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CA distance fluctuations for 2404131342263939023

---  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
LYS 101 0.40 SER 96 -1.25 LEU 206
LYS 101 0.80 VAL 97 -1.21 HIS 214
ARG 213 1.09 PRO 98 -0.46 ASN 131
ASN 263 1.58 SER 99 -0.77 SER 166
ARG 213 1.31 GLN 100 -0.72 ASN 131
PHE 212 1.34 LYS 101 -0.63 ALA 129
ASP 208 1.34 THR 102 -0.57 PRO 128
ASP 208 1.44 TYR 103 -0.35 PRO 98
ASP 208 1.58 GLN 104 -0.41 ASN 200
ASP 208 1.47 GLY 105 -0.31 PRO 98
ASP 208 1.42 SER 106 -0.34 TYR 220
ASP 208 1.34 TYR 107 -0.50 LEU 201
ASP 208 1.53 GLY 108 -0.52 LEU 201
ASP 208 1.35 PHE 109 -0.60 ASN 200
ASP 208 1.25 ARG 110 -0.60 ASN 200
ASP 208 1.04 LEU 111 -0.56 ASN 200
ASP 208 0.94 GLY 112 -0.52 ASN 200
ASP 208 0.75 PHE 113 -0.44 ASN 200
SER 227 0.88 LEU 114 -0.36 ASN 200
GLY 226 0.63 SER 121 -0.37 ASP 207
GLY 226 0.62 VAL 122 -0.32 TYR 205
GLY 226 0.57 THR 123 -0.40 SER 96
GLY 226 0.61 CYS 124 -0.36 TYR 205
GLY 226 0.65 THR 125 -0.30 TYR 205
THR 211 0.62 TYR 126 -0.38 GLN 100
THR 211 0.72 SER 127 -0.49 GLN 100
THR 211 0.88 PRO 128 -0.59 GLN 100
THR 211 0.89 ALA 129 -0.66 GLN 100
THR 211 0.80 LEU 130 -0.69 GLN 100
THR 211 0.85 ASN 131 -0.72 GLN 100
THR 211 0.66 LYS 132 -0.51 GLN 100
THR 211 0.54 MET 133 -0.33 GLN 100
GLY 226 0.49 PHE 134 -0.29 TYR 205
GLY 226 0.48 CYS 135 -0.36 TYR 205
GLY 226 0.44 GLN 136 -0.46 ASP 207
TYR 220 0.40 LEU 137 -0.61 ASP 207
TYR 220 0.46 ALA 138 -0.70 SER 96
TYR 220 0.55 LYS 139 -0.60 SER 96
TYR 220 0.69 THR 140 -0.58 SER 96
TYR 220 0.68 CYS 141 -0.47 SER 96
TYR 220 0.82 PRO 142 -0.45 ASN 200
VAL 157 0.72 VAL 143 -0.59 ASN 200
ASP 208 0.83 GLN 144 -0.66 ASN 200
ASP 208 0.95 LEU 145 -0.78 ASN 200
ASP 208 1.10 TRP 146 -0.68 ASN 200
ASP 208 1.21 VAL 147 -0.75 LEU 201
ASP 208 1.31 ASP 148 -0.70 LEU 201
ASP 208 1.18 SER 149 -0.72 LEU 201
ASP 208 0.94 THR 150 -0.81 LEU 201
ASP 208 0.89 PRO 151 -0.78 TYR 220
SER 99 0.94 PRO 152 -0.51 TYR 220
GLU 221 1.75 PRO 153 -0.67 SER 96
GLU 221 1.05 GLY 154 -0.73 SER 96
SER 99 1.02 THR 155 -0.63 SER 96
SER 99 1.01 ARG 156 -0.72 SER 96
ILE 232 1.13 VAL 157 -0.66 SER 96
ILE 232 0.79 ARG 158 -0.73 VAL 97
VAL 143 0.57 ALA 159 -0.76 VAL 97
VAL 143 0.49 MET 160 -0.98 VAL 97
