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* SECYEG_ITASSER_HDS_HIS_31 *

CA distance fluctuations for 260811202712365370

--- normal mode 8 ---

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 increase ref largest decrease
PHE 407 0.02 MET 1 -0.19 LEU 422

ASP 254 0.02 ASN 2 -0.18 TRP 429

SER 253 0.02 VAL 3 -0.24 TRP 429

MET 335 0.02 GLY 4 -0.25 LYS 425

VAL 410 0.02 ALA 5 -0.14 LEU 422

MET 335 0.02 ARG 6 -0.15 LYS 425

MET 335 0.02 GLY 7 -0.21 LYS 425

GLU 331 0.02 ASN 8 -0.16 ALA 421

LYS 433 0.03 ALA 9 -0.07 SER 420

LYS 433 0.13 GLY 10 -0.02 GLY 417

LYS 433 0.06 LEU 11 -0.04 ARG 418

LYS 433 0.03 PHE 12 -0.05 ARG 418

LYS 433 0.11 TRP 13 -0.01 ARG 418

LYS 433 0.14 ARG 14 -0.01 VAL 414

LYS 433 0.07 PHE 15 -0.04 ARG 418

LYS 433 0.08 GLY 16 -0.03 ARG 418

LYS 433 0.14 PHE 17 -0.01 VAL 414

LYS 433 0.12 THR 18 -0.02 VAL 414

LYS 433 0.07 LEU 19 -0.03 ARG 418

LYS 433 0.11 LEU 20 -0.02 ARG 418

LYS 433 0.14 ALA 21 -0.01 VAL 414

LYS 433 0.10 LEU 22 -0.02 ARG 418

LYS 433 0.09 ILE 23 -0.02 ARG 418

LYS 433 0.13 VAL 24 -0.01 VAL 414

LYS 433 0.13 TYR 25 -0.01 VAL 414

LYS 433 0.09 ARG 26 -0.02 ARG 418

LYS 433 0.10 LEU 27 -0.01 ARG 418

LYS 433 0.13 GLY 28 -0.01 VAL 414

LYS 433 0.11 THR 29 -0.01 VAL 414

LYS 433 0.09 TYR 30 -0.01 ARG 418

LYS 433 0.11 ILE 31 -0.01 VAL 414

LYS 433 0.11 PRO 32 -0.01 VAL 414

LYS 433 0.13 ILE 33 -0.01 GLY 248

LYS 433 0.13 PRO 34 -0.01 GLY 248

LYS 433 0.12 GLY 35 -0.01 LYS 338

LYS 433 0.11 VAL 36 -0.01 VAL 414

LYS 433 0.08 ASN 37 -0.01 ARG 418

LYS 433 0.07 PRO 38 -0.01 ARG 418

LYS 433 0.05 SER 39 -0.02 ARG 418

LYS 433 0.06 VAL 40 -0.01 ARG 418

LYS 433 0.07 VAL 41 -0.01 ARG 418

LYS 433 0.05 GLU 42 -0.02 ARG 418

LYS 433 0.04 ASP 43 -0.02 SER 426

LYS 433 0.05 ILE 44 -0.02 ARG 418

LYS 433 0.05 ILE 45 -0.02 ARG 418

LYS 433 0.03 SER 46 -0.03 SER 426

LYS 433 0.04 SER 47 -0.03 SER 426

SER 420 0.04 HIS 48 -0.03 SER 426

LYS 433 0.05 ALA 49 -0.01 SER 426

LYS 433 0.06 THR 50 -0.02 ARG 418

LYS 433 0.04 GLY 51 -0.03 SER 426

LYS 433 0.06 VAL 52 -0.02 ARG 418

LYS 433 0.07 LEU 53 -0.01 ARG 418

LYS 433 0.05 GLY 54 -0.02 SER 426

LYS 433 0.06 ILE 55 -0.02 ARG 418

LYS 433 0.09 PHE 56 -0.01 VAL 414

LYS 433 0.07 ASN 57 -0.02 ARG 418

LYS 433 0.06 VAL 58 -0.02 ARG 418

LYS 433 0.08 PHE 59 -0.01 VAL 414

LYS 433 0.10 SER 60 -0.01 VAL 414

LYS 433 0.07 GLY 61 -0.02 ARG 418

LYS 433 0.06 GLY 62 -0.02 ARG 418

LYS 433 0.09 ALA 63 -0.01 VAL 414

LYS 433 0.09 LEU 64 -0.01 VAL 414

LYS 433 0.07 GLY 65 -0.02 ARG 418

LYS 433 0.07 ARG 66 -0.02 ARG 418

LYS 433 0.10 MET 67 -0.01 VAL 414

LYS 433 0.11 THR 68 -0.01 VAL 414

LYS 433 0.14 ILE 69 -0.01 GLY 248

LYS 433 0.14 PHE 70 -0.01 GLU 331

LYS 433 0.13 ALA 71 -0.01 GLU 331

LYS 433 0.14 LEU 72 -0.01 GLU 331

LYS 433 0.14 ASN 73 -0.01 GLU 331

