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***  close cutoff 10 melek  ***

CA distance fluctuations for 260522120726406031

---  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
PRO 422 0.25 ALA 1 -0.27 LYS 339
PRO 422 0.21 SER 2 -0.28 LYS 339
PRO 422 0.19 SER 3 -0.27 LYS 339
SER 424 0.18 THR 4 -0.26 LYS 339
SER 424 0.20 ASN 5 -0.23 LYS 339
GLY 312 0.22 LEU 6 -0.24 LYS 339
GLY 312 0.23 LYS 7 -0.21 LYS 339
PRO 422 0.26 ASP 8 -0.21 LYS 339
PRO 422 0.27 VAL 9 -0.23 LYS 339
PRO 422 0.31 LEU 10 -0.21 LYS 339
PRO 422 0.34 ALA 11 -0.23 LYS 166
PRO 422 0.37 SER 12 -0.19 LYS 339
PRO 422 0.41 LEU 13 -0.20 LYS 339
PRO 422 0.45 ILE 14 -0.18 LYS 339
PRO 422 0.49 PRO 15 -0.19 LYS 339
PRO 422 0.50 LYS 16 -0.22 LYS 339
PRO 422 0.54 GLU 17 -0.28 GLY 99
PRO 422 0.60 GLN 18 -0.22 GLY 99
PRO 422 0.61 ALA 19 -0.22 LYS 339
PRO 422 0.61 ARG 20 -0.27 GLY 68
PRO 422 0.70 ILE 21 -0.38 GLY 99
PRO 422 0.72 LYS 22 -0.25 GLY 68
PRO 422 0.64 THR 23 -0.30 GLY 68
PRO 422 0.66 PHE 24 -0.33 GLY 68
PRO 422 0.73 ARG 25 -0.49 GLU 54
PRO 422 0.65 GLN 26 -0.35 GLU 54
PRO 422 0.60 GLN 27 -0.44 GLY 50
PRO 422 0.66 HIS 28 -0.55 GLY 50
PRO 422 0.73 GLY 29 -0.91 ILE 52
PRO 422 0.60 ASN 30 -0.80 LEU 51
PRO 422 0.67 THR 31 -0.57 GLY 50
VAL 33 0.73 ALA 32 -0.77 GLY 50
PRO 422 0.94 VAL 33 -0.32 GLU 62
PRO 422 0.97 GLY 34 -0.51 ASP 61
PRO 422 1.04 GLN 35 -0.56 ASP 61
PRO 422 1.04 ILE 36 -0.44 ASP 61
LYS 423 0.81 THR 37 -0.46 ASP 61
GLY 312 0.74 VAL 38 -0.36 ASP 61
GLY 312 0.79 ASP 39 -0.43 ASP 61
GLY 312 0.78 MET 40 -0.44 PRO 60
GLY 312 0.81 SER 41 -0.46 ALA 32
GLY 312 0.89 TYR 42 -0.34 PRO 60
GLY 312 0.92 GLY 43 -0.37 PRO 60
GLY 312 0.91 GLY 44 -0.50 ASN 30
GLY 312 0.79 MET 45 -0.50 ALA 32
GLY 312 0.78 ARG 46 -0.50 PRO 60
GLY 312 0.66 GLY 47 -0.81 PRO 60
PRO 422 0.73 MET 48 -0.52 ASP 59
PRO 422 0.77 LYS 49 -0.44 ASP 59
PRO 422 1.01 GLY 50 -0.77 ALA 32
PRO 422 0.74 LEU 51 -0.80 ASN 30
PRO 422 0.65 ILE 52 -0.91 GLY 29
GLY 312 0.45 TYR 53 -0.70 GLY 29
PRO 422 0.40 GLU 54 -0.62 GLY 29
GLY 312 0.36 THR 55 -0.49 GLY 29
GLY 312 0.38 SER 56 -0.49 GLY 29
GLY 312 0.42 VAL 57 -0.51 GLY 29
GLY 312 0.45 LEU 58 -0.45 GLY 47
GLY 312 0.42 ASP 59 -0.71 GLY 47
