Should you encounter any unexpected behaviour,
please let us know.

* EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA distance fluctuations for 24021912332929451

--- normal mode 10 ---

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
GLY 38 0.53 PRO 1 -1.68 THR 166

GLY 38 0.45 LEU 2 -1.47 THR 166

LEU 39 0.59 ILE 3 -1.00 THR 166

LEU 39 0.29 ASN 4 -0.76 ALA 165

LEU 39 0.18 SER 5 -0.59 ALA 169

GLY 8 0.24 ARG 6 -0.69 ALA 169

ASP 68 0.29 THR 7 -0.45 ALA 169

PRO 40 0.33 GLY 8 -0.44 THR 166

ILE 3 0.24 SER 9 -0.32 ALA 169

ILE 3 0.21 ILE 10 -0.24 ALA 169

ARG 125 0.03 TYR 11 -0.24 VAL 13

VAL 71 0.07 ILE 12 -0.24 VAL 13

LYS 238 0.08 VAL 13 -0.40 ASN 4

CYS 236 0.12 LYS 14 -0.29 LEU 2

CYS 236 0.10 PRO 15 -0.39 LEU 2

MET 17 0.12 LYS 16 -0.37 PRO 1

LYS 16 0.12 MET 17 -0.28 LEU 2

THR 145 0.09 HIS 18 -0.26 PRO 1

HIS 332 0.08 GLY 19 -0.22 LEU 2

THR 7 0.09 PRO 20 -0.16 LEU 2

HIS 332 0.11 ALA 21 -0.11 LEU 2

GLY 233 0.12 GLU 22 -0.14 LEU 2

GLY 233 0.10 VAL 23 -0.14 LEU 2

THR 7 0.12 ALA 24 -0.09 PHE 25

GLY 233 0.16 PHE 25 -0.09 ALA 24

GLY 235 0.15 THR 26 -0.09 ILE 12

ILE 3 0.14 CYS 27 -0.11 HIS 173

ILE 3 0.19 GLU 28 -0.10 HIS 173

ILE 3 0.19 LEU 29 -0.09 HIS 173

ILE 3 0.23 PHE 30 -0.12 HIS 173

ILE 3 0.29 SER 31 -0.14 HIS 173

ILE 3 0.31 ARG 32 -0.12 HIS 173

ILE 3 0.34 VAL 33 -0.12 HIS 173

ILE 3 0.43 GLU 34 -0.15 HIS 173

ILE 3 0.42 ASP 35 -0.15 HIS 173

ILE 3 0.43 VAL 36 -0.12 HIS 173

ILE 3 0.53 LEU 37 -0.14 HIS 173

ILE 3 0.57 GLY 38 -0.17 HIS 173

ILE 3 0.59 LEU 39 -0.20 HIS 173

ILE 3 0.51 PRO 40 -0.23 HIS 173

ILE 3 0.39 GLN 41 -0.21 HIS 173

ILE 3 0.29 ASN 42 -0.22 HIS 173

ILE 3 0.37 THR 43 -0.23 HIS 173

ILE 3 0.24 MET 44 -0.18 ALA 169

ARG 69 0.09 LYS 45 -0.18 ALA 169

LYS 238 0.05 ILE 46 -0.19 LEU 2

LYS 238 0.05 GLY 47 -0.35 LEU 2

LYS 238 0.05 ILE 48 -0.35 LEU 2

THR 26 0.06 MET 49 -0.44 LEU 2

ALA 148 0.09 ASP 50 -0.43 PRO 1

THR 145 0.11 GLU 51 -0.46 PRO 1

THR 145 0.12 GLU 52 -0.39 PRO 1

THR 145 0.13 ARG 53 -0.37 PRO 1

ALA 148 0.10 ARG 54 -0.30 PRO 1

ALA 148 0.09 THR 55 -0.31 PRO 1

ALA 148 0.11 THR 56 -0.36 PRO 1

ALA 148 0.10 VAL 57 -0.31 PRO 1

ALA 148 0.08 ASN 58 -0.25 PRO 1

ALA 148 0.07 LEU 59 -0.28 LEU 2

THR 7 0.10 LYS 60 -0.22 LEU 2

THR 7 0.12 ALA 61 -0.17 LEU 2

THR 7 0.09 CYS 62 -0.20 LEU 2

THR 7 0.12 ILE 63 -0.19 LEU 2

THR 7 0.17 LYS 64 -0.11 LEU 2

THR 7 0.16 ALA 65 -0.08 ARG 125

THR 7 0.16 ALA 66 -0.10 HIS 173

THR 7 0.22 ALA 67 -0.13 ARG 125

THR 7 0.29 ASP 68 -0.17 ARG 125

THR 7 0.19 ARG 69 -0.16 HIS 173

THR 7 0.12 VAL 70 -0.17 LEU 2

ILE 12 0.07 VAL 71 -0.27 LEU 2

GLY 98 0.04 PHE 72 -0.43 LEU 2

GLY 98 0.04 ILE 73 -0.45 LEU 2

GLY 98 0.06 ASN 74 -0.56 LEU 2