LYS 433 0.16 VAL 74 -0.01 GLU 331

LYS 433 0.15 MET 75 -0.01 GLU 331

LYS 433 0.18 PRO 76 -0.01 GLU 331

LYS 433 0.19 TYR 77 -0.01 GLU 331

LYS 433 0.17 ILE 78 -0.01 GLU 331

LYS 433 0.18 VAL 79 -0.02 GLU 331

LYS 433 0.21 SER 80 -0.02 GLU 331

LYS 433 0.21 SER 81 -0.02 GLU 331

LYS 433 0.19 ILE 82 -0.02 GLU 331

LYS 433 0.21 ILE 83 -0.02 GLU 331

LYS 433 0.24 VAL 84 -0.02 GLU 331

LYS 433 0.22 GLN 85 -0.02 GLU 331

LYS 433 0.21 LEU 86 -0.02 GLU 331

LYS 433 0.23 LEU 87 -0.02 GLU 331

LYS 433 0.25 SER 88 -0.03 GLU 331

LYS 433 0.22 VAL 89 -0.03 LYS 330

LYS 433 0.22 ALA 90 -0.02 LYS 330

LYS 433 0.25 ILE 91 -0.03 GLU 334

LYS 433 0.27 PRO 92 -0.03 GLU 334

LYS 433 0.29 THR 93 -0.03 GLU 334

LYS 433 0.28 LEU 94 -0.03 GLU 331

LYS 433 0.28 ASN 95 -0.04 GLU 331

LYS 433 0.31 GLU 96 -0.04 GLU 334

LYS 433 0.33 MET 97 -0.03 GLU 334

LYS 433 0.32 ARG 98 -0.04 GLU 331

LYS 433 0.33 GLN 99 -0.05 GLU 331

LYS 433 0.37 ASP 100 -0.04 LYS 338

LYS 433 0.38 GLY 101 -0.04 MET 335

LYS 433 0.41 GLU 102 -0.04 MET 335

LYS 433 0.41 LEU 103 -0.03 LYS 338

LYS 433 0.36 GLY 104 -0.03 MET 335

LYS 433 0.35 ARG 105 -0.03 MET 335

LYS 433 0.37 MET 106 -0.03 MET 335

LYS 433 0.35 LYS 107 -0.03 LYS 338

LYS 433 0.31 MET 108 -0.03 GLU 331

LYS 433 0.31 SER 109 -0.03 MET 335

LYS 433 0.32 THR 110 -0.02 MET 335

LYS 433 0.30 TYR 111 -0.02 MET 335

LYS 433 0.27 THR 112 -0.02 GLU 331

LYS 433 0.27 ARG 113 -0.02 MET 335

LYS 433 0.27 TYR 114 -0.02 LYS 338

LYS 433 0.25 LEU 115 -0.02 GLU 331

LYS 433 0.23 SER 116 -0.02 GLU 331

LYS 433 0.23 VAL 117 -0.02 LYS 338

LYS 433 0.23 ALA 118 -0.02 LYS 338

LYS 433 0.20 PHE 119 -0.02 GLU 331

LYS 433 0.19 CYS 120 -0.01 GLU 331

LYS 433 0.20 ILE 121 -0.01 LYS 338

LYS 433 0.19 ALA 122 -0.01 GLU 331

LYS 433 0.17 GLN 123 -0.01 GLU 331

LYS 433 0.17 GLY 124 -0.01 GLU 331

LYS 433 0.17 LEU 125 -0.01 LYS 338

LYS 433 0.16 VAL 126 -0.01 GLU 331

LYS 433 0.14 ILE 127 -0.01 GLU 331

LYS 433 0.14 LEU 128 -0.01 LYS 338

LYS 433 0.15 LEU 129 -0.01 LYS 338

LYS 433 0.13 GLY 130 -0.01 GLU 331

LYS 433 0.12 LEU 131 -0.01 GLU 331

LYS 433 0.12 GLU 132 -0.01 GLU 331

LYS 433 0.12 ARG 133 -0.01 LYS 338

LYS 433 0.11 MET 134 -0.01 GLU 331

LYS 433 0.10 ASN 135 -0.01 GLU 331

LYS 433 0.11 SER 136 -0.01 LYS 338

LYS 433 0.10 ASP 137 -0.01 LYS 338

LYS 433 0.09 GLU 138 -0.01 VAL 414

LYS 433 0.07 VAL 139 -0.01 ARG 418

LYS 433 0.08 MET 140 -0.01 VAL 414

LYS 433 0.10 VAL 141 -0.01 VAL 414

LYS 433 0.10 VAL 142 -0.01 LYS 338

LYS 433 0.12 ILE 143 -0.01 LYS 338

LYS 433 0.13 ASN 144 -0.01 LYS 338

LYS 433 0.14 PRO 145 -0.01 LYS 338

LYS 433 0.15 GLY 146 -0.01 LYS 338

LYS 433 0.17 ILE 147 -0.01 LYS 338

LYS 433 0.17 MET 148 -0.01 GLY 248

LYS 433 0.16 PHE 149 -0.01 LYS 338

LYS 433 0.16 ARG 150 -0.01 LYS 338

LYS 433 0.18 VAL 151 -0.01 LYS 338

