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***  3JWO  ***

CA distance fluctuations for 240228060919933712

---  normal mode 16  ---

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 353 0.50 LEU 1 -0.17 ASN 47
ALA 353 0.05 TRP 2 -0.49 THR 4
ALA 353 0.13 VAL 3 -0.20 GLY 8
LEU 1 0.30 THR 4 -0.49 TRP 2
ALA 115 0.08 VAL 5 -0.45 ASN 55
PRO 349 0.08 TYR 6 -0.31 TRP 2
ALA 115 0.26 TYR 7 -0.42 ASN 55
LEU 350 0.37 GLY 8 -0.52 VAL 54
VAL 51 0.64 VAL 9 -0.22 TYR 7
GLY 116 0.46 PRO 10 -0.32 VAL 56
GLY 351 0.50 VAL 11 -0.14 PRO 10
GLY 351 0.40 TRP 12 -0.09 TRP 2
GLY 351 0.33 LYS 13 -0.13 TYR 7
GLY 351 0.30 GLU 14 -0.12 TYR 7
ALA 353 0.18 ALA 15 -0.08 TRP 2
ALA 353 0.16 THR 16 -0.08 TRP 2
PRO 10 0.18 THR 17 -0.10 PRO 349
PRO 10 0.20 THR 18 -0.13 PRO 349
PRO 10 0.24 LEU 19 -0.17 PRO 349
VAL 9 0.26 PHE 20 -0.19 PRO 349
VAL 9 0.28 CYS 21 -0.18 PRO 349
VAL 9 0.32 ALA 22 -0.19 PRO 349
VAL 9 0.29 SER 23 -0.17 PRO 349
VAL 9 0.30 ASP 24 -0.17 PRO 349
VAL 9 0.27 ALA 25 -0.16 PRO 349
VAL 9 0.26 LYS 26 -0.15 PRO 349
VAL 9 0.24 ALA 27 -0.15 PRO 349
VAL 9 0.23 TYR 28 -0.14 PRO 349
VAL 9 0.22 ASP 29 -0.13 PRO 349
VAL 9 0.20 THR 30 -0.12 PRO 349
ALA 353 0.22 GLU 31 -0.11 PRO 349
ALA 353 0.21 VAL 32 -0.11 PRO 349
ALA 353 0.24 HIS 33 -0.12 PRO 349
ALA 353 0.23 ASN 34 -0.13 PRO 349
VAL 9 0.21 VAL 35 -0.13 PRO 349
VAL 9 0.20 TRP 36 -0.13 PRO 349
VAL 9 0.23 ALA 37 -0.15 PRO 349
VAL 9 0.25 THR 38 -0.16 PRO 349
VAL 9 0.23 HIS 39 -0.15 PRO 349
VAL 9 0.23 ALA 40 -0.16 PRO 349
VAL 9 0.27 CYS 41 -0.18 PRO 349
VAL 9 0.33 VAL 42 -0.21 PRO 349
VAL 9 0.35 PRO 43 -0.21 PRO 349
VAL 9 0.37 THR 44 -0.22 PRO 349
VAL 9 0.40 ASP 45 -0.28 PRO 349
VAL 9 0.37 PRO 46 -0.29 PRO 349
ALA 353 0.39 ASN 47 -0.33 PRO 349
ALA 353 0.45 PRO 48 -0.29 PRO 349
ALA 353 0.52 GLN 49 -0.29 PRO 349
ALA 353 0.61 GLU 50 -0.27 PRO 349
ALA 353 0.68 VAL 51 -0.29 PRO 349
ALA 353 0.88 VAL 52 -0.34 GLY 8
ALA 353 0.98 LEU 53 -0.45 GLY 8
ALA 353 1.28 VAL 54 -0.52 GLY 8
ALA 353 1.45 ASN 55 -0.47 GLY 8
ALA 353 1.14 VAL 56 -0.41 GLY 8
ALA 353 0.99 THR 57 -0.37 TYR 7
