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***  open cutoff 10 melek new  ***

CA distance fluctuations for 260522120748406586

---  normal mode 14  ---

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
PRO 422 0.29 ALA 1 -0.09 LYS 355
PRO 422 0.34 SER 2 -0.09 LYS 355
PRO 422 0.39 SER 3 -0.09 LYS 355
PRO 422 0.47 THR 4 -0.09 LYS 355
PRO 422 0.53 ASN 5 -0.07 LYS 355
PRO 422 0.56 LEU 6 -0.07 LYS 355
PRO 422 0.62 LYS 7 -0.05 LYS 355
PRO 422 0.63 ASP 8 -0.06 LYS 355
PRO 422 0.66 VAL 9 -0.07 GLY 99
PRO 422 0.72 LEU 10 -0.07 GLY 99
PRO 422 0.77 ALA 11 -0.07 ALA 432
PRO 422 0.78 ALA 12 -0.09 ALA 432
PRO 422 0.81 LEU 13 -0.10 ALA 432
PRO 422 0.90 ILE 14 -0.11 ALA 432
PRO 422 0.95 PRO 15 -0.14 ALA 432
PRO 422 0.93 LYS 16 -0.15 ALA 432
PRO 422 0.97 GLU 17 -0.14 ALA 432
PRO 422 1.07 GLN 18 -0.16 ALA 432
PRO 422 1.09 ALA 19 -0.18 ALA 432
PRO 422 1.08 ARG 20 -0.19 ALA 432
PRO 422 1.17 ILE 21 -0.20 ALA 432
PRO 422 1.24 LYS 22 -0.22 ALA 432
PRO 422 1.21 THR 23 -0.22 ALA 432
PRO 422 1.23 PHE 24 -0.24 ALA 432
PRO 422 1.37 ARG 25 -0.26 ALA 432
PRO 422 1.37 GLN 26 -0.26 ALA 432
PRO 422 1.33 GLN 27 -0.26 ALA 432
PRO 422 1.33 HIS 28 -0.28 ALA 432
PRO 422 1.45 GLY 29 -0.30 ALA 432
PRO 422 1.54 GLY 30 -0.35 ALA 432
PRO 422 1.40 THR 31 -0.32 ALA 432
PRO 422 1.37 ALA 32 -0.33 ALA 432
PRO 422 1.26 LEU 33 -0.29 ALA 432
PRO 422 1.21 GLY 34 -0.30 ALA 432
PRO 422 1.21 GLN 35 -0.36 ALA 432
PRO 422 1.18 ILE 36 -0.15 LEU 419
PRO 422 1.06 THR 37 -0.11 GLY 34
PRO 422 1.01 VAL 38 -0.11 GLN 287
PRO 422 0.87 ASP 39 -0.12 GLN 287
PRO 422 0.92 MET 40 -0.13 ARG 421
PRO 422 0.98 SER 41 -0.12 GLN 287
PRO 422 0.81 TYR 42 -0.14 GLN 287
PRO 422 0.74 GLY 43 -0.21 ARG 421
PRO 422 0.77 GLY 44 -0.34 ARG 421
PRO 422 0.93 MET 45 -0.24 ARG 421
PRO 422 0.82 ARG 46 -0.20 ARG 421
PRO 422 0.88 GLY 47 -0.13 GLU 280
PRO 422 1.05 MET 48 -0.13 PRO 418
PRO 422 1.11 LYS 49 -0.12 GLU 280
PRO 422 1.18 GLY 50 -0.14 PRO 418
PRO 422 1.09 LEU 51 -0.09 ALA 277
PRO 422 1.08 VAL 52 -0.08 ALA 432
PRO 422 0.93 TYR 53 -0.07 ALA 277
PRO 422 0.88 GLU 54 -0.07 GLU 17
PRO 422 0.73 THR 55 -0.05 ARG 20
PRO 422 0.69 SER 56 -0.08 LYS 423
PRO 422 0.71 VAL 57 -0.20 LYS 423
PRO 422 0.63 LEU 58 -0.40 LYS 423