LYS 433 0.18 VAL 152 -0.01 GLY 248

LYS 433 0.16 GLY 153 -0.01 LYS 338

LYS 433 0.18 ILE 154 -0.01 LYS 338

LYS 433 0.20 SER 155 -0.01 GLY 248

LYS 433 0.18 SER 156 -0.01 GLY 248

LYS 433 0.18 LEU 157 -0.01 LYS 338

LYS 433 0.21 LEU 158 -0.01 LYS 338

LYS 433 0.21 ALA 159 -0.01 GLY 248

LYS 433 0.18 GLY 160 -0.01 GLY 248

LYS 433 0.20 THR 161 -0.01 MET 335

LYS 433 0.23 MET 162 -0.01 GLY 248

LYS 433 0.21 PHE 163 -0.01 ASP 254

LYS 433 0.19 LEU 164 -0.01 ASP 254

LYS 433 0.23 LEU 165 -0.02 ASP 254

LYS 433 0.25 TRP 166 -0.02 ASP 254

LYS 433 0.21 LEU 167 -0.01 ASP 254

LYS 433 0.21 GLY 168 -0.01 ASP 254

LYS 433 0.26 GLU 169 -0.02 ASP 254

LYS 433 0.26 ARG 170 -0.02 SER 253

LYS 433 0.21 ILE 171 -0.02 SER 253

LYS 433 0.24 ASN 172 -0.02 ASP 254

LYS 433 0.29 ALA 173 -0.02 SER 253

LYS 433 0.27 LYS 174 -0.02 SER 253

LYS 433 0.19 GLY 175 -0.01 SER 253

LYS 433 0.18 ILE 176 -0.02 GLY 39

LYS 433 0.14 GLY 177 -0.02 VAL 414

LYS 433 0.17 ASN 178 -0.02 ASP 254

LYS 433 0.17 GLY 179 -0.01 ASP 254

LYS 433 0.15 ILE 180 -0.01 ASP 254

LYS 433 0.12 SER 181 -0.02 VAL 414

LYS 433 0.10 LEU 182 -0.02 VAL 414

LYS 433 0.11 ILE 183 -0.02 VAL 414

LYS 433 0.09 ILE 184 -0.02 VAL 414

LYS 433 0.05 PHE 185 -0.03 ARG 418

LYS 433 0.05 VAL 186 -0.04 ARG 418

LYS 433 0.05 GLY 187 -0.03 ARG 418

SER 420 0.03 ILE 188 -0.04 SER 426

SER 420 0.02 ILE 189 -0.07 SER 426

SER 420 0.02 SER 190 -0.06 SER 426

SER 420 0.02 GLU 191 -0.06 SER 426

PRO 41 0.01 LEU 192 -0.08 TRP 429

PRO 41 0.01 PRO 193 -0.10 TRP 429

PRO 41 0.01 SER 194 -0.08 TRP 429

PRO 41 0.01 SER 195 -0.09 TRP 429

PRO 41 0.01 ILE 196 -0.12 TRP 429

LEU 57 0.01 SER 197 -0.11 TRP 429

SER 88 0.01 SER 198 -0.10 TRP 429

TYR 68 0.01 VAL 199 -0.12 TRP 429

TYR 68 0.01 PHE 200 -0.13 TRP 429

TYR 68 0.01 LEU 201 -0.12 TRP 429

SER 39 0.01 LEU 202 -0.12 TRP 429

SER 39 0.01 GLY 203 -0.14 TRP 429

TYR 68 0.01 LYS 204 -0.14 TRP 429

SER 39 0.01 ASN 205 -0.13 TRP 429

ASP 43 0.01 GLY 206 -0.13 TRP 429

ASP 43 0.01 GLU 207 -0.12 TRP 429

ASP 43 0.01 VAL 208 -0.13 TRP 429

TYR 68 0.01 SER 209 -0.14 TRP 429

TYR 68 0.01 GLY 210 -0.16 TRP 429

PHE 238 0.01 LEU 211 -0.17 TRP 429

PHE 238 0.01 VAL 212 -0.15 TRP 429

PHE 238 0.01 VAL 213 -0.15 TRP 429

SER 253 0.01 LEU 214 -0.18 TRP 429

PHE 238 0.01 SER 215 -0.17 TRP 429

PHE 238 0.01 MET 216 -0.15 TRP 429

SER 253 0.01 LEU 217 -0.17 TRP 429

SER 253 0.01 LEU 218 -0.18 TRP 429

SER 233 0.01 ALA 219 -0.16 TRP 429

SER 233 0.01 PHE 220 -0.15 TRP 429

SER 253 0.01 PHE 221 -0.18 TRP 429

SER 233 0.01 ALA 222 -0.18 TRP 429

SER 233 0.01 LEU 223 -0.15 TRP 429

SER 233 0.01 PHE 224 -0.15 TRP 429

SER 253 0.01 LEU 225 -0.19 TRP 429

SER 233 0.01 LEU 226 -0.17 TRP 429

SER 420 0.01 ILE 227 -0.13 TRP 429

SER 233 0.01 ILE 228 -0.16 TRP 429

