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***  6csc_aligned_close  ***

CA distance fluctuations for 2604241133101949041

---  normal mode 11  ---

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 423 0.28 ALA 1 -0.11 VAL 33
LYS 423 0.25 SER 2 -0.10 VAL 33
LYS 423 0.21 SER 3 -0.09 VAL 33
PRO 422 0.19 THR 4 -0.08 VAL 33
PRO 422 0.18 ASN 5 -0.08 VAL 33
PRO 422 0.21 LEU 6 -0.09 VAL 33
PRO 422 0.17 LYS 7 -0.09 VAL 33
LYS 423 0.16 ASP 8 -0.10 VAL 33
LYS 423 0.21 VAL 9 -0.11 VAL 33
LYS 423 0.22 LEU 10 -0.11 VAL 33
LYS 423 0.18 ALA 11 -0.11 VAL 33
LYS 423 0.21 SER 12 -0.12 VAL 33
LYS 423 0.26 LEU 13 -0.14 VAL 33
LYS 423 0.25 ILE 14 -0.13 VAL 33
LYS 423 0.25 PRO 15 -0.11 VAL 33
LYS 423 0.31 LYS 16 -0.13 VAL 33
LYS 423 0.35 GLU 17 -0.16 VAL 33
LYS 423 0.33 GLN 18 -0.13 VAL 33
LYS 423 0.35 ALA 19 -0.11 THR 165
LYS 423 0.44 ARG 20 -0.12 VAL 33
LYS 423 0.49 ILE 21 -0.16 VAL 33
LYS 423 0.42 LYS 22 -0.10 VAL 33
LYS 423 0.48 THR 23 -0.07 THR 165
LYS 423 0.62 PHE 24 -0.08 THR 31
LYS 423 0.62 ARG 25 -0.08 VAL 33
LYS 423 0.54 GLN 26 -0.04 GLY 29
LYS 423 0.64 GLN 27 -0.06 GLY 29
LYS 423 0.80 HIS 28 -0.08 PHE 24
LYS 423 0.79 GLY 29 -0.06 GLN 27
LYS 423 0.87 ASN 30 -0.03 GLN 35
LYS 423 0.98 THR 31 -0.10 ILE 21
LYS 423 1.19 ALA 32 -0.09 ILE 21
LYS 423 1.23 VAL 33 -0.16 ILE 21
LYS 423 1.41 GLY 34 -0.11 GLU 54
LYS 423 1.35 GLN 35 -0.10 ILE 52
LYS 423 1.25 ILE 36 -0.14 GLY 50
LYS 423 0.92 THR 37 -0.11 GLY 50
LYS 423 0.66 VAL 38 -0.09 GLY 50
LYS 423 0.71 ASP 39 -0.08 SER 426
LYS 423 0.92 MET 40 -0.10 ASP 59
LYS 423 0.73 SER 41 -0.12 GLY 44
PRO 422 0.62 TYR 42 -0.22 SER 426
PRO 422 0.80 GLY 43 -0.20 SER 426
PRO 422 1.04 GLY 44 -0.27 SER 426
PRO 422 1.20 MET 45 -0.12 VAL 322
PRO 422 1.01 ARG 46 -0.14 PRO 60
LYS 423 1.12 GLY 47 -0.14 ASP 59
LYS 423 1.39 MET 48 -0.12 VAL 57
LYS 423 1.33 LYS 49 -0.13 VAL 57
LYS 423 1.21 GLY 50 -0.14 ILE 36
LYS 423 0.85 LEU 51 -0.10 ILE 36
LYS 423 0.71 ILE 52 -0.14 VAL 33
PRO 422 0.61 TYR 53 -0.12 VAL 33
LYS 423 0.53 GLU 54 -0.14 VAL 33
PRO 422 0.49 THR 55 -0.11 VAL 33
PRO 422 0.56 SER 56 -0.10 LYS 49
LYS 423 0.64 VAL 57 -0.13 LYS 49
LYS 423 0.67 LEU 58 -0.10 MET 48
LYS 423 0.70 ASP 59 -0.14 GLY 47
