.23 PRO 202
PRO 186 0.10 GLY 81 -0.21 PRO 202
ASP 9 0.11 GLY 82 -0.19 PRO 202
ARG 254 0.13 PRO 83 -0.21 PRO 202
ARG 254 0.14 PHE 84 -0.25 PRO 202
ARG 254 0.15 SER 85 -0.26 PRO 202
ARG 254 0.16 ASP 86 -0.28 PRO 202
ARG 254 0.14 SER 87 -0.28 PRO 202
ARG 254 0.12 TYR 88 -0.32 PRO 202
PRO 195 0.10 ARG 89 -0.38 TRP 5
PRO 195 0.09 LEU 90 -0.35 TRP 5
ALA 135 0.21 PHE 91 -0.41 TRP 5
ALA 135 0.25 GLN 92 -0.36 GLY 6
ALA 135 0.21 PHE 93 -0.24 GLY 6
TYR 204 0.19 HIS 94 -0.22 GLY 6
TYR 204 0.13 PHE 95 -0.10 GLY 6
ASP 9 0.12 HIS 96 -0.10 ALA 132
ASP 9 0.19 TRP 97 -0.13 THR 248
ASP 9 0.29 GLY 98 -0.20 THR 248
ASP 8 0.25 SER 99 -0.21 THR 248
ASP 9 0.34 THR 100 -0.20 THR 248
ASP 9 0.30 ASN 101 -0.16 PRO 250
ASP 9 0.42 GLU 102 -0.19 PRO 250
ASP 9 0.52 HIS 103 -0.21 PRO 250
ASP 9 0.41 GLY 104 -0.19 THR 248
ASP 9 0.38 SER 105 -0.12 PRO 250
ASP 9 0.37 GLU 106 -0.13 ALA 132
ASP 9 0.40 HIS 107 -0.14 LEU 251
ASP 9 0.51 THR 108 -0.17 LEU 251
ASP 9 0.51 VAL 109 -0.17 LYS 149
ASP 9 0.59 ASP 110 -0.19 GLY 151
ASP 9 0.70 GLY 111 -0.21 GLY 253
ASP 9 0.63 VAL 112 -0.19 GLY 151
ASP 9 0.58 LYS 113 -0.19 LEU 251
ASP 9 0.45 TYR 114 -0.15 VAL 150
ASP 9 0.36 SER 115 -0.15 PRO 250
ASP 9 0.27 ALA 116 -0.10 PRO 250
ASP 9 0.22 GLU 117 -0.08 THR 35
ASP 9 0.11 LEU 118 -0.09 HIS 64
SER 206 0.10 HIS 119 -0.16 TRP 5
SER 206 0.12 VAL 120 -0.22 TRP 5
SER 206 0.14 ALA 121 -0.33 TRP 5
PRO 195 0.11 HIS 122 -0.37 TRP 5
LYS 57 0.13 TRP 123 -0.44 PRO 202
ARG 254 0.15 ASN 124 -0.40 PRO 202
ARG 254 0.13 SER 125 -0.41 TRP 5
ARG 254 0.17 ALA 126 -0.34 TRP 5
ARG 254 0.20 LYS 127 -0.34 TRP 5
ARG 254 0.14 TYR 128 -0.43 TRP 5
LYS 57 0.12 SER 129 -0.50 TRP 5
LYS 57 0.18 SER 130 -0.59 TRP 5
LYS 57 0.23 LEU 131 -0.62 TRP 5
LYS 57 0.27 ALA 132 -0.74 PRO 202
LYS 57 0.23 GLU 133 -0.60 PRO 202
GLU 58 0.21 ALA 134 -0.54 PRO 202
ASN 69 0.32 ALA 135 -0.60 PRO 202
ARG 173 0.29 SER 136 -0.43 TYR 20
ARG 173 0.22 LYS 137 -0.32 PRO 202
ASN 26 0.22 ALA 138 -0.20 PRO 202
PRO 195 0.25 ASP 139 -0.27 PRO 202
ASN 69 0.18 GLY 140 -0.43 PRO 202
ASN 69 0.17 LEU 141 -0.41 PRO 202