SER 233 0.01 PHE 229 -0.18 TRP 429

SER 233 0.02 PHE 230 -0.14 TRP 429

SER 420 0.03 GLU 231 -0.11 SER 426

PRO 259 0.01 ARG 232 -0.15 SER 426

PHE 230 0.02 SER 233 -0.15 TRP 429

SER 420 0.03 TYR 234 -0.13 SER 426

SER 420 0.04 ARG 235 -0.11 LYS 430

SER 420 0.03 LYS 236 -0.12 LYS 430

SER 420 0.05 VAL 237 -0.09 LYS 430

SER 420 0.03 PHE 238 -0.11 LYS 430

SER 420 0.05 VAL 239 -0.07 LYS 430

SER 420 0.02 GLN 240 -0.09 LYS 430

SER 420 0.05 TYR 241 -0.03 LYS 430

SER 420 0.05 PRO 242 -0.03 GLY 101

SER 420 0.03 LYS 243 -0.03 LYS 430

MET 423 0.05 ARG 244 -0.03 GLY 101

MET 423 0.06 GLN 245 -0.03 GLY 101

SER 426 0.12 THR 246 -0.03 GLY 101

GLU 427 0.15 GLY 247 -0.03 GLY 101

GLU 427 0.21 GLY 248 -0.04 GLY 101

GLU 427 0.19 ARG 249 -0.04 GLY 101

MET 423 0.11 PHE 250 -0.03 GLY 101

LEU 422 0.08 TYR 251 -0.03 GLY 101

TYR 419 0.06 ASN 252 -0.03 GLY 101

ARG 418 0.05 SER 253 -0.04 LEU 35

TYR 419 0.09 ASP 254 -0.04 LEU 35

SER 420 0.06 SER 255 -0.06 LYS 430

SER 420 0.04 SER 256 -0.09 LYS 430

SER 420 0.04 TYR 257 -0.09 LYS 430

SER 420 0.09 ILE 258 -0.04 LYS 430

SER 420 0.07 PRO 259 -0.07 SER 426

SER 420 0.09 LEU 260 -0.05 SER 426

SER 420 0.08 LYS 261 -0.06 SER 426

SER 420 0.08 ILE 262 -0.06 SER 426

SER 420 0.09 ASN 263 -0.04 SER 426

SER 420 0.12 THR 264 -0.02 GLY 36

SER 420 0.10 ALA 265 -0.02 SER 426

SER 420 0.12 GLY 266 -0.01 VAL 414

SER 420 0.10 VAL 267 -0.01 VAL 414

LYS 433 0.13 ILE 268 -0.01 ASP 254

LYS 433 0.12 PRO 269 -0.01 LEU 325

SER 420 0.09 PRO 270 -0.01 VAL 414

LYS 433 0.11 ILE 271 -0.01 VAL 414

LYS 433 0.13 PHE 272 -0.01 LEU 325

LYS 433 0.11 ALA 273 -0.01 LEU 325

LYS 433 0.09 ASN 274 -0.01 VAL 414

LYS 433 0.12 ALA 275 -0.01 GLU 331

LYS 433 0.13 LEU 276 -0.01 LYS 330

LYS 433 0.10 LEU 277 -0.01 LYS 330

LYS 433 0.10 LEU 278 -0.01 LYS 330

LYS 433 0.12 SER 279 -0.01 GLU 331

LYS 433 0.11 SER 280 -0.01 LYS 330

LYS 433 0.10 ILE 281 -0.01 LYS 330

LYS 433 0.11 SER 282 -0.01 GLU 331

LYS 433 0.12 LEU 283 -0.01 GLU 331

LYS 433 0.10 VAL 284 -0.01 LYS 330

LYS 433 0.10 ARG 285 -0.01 GLU 331

LYS 433 0.12 PHE 286 -0.01 GLU 331

LYS 433 0.11 HIS 287 -0.01 GLU 331

LYS 433 0.09 SER 288 -0.01 VAL 414

LYS 433 0.09 GLY 289 -0.01 VAL 414

LYS 433 0.08 SER 290 -0.01 VAL 414

LYS 433 0.08 GLU 291 -0.01 VAL 414

LYS 433 0.09 TRP 292 -0.01 LYS 330

LYS 433 0.09 ALA 293 -0.01 LYS 330

LYS 433 0.08 ASP 294 -0.01 VAL 414

LYS 433 0.07 VAL 295 -0.01 VAL 414

LYS 433 0.08 LEU 296 -0.01 VAL 414

LYS 433 0.07 LEU 297 -0.01 VAL 414

LYS 433 0.05 ARG 298 -0.02 SER 426

LYS 433 0.05 TYR 299 -0.02 SER 426

LYS 433 0.06 LEU 300 -0.01 SER 426

SER 420 0.05 SER 301 -0.02 SER 426

SER 420 0.05 SER 302 -0.03 SER 426

SER 420 0.04 GLU 303 -0.05 TRP 429

SER 420 0.04 GLY 304 -0.04 TRP 429

SER 420 0.04 ILE 305 -0.05 TRP 429