LYS 423 0.71 PRO 60 -0.14 ARG 46
LYS 423 0.65 ASP 61 -0.12 GLY 43
LYS 423 0.60 GLU 62 -0.10 SER 426
LYS 423 0.58 GLY 63 -0.11 SER 426
PRO 422 0.57 ILE 64 -0.10 SER 426
LYS 423 0.54 ARG 65 -0.09 MET 48
PRO 422 0.48 PHE 66 -0.08 VAL 33
LYS 423 0.47 ARG 67 -0.11 VAL 33
LYS 423 0.51 GLY 68 -0.11 VAL 33
LYS 423 0.47 PHE 69 -0.09 GLY 34
LYS 423 0.47 SER 70 -0.08 SER 426
PRO 422 0.44 ILE 71 -0.09 SER 426
LYS 423 0.40 PRO 72 -0.08 SER 426
LYS 423 0.41 GLU 73 -0.07 SER 426
PRO 422 0.39 CYS 74 -0.07 SER 426
PRO 422 0.38 GLN 75 -0.08 SER 426
LYS 423 0.34 LYS 76 -0.07 SER 426
LYS 423 0.34 LEU 77 -0.07 VAL 33
PRO 422 0.33 LEU 78 -0.07 VAL 33
PRO 422 0.30 PRO 79 -0.06 VAL 33
PRO 422 0.31 LYS 80 -0.07 SER 424
PRO 422 0.29 ALA 81 -0.07 SER 424
PRO 422 0.26 GLY 82 -0.07 SER 424
PRO 422 0.30 GLY 84 -0.08 SER 424
PRO 422 0.32 GLU 85 -0.08 SER 424
PRO 422 0.35 GLU 86 -0.09 SER 424
PRO 422 0.35 PRO 87 -0.08 SER 424
PRO 422 0.34 LEU 88 -0.08 SER 424
PRO 422 0.37 PRO 89 -0.09 SER 424
PRO 422 0.33 GLU 90 -0.08 SER 424
PRO 422 0.33 GLY 91 -0.07 VAL 33
PRO 422 0.38 LEU 92 -0.07 SER 424
PRO 422 0.37 PHE 93 -0.07 VAL 33
PRO 422 0.32 TRP 94 -0.09 VAL 33
PRO 422 0.35 LEU 95 -0.09 VAL 33
PRO 422 0.40 LEU 96 -0.10 VAL 33
PRO 422 0.33 VAL 97 -0.10 VAL 33
LYS 423 0.32 THR 98 -0.12 VAL 33
LYS 423 0.38 GLY 99 -0.12 VAL 33
LYS 423 0.35 GLN 100 -0.11 VAL 33
LYS 423 0.33 ILE 101 -0.09 VAL 33
LYS 423 0.28 PRO 102 -0.09 VAL 33
LYS 423 0.26 THR 103 -0.08 VAL 33
PRO 422 0.25 PRO 104 -0.07 VAL 33
PRO 422 0.23 GLU 105 -0.07 VAL 33
PRO 422 0.24 GLN 106 -0.08 VAL 33
PRO 422 0.27 VAL 107 -0.07 VAL 33
PRO 422 0.25 SER 108 -0.06 VAL 33
PRO 422 0.23 TRP 109 -0.07 VAL 33
PRO 422 0.26 VAL 110 -0.07 VAL 33
PRO 422 0.26 SER 111 -0.07 SER 424
PRO 422 0.23 LYS 112 -0.06 SER 424
PRO 422 0.22 GLU 113 -0.06 SER 424
PRO 422 0.25 TRP 114 -0.07 SER 424
PRO 422 0.23 ALA 115 -0.08 SER 424
PRO 422 0.20 LYS 116 -0.07 SER 424
PRO 422 0.21 ARG 117 -0.07 SER 424
PRO 422 0.23 ALA 118 -0.09 SER 424
PRO 422 0.20 ALA 119 -0.09 SER 424
PRO 422 0.20 LEU 120 -0.10 SER 424
PRO 422 0.17 PRO 121 -0.10 SER 424
PRO 422 0.16 SER 122 -0.10 SER 424
PRO 422 0.15 HIS 123 -0.13 LYS 423