PRO 422 0.61 ASP 59 -0.48 LYS 423
PRO 422 0.57 PRO 60 -0.67 LYS 423
PRO 422 0.52 ASP 61 -0.66 LYS 423
PRO 422 0.47 GLU 62 -0.59 LYS 423
PRO 422 0.45 GLY 63 -0.59 LYS 423
PRO 422 0.50 ILE 64 -0.42 LYS 423
PRO 422 0.56 ARG 65 -0.29 LYS 423
PRO 422 0.57 PHE 66 -0.16 LYS 423
PRO 422 0.67 ARG 67 -0.11 LYS 423
PRO 422 0.64 GLY 68 -0.22 LYS 423
PRO 422 0.53 PHE 69 -0.27 LYS 423
PRO 422 0.46 SER 70 -0.38 LYS 423
PRO 422 0.35 ILE 71 -0.42 LYS 423
SER 424 0.32 PRO 72 -0.47 LYS 423
PRO 422 0.38 GLU 73 -0.37 LYS 423
PRO 422 0.37 CYS 74 -0.30 LYS 423
SER 424 0.30 GLN 75 -0.36 LYS 423
SER 424 0.30 LYS 76 -0.35 LYS 423
PRO 422 0.34 LEU 77 -0.26 LYS 423
PRO 422 0.33 LEU 78 -0.20 LYS 423
SER 424 0.30 PRO 79 -0.18 LYS 423
SER 424 0.27 LYS 80 -0.22 LYS 423
SER 424 0.24 GLY 81 -0.19 LYS 423
SER 424 0.23 GLY 82 -0.19 LYS 423
SER 424 0.21 GLY 84 -0.29 LYS 423
SER 424 0.22 GLY 85 -0.35 LYS 423
SER 424 0.23 GLU 86 -0.33 LYS 423
SER 424 0.27 PRO 87 -0.26 LYS 423
SER 424 0.28 LEU 88 -0.16 LYS 423
SER 424 0.31 PRO 89 -0.11 LYS 423
SER 424 0.33 GLU 90 -0.08 LYS 355
PRO 422 0.36 GLY 91 -0.10 LYS 355
PRO 422 0.40 LEU 92 -0.09 LYS 355
PRO 422 0.45 PHE 93 -0.07 LYS 355
PRO 422 0.49 TRP 94 -0.08 LYS 355
PRO 422 0.53 LEU 95 -0.08 LYS 355
PRO 422 0.60 LEU 96 -0.06 LYS 355
PRO 422 0.65 VAL 97 -0.05 LYS 355
PRO 422 0.67 THR 98 -0.08 GLY 99
PRO 422 0.67 GLY 99 -0.08 THR 98
PRO 422 0.59 GLN 100 -0.09 LYS 355
PRO 422 0.48 ILE 101 -0.11 LYS 355
PRO 422 0.44 PRO 102 -0.11 LYS 355
PRO 422 0.38 THR 103 -0.12 LYS 355
SER 424 0.31 GLY 104 -0.13 LYS 355
PRO 422 0.32 ALA 105 -0.11 LYS 355
PRO 422 0.39 GLN 106 -0.10 LYS 355
PRO 422 0.33 VAL 107 -0.10 LYS 355
SER 424 0.30 SER 108 -0.10 LYS 355
PRO 422 0.33 TRP 109 -0.08 LYS 355
PRO 422 0.34 LEU 110 -0.07 LYS 355
THR 427 0.29 SER 111 -0.08 LYS 355
THR 427 0.29 LYS 112 -0.07 LYS 355
THR 427 0.32 GLU 113 -0.06 LYS 355
THR 427 0.33 TRP 114 -0.06 LYS 355
THR 427 0.31 ALA 115 -0.06 LYS 355
THR 427 0.32 LYS 116 -0.05 LYS 355
THR 427 0.34 ARG 117 -0.05 LYS 339
THR 427 0.34 ALA 118 -0.05 LYS 339
THR 427 0.35 ALA 119 -0.05 LYS 339
THR 427 0.36 LEU 120 -0.05 LYS 339
THR 427 0.38 PRO 121 -0.04 LYS 339
THR 427 0.37 SER 122 -0.04 LYS 339