SER 420 0.05 LEU 306 -0.03 TRP 429

SER 420 0.06 TYR 307 -0.02 SER 426

SER 420 0.05 VAL 308 -0.04 TRP 429

SER 420 0.06 SER 309 -0.04 TRP 429

SER 420 0.07 VAL 310 -0.02 SER 426

SER 420 0.07 TYR 311 -0.02 SER 426

SER 420 0.06 ILE 312 -0.03 SER 426

SER 420 0.07 ALA 313 -0.02 SER 426

SER 420 0.09 LEU 314 -0.01 LYS 330

SER 420 0.08 ILE 315 -0.01 VAL 414

SER 420 0.08 MET 316 -0.02 SER 426

SER 420 0.10 PHE 317 -0.01 LYS 330

SER 420 0.11 PHE 318 -0.01 LYS 330

SER 420 0.11 THR 319 -0.01 LYS 330

SER 420 0.11 PHE 320 -0.01 LYS 330

SER 420 0.13 PHE 321 -0.01 LYS 330

SER 420 0.14 TYR 322 -0.01 LEU 325

SER 420 0.13 THR 323 -0.01 ARG 98

SER 420 0.14 SER 324 -0.01 THR 329

LYS 424 0.17 LEU 325 -0.02 GLN 85

SER 420 0.18 VAL 326 -0.02 ARG 98

SER 420 0.17 PHE 327 -0.02 GLN 99

SER 420 0.20 ASP 328 -0.03 GLN 99

SER 420 0.18 THR 329 -0.03 GLN 99

LYS 424 0.21 LYS 330 -0.04 GLN 99

LYS 424 0.24 GLU 331 -0.05 GLN 99

SER 420 0.20 THR 332 -0.04 GLN 99

LYS 424 0.19 SER 333 -0.04 GLN 99

LYS 424 0.23 GLU 334 -0.04 GLN 99

LYS 424 0.24 MET 335 -0.04 GLY 101

LYS 424 0.18 LEU 336 -0.04 GLY 101

LYS 424 0.19 LYS 337 -0.04 GLN 99

GLU 427 0.25 LYS 338 -0.04 GLY 101

MET 423 0.20 ASN 339 -0.04 GLY 101

LYS 424 0.16 GLY 340 -0.03 GLY 101

SER 420 0.12 GLY 341 -0.03 GLY 101

SER 420 0.10 PHE 342 -0.03 GLY 101

SER 420 0.08 VAL 343 -0.02 GLY 101

SER 420 0.06 PRO 344 -0.04 LYS 430

SER 420 0.07 GLY 345 -0.03 LYS 430

SER 420 0.10 LYS 346 -0.02 GLN 99

SER 420 0.10 ARG 347 -0.02 GLN 99

LYS 424 0.13 PRO 348 -0.03 GLN 99

LYS 424 0.15 GLY 349 -0.03 GLN 99

LYS 424 0.14 LYS 350 -0.02 GLN 99

SER 420 0.12 ALA 351 -0.02 GLN 99

SER 420 0.12 THR 352 -0.02 GLN 99

SER 420 0.14 LYS 353 -0.02 GLN 99

SER 420 0.12 GLU 354 -0.02 GLN 99

SER 420 0.10 TYR 355 -0.02 GLN 99

SER 420 0.12 PHE 356 -0.02 GLN 99

SER 420 0.12 ASP 357 -0.02 GLN 99

SER 420 0.10 GLN 358 -0.01 GLN 99

SER 420 0.09 VAL 359 -0.02 TRP 429

SER 420 0.11 ILE 360 -0.01 GLN 99

SER 420 0.10 GLY 361 -0.01 GLN 99

SER 420 0.08 ARG 362 -0.04 TRP 429

SER 420 0.07 ILE 363 -0.05 TRP 429

SER 420 0.09 THR 364 -0.03 SER 426

SER 420 0.07 VAL 365 -0.04 TRP 429

SER 420 0.06 LEU 366 -0.07 TRP 429

SER 420 0.06 GLY 367 -0.06 TRP 429

SER 420 0.07 ALA 368 -0.04 TRP 429

SER 420 0.05 ILE 369 -0.07 TRP 429

SER 420 0.04 TYR 370 -0.09 TRP 429

SER 420 0.05 LEU 371 -0.07 TRP 429

SER 420 0.05 SER 372 -0.06 TRP 429

SER 420 0.04 VAL 373 -0.09 TRP 429

SER 420 0.03 VAL 374 -0.10 TRP 429

SER 420 0.04 CYS 375 -0.07 TRP 429

SER 420 0.03 VAL 376 -0.08 TRP 429

SER 420 0.02 VAL 377 -0.10 TRP 429

SER 420 0.02 PRO 378 -0.09 TRP 429

SER 420 0.03 GLU 379 -0.08 TRP 429

SER 420 0.02 ILE 380 -0.09 TRP 429

SER 420 0.01 VAL 381 -0.11 TRP 429

SER 420 0.02 ARG 382 -0.09 TRP 429

SER 420 0.02 HIS 383 -0.09 TRP 429