GLY 312 0.47 PRO 60 -0.81 GLY 47
GLY 312 0.42 ASP 61 -0.63 GLY 47
GLY 312 0.37 GLU 62 -0.50 GLY 47
GLY 312 0.39 GLY 63 -0.43 GLY 47
GLY 312 0.38 ILE 64 -0.39 GLY 29
GLY 312 0.34 ARG 65 -0.40 GLY 29
GLY 312 0.31 PHE 66 -0.39 GLY 29
GLY 312 0.30 ARG 67 -0.39 GLY 29
GLY 312 0.31 GLY 68 -0.38 GLY 29
GLY 312 0.27 PHE 69 -0.33 GLY 29
GLY 312 0.26 SER 70 -0.37 LYS 355
GLY 312 0.23 ILE 71 -0.36 LYS 355
GLY 312 0.18 PRO 72 -0.48 LYS 355
GLY 312 0.18 GLU 73 -0.42 LYS 355
GLY 312 0.17 CYS 74 -0.40 GLU 335
PRO 72 0.15 GLN 75 -0.53 GLU 335
GLY 312 0.09 LYS 76 -0.54 LYS 339
GLY 312 0.13 LEU 77 -0.45 LYS 339
GLY 312 0.13 LEU 78 -0.47 LYS 339
GLY 312 0.09 PRO 79 -0.52 LYS 339
SER 210 0.09 LYS 80 -0.60 LYS 339
HIS 211 0.09 ALA 81 -0.51 LYS 339
HIS 211 0.07 GLY 82 -0.52 LYS 339
HIS 211 0.13 GLY 84 -0.75 LYS 339
PRO 222 0.09 GLU 85 -1.04 LYS 339
PRO 72 0.11 GLU 86 -0.68 LYS 339
PRO 72 0.10 PRO 87 -0.51 LYS 339
GLY 312 0.11 LEU 88 -0.39 LYS 339
GLY 312 0.17 PRO 89 -0.28 LYS 339
GLY 312 0.17 GLU 90 -0.29 LYS 339
GLY 312 0.17 GLY 91 -0.34 LYS 339
GLY 312 0.21 LEU 92 -0.29 LYS 339
GLY 312 0.24 PHE 93 -0.30 GLY 29
GLY 312 0.22 TRP 94 -0.27 GLY 29
GLY 312 0.24 LEU 95 -0.30 GLY 29
GLY 312 0.28 LEU 96 -0.36 GLY 29
GLY 312 0.28 VAL 97 -0.33 GLY 29
GLY 312 0.26 THR 98 -0.29 ILE 21
GLY 312 0.27 GLY 99 -0.38 ILE 21
GLY 312 0.23 GLN 100 -0.31 ILE 21
GLY 312 0.19 ILE 101 -0.33 LYS 339
GLY 312 0.16 PRO 102 -0.35 LYS 339
GLY 312 0.12 THR 103 -0.39 LYS 339
SER 424 0.10 PRO 104 -0.41 LYS 339
SER 424 0.12 GLU 105 -0.36 LYS 339
GLY 312 0.14 GLN 106 -0.33 LYS 339
GLY 312 0.13 VAL 107 -0.34 LYS 339
SER 424 0.11 SER 108 -0.33 LYS 339
SER 424 0.14 TRP 109 -0.28 LYS 339
GLY 312 0.16 VAL 110 -0.26 LYS 339
GLY 312 0.12 SER 111 -0.26 LYS 339
GLY 312 0.11 LYS 112 -0.24 LYS 339
GLY 312 0.15 GLU 113 -0.21 LYS 339
GLY 312 0.16 TRP 114 -0.21 GLY 29
GLY 312 0.11 ALA 115 -0.19 GLY 29
SER 426 0.13 LYS 116 -0.19 ASN 30
GLY 312 0.16 ARG 117 -0.21 ASN 30
TYR 304 0.15 ALA 118 -0.22 ASN 30
TYR 304 0.17 ALA 119 -0.22 ASN 30
TYR 304 0.21 LEU 120 -0.25 PRO 422
TYR 304 0.22 PRO 121 -0.25 PRO 422
TYR 304 0.23 SER 122 -0.30 PRO 422
TYR 304 0.26 HIS 123 -0.35 PRO 422
