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***  DNA polimerase com DNA  ***

CA distance fluctuations for 2610141417151088793

---  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
SER 334 0.50 PRO 7 -0.03 PRO 50
ALA 185 0.47 GLN 8 -0.02 HIS 51
GLU 186 0.43 GLU 9 -0.01 LEU 11
GLU 186 0.37 THR 10 -0.02 LYS 54
ALA 185 0.35 LEU 11 -0.02 PRO 63
ALA 185 0.30 ASN 12 -0.02 VAL 65
ALA 185 0.30 GLY 13 -0.01 VAL 65
SER 187 0.24 GLY 14 -0.01 VAL 65
ALA 185 0.22 ILE 15 -0.01 VAL 65
SER 180 0.25 THR 16 -0.01 VAL 65
GLY 189 0.24 ASP 17 -0.01 VAL 65
GLY 189 0.18 MET 18 -0.01 ASP 91
ASP 276 0.17 LEU 19 -0.01 SER 30
GLY 189 0.19 THR 20 -0.01 GLU 21
GLY 189 0.15 GLU 21 -0.01 THR 20
GLY 189 0.11 LEU 22 -0.02 SER 30
PHE 272 0.10 ALA 23 -0.01 PHE 25
SER 104 0.09 ASN 24 -0.02 GLU 335
GLY 189 0.05 PHE 25 -0.02 THR 304
ARG 258 0.05 GLU 26 -0.03 GLU 335
LYS 234 0.05 LYS 27 -0.06 GLU 335
PRO 108 0.04 ASN 28 -0.06 GLU 335
ILE 257 0.02 VAL 29 -0.05 THR 304
ILE 257 0.02 SER 30 -0.05 THR 304
LYS 27 0.03 GLN 31 -0.07 THR 304
LYS 234 0.03 ALA 32 -0.07 ILE 277
LYS 234 0.05 ILE 33 -0.11 ILE 277
LYS 234 0.06 HIS 34 -0.08 ILE 277
GLU 295 0.07 LYS 35 -0.04 ALA 32
LYS 234 0.08 TYR 36 -0.05 GLU 335
GLU 295 0.13 ASN 37 -0.07 GLU 335
GLU 295 0.14 ALA 38 -0.02 ALA 32
ASP 276 0.15 TYR 39 -0.02 SER 30
ASP 276 0.20 ARG 40 -0.01 LYS 48
ASP 276 0.30 LYS 41 -0.02 LYS 48
ASP 276 0.29 ALA 42 -0.01 TYR 49
ASP 276 0.30 ALA 43 -0.01 PRO 50
ASP 276 0.43 SER 44 -0.03 LYS 48
ILE 277 0.47 VAL 45 -0.02 LYS 48
ILE 277 0.37 ILE 46 -0.05 ALA 47
SER 275 0.39 ALA 47 -0.05 ILE 46
SER 334 0.48 LYS 48 -0.03 SER 44
SER 334 0.45 TYR 49 -0.04 PRO 63
SER 334 0.46 PRO 50 -0.03 ALA 47
SER 334 0.38 HIS 51 -0.03 PRO 63
SER 334 0.32 LYS 52 -0.02 PRO 63
SER 334 0.29 ILE 53 -0.02 ALA 59
SER 334 0.26 LYS 54 -0.02 THR 10
SER 334 0.23 SER 55 -0.01 ASP 116
ILE 277 0.22 GLY 56 -0.02 ASP 116
ILE 277 0.23 ALA 57 -0.02 ASP 116
ILE 277 0.27 GLU 58 -0.01 SER 30
ILE 277 0.29 ALA 59 -0.02 LYS 52
ILE 277 0.25 LYS 60 -0.02 SER 30
ASN 281 0.30 LYS 61 -0.02 HIS 51
ILE 277 0.36 LEU 62 -0.03 PRO 63
LYS 280 0.37 PRO 63 -0.04 TYR 49
LYS 280 0.27 GLY 64 -0.03 TYR 49
ASP 276 0.24 VAL 65 -0.02 SER 30
LYS 280 0.19 GLY 66 -0.03 SER 30
LYS 280 0.16 THR 67 -0.03 ASP 116