THR 427 0.39 HIS 123 -0.05 ARG 421
THR 427 0.40 VAL 124 -0.07 ARG 421
THR 427 0.36 VAL 125 -0.07 PRO 422
THR 427 0.37 THR 126 -0.12 PRO 422
THR 427 0.39 MET 127 -0.11 ARG 421
THR 427 0.37 LEU 128 -0.16 PRO 422
THR 427 0.34 ASP 129 -0.27 PRO 422
THR 427 0.35 ASN 130 -0.31 PRO 422
THR 427 0.36 PHE 131 -0.29 PRO 422
THR 427 0.34 PRO 132 -0.43 PRO 422
THR 427 0.31 THR 133 -0.51 PRO 422
GLY 312 0.35 ASN 134 -0.51 PRO 422
THR 427 0.37 LEU 135 -0.34 PRO 422
THR 427 0.35 HIS 136 -0.30 PRO 422
THR 427 0.35 PRO 137 -0.23 ARG 421
THR 427 0.39 MET 138 -0.25 ARG 421
THR 427 0.43 SER 139 -0.27 ARG 421
THR 427 0.40 GLN 140 -0.20 ARG 421
THR 427 0.41 LEU 141 -0.17 ARG 421
THR 427 0.46 SER 142 -0.19 ARG 421
THR 427 0.46 ALA 143 -0.17 ARG 421
THR 427 0.43 ALA 144 -0.11 ARG 421
THR 427 0.45 ILE 145 -0.08 GLU 420
THR 427 0.49 THR 146 -0.08 ARG 421
THR 427 0.46 ALA 147 -0.07 ARG 421
THR 427 0.44 LEU 148 -0.05 GLU 420
LYS 423 0.49 ASN 149 -0.04 GLU 420
LYS 423 0.51 SER 150 -0.03 LYS 339
LYS 423 0.46 GLU 151 -0.03 LYS 339
LYS 423 0.52 SER 152 -0.03 LYS 339
PRO 422 0.56 ASN 153 -0.03 LYS 339
PRO 422 0.68 PHE 154 -0.03 GLN 35
LYS 423 0.67 ALA 155 -0.03 GLN 35
LYS 423 0.64 ARG 156 -0.03 GLN 35
PRO 422 0.70 ALA 157 -0.03 GLN 35
PRO 422 0.78 TYR 158 -0.03 GLN 35
LYS 423 0.77 ALA 159 -0.02 SER 3
PRO 422 0.72 GLU 160 -0.04 SER 3
PRO 422 0.83 GLY 161 -0.03 ASN 5
PRO 422 0.84 ILE 162 -0.03 LYS 7
PRO 422 0.94 LEU 163 -0.04 GLN 35
PRO 422 1.03 ARG 164 -0.05 ALA 432
PRO 422 0.99 THR 165 -0.08 ALA 432
PRO 422 0.88 LYS 166 -0.05 PRO 15
PRO 422 0.89 TYR 167 -0.04 GLN 35
PRO 422 0.83 TRP 168 -0.04 GLN 35
PRO 422 0.75 GLU 169 -0.04 GLY 99
PRO 422 0.69 MET 170 -0.04 GLY 99
PRO 422 0.71 VAL 171 -0.03 GLN 35
PRO 422 0.64 TYR 172 -0.04 VAL 97
PRO 422 0.56 GLU 173 -0.04 TRP 94
PRO 422 0.53 SER 174 -0.03 LYS 339
PRO 422 0.54 ALA 175 -0.04 TRP 94
PRO 422 0.44 MET 176 -0.05 TRP 94
THR 427 0.38 ASP 177 -0.04 LYS 339
THR 427 0.40 LEU 178 -0.05 GLU 420
THR 427 0.37 ILE 179 -0.06 GLU 420
THR 427 0.35 ALA 180 -0.05 LYS 339
THR 427 0.36 LYS 181 -0.06 GLU 420
THR 427 0.37 LEU 182 -0.08 GLU 420
THR 427 0.33 PRO 183 -0.08 GLU 420
THR 427 0.33 CYS 184 -0.07 GLU 420