PRO 195 0.14 ALA 142 -0.30 PRO 202
PRO 195 0.10 VAL 143 -0.24 PRO 201
ASP 9 0.10 ILE 144 -0.16 PRO 201
ASP 9 0.17 GLY 145 -0.09 PRO 201
ASP 9 0.21 VAL 146 -0.13 THR 35
ASP 9 0.29 LEU 147 -0.15 THR 35
ASP 9 0.27 MET 148 -0.14 THR 35
ASP 9 0.32 LYS 149 -0.19 ASP 110
ASP 9 0.28 VAL 150 -0.19 VAL 112
ASP 9 0.24 GLY 151 -0.19 ASP 110
ALA 238 0.21 GLU 152 -0.18 SER 36
ALA 238 0.24 ALA 153 -0.16 THR 35
ALA 238 0.21 ASN 154 -0.16 THR 35
GLY 235 0.24 PRO 155 -0.17 THR 35
GLY 235 0.20 LYS 156 -0.15 THR 35
ALA 238 0.21 LEU 157 -0.13 THR 35
GLY 235 0.27 GLN 158 -0.12 THR 35
GLY 235 0.27 LYS 159 -0.13 ASN 11
GLY 235 0.23 VAL 160 -0.15 ASN 11
GLY 235 0.30 LEU 161 -0.12 ASP 8
GLY 235 0.36 ASP 162 -0.15 LYS 10
GLY 235 0.29 ALA 163 -0.21 LYS 10
GLY 235 0.32 LEU 164 -0.23 ASP 8
GLY 235 0.46 GLN 165 -0.26 LYS 10
GLY 235 0.36 ALA 166 -0.30 LYS 10
GLY 235 0.25 ILE 167 -0.35 LYS 10
GLY 235 0.33 LYS 168 -0.38 ASP 8
LYS 168 0.21 THR 169 -0.51 ASP 8
TYR 204 0.12 LYS 170 -0.54 LYS 10
TYR 204 0.23 GLY 171 -0.48 LYS 10
SER 136 0.24 LYS 172 -0.42 LYS 10
ALA 135 0.30 ARG 173 -0.36 LYS 10
ALA 135 0.29 ALA 174 -0.30 LYS 10
ALA 135 0.27 PRO 175 -0.28 LYS 10
ALA 135 0.25 PHE 176 -0.24 LYS 10
ALA 135 0.21 THR 177 -0.22 LYS 10
ALA 163 0.17 ASN 178 -0.18 ASN 11
ALA 135 0.15 PHE 179 -0.18 TRP 5
LYS 156 0.17 ASP 180 -0.18 TRP 5
LEU 157 0.16 PRO 181 -0.17 TRP 5
THR 183 0.18 SER 182 -0.21 LEU 189
SER 182 0.18 THR 183 -0.22 SER 187
SER 182 0.15 LEU 184 -0.14 SER 187
SER 217 0.17 LEU 185 -0.12 THR 35
SER 48 0.17 PRO 186 -0.15 THR 35
ASP 9 0.17 SER 187 -0.22 THR 183
ASP 9 0.21 SER 188 -0.16 THR 183
ASP 9 0.18 LEU 189 -0.21 SER 182
ASP 9 0.24 ASP 190 -0.15 SER 182
ASP 9 0.25 PHE 191 -0.11 SER 182
ASP 9 0.28 TRP 192 -0.08 PRO 202
ASP 9 0.21 THR 193 -0.12 PRO 202
ASP 9 0.21 TYR 194 -0.11 PRO 195
ASP 139 0.25 PRO 195 -0.12 ASN 237
ASP 139 0.15 GLY 196 -0.14 ASN 237
ILE 60 0.19 SER 197 -0.15 ASN 237
ILE 60 0.22 LEU 198 -0.22 ALA 132
VAL 62 0.12 THR 199 -0.25 ALA 132
VAL 62 0.12 HIS 200 -0.43 ALA 132
VAL 62 0.14 PRO 201 -0.65 ALA 132