PRO 422 0.20 VAL 124 -0.12 SER 424
PRO 422 0.20 VAL 125 -0.12 SER 424
PRO 422 0.17 THR 126 -0.12 SER 424
PRO 422 0.19 MET 127 -0.14 SER 424
PRO 422 0.23 LEU 128 -0.14 SER 424
PRO 422 0.21 ASP 129 -0.13 SER 424
PRO 422 0.20 ASN 130 -0.14 SER 424
PRO 422 0.23 PHE 131 -0.16 SER 424
PRO 422 0.24 PRO 132 -0.16 SER 424
PRO 422 0.27 THR 133 -0.17 SER 424
PRO 422 0.28 ASN 134 -0.18 SER 424
PRO 422 0.30 LEU 135 -0.19 SER 424
PRO 422 0.35 HIS 136 -0.20 SER 424
PRO 422 0.36 PRO 137 -0.19 SER 424
PRO 422 0.41 MET 138 -0.21 SER 424
PRO 422 0.36 SER 139 -0.21 SER 424
PRO 422 0.32 GLN 140 -0.18 SER 424
PRO 422 0.35 LEU 141 -0.18 SER 424
PRO 422 0.36 SER 142 -0.19 SER 424
PRO 422 0.28 ALA 143 -0.18 SER 424
PRO 422 0.27 ALA 144 -0.15 SER 424
PRO 422 0.29 ILE 145 -0.15 SER 424
PRO 422 0.25 THR 146 -0.15 SER 424
PRO 422 0.19 ALA 147 -0.15 LYS 423
PRO 422 0.20 LEU 148 -0.12 SER 424
PRO 422 0.17 ASN 149 -0.13 LYS 423
PRO 422 0.11 SER 150 -0.16 LYS 423
PRO 422 0.13 GLU 151 -0.11 LYS 423
PRO 422 0.13 SER 152 -0.10 LYS 423
PRO 422 0.10 ASN 153 -0.08 LYS 423
ASN 30 0.10 PHE 154 -0.08 LYS 423
ASN 30 0.10 ALA 155 -0.16 LYS 423
ASN 30 0.09 ARG 156 -0.17 LYS 423
ASN 30 0.08 ALA 157 -0.14 LYS 423
ASN 30 0.10 TYR 158 -0.18 LYS 423
ASN 30 0.10 ALA 159 -0.25 LYS 423
ASN 30 0.08 GLU 160 -0.21 LYS 423
ASN 30 0.08 GLY 161 -0.21 LYS 423
ASN 30 0.08 ILE 162 -0.13 LYS 423
ASN 30 0.07 ASN 163 -0.12 PRO 422
ASN 30 0.09 ARG 164 -0.10 PRO 422
ASN 30 0.06 THR 165 -0.11 ALA 19
ASN 30 0.06 LYS 166 -0.09 VAL 33
ASN 30 0.09 TYR 167 -0.08 VAL 33
PRO 422 0.12 TRP 168 -0.09 VAL 33
PRO 422 0.11 GLU 169 -0.09 VAL 33
PRO 422 0.11 PHE 170 -0.07 VAL 33
PRO 422 0.18 VAL 171 -0.07 VAL 33
PRO 422 0.21 TYR 172 -0.08 VAL 33
PRO 422 0.18 GLU 173 -0.07 VAL 33
PRO 422 0.21 ASP 174 -0.07 SER 424
PRO 422 0.28 ALA 175 -0.08 SER 424
PRO 422 0.26 MET 176 -0.07 SER 424
PRO 422 0.23 ASP 177 -0.08 SER 424
PRO 422 0.29 LEU 178 -0.10 SER 424
PRO 422 0.32 ILE 179 -0.10 SER 424
PRO 422 0.28 ALA 180 -0.09 SER 424
PRO 422 0.27 LYS 181 -0.11 SER 424
PRO 422 0.32 LEU 182 -0.12 SER 424
PRO 422 0.32 PRO 183 -0.12 SER 424
PRO 422 0.28 CYS 184 -0.12 SER 424
PRO 422 0.29 VAL 185 -0.13 SER 424