THR 427 0.36 VAL 185 -0.09 ARG 421
THR 427 0.34 ALA 186 -0.12 ARG 421
THR 427 0.31 ALA 187 -0.16 PRO 422
THR 427 0.32 LYS 188 -0.20 PRO 422
THR 427 0.32 ILE 189 -0.23 PRO 422
THR 427 0.29 TYR 190 -0.33 PRO 422
THR 427 0.27 ARG 191 -0.39 PRO 422
THR 427 0.29 ASN 192 -0.41 PRO 422
THR 427 0.28 LEU 193 -0.48 PRO 422
THR 427 0.25 TYR 194 -0.55 PRO 422
THR 427 0.24 ARG 195 -0.54 PRO 422
THR 427 0.24 ALA 196 -0.62 PRO 422
THR 427 0.27 GLY 197 -0.48 PRO 422
THR 427 0.26 SER 198 -0.45 PRO 422
THR 427 0.27 SER 199 -0.34 PRO 422
THR 427 0.28 ILE 200 -0.24 PRO 422
THR 427 0.27 GLY 201 -0.21 PRO 422
THR 427 0.28 ALA 202 -0.11 PRO 422
THR 427 0.29 ILE 203 -0.07 LYS 339
THR 427 0.27 ASP 204 -0.07 LYS 339
THR 427 0.28 SER 205 -0.07 LYS 355
THR 427 0.26 LYS 206 -0.09 LYS 355
THR 427 0.26 LEU 207 -0.09 LYS 355
THR 427 0.27 ASP 208 -0.09 LYS 355
THR 427 0.29 TRP 209 -0.07 LYS 355
THR 427 0.28 SER 210 -0.11 LYS 423
THR 427 0.26 HIS 211 -0.11 LYS 423
THR 427 0.28 ASN 212 -0.08 LYS 339
THR 427 0.29 PHE 213 -0.08 LYS 339
THR 427 0.26 THR 214 -0.15 PRO 422
THR 427 0.26 ASN 215 -0.18 PRO 422
THR 427 0.28 MET 216 -0.17 PRO 422
THR 427 0.27 LEU 217 -0.24 PRO 422
THR 427 0.25 GLY 218 -0.32 PRO 422
THR 427 0.22 TYR 219 -0.34 PRO 422
THR 427 0.21 THR 220 -0.32 PRO 422
THR 427 0.19 ASP 221 -0.32 PRO 422
THR 427 0.19 ALA 222 -0.28 LYS 423
THR 427 0.18 GLN 223 -0.35 LYS 423
THR 427 0.20 PHE 224 -0.31 LYS 423
THR 427 0.23 THR 225 -0.24 LYS 423
THR 427 0.21 GLU 226 -0.30 LYS 423
THR 427 0.22 LEU 227 -0.34 LYS 423
THR 427 0.25 MET 228 -0.25 LYS 423
THR 427 0.25 ARG 229 -0.23 LYS 423
THR 427 0.24 LEU 230 -0.31 LYS 423
THR 427 0.26 TYR 231 -0.31 LYS 423
THR 427 0.29 LEU 232 -0.19 LYS 423
SER 424 0.30 THR 233 -0.21 LYS 423
SER 424 0.30 ILE 234 -0.31 LYS 423
THR 427 0.30 HIS 235 -0.26 LYS 423
SER 424 0.35 SER 236 -0.13 LYS 423
PRO 422 0.49 ASP 237 -0.10 GLU 420
PRO 422 0.53 HIS 238 -0.18 LYS 423
PRO 422 0.69 GLU 239 -0.10 ALA 277
PRO 422 0.79 GLY 240 -0.14 GLU 420
PRO 422 0.78 GLY 241 -0.19 GLU 420
PRO 422 0.60 ASN 242 -0.19 GLU 420
PRO 422 0.54 VAL 243 -0.31 ARG 421
PRO 422 0.49 SER 244 -0.22 GLU 420
PRO 422 0.64 ALA 245 -0.19 GLU 420
PRO 422 0.77 HIS 246 -0.30 GLU 420