TYR 304 0.27 VAL 124 -0.38 PRO 422
TYR 304 0.25 VAL 125 -0.39 PRO 422
LYS 300 0.28 THR 126 -0.42 PRO 422
TYR 304 0.31 MET 127 -0.49 PRO 422
TYR 304 0.31 LEU 128 -0.51 PRO 422
LYS 300 0.30 ASP 129 -0.50 PRO 422
LYS 300 0.34 ASN 130 -0.56 PRO 422
LYS 300 0.37 PHE 131 -0.64 PRO 422
LYS 300 0.41 PRO 132 -0.69 PRO 422
LYS 300 0.43 THR 133 -0.66 PRO 422
LYS 300 0.48 ASN 134 -0.76 PRO 422
TYR 304 0.46 LEU 135 -0.80 PRO 422
TYR 304 0.46 HIS 136 -0.76 PRO 422
TYR 304 0.39 PRO 137 -0.65 PRO 422
TYR 304 0.41 MET 138 -0.67 PRO 422
TYR 304 0.42 SER 139 -0.78 PRO 422
TYR 304 0.37 GLN 140 -0.65 PRO 422
TYR 304 0.34 LEU 141 -0.55 PRO 422
SER 311 0.38 SER 142 -0.59 PRO 422
SER 311 0.36 ALA 143 -0.61 PRO 422
TYR 304 0.32 ALA 144 -0.49 PRO 422
SER 311 0.32 ILE 145 -0.39 PRO 422
SER 311 0.36 THR 146 -0.40 PRO 422
SER 311 0.32 ALA 147 -0.38 PRO 422
SER 311 0.28 LEU 148 -0.29 ASN 30
SER 311 0.32 ASN 149 -0.31 ASN 30
SER 311 0.29 SER 150 -0.28 ASN 30
SER 311 0.26 GLU 151 -0.26 ASN 30
GLY 312 0.29 SER 152 -0.28 ASN 30
GLY 312 0.28 ASN 153 -0.25 ASN 30
GLY 312 0.32 PHE 154 -0.28 ASN 30
GLY 312 0.35 ALA 155 -0.29 ASN 30
GLY 312 0.31 ARG 156 -0.24 ASN 30
SER 426 0.33 ALA 157 -0.19 ASN 30
GLY 161 0.41 TYR 158 -0.23 ASN 30
SER 426 0.42 ALA 159 -0.17 ASN 30
SER 426 0.40 GLU 160 -0.12 ASP 8
SER 424 0.47 GLY 161 -0.11 ASP 8
PRO 422 0.44 ILE 162 -0.14 ASP 8
PRO 422 0.54 ASN 163 -0.14 SER 12
PRO 422 0.59 ARG 164 -0.11 ASN 30
PRO 422 0.53 THR 165 -0.18 ALA 11
PRO 422 0.42 LYS 166 -0.23 ALA 11
PRO 422 0.40 TYR 167 -0.23 ASN 30
PRO 422 0.35 TRP 168 -0.25 ASN 30
GLY 312 0.28 GLU 169 -0.20 ASN 30
GLY 312 0.29 PHE 170 -0.24 ASN 30
GLY 312 0.32 VAL 171 -0.30 ASN 30
GLY 312 0.28 TYR 172 -0.25 ASN 30
GLY 312 0.25 GLU 173 -0.24 ASN 30
GLY 312 0.28 ASP 174 -0.28 ASN 30
GLY 312 0.28 ALA 175 -0.29 ASN 30
GLY 312 0.23 MET 176 -0.25 ASN 30
GLY 312 0.22 ASP 177 -0.25 ASN 30
GLY 312 0.25 LEU 178 -0.28 ASN 30
GLY 312 0.22 ILE 179 -0.27 ASN 30
GLY 312 0.18 ALA 180 -0.24 ASN 30
TYR 304 0.19 LYS 181 -0.25 ASN 30
TYR 304 0.22 LEU 182 -0.27 PRO 422
TYR 304 0.19 PRO 183 -0.28 PRO 422
LYS 300 0.20 CYS 184 -0.30 PRO 422
TYR 304 0.25 VAL 185 -0.37 PRO 422