SER 420 0.01 TYR 384 -0.10 TRP 429

LEU 21 0.01 CYS 385 -0.11 TRP 429

SER 420 0.01 ALA 386 -0.10 TRP 429

SER 420 0.01 VAL 387 -0.10 TRP 429

SER 420 0.01 SER 388 -0.09 TRP 429

SER 420 0.02 PHE 389 -0.07 TRP 429

SER 420 0.02 THR 390 -0.07 TRP 429

SER 420 0.02 LEU 391 -0.09 TRP 429

SER 420 0.03 GLY 392 -0.07 TRP 429

SER 420 0.03 GLY 393 -0.07 TRP 429

SER 420 0.05 THR 394 -0.05 SER 426

SER 420 0.04 SER 395 -0.06 SER 426

SER 420 0.03 PHE 396 -0.08 TRP 429

SER 420 0.04 LEU 397 -0.07 SER 426

SER 420 0.05 ILE 398 -0.05 SER 426

SER 420 0.04 ILE 399 -0.07 SER 426

SER 420 0.03 VAL 400 -0.09 SER 426

SER 420 0.06 ASN 401 -0.06 SER 426

SER 420 0.06 VAL 402 -0.05 SER 426

SER 420 0.03 ILE 403 -0.09 SER 426

SER 420 0.04 ASN 404 -0.09 SER 426

SER 420 0.08 ASP 405 -0.04 SER 426

SER 420 0.05 THR 406 -0.05 ARG 418

MET 1 0.02 PHE 407 -0.11 SER 426

SER 420 0.06 SER 408 -0.07 SER 426

SER 420 0.10 GLN 409 -0.04 VAL 414

SER 420 0.03 VAL 410 -0.08 ARG 418

GLU 331 0.02 GLN 411 -0.12 ARG 418

GLY 417 0.12 THR 412 -0.04 VAL 414

GLY 417 0.16 GLN 413 -0.02 GLN 42

ASN 44 0.05 VAL 414 -0.11 ARG 418

GLY 417 0.08 TYR 415 -0.10 ARG 418

GLY 417 0.31 SER 416 -0.04 GLY 4

SER 416 0.31 GLY 417 -0.14 GLY 4

SER 47 0.17 ARG 418 -0.19 GLY 4

THR 34 0.17 TYR 419 -0.13 GLY 4

THR 34 0.31 SER 420 -0.14 GLY 4

SER 47 0.44 ALA 421 -0.22 GLY 4

SER 47 0.30 LEU 422 -0.24 GLY 4

SER 47 0.29 MET 423 -0.19 LYS 29

SER 47 0.43 LYS 424 -0.20 GLY 4

SER 47 0.42 LYS 425 -0.25 GLY 4

SER 47 0.31 SER 426 -0.29 LYS 29

SER 47 0.34 GLU 427 -0.23 LYS 29

SER 47 0.42 LEU 428 -0.23 LYS 29

GLY 50 0.35 TRP 429 -0.31 LYS 29

SER 54 0.33 LYS 430 -0.30 LYS 29

SER 54 0.39 LYS 431 -0.25 LYS 29

SER 53 0.42 VAL 432 -0.26 LYS 29

SER 53 0.50 LYS 433 -0.21 LYS 29

SER 420 0.07 MET 1 -0.01 ILE 380

SER 420 0.06 PHE 2 -0.02 TRP 429

SER 420 0.06 LEU 3 -0.02 TRP 429

SER 420 0.07 ALA 4 -0.01 TRP 429

SER 420 0.07 MET 5 -0.01 TRP 429

SER 420 0.06 ILE 6 -0.03 TRP 429

SER 420 0.06 GLY 7 -0.02 TRP 429

SER 420 0.07 SER 8 -0.01 TRP 429

SER 420 0.07 PHE 9 -0.03 TRP 429

SER 420 0.06 ALA 10 -0.04 TRP 429

SER 420 0.07 ARG 11 -0.03 TRP 429

SER 420 0.07 PHE 12 -0.03 TRP 429

SER 420 0.05 LEU 13 -0.06 TRP 429

SER 420 0.05 CYS 14 -0.06 TRP 429

SER 420 0.06 ASP 15 -0.05 TRP 429

SER 420 0.06 VAL 16 -0.06 TRP 429

SER 420 0.04 LYS 17 -0.09 TRP 429

SER 420 0.04 GLN 18 -0.09 TRP 429

SER 420 0.05 GLU 19 -0.08 TRP 429

SER 420 0.03 ALA 20 -0.11 TRP 429

SER 420 0.02 LEU 21 -0.13 LYS 430

SER 420 0.03 GLN 22 -0.12 LYS 430

SER 420 0.02 VAL 23 -0.13 TRP 429

TRP 25 0.02 SER 24 -0.16 LYS 430

SER 24 0.02 TRP 25 -0.18 TRP 429

SER 255 0.01 ALA 26 -0.20 TRP 429

SER 255 0.02 SER 27 -0.25 TRP 429

SER 253 0.02 ARG 28 -0.27 TRP 429

SER 253 0.02 LYS 29 -0.31 TRP 429

SER 255 0.02 GLU 30 -0.26 TRP 429