ASP 276 0.14 LYS 68 -0.04 ASP 116
ASP 276 0.17 ILE 69 -0.03 SER 30
ILE 277 0.19 ALA 70 -0.02 SER 30
ASP 276 0.16 GLU 71 -0.03 ASP 116
ASP 276 0.15 LYS 72 -0.03 ASP 116
ASP 276 0.19 ILE 73 -0.02 ASP 116
SER 334 0.18 ASP 74 -0.02 ASP 116
SER 334 0.15 GLU 75 -0.03 ASP 116
ALA 185 0.17 PHE 76 -0.02 ASP 116
SER 334 0.20 LEU 77 -0.01 ASP 116
GLU 186 0.18 ALA 78 -0.02 ASP 116
GLU 186 0.17 THR 79 -0.02 ASP 116
GLU 186 0.19 GLY 80 -0.01 ASP 116
GLU 186 0.16 LYS 81 -0.01 ASP 116
ALA 185 0.13 LEU 82 -0.03 ASP 116
GLU 186 0.11 ARG 83 -0.04 ASP 116
ALA 185 0.09 LYS 84 -0.05 ASP 116
GLY 189 0.11 LEU 85 -0.03 ASP 116
ARG 149 0.11 GLU 86 -0.02 ASP 116
ARG 149 0.08 LYS 87 -0.04 ASP 116
GLY 189 0.07 ILE 88 -0.04 ASP 116
ARG 149 0.08 ARG 89 -0.01 ASP 91
ARG 149 0.07 GLN 90 -0.02 GLY 118
ARG 149 0.05 ASP 91 -0.03 ASP 116
ARG 149 0.04 ASP 92 -0.03 GLY 118
ARG 149 0.02 THR 93 -0.04 THR 304
GLY 189 0.03 SER 94 -0.04 THR 304
ARG 89 0.05 SER 95 -0.03 GLY 305
GLU 9 0.04 SER 96 -0.04 GLY 305
GLU 9 0.04 ILE 97 -0.05 GLY 305
GLU 21 0.06 ASN 98 -0.04 GLY 305
ASP 17 0.09 PHE 99 -0.04 GLY 305
ASP 17 0.08 LEU 100 -0.05 GLY 305
ASP 17 0.10 THR 101 -0.05 GLY 305
ASP 17 0.15 ARG 102 -0.04 GLY 305
GLU 9 0.13 VAL 103 -0.05 VAL 306
GLU 9 0.15 SER 104 -0.05 VAL 306
GLU 9 0.13 GLY 105 -0.07 VAL 306
GLU 9 0.10 ILE 106 -0.07 GLY 305
THR 20 0.09 GLY 107 -0.07 GLY 305
ASN 24 0.06 PRO 108 -0.07 GLY 305
GLU 9 0.05 SER 109 -0.09 GLY 305
GLU 9 0.06 ALA 110 -0.08 GLY 305
GLU 9 0.06 ALA 111 -0.07 GLY 305
GLU 9 0.04 ARG 112 -0.07 GLY 305
GLU 9 0.04 LYS 113 -0.08 GLY 305
GLU 9 0.06 PHE 114 -0.07 GLY 305
GLU 9 0.04 VAL 115 -0.06 GLY 305
GLU 9 0.03 ASP 116 -0.07 THR 304
GLU 9 0.03 GLU 117 -0.07 THR 304
GLU 9 0.03 GLY 118 -0.06 GLY 305
GLU 9 0.05 ILE 119 -0.06 GLY 305
GLU 9 0.05 LYS 120 -0.05 GLY 305
GLU 9 0.07 THR 121 -0.04 VAL 306
GLU 9 0.09 LEU 122 -0.05 VAL 306
GLU 9 0.08 GLU 123 -0.05 VAL 306
GLU 9 0.07 ASP 124 -0.05 VAL 306
GLU 9 0.08 LEU 125 -0.06 VAL 306
GLU 9 0.09 ARG 126 -0.05 VAL 306
GLU 9 0.07 LYS 127 -0.06 VAL 306
GLU 9 0.07 ASN 128 -0.06 VAL 306
GLU 9 0.09 GLU 129 -0.07 VAL 306
GLU 9 0.08 ASP 130 -0.07 VAL 306
GLU 9 0.08 LYS 131 -0.08 VAL 306
GLU 9 0.09 LEU 132 -0.08 VAL 306
GLU 9 0.11 ASN 133 -0.09 VAL 306
GLU 9 0.12 HIS 134 -0.08 VAL 306