ALA 353 0.77 GLU 58 -0.29 TYR 7
ALA 353 0.65 ASN 59 -0.27 TYR 7
ALA 353 0.58 PHE 60 -0.20 VAL 5
ALA 353 0.49 ASN 61 -0.18 VAL 5
ALA 353 0.47 MET 62 -0.15 VAL 5
ALA 353 0.40 TRP 63 -0.15 VAL 5
ALA 353 0.34 LYS 64 -0.14 VAL 5
ALA 353 0.36 ASN 65 -0.12 VAL 5
ALA 353 0.27 ASP 66 -0.08 VAL 5
ALA 353 0.31 MET 67 -0.09 TRP 2
ALA 353 0.32 VAL 68 -0.08 TRP 2
ALA 353 0.25 GLU 69 -0.08 TRP 2
ALA 353 0.22 GLN 70 -0.08 TRP 2
ALA 353 0.27 MET 71 -0.09 PRO 349
ALA 353 0.25 HIS 72 -0.08 TRP 2
ALA 353 0.19 GLU 73 -0.07 TRP 2
ALA 353 0.20 ASP 74 -0.10 PRO 349
ALA 353 0.24 ILE 75 -0.09 PRO 349
ALA 353 0.20 ILE 76 -0.07 TRP 2
ALA 353 0.17 SER 77 -0.08 PRO 349
ALA 353 0.19 LEU 78 -0.09 PRO 349
ALA 353 0.20 TRP 79 -0.08 PRO 349
ALA 353 0.16 ASP 80 -0.07 PRO 349
ALA 353 0.15 GLN 81 -0.09 PRO 349
ALA 353 0.18 SER 82 -0.09 PRO 349
ALA 353 0.19 LEU 83 -0.08 PRO 349
ALA 353 0.16 LYS 84 -0.07 PRO 349
ALA 353 0.17 PRO 85 -0.07 ASN 316
ALA 353 0.15 CYS 86 -0.08 ASN 316
ALA 353 0.15 VAL 87 -0.09 ASN 316
ALA 353 0.14 LYS 88 -0.10 ASN 316
ALA 353 0.14 LEU 89 -0.12 ASN 316
ALA 353 0.13 THR 90 -0.13 ASN 316
ALA 353 0.12 GLY 91 -0.15 ASN 316
ALA 353 0.11 GLY 92 -0.15 ASN 316
ALA 353 0.10 SER 93 -0.13 ASN 316
ALA 353 0.11 VAL 94 -0.12 ASN 316
ALA 353 0.11 ILE 95 -0.10 ASN 316
ALA 353 0.11 THR 96 -0.09 ASN 316
ALA 353 0.12 GLN 97 -0.08 ASN 316
ALA 353 0.13 ALA 98 -0.07 PRO 349
ALA 353 0.15 CYS 99 -0.07 PRO 349
ALA 353 0.16 PRO 100 -0.08 PRO 349
ALA 353 0.19 LYS 101 -0.08 PRO 349
ALA 353 0.20 VAL 102 -0.09 PRO 349
ALA 353 0.23 SER 103 -0.10 PRO 349
ALA 353 0.25 PHE 104 -0.09 PRO 349
ALA 353 0.29 GLU 105 -0.10 PRO 349
ALA 353 0.31 PRO 106 -0.10 PRO 349
ALA 353 0.31 ILE 107 -0.12 PRO 349
ALA 353 0.35 PRO 108 -0.13 PRO 349
ALA 353 0.33 ILE 109 -0.14 PRO 349
ALA 353 0.35 HIS 110 -0.17 PRO 349
ALA 353 0.32 TYR 111 -0.17 PRO 349
VAL 9 0.33 CYS 112 -0.21 PRO 349
PRO 10 0.34 ALA 113 -0.24 PRO 349
PRO 10 0.36 PRO 114 -0.28 PRO 349
PRO 10 0.44 ALA 115 -0.36 PRO 349
PRO 10 0.46 GLY 116 -0.42 PRO 349
PRO 10 0.42 PHE 117 -0.29 PRO 349