SER 255 0.01 VAL 31 -0.23 TRP 429

SER 253 0.01 SER 32 -0.26 TRP 429

SER 253 0.02 VAL 33 -0.27 TRP 429

SER 255 0.01 PHE 34 -0.20 TRP 429

SER 253 0.01 LEU 35 -0.20 TRP 429

SER 253 0.01 LEU 36 -0.23 TRP 429

SER 253 0.01 ILE 37 -0.19 TRP 429

SER 253 0.01 VAL 38 -0.15 TRP 429

SER 253 0.01 LEU 39 -0.17 TRP 429

SER 253 0.01 LEU 40 -0.18 TRP 429

PRO 41 0.01 THR 41 -0.13 TRP 429

PRO 41 0.01 VAL 42 -0.12 TRP 429

PRO 41 0.01 VAL 43 -0.14 TRP 429

PRO 41 0.01 VAL 44 -0.12 TRP 429

PRO 41 0.01 SER 45 -0.08 SER 426

PRO 41 0.01 SER 46 -0.10 TRP 429

PRO 41 0.01 ILE 47 -0.11 TRP 429

PRO 41 0.01 LEU 48 -0.07 SER 426

PRO 41 0.01 PHE 49 -0.06 SER 426

PRO 41 0.01 SER 50 -0.08 TRP 429

PRO 41 0.01 CYS 51 -0.07 SER 426

LYS 433 0.02 VAL 52 -0.04 SER 426

LYS 433 0.01 ASP 53 -0.05 SER 426

SER 194 0.01 PHE 54 -0.06 SER 426

LYS 433 0.02 VAL 55 -0.04 LEU 422

LYS 433 0.04 PHE 56 -0.03 ARG 418

LYS 433 0.01 LEU 57 -0.04 SER 426

LYS 433 0.01 ARG 58 -0.04 SER 426

LYS 433 0.04 LEU 59 -0.02 ARG 418

LYS 433 0.04 VAL 60 -0.02 ARG 418

LYS 433 0.02 LYS 61 -0.03 SER 426

LYS 433 0.03 ILE 62 -0.02 ARG 418

LYS 433 0.06 ALA 63 -0.02 ARG 418

LYS 433 0.04 LEU 64 -0.02 ARG 418

LYS 433 0.03 GLY 65 -0.02 LEU 422

LYS 433 0.05 VAL 66 -0.02 ARG 418

LYS 433 0.06 VAL 67 -0.02 ARG 418

LYS 433 0.04 TYR 68 -0.02 ARG 418

LYS 433 0.04 ALA 69 -0.02 ARG 418

LYS 433 0.06 ALA 70 -0.01 ARG 418

LYS 433 0.15 MET 1 -0.01 GLY 248

LYS 433 0.16 SER 2 -0.01 GLY 248

LYS 433 0.15 PHE 3 -0.01 GLY 248

LYS 433 0.16 VAL 4 -0.01 GLY 248

LYS 433 0.18 SER 5 -0.01 GLY 248

LYS 433 0.18 CYS 6 -0.01 GLY 248

LYS 433 0.17 LEU 7 -0.01 GLY 248

LYS 433 0.19 MET 8 -0.01 GLY 248

LYS 433 0.20 PHE 9 -0.01 GLY 248

LYS 433 0.19 LEU 10 -0.01 GLY 248

LYS 433 0.20 THR 11 -0.01 GLY 248

LYS 433 0.22 ALA 12 -0.01 GLY 248

LYS 433 0.23 ALA 13 -0.01 GLY 248

LYS 433 0.21 GLN 14 -0.01 GLY 248

LYS 433 0.23 VAL 15 -0.01 GLY 248

LYS 433 0.25 PHE 16 -0.01 GLY 248

LYS 433 0.25 LEU 17 -0.01 GLY 248

LYS 433 0.24 ALA 18 -0.01 GLY 248

LYS 433 0.26 PHE 19 -0.02 GLY 248

LYS 433 0.28 LEU 20 -0.02 GLY 248

LYS 433 0.26 LEU 21 -0.01 GLY 248

LYS 433 0.27 VAL 22 -0.02 GLY 248

LYS 433 0.30 LEU 23 -0.02 GLY 248

LYS 433 0.31 LEU 24 -0.02 GLY 248

LYS 433 0.28 VAL 25 -0.02 ASP 254

LYS 433 0.30 LEU 26 -0.02 ASP 254

LYS 433 0.35 LEU 27 -0.02 SER 253

LYS 433 0.33 GLN 28 -0.02 SER 253

LYS 433 0.31 SER 29 -0.02 ASP 254

LYS 433 0.30 PRO 30 -0.02 ASP 254

LYS 433 0.36 GLU 31 -0.03 ASP 254

LYS 433 0.35 SER 32 -0.03 ASP 254

LYS 433 0.38 ASP 33 -0.03 ASP 254

LYS 424 0.37 THR 34 -0.04 ASP 254

LYS 424 0.32 LEU 35 -0.04 ASP 254

LYS 433 0.26 GLY 36 -0.03 ASP 254

LYS 433 0.23 GLY 37 -0.03 ASP 254

LYS 424 0.23 PHE 38 -0.03 ASP 254

LYS 433 0.21 GLY 39 -0.03 ASP 254

LYS 433 0.19 GLY 40 -0.02 SER 253