GLU 9 0.13 HIS 135 -0.07 VAL 306
GLU 9 0.12 GLN 136 -0.07 VAL 306
GLU 9 0.12 ARG 137 -0.06 VAL 306
GLU 9 0.14 ILE 138 -0.06 VAL 306
GLU 9 0.15 GLY 139 -0.05 VAL 306
GLU 9 0.13 LEU 140 -0.05 VAL 306
GLU 9 0.14 LYS 141 -0.05 VAL 306
GLU 9 0.16 TYR 142 -0.04 VAL 306
GLU 9 0.16 PHE 143 -0.04 VAL 306
GLU 9 0.18 GLY 144 -0.03 VAL 306
GLU 9 0.21 ASP 145 -0.03 VAL 306
GLU 9 0.22 PHE 146 -0.03 VAL 306
GLU 9 0.24 GLU 147 -0.03 GLU 335
GLU 9 0.28 LYS 148 -0.02 VAL 306
GLU 9 0.35 ARG 149 -0.02 GLU 335
GLU 9 0.33 ILE 150 -0.02 SER 229
GLN 8 0.34 PRO 151 -0.02 SER 229
GLN 8 0.36 ARG 152 -0.02 SER 229
GLN 8 0.31 GLU 153 -0.02 SER 229
GLN 8 0.29 GLU 154 -0.02 SER 229
GLN 8 0.30 MET 155 -0.02 MET 191
GLN 8 0.29 LEU 156 -0.02 SER 229
GLN 8 0.26 GLN 157 -0.01 SER 229
GLN 8 0.25 MET 158 -0.02 VAL 306
GLN 8 0.26 GLN 159 -0.02 ILE 257
GLN 8 0.24 ASP 160 -0.02 ILE 257
GLN 8 0.22 ILE 161 -0.02 VAL 306
GLN 8 0.23 VAL 162 -0.02 VAL 306
GLN 8 0.23 LEU 163 -0.02 LYS 230
GLN 8 0.21 ASN 164 -0.01 LYS 230
GLN 8 0.20 GLU 165 -0.02 VAL 306
GLN 8 0.20 VAL 166 -0.02 VAL 306
GLN 8 0.20 LYS 167 -0.01 LYS 230
GLN 8 0.19 LYS 168 -0.02 VAL 306
GLN 8 0.18 VAL 169 -0.02 VAL 306
PRO 7 0.18 ASP 170 -0.02 VAL 306
PRO 7 0.19 SER 171 -0.01 ASP 130
PRO 7 0.19 GLU 172 -0.01 ASP 130
PRO 7 0.20 TYR 173 -0.02 VAL 306
PRO 7 0.22 ILE 174 -0.02 LYS 234
PRO 7 0.23 ALA 175 -0.02 LYS 234
PRO 7 0.26 THR 176 -0.02 LYS 234
PRO 7 0.28 VAL 177 -0.02 LYS 234
PRO 7 0.31 CYS 178 -0.03 LYS 234
PRO 7 0.34 GLY 179 -0.03 SER 229
PRO 7 0.40 SER 180 -0.03 SER 229
GLN 8 0.37 PHE 181 -0.02 SER 229
PRO 7 0.35 ARG 182 -0.02 SER 229
PRO 7 0.40 ARG 183 -0.03 ILE 33
PRO 7 0.41 GLY 184 -0.03 ILE 33
GLN 8 0.47 ALA 185 -0.03 ILE 33
GLN 8 0.47 GLU 186 -0.02 ILE 33
GLU 9 0.41 SER 187 -0.02 ILE 33
GLU 9 0.38 SER 188 -0.02 SER 229
GLU 9 0.34 GLY 189 -0.03 GLU 335
GLU 9 0.29 ASP 190 -0.03 VAL 306
GLN 8 0.27 MET 191 -0.03 VAL 306
GLN 8 0.26 ASP 192 -0.03 SER 229
PRO 7 0.25 VAL 193 -0.03 VAL 306
PRO 7 0.24 LEU 194 -0.03 LYS 234
PRO 7 0.22 LEU 195 -0.03 VAL 306
PRO 7 0.21 THR 196 -0.03 VAL 306
PRO 7 0.19 HIS 197 -0.02 VAL 306
PRO 7 0.18 PRO 198 -0.02 ASP 130
PRO 7 0.17 SER 199 -0.02 VAL 306
PRO 7 0.18 PHE 200 -0.03 VAL 306
PRO 7 0.18 THR 201 -0.04 VAL 306
PRO 7 0.17 SER 202 -0.05 VAL 306