PRO 10 0.43 ALA 118 -0.26 PRO 349
ALA 353 0.43 ILE 119 -0.19 PRO 349
ALA 353 0.57 LEU 120 -0.15 GLY 8
ALA 353 0.65 LYS 121 -0.16 GLY 8
ALA 353 0.76 CYS 122 -0.20 GLY 8
ALA 353 0.83 ASN 123 -0.22 GLY 8
ALA 353 0.86 ASN 124 -0.23 VAL 5
ALA 353 0.79 LYS 125 -0.19 VAL 5
ALA 353 0.76 THR 126 -0.21 VAL 5
ALA 353 0.73 PHE 127 -0.21 VAL 5
ALA 353 0.64 ASN 128 -0.20 VAL 5
ALA 353 0.60 GLY 129 -0.19 VAL 5
ALA 353 0.58 THR 130 -0.20 VAL 5
ALA 353 0.66 GLY 131 -0.25 TYR 7
ALA 353 0.78 PRO 132 -0.29 TYR 7
ALA 353 0.87 CYS 133 -0.27 VAL 5
ALA 353 1.05 THR 134 -0.32 VAL 5
ALA 353 1.03 ASN 135 -0.30 GLY 8
ALA 353 0.88 VAL 136 -0.27 GLY 8
ALA 353 0.77 SER 137 -0.25 GLY 8
ALA 353 0.59 THR 138 -0.25 PRO 349
ALA 353 0.50 VAL 139 -0.25 PRO 349
VAL 9 0.48 GLN 140 -0.28 PRO 349
ALA 353 0.39 CYS 141 -0.22 PRO 349
ALA 353 0.44 THR 142 -0.16 PRO 349
ALA 353 0.47 HIS 143 -0.15 PRO 349
ALA 353 0.42 GLY 144 -0.14 PRO 349
ALA 353 0.40 ILE 145 -0.11 PRO 349
ALA 353 0.37 ARG 146 -0.10 PRO 349
ALA 353 0.33 PRO 147 -0.09 PRO 349
ALA 353 0.34 VAL 148 -0.08 TRP 2
ALA 353 0.32 VAL 149 -0.08 TRP 2
ALA 353 0.33 SER 150 -0.07 TRP 2
ALA 353 0.35 SER 151 -0.08 VAL 5
ALA 353 0.38 GLN 152 -0.11 GLY 266
ALA 353 0.40 LEU 153 -0.09 VAL 5
ALA 353 0.42 LEU 154 -0.09 VAL 5
ALA 353 0.41 LEU 155 -0.08 TRP 2
ALA 353 0.42 ASN 156 -0.09 TRP 2
ALA 353 0.46 GLY 157 -0.09 TRP 2
ALA 353 0.52 SER 158 -0.10 VAL 5
ALA 353 0.57 LEU 159 -0.11 VAL 5
ALA 353 0.64 ALA 160 -0.14 VAL 5
ALA 353 0.69 GLU 161 -0.14 VAL 5
ALA 353 0.71 GLU 162 -0.16 VAL 5
ALA 353 0.67 GLU 163 -0.16 VAL 5
ALA 353 0.61 VAL 164 -0.15 VAL 5
ALA 353 0.61 VAL 165 -0.16 VAL 5
ALA 353 0.56 ILE 166 -0.16 VAL 5
ALA 353 0.53 ARG 167 -0.16 VAL 5
ALA 353 0.48 SER 168 -0.16 VAL 5
ALA 353 0.44 VAL 169 -0.17 VAL 5
ALA 353 0.43 ASN 170 -0.17 TYR 7
ALA 353 0.46 PHE 171 -0.17 VAL 5
ALA 353 0.42 THR 172 -0.18 TYR 7
ALA 353 0.37 ASP 173 -0.16 TYR 7
ALA 353 0.37 ASN 174 -0.15 VAL 5
ALA 353 0.33 ALA 175 -0.14 VAL 5
ALA 353 0.37 LYS 176 -0.14 VAL 5
ALA 353 0.40 THR 177 -0.13 VAL 5
ALA 353 0.45 ILE 178 -0.14 VAL 5