LYS 433 0.20 PRO 41 -0.02 SER 253

ALA 421 0.22 GLN 42 -0.02 SER 253

LYS 433 0.21 CYS 43 -0.02 SER 253

LYS 433 0.12 ASN 44 -0.03 GLY 4

LYS 433 0.18 LEU 45 -0.01 SER 416

LYS 425 0.37 GLY 46 -0.01 SER 253

ALA 421 0.44 SER 47 -0.03 SER 253

LYS 433 0.41 MET 48 -0.03 SER 253

LYS 433 0.40 PHE 49 -0.02 SER 253

LYS 433 0.48 GLY 50 -0.02 SER 253

LYS 433 0.48 LYS 51 -0.02 SER 253

LYS 433 0.48 SER 52 -0.02 SER 253

LYS 433 0.50 SER 53 -0.02 SER 253

LYS 433 0.49 SER 54 -0.03 SER 253

LYS 433 0.42 SER 55 -0.02 SER 253

LYS 433 0.40 SER 56 -0.02 SER 253

LYS 433 0.39 PHE 57 -0.02 SER 253

LYS 433 0.36 ILE 58 -0.02 SER 253

LYS 433 0.33 ALA 59 -0.02 SER 253

LYS 433 0.31 LYS 60 -0.01 SER 253

LYS 433 0.31 LEU 61 -0.01 SER 253

LYS 433 0.28 THR 62 -0.01 SER 253

LYS 433 0.25 ALA 63 -0.01 SER 253

LYS 433 0.25 VAL 64 -0.01 GLY 248

LYS 433 0.25 VAL 65 -0.01 GLY 248

LYS 433 0.22 ALA 66 -0.01 GLY 248

LYS 433 0.20 ALA 67 -0.01 GLY 248

LYS 433 0.21 ALA 68 -0.01 GLY 248

LYS 433 0.20 PHE 69 -0.01 GLY 248

LYS 433 0.17 ILE 70 -0.01 GLY 248

LYS 433 0.17 VAL 71 -0.01 GLY 248

LYS 433 0.18 ASN 72 -0.01 GLY 248

LYS 433 0.16 THR 73 -0.01 GLY 248

LYS 433 0.14 ILE 74 -0.01 GLY 248

LYS 433 0.15 LEU 75 -0.01 GLY 248

LYS 433 0.15 LEU 76 -0.01 GLY 248

LYS 433 0.13 VAL 77 -0.01 GLY 248

LYS 433 0.12 GLY 78 -0.01 GLY 248

LYS 433 0.13 THR 79 -0.01 GLY 248

LYS 433 0.13 ASN 80 -0.01 GLY 248

LYS 433 0.11 ALA 81 -0.01 GLY 248

LYS 433 0.09 ARG 82 -0.01 VAL 414

LYS 433 0.09 ARG 83 -0.01 VAL 414

LYS 433 0.07 VAL 84 -0.01 ARG 418

LYS 433 0.08 ARG 85 -0.01 ARG 418

LYS 433 0.10 GLU 86 -0.01 VAL 414

LYS 433 0.08 VAL 87 -0.01 ARG 418

LYS 433 0.07 SER 88 -0.01 ARG 418

LYS 433 0.09 VAL 89 -0.01 ARG 418

LYS 433 0.10 VAL 90 -0.01 VAL 414

LYS 433 0.07 SER 91 -0.02 ARG 418

LYS 433 0.08 LYS 92 -0.02 ARG 418

LYS 433 0.10 THR 93 -0.01 VAL 414

LYS 433 0.09 GLU 94 -0.01 ARG 418

LYS 433 0.06 ALA 95 -0.02 ARG 418

LYS 433 0.08 VAL 96 -0.02 ARG 418

LYS 433 0.10 SER 97 -0.01 ARG 418

LYS 433 0.08 GLY 98 -0.02 ARG 418

LYS 433 0.06 GLN 99 -0.03 ARG 418

LYS 433 0.10 GLU 100 -0.02 ARG 418

LYS 433 0.11 SER 101 -0.01 ARG 418

LYS 433 0.14 ASN 102 -0.01 PHE 12

LYS 433 0.15 GLY 103 -0.01 SER 253

LYS 433 0.20 SER 104 -0.01 SER 253

LYS 433 0.20 GLU 105 -0.01 GLY 248

LYS 433 0.24 VAL 106 -0.01 GLY 248

LYS 433 0.26 PRO 107 -0.01 GLY 248

LYS 433 0.30 PHE 108 -0.01 GLY 248

LYS 433 0.31 GLU 109 -0.01 GLY 248

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

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.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** SECYEG_ITASSER_HDS_HIS_31 ***

CA distance fluctuations for 260811202712365370

--- normal mode 8 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* SECYEG_ITASSER_HDS_HIS_31 *