VAL 62 0.23 PRO 202 -0.74 ALA 132
ILE 60 0.20 LEU 203 -0.35 ALA 132
ILE 60 0.27 TYR 204 -0.33 TYR 20
ARG 173 0.22 GLU 205 -0.19 TYR 20
ARG 173 0.23 SER 206 -0.25 PRO 202
ASN 69 0.17 VAL 207 -0.28 PRO 202
PRO 195 0.18 THR 208 -0.20 PRO 202
ASP 9 0.15 TRP 209 -0.16 PRO 202
ASP 9 0.17 ILE 210 -0.14 PRO 202
ASP 9 0.24 ILE 211 -0.08 PRO 202
ASP 9 0.24 CYS 212 -0.12 THR 35
ASP 9 0.32 LYS 213 -0.17 THR 35
ASP 9 0.30 GLU 214 -0.19 THR 35
ASP 9 0.28 SER 215 -0.23 THR 35
ASP 9 0.22 ILE 216 -0.18 THR 35
ASP 9 0.20 SER 217 -0.19 THR 35
ALA 238 0.20 VAL 218 -0.15 THR 35
ALA 238 0.24 SER 219 -0.14 ASP 110
ALA 238 0.27 SER 220 -0.13 VAL 112
ALA 238 0.34 GLU 221 -0.11 VAL 112
ALA 238 0.30 GLN 222 -0.11 GLN 165
ALA 238 0.25 LEU 223 -0.12 GLN 165
ALA 238 0.35 ALA 224 -0.14 GLN 165
ALA 238 0.38 GLN 225 -0.17 GLN 165
ALA 238 0.25 PHE 226 -0.13 ASP 8
ALA 238 0.26 ARG 227 -0.17 GLU 14
ALA 238 0.43 SER 228 -0.23 ASP 8
ALA 238 0.23 LEU 229 -0.36 ASP 8
ALA 238 0.16 LEU 230 -0.55 ASP 8
SER 228 0.07 SER 231 -0.73 ASP 8
GLN 165 0.12 ASN 232 -0.83 ASP 8
GLN 165 0.18 VAL 233 -0.77 LYS 10
GLN 165 0.33 GLU 234 -0.71 LYS 10
GLN 165 0.46 GLY 235 -0.85 LYS 10
GLN 165 0.34 ASP 236 -1.05 LYS 10
GLN 165 0.31 ASN 237 -1.12 ASP 9
SER 228 0.43 ALA 238 -0.87 ASP 9
SER 228 0.16 VAL 239 -0.82 ASP 8
ALA 224 0.15 PRO 240 -0.46 ASP 8
HIS 64 0.10 MET 241 -0.34 ASP 8
GLY 6 0.13 GLN 242 -0.26 GLU 14
GLY 98 0.17 HIS 243 -0.22 GLU 14
GLY 111 0.13 ASN 244 -0.23 ALA 132
ASP 9 0.28 ASN 245 -0.19 ALA 132
ASP 9 0.33 ARG 246 -0.23 ASN 237
ASP 9 0.52 PRO 247 -0.25 ASN 237
ASP 9 0.45 THR 248 -0.21 ASN 237
GLU 14 0.40 GLN 249 -0.22 ASN 237
GLU 14 0.37 PRO 250 -0.21 HIS 103
ASP 9 0.31 LEU 251 -0.19 LYS 113
ASP 9 0.25 LYS 252 -0.19 ASN 237
ASP 9 0.24 GLY 253 -0.21 GLY 111
ASP 139 0.23 ARG 254 -0.18 GLY 111
ASP 9 0.27 THR 255 -0.12 GLY 111
ASP 9 0.30 VAL 256 -0.09 SER 215
ASP 9 0.27 ARG 257 -0.07 SER 206
ASP 9 0.29 ALA 258 -0.08 SER 182
ASP 9 0.24 SER 259 -0.10 PRO 202
ASP 9 0.29 PHE 260 -0.11 SER 182

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.