ALA 353 0.47 ILE 179 -0.13 VAL 5
ALA 353 0.51 VAL 180 -0.13 VAL 5
ALA 353 0.55 GLN 181 -0.13 VAL 5
ALA 353 0.56 LEU 182 -0.12 VAL 5
ALA 353 0.60 ASN 183 -0.12 VAL 5
ALA 353 0.55 THR 184 -0.10 VAL 5
ALA 353 0.51 SER 185 -0.09 VAL 5
ALA 353 0.47 VAL 186 -0.08 VAL 5
ALA 353 0.43 GLU 187 -0.07 TRP 2
ALA 353 0.40 ILE 188 -0.07 TRP 2
ALA 353 0.37 ASN 189 -0.07 TRP 2
ALA 353 0.34 CYS 190 -0.07 TRP 2
ALA 353 0.31 THR 191 -0.07 TRP 2
ALA 353 0.28 GLY 192 -0.07 TRP 2
ALA 353 0.28 ALA 193 -0.06 TRP 2
ALA 353 0.29 GLY 194 -0.06 TRP 2
ALA 353 0.32 HIS 195 -0.06 TRP 2
ALA 353 0.35 CYS 196 -0.06 TRP 2
ALA 353 0.37 ASN 197 -0.06 VAL 5
ALA 353 0.41 ILE 198 -0.07 VAL 5
ALA 353 0.43 ALA 199 -0.07 VAL 5
ALA 353 0.43 ARG 200 -0.09 GLY 266
ALA 353 0.46 ALA 201 -0.10 GLY 266
ALA 353 0.48 LYS 202 -0.09 VAL 5
ALA 353 0.46 TRP 203 -0.13 GLY 266
ALA 353 0.47 ASN 204 -0.23 GLY 266
ALA 353 0.51 ASN 205 -0.17 GLY 266
ALA 353 0.51 THR 206 -0.14 GLY 266
ALA 353 0.49 LEU 207 -0.20 GLY 266
ALA 353 0.52 LYS 208 -0.20 GLY 266
ALA 353 0.56 GLN 209 -0.15 GLY 266
ALA 353 0.53 ILE 210 -0.16 GLY 266
ALA 353 0.52 ALA 211 -0.19 GLY 266
ALA 353 0.57 SER 212 -0.17 GLY 266
ALA 353 0.58 LYS 213 -0.16 VAL 5
ALA 353 0.53 LEU 214 -0.16 VAL 5
ALA 353 0.54 ARG 215 -0.17 GLU 265
ALA 353 0.59 GLU 216 -0.18 VAL 5
ALA 353 0.56 GLN 217 -0.18 VAL 5
ALA 353 0.51 PHE 218 -0.17 VAL 5
ALA 353 0.53 GLY 219 -0.18 VAL 5
ALA 353 0.55 ASN 220 -0.17 VAL 5
ALA 353 0.51 ASN 221 -0.17 GLU 265
ALA 353 0.48 LYS 222 -0.19 GLU 265
ALA 353 0.46 THR 223 -0.22 GLU 265
ALA 353 0.46 ILE 224 -0.22 GLU 265
ALA 353 0.43 ILE 225 -0.24 GLU 265
ALA 353 0.42 PHE 226 -0.24 GLY 266
ALA 353 0.38 LYS 227 -0.22 GLY 266
ALA 353 0.36 GLN 228 -0.19 GLY 266
ALA 353 0.34 SER 229 -0.16 GLY 266
ALA 353 0.32 SER 230 -0.16 GLU 265
ALA 353 0.29 GLY 231 -0.14 GLU 265
ALA 353 0.28 GLY 232 -0.12 ASN 316
ALA 353 0.26 ASP 233 -0.11 ASN 316
ALA 353 0.27 PRO 234 -0.09 GLY 266
ALA 353 0.28 GLU 235 -0.08 GLY 266
ALA 353 0.30 ILE 236 -0.11 GLY 266
ALA 353 0.31 VAL 237 -0.12 GLY 266