PRO 422 0.33 ALA 186 -0.14 SER 424
PRO 422 0.30 ALA 187 -0.13 SER 424
PRO 422 0.27 LYS 188 -0.13 SER 424
PRO 422 0.30 ILE 189 -0.15 SER 424
PRO 422 0.31 TYR 190 -0.15 SER 424
PRO 422 0.27 ARG 191 -0.13 SER 424
PRO 422 0.26 ASN 192 -0.14 SER 424
PRO 422 0.28 LEU 193 -0.15 SER 424
PRO 422 0.29 TYR 194 -0.14 SER 424
PRO 422 0.26 ARG 195 -0.13 SER 424
PRO 422 0.24 ALA 196 -0.13 SER 424
PRO 422 0.23 GLY 197 -0.13 SER 424
PRO 422 0.23 SER 198 -0.12 SER 424
PRO 422 0.22 SER 199 -0.11 SER 424
PRO 422 0.24 ILE 200 -0.11 SER 424
PRO 422 0.22 GLY 201 -0.10 SER 424
PRO 422 0.22 ALA 202 -0.09 SER 424
PRO 422 0.23 ILE 203 -0.09 SER 424
PRO 422 0.23 ASP 204 -0.08 SER 424
PRO 422 0.22 SER 205 -0.07 SER 424
PRO 422 0.22 LYS 206 -0.07 SER 424
PRO 422 0.25 LEU 207 -0.08 SER 424
PRO 422 0.28 ASP 208 -0.08 SER 424
PRO 422 0.30 TRP 209 -0.09 SER 424
PRO 422 0.33 SER 210 -0.10 SER 424
PRO 422 0.30 HIS 211 -0.09 SER 424
PRO 422 0.28 ASN 212 -0.10 SER 424
PRO 422 0.31 PHE 213 -0.11 SER 424
PRO 422 0.31 THR 214 -0.11 SER 424
PRO 422 0.28 ASN 215 -0.10 SER 424
PRO 422 0.27 MET 216 -0.11 SER 424
PRO 422 0.30 LEU 217 -0.12 SER 424
PRO 422 0.28 GLY 218 -0.11 SER 424
PRO 422 0.30 TYR 219 -0.11 SER 424
PRO 422 0.28 THR 220 -0.10 SER 424
PRO 422 0.29 ASP 221 -0.10 SER 424
PRO 422 0.30 PRO 222 -0.10 SER 424
PRO 422 0.32 GLN 223 -0.10 SER 424
PRO 422 0.33 PHE 224 -0.11 SER 424
PRO 422 0.32 THR 225 -0.10 SER 424
PRO 422 0.34 GLU 226 -0.10 SER 424
PRO 422 0.37 LEU 227 -0.11 SER 424
PRO 422 0.37 MET 228 -0.12 SER 424
PRO 422 0.37 ARG 229 -0.10 SER 424
PRO 422 0.40 LEU 230 -0.11 SER 424
PRO 422 0.43 TYR 231 -0.12 SER 424
PRO 422 0.43 LEU 232 -0.12 SER 424
PRO 422 0.43 THR 233 -0.11 SER 424
PRO 422 0.48 ILE 234 -0.12 SER 424
PRO 422 0.53 HIS 235 -0.14 SER 424
PRO 422 0.51 SER 236 -0.12 SER 424
PRO 422 0.59 ASP 237 -0.12 SER 424
PRO 422 0.67 HIS 238 -0.13 SER 424
PRO 422 0.72 GLU 239 -0.11 SER 424
PRO 422 0.83 GLY 240 -0.13 SER 424
PRO 422 1.05 GLY 241 -0.17 SER 424
PRO 422 0.93 ASN 242 -0.22 SER 424
PRO 422 0.92 VAL 243 -0.28 SER 424
PRO 422 0.75 SER 244 -0.23 SER 424
PRO 422 0.76 ALA 245 -0.18 SER 424
PRO 422 0.95 HIS 246 -0.20 SER 424
PRO 422 0.77 THR 247 -0.24 SER 424