ARG 213 0.61 ALA 161 -0.76 VAL 97
ARG 213 0.89 ILE 162 -0.54 VAL 97
ARG 213 0.62 TYR 163 -0.29 SER 99
ARG 213 0.62 LYS 164 -0.49 SER 99
ARG 213 0.51 GLN 165 -0.73 SER 99
ARG 213 0.53 SER 166 -0.77 SER 99
ARG 213 0.48 GLN 167 -0.73 SER 99
ARG 213 0.53 HIS 168 -0.46 SER 99
ARG 213 0.72 MET 169 -0.37 SER 99
GLN 100 0.91 THR 170 -0.39 GLY 245
PRO 98 0.78 GLU 171 -0.54 GLY 245
PRO 98 0.69 VAL 172 -1.08 VAL 97
PRO 98 0.39 VAL 173 -0.95 VAL 97
PRO 98 0.46 ARG 174 -0.98 VAL 97
LEU 201 0.37 ARG 175 -0.82 VAL 97
LEU 201 0.38 CYS 176 -0.77 PHE 212
LEU 201 0.45 PRO 177 -1.02 PHE 212
LEU 201 0.52 HIS 178 -1.03 PHE 212
LEU 201 0.55 HIS 179 -0.93 PHE 212
LEU 201 0.60 GLU 180 -1.11 ASP 207
LEU 201 0.69 ARG 181 -1.27 PHE 212
LEU 201 0.82 CYS 182 -1.12 PHE 212
LEU 201 1.15 SER 185 -1.07 ASP 207
LEU 201 1.41 ASP 186 -0.91 SER 96
LEU 201 1.39 GLY 187 -1.08 SER 96
VAL 203 1.32 LEU 188 -1.07 SER 96
VAL 203 1.07 ALA 189 -1.02 SER 96
SER 99 0.77 PRO 190 -1.17 SER 96
LEU 201 0.69 PRO 191 -1.31 ASP 207
PRO 98 0.57 GLN 192 -1.01 SER 96
PRO 98 0.54 HIS 193 -0.98 SER 96
SER 185 0.33 LEU 194 -0.86 VAL 97
SER 185 0.61 ILE 195 -0.81 VAL 97
SER 185 0.86 ARG 196 -0.99 TYR 205
VAL 218 0.75 VAL 197 -0.97 TYR 205
PRO 219 0.82 GLU 198 -0.88 TYR 205
PRO 219 0.94 GLY 199 -0.83 SER 96
ASP 186 1.28 ASN 200 -0.93 THR 230
ASP 186 1.41 LEU 201 -1.15 PRO 222
ASP 186 1.20 ARG 202 -0.90 GLU 221
LEU 188 1.32 VAL 203 -0.92 GLU 221
SER 99 1.22 GLU 204 -1.08 SER 96
SER 99 1.11 TYR 205 -1.01 SER 96
SER 99 1.14 LEU 206 -1.25 SER 96
LYS 101 1.31 ASP 207 -1.31 PRO 191
GLN 104 1.58 ASP 208 -0.69 ARG 181
SER 106 1.02 ARG 209 -0.62 ARG 181
ASP 148 0.94 ASN 210 -0.52 ARG 181
GLN 104 1.26 THR 211 -0.61 ARG 181
LYS 101 1.34 PHE 212 -1.27 ARG 181
GLN 100 1.31 ARG 213 -0.97 VAL 97
PRO 98 0.95 HIS 214 -1.21 VAL 97
SER 99 0.72 SER 215 -1.08 VAL 97
ALA 189 0.90 VAL 216 -0.89 SER 96
SER 99 0.96 VAL 217 -0.90 SER 96
ASP 186 1.03 VAL 218 -0.85 GLU 221
GLY 199 0.94 PRO 219 -0.82 SER 96
ILE 232 1.15 TYR 220 -0.78 PRO 151
PRO 153 1.75 GLU 221 -0.95 LEU 201
PRO 153 0.99 PRO 222 -1.15 LEU 201
PRO 153 0.79 PRO 223 -1.10 LEU 201
PRO 153 0.78 GLU 224 -1.08 LEU 201
LEU 114 0.64 VAL 225 -0.89 LEU 201
LEU 114 0.88 GLY 226 -0.68 LEU 201