LYS 300 0.26 ALA 186 -0.41 PRO 422
LYS 300 0.23 ALA 187 -0.38 PRO 422
LYS 300 0.26 LYS 188 -0.42 PRO 422
LYS 300 0.31 ILE 189 -0.50 PRO 422
LYS 300 0.30 TYR 190 -0.47 PRO 422
LYS 300 0.28 ARG 191 -0.44 PRO 422
LYS 300 0.31 ASN 192 -0.50 PRO 422
LYS 300 0.36 LEU 193 -0.54 PRO 422
LYS 300 0.34 TYR 194 -0.50 PRO 422
LYS 300 0.29 ARG 195 -0.44 PRO 422
LYS 300 0.31 ALA 196 -0.46 PRO 422
LYS 300 0.28 GLY 197 -0.45 PRO 422
LYS 300 0.23 SER 198 -0.39 PRO 422
LYS 300 0.20 SER 199 -0.35 PRO 422
LYS 300 0.18 ILE 200 -0.32 PRO 422
LYS 300 0.14 GLY 201 -0.27 PRO 422
LYS 300 0.12 ALA 202 -0.22 PRO 422
LYS 300 0.10 ILE 203 -0.18 ASN 30
MET 425 0.08 ASP 204 -0.17 GLY 29
MET 425 0.09 SER 205 -0.20 LYS 339
MET 425 0.08 LYS 206 -0.23 LYS 339
MET 425 0.07 LEU 207 -0.25 LYS 339
MET 425 0.07 ASP 208 -0.28 LYS 339
GLY 312 0.10 TRP 209 -0.22 LYS 339
GLY 84 0.11 SER 210 -0.23 GLY 29
GLY 84 0.13 HIS 211 -0.21 GLY 29
GLY 84 0.09 ASN 212 -0.20 GLY 29
LYS 300 0.14 PHE 213 -0.25 PRO 422
LYS 300 0.12 THR 214 -0.27 PRO 422
LYS 300 0.11 ASN 215 -0.26 PRO 422
LYS 300 0.16 MET 216 -0.29 PRO 422
LYS 300 0.19 LEU 217 -0.33 PRO 422
LYS 300 0.16 GLY 218 -0.32 PRO 422
LYS 300 0.13 TYR 219 -0.28 PRO 422
PRO 72 0.10 THR 220 -0.24 PRO 422
CYS 332 0.11 ASP 221 -0.21 PRO 422
PRO 72 0.12 PRO 222 -0.25 LEU 341
CYS 332 0.16 GLN 223 -0.29 LEU 341
CYS 332 0.13 PHE 224 -0.21 PRO 422
PRO 72 0.11 THR 225 -0.26 LEU 341
PRO 72 0.13 GLU 226 -0.42 LEU 341
CYS 332 0.18 LEU 227 -0.28 MET 228
PRO 72 0.11 MET 228 -0.28 LEU 227
PRO 72 0.12 ARG 229 -0.28 ALA 337
PRO 72 0.17 LEU 230 -0.28 ALA 337
GLY 312 0.14 TYR 231 -0.26 GLY 29
GLY 312 0.18 LEU 232 -0.27 GLY 29
GLY 312 0.19 THR 233 -0.29 GLY 29
GLY 312 0.23 ILE 234 -0.31 GLY 29
GLY 312 0.29 HIS 235 -0.31 GLY 29
GLY 312 0.30 SER 236 -0.34 GLY 29
GLY 312 0.37 ASP 237 -0.39 GLY 29
GLY 312 0.43 HIS 238 -0.41 GLY 29
GLY 312 0.46 GLU 239 -0.49 GLY 29
GLY 312 0.50 GLY 240 -0.51 GLY 29
GLY 312 0.58 GLY 241 -0.50 ASN 30
GLY 312 0.59 ASN 242 -0.41 ASN 30
ARG 313 0.61 VAL 243 -0.40 ASN 30
ARG 313 0.52 SER 244 -0.40 ASN 30
GLY 312 0.49 ALA 245 -0.45 ASN 30
GLY 312 0.55 HIS 246 -0.52 ASN 30