PRO 422 0.69 THR 247 -0.30 GLU 420
PRO 422 0.68 SER 248 -0.19 GLU 420
PRO 422 0.86 HIS 249 -0.20 GLU 420
PRO 422 0.91 LEU 250 -0.28 GLU 420
PRO 422 0.81 VAL 251 -0.13 GLU 420
PRO 422 0.84 GLY 252 -0.08 PHE 417
PRO 422 1.01 SER 253 -0.08 PHE 417
PRO 422 0.97 ALA 254 -0.06 GLN 35
PRO 422 0.92 LEU 255 -0.09 PHE 417
PRO 422 0.77 SER 256 -0.06 PHE 417
PRO 422 0.67 ASP 257 -0.04 PHE 417
PRO 422 0.62 PRO 258 -0.04 GLU 420
THR 427 0.48 TYR 259 -0.07 GLU 420
LYS 423 0.56 LEU 260 -0.08 GLU 420
PRO 422 0.61 SER 261 -0.12 GLU 420
THR 427 0.50 PHE 262 -0.12 GLU 420
THR 427 0.51 ALA 263 -0.13 ARG 421
THR 427 0.57 ALA 264 -0.21 ARG 421
THR 427 0.53 ALA 265 -0.19 GLU 420
THR 427 0.48 MET 266 -0.23 ARG 421
THR 427 0.53 ASN 267 -0.34 ARG 421
THR 427 0.53 GLY 268 -0.38 ARG 421
THR 427 0.44 LEU 269 -0.30 ARG 421
THR 427 0.44 ALA 270 -0.34 ARG 421
THR 427 0.45 GLY 271 -0.42 ARG 421
ARG 313 0.47 PRO 272 -0.40 ARG 421
VAL 314 0.49 LEU 273 -0.44 ARG 421
VAL 314 0.39 HIS 274 -0.38 ARG 421
ARG 313 0.35 GLY 275 -0.31 ARG 421
ARG 313 0.37 LEU 276 -0.37 LYS 423
VAL 314 0.38 ALA 277 -0.55 LYS 423
ARG 313 0.25 ASN 278 -0.56 LYS 423
ARG 313 0.30 GLN 279 -0.53 LYS 423
ARG 313 0.40 GLU 280 -0.66 LYS 423
THR 308 0.34 VAL 281 -0.78 LYS 423
THR 308 0.27 LEU 282 -0.68 LYS 423
THR 308 0.32 GLY 283 -0.69 LYS 423
THR 308 0.40 TRP 284 -0.84 LYS 423
TYR 304 0.31 LEU 285 -0.83 LYS 423
TYR 304 0.24 ALA 286 -0.74 LYS 423
TYR 304 0.28 GLN 287 -0.84 LYS 423
SER 300 0.29 LEU 288 -0.94 LYS 423
SER 300 0.18 GLN 289 -0.82 LYS 423
THR 388 0.19 LYS 290 -0.82 LYS 423
SER 300 0.20 ALA 291 -0.92 LYS 423
LEU 288 0.19 ALA 295 -0.72 LYS 423
LEU 288 0.19 GLY 296 -0.78 LYS 423
LEU 288 0.20 ALA 297 -0.81 LYS 423
TRP 284 0.21 ASP 298 -0.84 LYS 423
TRP 284 0.25 ALA 299 -0.86 LYS 423
LEU 288 0.29 SER 300 -0.90 LYS 423
TRP 284 0.30 LEU 301 -0.95 LYS 423
TRP 284 0.29 ARG 302 -0.99 LYS 423
TRP 284 0.32 ASP 303 -1.00 LYS 423
TRP 284 0.39 TYR 304 -1.03 LYS 423
TRP 284 0.39 ILE 305 -1.14 LYS 423
LEU 273 0.33 TRP 306 -1.15 LYS 423
TRP 284 0.36 ASN 307 -1.14 LYS 423
TRP 284 0.40 THR 308 -1.21 LYS 423
LEU 273 0.41 LEU 309 -1.36 LYS 423
LEU 273 0.39 ASN 310 -1.27 LYS 423
PRO 272 0.41 SER 311 -1.21 LYS 423