LEU 114 0.88 SER 227 -0.72 LEU 201
ASP 208 0.87 ASP 228 -0.74 LEU 201
ASP 208 0.89 CYS 229 -0.74 LEU 201
THR 155 0.87 THR 230 -0.93 ASN 200
TYR 220 1.06 THR 231 -0.82 ASN 200
TYR 220 1.15 ILE 232 -0.92 ASN 200
TYR 220 0.99 HIS 233 -0.61 SER 96
TYR 220 0.67 TYR 234 -0.64 SER 96
TYR 220 0.54 ASN 235 -0.69 SER 96
TYR 220 0.39 TYR 236 -0.64 SER 96
LEU 201 0.34 MET 237 -0.75 SER 96
LEU 201 0.30 CYS 238 -0.67 ASP 207
GLY 226 0.32 ASN 239 -0.53 ASP 207
GLY 226 0.31 SER 240 -0.38 VAL 97
GLY 226 0.30 SER 241 -0.43 PHE 212
GLY 226 0.26 CYS 242 -0.59 PHE 212
LEU 201 0.28 GLY 245 -0.66 VAL 97
GLY 226 0.25 MET 246 -0.53 VAL 97
GLY 226 0.25 ASN 247 -0.46 GLU 171
GLY 226 0.28 ARG 248 -0.41 SER 99
GLY 226 0.27 ARG 249 -0.46 HIS 168
ARG 213 0.37 PRO 250 -0.41 SER 99
ARG 213 0.49 ILE 251 -0.28 GLU 221
ARG 213 0.68 LEU 252 -0.33 GLU 221
ARG 213 0.62 THR 253 -0.38 GLU 221
ARG 213 0.85 ILE 254 -0.39 PRO 98
ASP 208 0.73 ILE 255 -0.46 GLU 221
ASP 208 0.81 THR 256 -0.41 PRO 98
SER 99 0.85 LEU 257 -0.40 SER 96
SER 99 1.15 GLU 258 -0.47 SER 96
SER 99 1.32 ASP 259 -0.52 SER 96
SER 99 1.31 SER 260 -0.68 SER 96
SER 99 1.54 SER 261 -0.56 SER 96
SER 99 1.52 GLY 262 -0.56 VAL 97
SER 99 1.58 ASN 263 -0.34 PRO 98
ASP 207 1.17 LEU 264 -0.43 PRO 98
ASP 207 1.05 LEU 265 -0.36 PRO 98
ASP 208 1.19 GLY 266 -0.38 PRO 98
ASP 208 1.13 ARG 267 -0.45 PRO 98
ASP 208 1.14 ASN 268 -0.53 GLU 221
ASP 208 0.94 SER 269 -0.54 ASN 200
ASP 208 0.76 PHE 270 -0.47 GLN 100
THR 211 0.61 GLU 271 -0.46 GLN 100
THR 211 0.44 VAL 272 -0.28 TYR 205
GLY 226 0.39 ARG 273 -0.25 TYR 205
GLY 226 0.38 VAL 274 -0.36 SER 96
GLY 226 0.40 CYS 275 -0.40 ASP 207
GLY 226 0.41 ALA 276 -0.46 ASP 207
GLY 226 0.47 CYS 277 -0.35 ASP 207
GLY 226 0.51 PRO 278 -0.29 TYR 205
GLY 226 0.57 GLY 279 -0.26 GLN 100
GLY 226 0.50 ARG 280 -0.27 GLN 100
GLY 226 0.46 ASP 281 -0.30 SER 99
GLY 226 0.51 ARG 282 -0.36 GLN 100
GLY 226 0.51 ARG 283 -0.36 GLN 100
GLY 226 0.45 THR 284 -0.45 SER 99
THR 211 0.51 GLU 285 -0.52 SER 99
THR 211 0.63 GLU 286 -0.48 SER 99
THR 211 0.58 GLU 287 -0.54 SER 99
THR 211 0.56 ASN 288 -0.67 SER 99
THR 211 0.69 LEU 289 -0.70 SER 99

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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.