GLY 312 0.55 THR 247 -0.48 ASN 30
GLY 312 0.47 SER 248 -0.47 ASN 30
GLY 312 0.48 HIS 249 -0.55 ASN 30
GLY 312 0.53 LEU 250 -0.56 ASN 30
GLY 312 0.50 VAL 251 -0.49 ASN 30
GLY 312 0.44 GLY 252 -0.49 ASN 30
PRO 422 0.51 SER 253 -0.58 ASN 30
GLY 312 0.47 ALA 254 -0.49 ASN 30
GLY 312 0.43 LEU 255 -0.43 ASN 30
GLY 312 0.43 SER 256 -0.41 ASN 30
GLY 312 0.38 ASP 257 -0.36 ASN 30
GLY 312 0.36 PRO 258 -0.36 ASN 30
GLY 312 0.34 TYR 259 -0.35 ASN 30
SER 311 0.40 LEU 260 -0.38 ASN 30
GLY 312 0.43 SER 261 -0.42 ASN 30
ARG 313 0.39 PHE 262 -0.38 ASN 30
SER 311 0.40 ALA 263 -0.43 PRO 422
ARG 313 0.47 ALA 264 -0.47 PRO 422
ARG 313 0.48 ALA 265 -0.40 PRO 422
ARG 313 0.44 MET 266 -0.55 PRO 422
ARG 313 0.51 ASN 267 -0.77 PRO 422
ARG 313 0.58 GLY 268 -0.63 PRO 422
ARG 313 0.51 LEU 269 -0.56 PRO 422
ARG 313 0.51 ALA 270 -0.71 PRO 422
ARG 313 0.67 GLY 271 -0.76 PRO 422
ARG 313 0.73 PRO 272 -0.64 PRO 422
ARG 313 0.78 LEU 273 -0.49 PRO 422
ARG 313 0.66 HIS 274 -0.48 PRO 422
ARG 313 0.49 GLY 275 -0.46 PRO 422
TYR 304 0.50 LEU 276 -0.55 PRO 422
TYR 304 0.53 ALA 277 -0.44 PRO 422
TYR 304 0.43 ASN 278 -0.40 PRO 422
TYR 304 0.48 GLN 279 -0.45 PRO 422
TYR 304 0.59 GLU 280 -0.42 PRO 422
TYR 304 0.57 VAL 281 -0.34 PRO 422
LYS 300 0.52 LEU 282 -0.35 PRO 422
LYS 300 0.55 LEU 283 -0.33 PRO 422
TYR 304 0.69 TRP 284 -0.29 PRO 422
LYS 300 0.61 LEU 285 -0.36 VAL 315
LYS 300 0.53 SER 286 -0.42 ARG 313
LYS 300 0.56 GLN 287 -0.65 ARG 313
LYS 300 0.66 LEU 288 -0.58 THR 308
LYS 300 0.50 GLN 289 -0.73 THR 308
LYS 300 0.48 LYS 290 -0.68 THR 308
LYS 300 0.59 ASP 291 -0.79 THR 308
SER 297 0.32 ASP 295 -0.40 THR 308
SER 297 0.64 ALA 296 -0.35 GLU 85
ALA 296 0.64 SER 297 -0.33 GLU 85
TRP 284 0.51 ASP 298 -0.34 GLU 85
TRP 284 0.54 GLU 299 -0.27 LYS 76
TRP 284 0.67 LYS 300 -0.17 GLU 85
TRP 284 0.62 LEU 301 -0.24 GLU 85
PRO 316 0.56 ARG 302 -0.21 GLU 85
PRO 316 0.55 ASP 303 -0.18 GLU 85
TRP 284 0.69 TYR 304 -0.29 ASP 295
PRO 316 0.64 ILE 305 -0.26 GLN 289
ASN 310 0.59 TRP 306 -0.30 GLN 289
GLY 44 0.60 ASN 307 -0.44 ASP 291
GLY 312 0.64 THR 308 -0.79 ASP 291
GLY 312 0.72 LEU 309 -0.50 GLN 287
GLY 44 0.69 ASN 310 -0.38 GLN 287
GLY 44 0.81 SER 311 -0.52 LYS 290