ALA 353 0.32 THR 238 -0.11 GLY 266
ALA 353 0.34 HIS 239 -0.09 GLY 266
ALA 353 0.31 TRP 240 -0.07 VAL 5
ALA 353 0.31 PHE 241 -0.07 TRP 2
ALA 353 0.29 ASN 242 -0.07 TRP 2
ALA 353 0.29 CYS 243 -0.07 TRP 2
ALA 353 0.27 GLY 244 -0.08 PRO 349
ALA 353 0.24 GLY 245 -0.08 PRO 349
ALA 353 0.25 GLU 246 -0.07 TRP 2
ALA 353 0.26 PHE 247 -0.07 TRP 2
ALA 353 0.29 PHE 248 -0.07 TRP 2
ALA 353 0.30 TYR 249 -0.06 VAL 5
ALA 353 0.32 CYS 250 -0.07 VAL 5
ALA 353 0.33 ASN 251 -0.10 GLY 266
ALA 353 0.36 SER 252 -0.14 GLY 266
ALA 353 0.36 THR 253 -0.18 GLY 266
ALA 353 0.38 GLN 254 -0.22 GLY 266
ALA 353 0.40 LEU 255 -0.21 GLY 266
ALA 353 0.40 PHE 256 -0.24 GLY 266
ALA 353 0.39 ASN 257 -0.30 GLY 266
ALA 353 0.42 SER 258 -0.33 GLY 266
ALA 353 0.43 THR 259 -0.30 GLU 265
ALA 353 0.47 TRP 260 -0.27 GLU 265
ALA 353 0.49 PHE 261 -0.24 GLU 265
ALA 353 0.45 ASN 262 -0.26 GLU 265
ALA 353 0.44 SER 263 -0.23 GLU 265
ALA 353 0.43 THR 264 -0.24 GLU 265
ALA 353 0.36 GLU 265 -0.31 SER 258
ALA 353 0.36 GLY 266 -0.33 SER 258
ALA 353 0.38 SER 267 -0.19 GLN 254
ALA 353 0.41 ASP 268 -0.10 ASN 257
ALA 353 0.40 THR 269 -0.06 VAL 5
ALA 353 0.38 ILE 270 -0.08 VAL 5
ALA 353 0.36 THR 271 -0.07 VAL 5
ALA 353 0.34 LEU 272 -0.07 VAL 5
ALA 353 0.32 PRO 273 -0.07 VAL 5
ALA 353 0.30 CYS 274 -0.06 TRP 2
ALA 353 0.28 ARG 275 -0.06 TRP 2
ALA 353 0.26 ILE 276 -0.06 TRP 2
ALA 353 0.24 LYS 277 -0.06 ASN 316
ALA 353 0.21 GLN 278 -0.07 ASN 316
ALA 353 0.21 ILE 279 -0.08 ASN 316
ALA 353 0.22 ILE 280 -0.08 ASN 316
ALA 353 0.22 ASN 281 -0.10 ASN 316
ALA 353 0.21 MET 282 -0.09 ASN 316
ALA 353 0.24 TRP 283 -0.09 ASN 316
ALA 353 0.21 GLN 284 -0.08 ASN 316
ALA 353 0.18 LYS 285 -0.11 ASN 316
ALA 353 0.18 VAL 286 -0.13 ASN 316
ALA 353 0.17 GLY 287 -0.12 ASN 316
ALA 353 0.18 LYS 288 -0.11 ASN 316
ALA 353 0.18 ALA 289 -0.09 ASN 316
ALA 353 0.18 MET 290 -0.08 ASN 316
ALA 353 0.19 TYR 291 -0.07 ASN 316
ALA 353 0.19 ALA 292 -0.06 TRP 2
ALA 353 0.20 PRO 293 -0.06 TRP 2
ALA 353 0.22 PRO 294 -0.07 TRP 2
ALA 353 0.21 ILE 295 -0.07 PRO 349
ALA 353 0.22 SER 296 -0.08 PRO 349