PRO 7 0.16 GLU 203 -0.05 VAL 306
PRO 7 0.15 SER 204 -0.05 VAL 306
PRO 7 0.15 GLN 207 -0.04 VAL 306
PRO 7 0.15 PRO 208 -0.06 VAL 306
PRO 7 0.15 LYS 209 -0.05 VAL 306
PRO 7 0.17 LEU 210 -0.04 VAL 306
PRO 7 0.18 LEU 211 -0.04 VAL 306
GLN 8 0.16 HIS 212 -0.05 VAL 306
GLN 8 0.17 GLN 213 -0.04 VAL 306
GLN 8 0.18 VAL 214 -0.03 VAL 306
GLN 8 0.18 VAL 215 -0.04 VAL 306
GLN 8 0.17 GLU 216 -0.04 VAL 306
GLN 8 0.18 GLN 217 -0.03 VAL 306
GLN 8 0.19 LEU 218 -0.03 VAL 306
GLN 8 0.17 GLN 219 -0.03 VAL 306
GLN 8 0.16 LYS 220 -0.03 VAL 306
GLN 8 0.17 VAL 221 -0.03 VAL 306
GLN 8 0.17 HIS 222 -0.03 VAL 306
GLN 8 0.19 PHE 223 -0.03 VAL 306
GLN 8 0.19 ILE 224 -0.03 VAL 306
GLU 9 0.17 THR 225 -0.04 VAL 306
GLU 9 0.16 ASP 226 -0.05 VAL 306
GLU 9 0.16 THR 227 -0.05 VAL 306
GLU 9 0.15 LEU 228 -0.06 VAL 306
GLU 9 0.15 SER 229 -0.07 VAL 306
GLN 8 0.15 LYS 230 -0.07 VAL 306
GLN 8 0.14 GLY 231 -0.08 VAL 306
PRO 7 0.15 GLU 232 -0.07 VAL 306
PRO 7 0.17 THR 233 -0.07 VAL 306
PRO 7 0.17 LYS 234 -0.07 VAL 306
GLN 8 0.18 PHE 235 -0.06 VAL 306
GLU 9 0.18 MET 236 -0.05 VAL 306
GLU 9 0.18 GLY 237 -0.05 VAL 306
GLU 9 0.19 VAL 238 -0.04 VAL 306
GLU 9 0.20 CYS 239 -0.03 VAL 306
GLN 8 0.20 GLN 240 -0.03 VAL 306
GLN 8 0.21 LEU 241 -0.02 VAL 306
GLN 8 0.19 PRO 242 -0.02 VAL 306
GLN 8 0.18 SER 243 -0.02 VAL 306
GLN 8 0.18 LYS 244 -0.02 VAL 306
GLN 8 0.16 ASN 245 -0.02 VAL 306
GLN 8 0.15 ASP 246 -0.02 VAL 306
GLN 8 0.16 GLU 247 -0.02 VAL 306
GLN 8 0.16 LYS 248 -0.02 VAL 306
GLN 8 0.17 GLU 249 -0.02 VAL 306
GLU 9 0.20 TYR 250 -0.02 VAL 306
GLU 9 0.21 PRO 251 -0.03 VAL 306
GLU 9 0.20 HIS 252 -0.03 VAL 306
GLU 9 0.23 ARG 253 -0.03 VAL 306
GLU 9 0.23 ARG 254 -0.04 VAL 306
GLU 9 0.23 ILE 255 -0.03 VAL 306
GLU 9 0.21 ASP 256 -0.04 VAL 306
GLN 8 0.21 ILE 257 -0.04 VAL 306
PRO 7 0.20 ARG 258 -0.05 VAL 306
PRO 7 0.20 LEU 259 -0.04 VAL 306
PRO 7 0.20 ILE 260 -0.04 VAL 306
PRO 7 0.19 PRO 261 -0.04 VAL 306
PRO 7 0.20 LYS 262 -0.03 THR 233
PRO 7 0.19 ASP 263 -0.03 THR 233
PRO 7 0.21 GLN 264 -0.04 THR 233
PRO 7 0.22 TYR 265 -0.04 LYS 234
PRO 7 0.24 TYR 266 -0.03 LYS 234
PRO 7 0.24 CYS 267 -0.04 LYS 234
PRO 7 0.24 GLY 268 -0.05 LYS 234
PRO 7 0.27 VAL 269 -0.04 LYS 234
PRO 7 0.28 LEU 270 -0.04 LYS 234
LYS 48 0.29 TYR 271 -0.04 LYS 234
PRO 7 0.29 PHE 272 -0.04 LYS 234