PRO 422 0.59 SER 248 -0.17 SER 424
PRO 422 0.61 HIS 249 -0.13 SER 424
PRO 422 0.60 LEU 250 -0.16 SER 424
PRO 422 0.39 VAL 251 -0.15 SER 424
PRO 422 0.31 GLY 252 -0.09 SER 424
PRO 422 0.21 SER 253 -0.08 LYS 432
ASN 30 0.19 ALA 254 -0.18 ARG 421
ASN 30 0.15 LEU 255 -0.14 ARG 421
ASN 30 0.14 SER 256 -0.16 LYS 423
PRO 422 0.18 ASP 257 -0.09 ARG 421
PRO 422 0.28 PRO 258 -0.10 SER 424
PRO 422 0.28 TYR 259 -0.12 SER 424
PRO 422 0.28 LEU 260 -0.14 SER 424
PRO 422 0.38 SER 261 -0.15 SER 424
PRO 422 0.43 PHE 262 -0.16 SER 424
PRO 422 0.40 ALA 263 -0.19 SER 424
PRO 422 0.47 ALA 264 -0.23 SER 424
PRO 422 0.59 ALA 265 -0.22 SER 424
PRO 422 0.52 MET 266 -0.22 SER 424
PRO 422 0.52 ASN 267 -0.26 SER 424
PRO 422 0.66 GLY 268 -0.29 SER 424
PRO 422 0.62 LEU 269 -0.25 SER 424
PRO 422 0.54 ALA 270 -0.26 SER 424
PRO 422 0.59 GLY 271 -0.29 SER 424
PRO 422 0.56 PRO 272 -0.28 SER 424
PRO 422 0.65 LEU 273 -0.29 SER 424
PRO 422 0.68 HIS 274 -0.26 SER 424
PRO 422 0.60 GLY 275 -0.22 SER 424
PRO 422 0.54 LEU 276 -0.23 SER 424
PRO 422 0.55 ALA 277 -0.22 SER 424
PRO 422 0.50 ASN 278 -0.19 SER 424
PRO 422 0.46 GLN 279 -0.20 SER 424
PRO 422 0.46 GLU 280 -0.21 SER 424
PRO 422 0.46 VAL 281 -0.19 SER 424
PRO 422 0.42 LEU 282 -0.18 SER 424
PRO 422 0.40 LEU 283 -0.19 SER 424
PRO 422 0.41 TRP 284 -0.19 SER 424
PRO 422 0.40 LEU 285 -0.17 SER 424
PRO 422 0.36 SER 286 -0.16 SER 424
PRO 422 0.35 GLN 287 -0.17 SER 424
PRO 422 0.36 LEU 288 -0.17 SER 426
PRO 422 0.34 GLN 289 -0.15 SER 426
PRO 422 0.32 LYS 290 -0.15 SER 426
PRO 422 0.32 ASP 291 -0.16 SER 426
PRO 422 0.31 ASP 295 -0.13 SER 426
PRO 422 0.32 ALA 296 -0.14 SER 426
PRO 422 0.32 SER 297 -0.14 SER 426
PRO 422 0.34 ASP 298 -0.15 SER 426
PRO 422 0.33 GLU 299 -0.15 SER 426
PRO 422 0.33 LYS 300 -0.16 SER 426
PRO 422 0.36 LEU 301 -0.16 SER 426
PRO 422 0.36 ARG 302 -0.17 SER 426
PRO 422 0.34 ASP 303 -0.18 SER 426
PRO 422 0.36 TYR 304 -0.18 SER 426
PRO 422 0.39 ILE 305 -0.19 SER 426
PRO 422 0.37 TRP 306 -0.20 SER 426
PRO 422 0.36 ASN 307 -0.20 SER 426
PRO 422 0.39 THR 308 -0.22 SER 426
PRO 422 0.41 LEU 309 -0.23 SER 426
PRO 422 0.36 ASN 310 -0.23 SER 426
PRO 422 0.36 SER 311 -0.24 SER 426