ALA 353 0.24 GLY 297 -0.07 PRO 349
ALA 353 0.26 GLN 298 -0.07 PRO 349
ALA 353 0.28 ILE 299 -0.07 TRP 2
ALA 353 0.31 ARG 300 -0.07 TRP 2
ALA 353 0.33 CYS 301 -0.08 TRP 2
ALA 353 0.37 SER 302 -0.08 TRP 2
ALA 353 0.39 SER 303 -0.08 TRP 2
ALA 353 0.44 ASN 304 -0.08 TRP 2
ALA 353 0.45 ILE 305 -0.09 VAL 5
ALA 353 0.49 THR 306 -0.10 VAL 5
ALA 353 0.48 GLY 307 -0.11 VAL 5
ALA 353 0.45 LEU 308 -0.11 VAL 5
ALA 353 0.42 LEU 309 -0.12 GLY 266
ALA 353 0.42 LEU 310 -0.14 GLY 266
ALA 353 0.39 THR 311 -0.14 GLY 266
ALA 353 0.40 ARG 312 -0.15 GLY 266
ALA 353 0.37 ASP 313 -0.16 GLU 265
ALA 353 0.38 GLY 314 -0.16 GLU 265
ALA 353 0.37 GLY 315 -0.18 GLU 265
ALA 353 0.39 ASN 316 -0.15 GLY 92
ALA 353 0.36 SER 317 -0.18 GLU 265
ALA 353 0.38 ASN 318 -0.18 GLU 265
ALA 353 0.40 ASN 319 -0.17 GLU 265
ALA 353 0.43 GLU 320 -0.18 GLU 265
ALA 353 0.43 SER 321 -0.20 GLU 265
ALA 353 0.43 GLU 322 -0.19 GLU 265
ALA 353 0.41 ILE 323 -0.20 GLU 265
ALA 353 0.42 PHE 324 -0.18 GLY 266
ALA 353 0.39 ARG 325 -0.17 GLY 266
ALA 353 0.38 PRO 326 -0.15 GLY 266
ALA 353 0.36 GLY 327 -0.13 GLY 266
ALA 353 0.35 GLY 328 -0.10 GLY 266
ALA 353 0.31 GLY 329 -0.09 GLY 266
ALA 353 0.30 ASP 330 -0.09 VAL 5
ALA 353 0.31 MET 331 -0.08 VAL 5
ALA 353 0.33 ARG 332 -0.09 VAL 5
ALA 353 0.38 ASP 333 -0.11 VAL 5
ALA 353 0.39 ASN 334 -0.09 VAL 5
ALA 353 0.38 TRP 335 -0.09 VAL 5
ALA 353 0.43 ARG 336 -0.11 VAL 5
ALA 353 0.47 SER 337 -0.12 VAL 5
ALA 353 0.48 GLU 338 -0.10 VAL 5
ALA 353 0.46 LEU 339 -0.11 VAL 5
ALA 353 0.53 TYR 340 -0.14 VAL 5
ALA 353 0.60 LYS 341 -0.15 VAL 5
ALA 353 0.53 TYR 342 -0.13 VAL 5
ALA 353 0.46 LYS 343 -0.12 VAL 5
ALA 353 0.35 VAL 344 -0.11 PRO 349
ALA 353 0.31 VAL 345 -0.10 TRP 2
PRO 10 0.23 LYS 346 -0.11 PRO 349
PRO 10 0.40 ILE 347 -0.25 PRO 349
PRO 10 0.22 GLU 348 -0.18 PRO 349
GLY 8 0.29 PRO 349 -0.42 GLY 116
GLY 8 0.37 LEU 350 -0.18 ASN 47
VAL 56 0.83 GLY 351 -0.19 PRO 349
ASN 55 0.74 VAL 352 -0.18 PRO 349
ASN 55 1.45 ALA 353 -0.11 PRO 349

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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.