LEU 273 0.46 GLY 312 -1.36 LYS 423
LEU 273 0.48 ARG 313 -1.31 LYS 423
LEU 273 0.49 VAL 314 -1.36 LYS 423
PRO 316 0.59 VAL 315 -1.17 LYS 423
VAL 315 0.59 PRO 316 -1.01 LYS 423
LEU 273 0.27 GLY 317 -0.98 LYS 423
LEU 273 0.31 TYR 318 -1.11 LYS 423
LEU 273 0.38 GLY 319 -1.26 LYS 423
PRO 422 0.37 HIS 320 -1.11 LYS 423
PRO 422 0.49 ALA 321 -1.10 LYS 423
PRO 422 0.55 VAL 322 -0.87 LYS 423
PRO 422 0.46 LEU 323 -0.86 LYS 423
PRO 422 0.43 ARG 324 -0.90 LYS 423
PRO 422 0.34 LYS 325 -0.87 LYS 423
SER 424 0.30 THR 326 -0.83 LYS 423
SER 424 0.30 ASP 327 -0.73 LYS 423
SER 424 0.30 PRO 328 -0.63 LYS 423
SER 424 0.27 ARG 329 -0.56 LYS 423
SER 424 0.23 TYR 330 -0.68 LYS 423
SER 424 0.23 THR 331 -0.68 LYS 423
SER 424 0.24 CYS 332 -0.56 LYS 423
SER 424 0.19 GLN 333 -0.57 LYS 423
SER 424 0.17 ARG 334 -0.65 LYS 423
SER 424 0.20 GLU 335 -0.59 LYS 423
THR 427 0.17 PHE 336 -0.52 LYS 423
THR 427 0.15 ALA 337 -0.56 LYS 423
THR 427 0.14 LEU 338 -0.58 LYS 423
THR 427 0.15 LYS 339 -0.51 LYS 423
THR 427 0.15 HIS 340 -0.49 LYS 423
THR 427 0.14 LEU 341 -0.53 LYS 423
ILE 431 0.13 PRO 342 -0.58 LYS 423
ILE 431 0.13 GLY 343 -0.59 LYS 423
ILE 431 0.14 ASP 344 -0.59 LYS 423
GLN 289 0.14 PRO 345 -0.65 LYS 423
ILE 431 0.14 MET 346 -0.68 LYS 423
ILE 431 0.15 PHE 347 -0.67 LYS 423
ILE 431 0.14 LYS 348 -0.71 LYS 423
ILE 431 0.15 LEU 349 -0.79 LYS 423
ILE 431 0.15 VAL 350 -0.80 LYS 423
ILE 431 0.15 ALA 351 -0.80 LYS 423
ILE 431 0.16 GLN 352 -0.85 LYS 423
PRO 316 0.20 LEU 353 -0.95 LYS 423
SER 424 0.17 TYR 354 -0.90 LYS 423
PRO 316 0.20 LYS 355 -0.87 LYS 423
PRO 316 0.25 ILE 356 -0.97 LYS 423
PRO 316 0.31 VAL 357 -1.09 LYS 423
LEU 273 0.27 PRO 358 -1.09 LYS 423
LEU 273 0.28 ASN 359 -1.04 LYS 423
LEU 273 0.33 VAL 360 -1.12 LYS 423
LEU 273 0.37 LEU 361 -1.28 LYS 423
LEU 273 0.34 LEU 362 -1.17 LYS 423
LEU 273 0.34 GLU 363 -1.09 LYS 423
LEU 273 0.41 GLN 364 -1.21 LYS 423
LEU 273 0.42 GLY 365 -1.28 LYS 423
LEU 273 0.46 ALA 366 -1.51 LYS 423
LEU 273 0.36 ALA 367 -1.38 LYS 423
PRO 422 0.39 ALA 368 -1.21 LYS 423
PRO 422 0.35 ASN 369 -1.14 LYS 423
LEU 273 0.29 PRO 370 -1.21 LYS 423
SER 424 0.27 TRP 371 -1.03 LYS 423
SER 424 0.23 PRO 372 -0.96 LYS 423
SER 424 0.25 ASN 373 -0.80 LYS 423