PRO 422 0.39 GLY 312 -0.27 SER 426
PRO 422 0.43 ARG 313 -0.26 SER 426
PRO 422 0.48 VAL 314 -0.25 SER 426
PRO 422 0.48 VAL 315 -0.22 SER 426
PRO 422 0.51 PRO 316 -0.21 SER 426
PRO 422 0.54 GLY 317 -0.19 SER 424
PRO 422 0.55 TYR 318 -0.20 SER 426
PRO 422 0.60 GLY 319 -0.21 SER 426
PRO 422 0.69 HIS 320 -0.20 SER 426
PRO 422 0.80 ALA 321 -0.20 SER 426
PRO 422 0.77 VAL 322 -0.16 SER 426
PRO 422 0.66 LEU 323 -0.15 SER 426
LYS 423 0.64 ARG 324 -0.15 SER 426
LYS 423 0.56 LYS 325 -0.14 SER 426
PRO 422 0.52 THR 326 -0.14 SER 426
PRO 422 0.55 ASP 327 -0.14 SER 426
PRO 422 0.50 PRO 328 -0.12 SER 426
PRO 422 0.51 ARG 329 -0.12 SER 426
PRO 422 0.49 TYR 330 -0.13 SER 426
PRO 422 0.45 THR 331 -0.12 SER 426
PRO 422 0.44 CYS 332 -0.11 SER 426
PRO 422 0.44 GLN 333 -0.12 SER 426
PRO 422 0.42 ARG 334 -0.12 SER 426
PRO 422 0.39 GLU 335 -0.11 SER 426
PRO 422 0.38 PHE 336 -0.11 SER 426
PRO 422 0.38 ALA 337 -0.11 SER 426
PRO 422 0.36 LEU 338 -0.11 SER 426
PRO 422 0.34 LYS 339 -0.10 SER 426
PRO 422 0.34 HIS 340 -0.10 SER 426
PRO 422 0.34 LEU 341 -0.11 SER 426
PRO 422 0.34 PRO 342 -0.11 SER 426
PRO 422 0.33 SER 343 -0.11 SER 426
PRO 422 0.34 ASP 344 -0.12 SER 426
PRO 422 0.34 PRO 345 -0.13 SER 426
PRO 422 0.37 MET 346 -0.14 SER 426
PRO 422 0.38 PHE 347 -0.13 SER 426
PRO 422 0.36 LYS 348 -0.13 SER 426
PRO 422 0.37 LEU 349 -0.14 SER 426
PRO 422 0.41 VAL 350 -0.15 SER 426
PRO 422 0.40 ALA 351 -0.14 SER 426
PRO 422 0.38 GLN 352 -0.14 SER 426
PRO 422 0.41 LEU 353 -0.16 SER 426
PRO 422 0.43 TYR 354 -0.15 SER 426
PRO 422 0.40 LYS 355 -0.15 SER 426
PRO 422 0.40 ILE 356 -0.16 SER 426
PRO 422 0.43 VAL 357 -0.18 SER 426
PRO 422 0.45 PRO 358 -0.17 SER 426
PRO 422 0.41 ASN 359 -0.17 SER 426
PRO 422 0.41 VAL 360 -0.19 SER 426
PRO 422 0.45 LEU 361 -0.20 SER 426
LYS 423 0.44 LEU 362 -0.18 SER 426
LYS 423 0.39 GLU 363 -0.19 SER 426
PRO 422 0.41 GLN 364 -0.21 SER 426
LYS 423 0.44 GLY 365 -0.21 SER 426
PRO 422 0.47 LYS 366 -0.24 SER 426
PRO 422 0.54 ALA 367 -0.23 SER 426
LYS 423 0.60 LYS 368 -0.20 SER 426
PRO 422 0.57 ASN 369 -0.18 SER 426
PRO 422 0.51 PRO 370 -0.18 SER 426
PRO 422 0.52 TRP 371 -0.17 SER 426
PRO 422 0.53 PRO 372 -0.17 SER 426
PRO 422 0.57 ASN 373 -0.16 SER 426