GLY 43 0.92 GLY 312 -0.35 GLN 287
GLY 44 0.85 ARG 313 -0.65 GLN 287
ARG 313 0.83 VAL 314 -0.42 GLN 287
PRO 316 0.72 VAL 315 -0.40 LEU 288
VAL 315 0.72 PRO 316 -0.31 PRO 422
TYR 304 0.50 GLY 317 -0.28 PRO 422
GLY 312 0.51 TYR 318 -0.17 PRO 422
GLY 312 0.60 GLY 319 -0.16 PRO 422
GLY 312 0.61 HIS 320 -0.17 ASN 30
GLY 312 0.64 ALA 321 -0.24 HIS 274
GLY 312 0.55 VAL 322 -0.27 HIS 274
GLY 312 0.52 LEU 323 -0.43 GLY 47
GLY 312 0.51 ARG 324 -0.42 GLY 47
GLY 312 0.43 LYS 325 -0.36 GLN 35
GLY 312 0.39 THR 326 -0.31 GLY 47
GLY 312 0.37 ASP 327 -0.30 GLY 47
GLY 312 0.29 PRO 328 -0.32 LYS 355
GLY 312 0.28 ARG 329 -0.31 GLY 29
GLY 312 0.26 TYR 330 -0.26 GLY 29
GLY 312 0.21 THR 331 -0.43 TYR 354
LEU 227 0.18 CYS 332 -0.36 LYS 355
GLY 312 0.15 GLN 333 -0.27 GLY 29
GLY 312 0.17 ARG 334 -0.43 GLU 85
THR 331 0.14 GLU 335 -0.53 GLN 75
TYR 385 0.19 PHE 336 -0.66 GLU 86
LEU 338 0.19 ALA 337 -0.64 GLU 85
ALA 337 0.19 LEU 338 -0.72 GLU 85
TYR 385 0.16 LYS 339 -1.04 GLU 85
TYR 385 0.22 HIS 340 -0.79 GLU 85
PRO 342 0.16 LEU 341 -0.62 GLU 85
ASN 134 0.17 PRO 342 -0.58 GLU 85
ASN 134 0.19 SER 343 -0.46 GLU 85
ASN 134 0.20 ASP 344 -0.41 GLU 85
ASN 134 0.25 PRO 345 -0.37 GLU 85
LYS 300 0.29 MET 346 -0.34 GLU 85
LYS 300 0.23 PHE 347 -0.41 GLU 85
ASN 134 0.21 LYS 348 -0.42 GLU 85
LYS 300 0.35 LEU 349 -0.38 GLU 85
GLN 352 0.36 VAL 350 -0.31 GLU 85
VAL 350 0.27 ALA 351 -0.42 GLU 85
TRP 284 0.37 GLN 352 -0.45 LYS 76
PRO 316 0.42 LEU 353 -0.32 LYS 76
GLY 312 0.34 TYR 354 -0.43 THR 331
GLY 312 0.41 LYS 355 -0.48 PRO 72
GLY 312 0.47 ILE 356 -0.32 LYS 76
GLY 312 0.49 VAL 357 -0.22 LYS 76
GLY 312 0.50 PRO 358 -0.23 GLN 35
GLY 312 0.52 ASN 359 -0.27 GLN 35
GLY 312 0.57 VAL 360 -0.17 GLU 85
GLY 312 0.61 LEU 361 -0.16 GLN 289
GLY 312 0.56 LEU 362 -0.24 GLU 431
GLY 312 0.54 GLU 363 -0.19 GLU 431
GLY 312 0.61 GLN 364 -0.23 GLN 287
GLY 312 0.61 GLY 365 -0.24 THR 427
GLY 312 0.72 LYS 366 -0.21 PRO 316
GLY 312 0.72 ALA 367 -0.22 THR 427
GLY 312 0.65 LYS 368 -0.35 THR 427
GLY 312 0.60 ASN 369 -0.26 THR 427
GLY 312 0.56 PRO 370 -0.20 GLU 431
GLY 312 0.47 TRP 371 -0.22 GLN 35
GLY 312 0.41 PRO 372 -0.22 GLY 29
GLY 312 0.41 ASN 373 -0.23 GLY 29