SER 424 0.22 VAL 374 -0.65 LYS 423
THR 427 0.20 ASP 375 -0.66 LYS 423
GLN 364 0.18 ALA 376 -0.78 LYS 423
THR 427 0.17 HIS 377 -0.68 LYS 423
THR 427 0.19 SER 378 -0.55 LYS 423
THR 308 0.19 GLY 379 -0.54 LYS 423
ILE 431 0.16 VAL 380 -0.59 LYS 423
THR 427 0.16 LEU 381 -0.52 LYS 423
THR 427 0.19 LEU 382 -0.43 LYS 423
SER 311 0.18 GLN 383 -0.45 LYS 423
LYS 290 0.16 TYR 384 -0.47 LYS 423
THR 427 0.17 TYR 385 -0.41 PRO 422
LYS 290 0.18 GLY 386 -0.50 PRO 422
SER 311 0.19 MET 387 -0.43 PRO 422
SER 311 0.23 THR 388 -0.54 PRO 422
SER 311 0.24 GLU 389 -0.52 PRO 422
SER 311 0.26 MET 390 -0.43 PRO 422
ARG 313 0.31 ASN 391 -0.37 PRO 422
THR 427 0.26 TYR 392 -0.29 PRO 422
THR 427 0.25 TYR 393 -0.27 LYS 423
THR 427 0.32 THR 394 -0.22 ARG 421
THR 427 0.34 VAL 395 -0.18 ARG 421
THR 427 0.31 LEU 396 -0.15 LYS 423
THR 427 0.33 PHE 397 -0.16 LYS 423
THR 427 0.37 GLY 398 -0.13 ARG 421
THR 427 0.35 VAL 399 -0.10 GLU 420
THR 427 0.34 SER 400 -0.10 GLU 420
THR 427 0.38 ARG 401 -0.12 GLU 420
THR 427 0.39 ALA 402 -0.10 GLU 420
PRO 422 0.43 LEU 403 -0.07 GLU 420
PRO 422 0.54 GLY 404 -0.08 GLU 420
PRO 422 0.60 VAL 405 -0.11 GLU 420
PRO 422 0.61 LEU 406 -0.07 GLU 420
PRO 422 0.64 ALA 407 -0.04 GLU 420
PRO 422 0.78 GLN 408 -0.04 GLU 17
PRO 422 0.79 LEU 409 -0.04 GLU 420
PRO 422 0.79 ILE 410 -0.03 PRO 15
PRO 422 0.89 TRP 411 -0.05 ALA 432
PRO 422 0.99 SER 412 -0.05 HIS 246
PRO 422 0.96 ARG 413 -0.05 GLN 35
PRO 422 0.95 ALA 414 -0.07 ALA 432
PRO 422 1.07 LEU 415 -0.12 ALA 432
PRO 422 1.13 GLY 416 -0.10 ALA 432
PRO 422 1.20 PHE 417 -0.09 ALA 432
PRO 422 1.27 PRO 418 -0.20 GLN 35
PRO 422 1.22 LEU 419 -0.19 GLN 35
PRO 422 1.21 GLU 420 -0.30 THR 247
PRO 422 1.30 ARG 421 -0.44 LEU 273
GLY 30 1.54 PRO 422 -0.63 LYS 290
PRO 422 1.30 LYS 423 -1.51 ALA 366
LYS 423 1.30 SER 424 -0.14 ASN 134
PRO 422 1.12 MET 425 -0.19 GLN 287
PRO 422 1.03 SER 426 -0.14 ALA 291
PRO 422 1.00 THR 427 -0.03 ALA 291
PRO 422 1.02 ASP 428 -0.01 ALA 291
PRO 422 1.09 GLY 429 -0.08 LYS 290
PRO 422 1.08 LEU 430 -0.19 GLN 35
PRO 422 1.04 ILE 431 -0.12 ALA 32
PRO 422 1.07 ALA 432 -0.36 GLN 35

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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.