PRO 422 0.55 VAL 374 -0.15 SER 424
PRO 422 0.54 ASP 375 -0.18 SER 424
PRO 422 0.50 ALA 376 -0.17 SER 424
PRO 422 0.46 HIS 377 -0.15 SER 424
PRO 422 0.46 SER 378 -0.15 SER 424
PRO 422 0.43 GLY 379 -0.16 SER 424
PRO 422 0.40 VAL 380 -0.14 SER 424
PRO 422 0.39 LEU 381 -0.13 SER 424
PRO 422 0.38 LEU 382 -0.14 SER 424
PRO 422 0.36 GLN 383 -0.14 SER 424
PRO 422 0.35 TYR 384 -0.13 SER 424
PRO 422 0.33 TYR 385 -0.12 SER 424
PRO 422 0.32 GLY 386 -0.13 SER 424
PRO 422 0.35 MET 387 -0.14 SER 424
PRO 422 0.35 THR 388 -0.15 SER 424
PRO 422 0.35 GLU 389 -0.16 SER 424
PRO 422 0.39 MET 390 -0.18 SER 424
PRO 422 0.39 ASN 391 -0.19 SER 424
PRO 422 0.39 TYR 392 -0.18 SER 424
PRO 422 0.43 TYR 393 -0.18 SER 424
PRO 422 0.48 THR 394 -0.19 SER 424
PRO 422 0.43 VAL 395 -0.18 SER 424
PRO 422 0.43 LEU 396 -0.16 SER 424
PRO 422 0.50 PHE 397 -0.17 SER 424
PRO 422 0.49 GLY 398 -0.17 SER 424
PRO 422 0.43 VAL 399 -0.15 SER 424
PRO 422 0.46 SER 400 -0.14 SER 424
PRO 422 0.53 ARG 401 -0.15 SER 424
PRO 422 0.46 ALA 402 -0.13 SER 424
PRO 422 0.44 LEU 403 -0.11 SER 424
PRO 422 0.51 GLY 404 -0.11 SER 424
PRO 422 0.53 VAL 405 -0.12 SER 424
PRO 422 0.41 LEU 406 -0.09 SER 424
PRO 422 0.40 ALA 407 -0.08 VAL 33
PRO 422 0.44 GLN 408 -0.09 VAL 33
PRO 422 0.38 LEU 409 -0.08 VAL 33
PRO 422 0.27 ILE 410 -0.09 VAL 33
PRO 422 0.29 TRP 411 -0.12 VAL 33
PRO 422 0.28 SER 412 -0.11 VAL 33
PRO 422 0.15 ARG 413 -0.10 VAL 33
LYS 423 0.19 ALA 414 -0.12 VAL 33
LYS 423 0.26 LEU 415 -0.15 VAL 33
LYS 423 0.17 GLY 416 -0.12 VAL 33
LYS 423 0.25 PHE 417 -0.11 VAL 33
ASN 30 0.20 PRO 418 -0.09 VAL 33
ASN 30 0.25 LEU 419 -0.09 LYS 432
ASN 30 0.28 GLU 420 -0.13 LYS 432
ASN 30 0.50 ARG 421 -0.18 ALA 254
MET 45 1.20 PRO 422 -0.30 LYS 432
GLY 34 1.41 LYS 423 -0.25 ALA 159
ASN 30 0.44 SER 424 -0.29 GLY 271
ASN 30 0.34 MET 425 -0.25 GLY 44
ASN 30 0.27 SER 426 -0.27 GLY 44
ALA 32 0.19 THR 427 -0.20 LYS 366
ALA 32 0.20 ALA 428 -0.16 GLY 312
ALA 32 0.26 GLY 429 -0.24 PRO 422
ILE 36 0.22 LEU 430 -0.16 GLY 44
ALA 32 0.14 GLU 431 -0.11 GLY 44
ALA 32 0.19 LYS 432 -0.30 PRO 422

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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.