GLY 312 0.33 VAL 374 -0.26 GLY 29
TYR 304 0.37 ASP 375 -0.29 PRO 422
LYS 300 0.38 ALA 376 -0.25 PRO 422
LYS 300 0.29 HIS 377 -0.23 PRO 422
LYS 300 0.27 SER 378 -0.26 PRO 422
LYS 300 0.35 GLY 379 -0.31 PRO 422
LYS 300 0.30 VAL 380 -0.26 PRO 422
LYS 300 0.21 LEU 381 -0.26 GLU 226
LYS 300 0.23 LEU 382 -0.29 PRO 422
LYS 300 0.27 GLN 383 -0.31 PRO 422
LYS 300 0.19 TYR 384 -0.26 PRO 422
HIS 340 0.22 TYR 385 -0.26 PRO 422
TYR 194 0.23 GLY 386 -0.31 PRO 422
LYS 300 0.26 MET 387 -0.34 PRO 422
LYS 300 0.34 THR 388 -0.38 PRO 422
LYS 300 0.40 GLU 389 -0.44 PRO 422
LYS 300 0.43 MET 390 -0.45 PRO 422
LYS 300 0.43 ASN 391 -0.56 PRO 422
LYS 300 0.37 TYR 392 -0.51 PRO 422
LYS 300 0.36 TYR 393 -0.44 PRO 422
TYR 304 0.37 THR 394 -0.48 PRO 422
TYR 304 0.32 VAL 395 -0.47 PRO 422
TYR 304 0.26 LEU 396 -0.36 PRO 422
TYR 304 0.29 PHE 397 -0.34 PRO 422
ARG 313 0.31 GLY 398 -0.36 PRO 422
TYR 304 0.24 VAL 399 -0.29 PRO 422
GLY 312 0.25 SER 400 -0.30 GLY 29
GLY 312 0.33 ARG 401 -0.33 ASN 30
GLY 312 0.31 ALA 402 -0.33 ASN 30
GLY 312 0.29 LEU 403 -0.34 GLY 29
GLY 312 0.34 GLY 404 -0.39 GLY 29
GLY 312 0.38 VAL 405 -0.40 GLY 29
GLY 312 0.34 LEU 406 -0.36 GLY 29
GLY 312 0.32 ALA 407 -0.38 GLY 29
GLY 312 0.37 GLN 408 -0.46 GLY 29
GLY 312 0.38 LEU 409 -0.42 ASN 30
GLY 312 0.34 ILE 410 -0.35 GLY 29
PRO 422 0.41 TRP 411 -0.41 GLY 29
PRO 422 0.51 SER 412 -0.46 GLY 29
PRO 422 0.48 ARG 413 -0.36 ASN 30
PRO 422 0.48 ALA 414 -0.28 GLY 29
PRO 422 0.60 LEU 415 -0.32 GLY 29
PRO 422 0.66 GLY 416 -0.34 ASN 30
PRO 422 0.77 PHE 417 -0.54 ASN 30
PRO 422 0.82 PRO 418 -0.76 ASN 30
PRO 422 0.81 LEU 419 -0.72 ASN 30
PRO 422 0.91 GLU 420 -0.72 ASN 30
PRO 422 1.02 ARG 421 -0.24 ASN 30
ILE 36 1.04 PRO 422 -0.80 LEU 135
ILE 36 1.01 LYS 423 -0.44 LEU 135
ILE 36 0.78 SER 424 -0.17 ASN 134
LYS 423 0.74 MET 425 -0.20 LYS 368
SER 311 0.52 SER 426 -0.30 LYS 368
GLY 312 0.57 THR 427 -0.35 LYS 368
SER 311 0.50 ALA 428 -0.31 LYS 368
LYS 423 0.61 GLY 429 -0.26 LYS 368
LYS 423 0.64 LEU 430 -0.25 LYS 368
LYS 423 0.56 GLU 431 -0.30 LYS 368
LYS 423 0.60 LYS 432 -0.24 LYS 368

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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.