PRO 7 0.33 THR 273 -0.04 SER 229
LYS 48 0.37 GLY 274 -0.05 GLY 107
LYS 48 0.43 SER 275 -0.06 ILE 33
VAL 45 0.44 ASP 276 -0.08 ILE 33
VAL 45 0.47 ILE 277 -0.11 ILE 33
LYS 48 0.39 PHE 278 -0.08 ILE 33
VAL 45 0.34 ASN 279 -0.06 ILE 33
PRO 63 0.37 LYS 280 -0.09 ILE 33
LEU 62 0.33 ASN 281 -0.09 ILE 33
TYR 49 0.29 MET 282 -0.06 ILE 33
PRO 63 0.29 ARG 283 -0.06 SER 109
PRO 63 0.30 ALA 284 -0.07 ILE 33
LEU 62 0.26 HIS 285 -0.06 ILE 33
LEU 62 0.23 ALA 286 -0.06 SER 109
PRO 63 0.24 LEU 287 -0.07 SER 109
LYS 61 0.23 GLU 288 -0.06 ILE 33
LYS 61 0.20 LYS 289 -0.06 SER 109
LYS 61 0.19 GLY 290 -0.06 SER 109
PRO 63 0.21 PHE 291 -0.05 SER 109
PRO 63 0.23 THR 292 -0.06 SER 109
PRO 63 0.24 ILE 293 -0.05 SER 109
PRO 63 0.25 ASN 294 -0.06 ASN 133
VAL 45 0.24 GLU 295 -0.05 LYS 234
VAL 45 0.21 TYR 296 -0.05 LYS 234
PRO 63 0.20 THR 297 -0.05 GLY 231
PRO 63 0.21 ILE 298 -0.05 ASN 133
PRO 63 0.19 ARG 299 -0.05 ASN 133
PRO 63 0.18 PRO 300 -0.05 SER 109
PRO 63 0.18 LEU 301 -0.07 SER 109
PRO 63 0.16 GLY 302 -0.07 SER 109
LYS 61 0.16 VAL 303 -0.07 SER 109
LYS 61 0.16 THR 304 -0.09 SER 109
PRO 63 0.17 GLY 305 -0.09 SER 109
PRO 63 0.17 VAL 306 -0.09 ASN 133
PRO 63 0.18 ALA 307 -0.07 ASN 133
PRO 63 0.17 GLY 308 -0.06 ASN 133
PRO 63 0.17 GLU 309 -0.05 ASN 133
PRO 63 0.18 PRO 310 -0.05 ASN 133
PRO 50 0.18 LEU 311 -0.04 ASN 133
PRO 7 0.18 PRO 312 -0.03 ASN 133
PRO 7 0.20 VAL 313 -0.03 ASN 133
PRO 7 0.21 ASP 314 -0.02 LYS 234
PRO 7 0.23 SER 315 -0.02 GLU 295
PRO 7 0.25 GLU 316 -0.03 GLU 295
PRO 7 0.24 LYS 317 -0.03 GLU 295
PRO 7 0.22 ASP 318 -0.03 GLU 295
PRO 50 0.23 ILE 319 -0.04 GLU 295
PRO 50 0.24 PHE 320 -0.04 GLU 295
PRO 50 0.22 ASP 321 -0.04 SER 109
PRO 50 0.21 TYR 322 -0.04 SER 109
PRO 50 0.22 ILE 323 -0.05 SER 109
PRO 50 0.23 GLN 324 -0.04 SER 109
PRO 50 0.25 LYS 326 -0.05 ILE 33
PRO 50 0.26 TYR 327 -0.04 ILE 33
PRO 7 0.30 ARG 328 -0.05 ILE 33
PRO 7 0.32 GLU 329 -0.04 ILE 33
PRO 7 0.36 PRO 330 -0.03 ILE 33
PRO 7 0.40 LYS 331 -0.04 ILE 33
PRO 7 0.41 ASP 332 -0.05 ILE 33
PRO 7 0.41 ARG 333 -0.06 ILE 33
PRO 7 0.50 SER 334 -0.07 ILE 33
TYR 49 0.44 GLU 335 -0.10 ILE 33

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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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.