ALA 148 0.10 THR 75 -0.57 PRO 1

THR 145 0.12 GLY 76 -0.59 PRO 1

THR 145 0.18 PHE 77 -0.59 PRO 1

THR 145 0.16 LEU 78 -0.61 PRO 1

THR 145 0.13 ASP 79 -0.53 PRO 1

THR 145 0.15 ARG 80 -0.49 PRO 1

THR 145 0.20 THR 81 -0.51 PRO 1

THR 145 0.16 GLY 82 -0.49 PRO 1

THR 145 0.15 ASP 83 -0.43 PRO 1

THR 145 0.18 GLU 84 -0.43 PRO 1

THR 145 0.19 ILE 85 -0.43 PRO 1

THR 145 0.15 HIS 86 -0.40 PRO 1

THR 145 0.14 THR 87 -0.36 PRO 1

THR 145 0.17 SER 88 -0.36 PRO 1

THR 145 0.17 MET 89 -0.37 PRO 1

THR 145 0.17 GLU 90 -0.34 PRO 1

THR 145 0.18 ALA 91 -0.35 PRO 1

THR 145 0.20 GLY 92 -0.37 PRO 1

THR 145 0.23 PRO 93 -0.40 PRO 1

THR 145 0.25 MET 94 -0.43 PRO 1

THR 145 0.30 VAL 95 -0.46 PRO 1

THR 145 0.31 ARG 96 -0.49 PRO 1

THR 145 0.31 LYS 97 -0.54 PRO 1

THR 145 0.40 GLY 98 -0.56 PRO 1

THR 145 0.41 THR 99 -0.53 PRO 1

THR 145 0.36 MET 100 -0.53 PRO 1

THR 145 0.43 LYS 101 -0.58 PRO 1

THR 145 0.44 SER 102 -0.54 PRO 1

THR 145 0.34 GLN 103 -0.50 PRO 1

ALA 148 0.29 PRO 104 -0.47 PRO 1

ALA 148 0.25 TRP 105 -0.46 PRO 1

ALA 148 0.29 ILE 106 -0.52 PRO 1

ALA 148 0.32 LEU 107 -0.53 PRO 1

ALA 148 0.22 ALA 108 -0.47 PRO 1

ALA 148 0.18 TYR 109 -0.48 PRO 1

ALA 148 0.20 GLU 110 -0.54 PRO 1

ALA 152 0.18 ASP 111 -0.50 PRO 1

ALA 152 0.11 HIS 112 -0.42 PRO 1

ALA 148 0.08 ASN 113 -0.44 PRO 1

ALA 152 0.07 VAL 114 -0.46 PRO 1

ALA 152 0.05 ASP 115 -0.39 PRO 1

THR 7 0.05 ALA 116 -0.32 LEU 2

THR 7 0.04 GLY 117 -0.35 LEU 2

THR 7 0.05 LEU 118 -0.33 LEU 2

THR 7 0.10 ALA 119 -0.25 LEU 2

THR 7 0.15 ALA 120 -0.20 LEU 2

THR 7 0.15 GLY 121 -0.20 LEU 2

THR 7 0.07 PHE 122 -0.30 LEU 2

SER 102 0.06 SER 123 -0.34 LEU 2

SER 102 0.06 GLY 124 -0.31 LEU 2

THR 7 0.07 ARG 125 -0.22 LEU 2

ILE 12 0.05 ALA 126 -0.34 LEU 2

GLY 98 0.06 GLN 127 -0.53 LEU 2

LYS 101 0.06 VAL 128 -0.57 LEU 2

GLY 98 0.07 GLY 129 -0.69 LEU 2

LYS 101 0.11 LYS 130 -0.73 PRO 1

GLY 98 0.10 GLY 131 -0.76 PRO 1

GLY 98 0.13 MET 132 -0.88 PRO 1

GLY 98 0.22 TRP 133 -0.97 PRO 1

GLY 98 0.14 THR 134 -0.88 PRO 1

GLY 98 0.21 MET 135 -0.94 PRO 1

GLY 98 0.14 THR 136 -1.02 PRO 1

GLY 98 0.17 GLU 137 -1.03 PRO 1

GLY 98 0.25 LEU 138 -1.03 PRO 1

GLY 98 0.26 MET 139 -1.19 PRO 1

GLY 98 0.31 ALA 140 -1.12 PRO 1

GLY 98 0.39 ASP 141 -1.03 PRO 1

GLY 98 0.33 MET 142 -1.10 PRO 1

GLY 98 0.30 VAL 143 -1.15 PRO 1

THR 99 0.39 GLU 144 -1.02 PRO 1

SER 102 0.44 THR 145 -0.95 PRO 1

LYS 101 0.34 LYS 146 -0.99 PRO 1

SER 102 0.33 ILE 147 -0.96 PRO 1

SER 102 0.38 ALA 148 -0.84 PRO 1

SER 102 0.25 GLN 149 -0.82 PRO 1

SER 102 0.21 PRO 150 -0.81 PRO 1

SER 102 0.24 ARG 151 -0.74 PRO 1

LEU 107 0.23 ALA 152 -0.66 PRO 1

LEU 107 0.13 GLY 153 -0.61 LEU 2

SER 102 0.12 ALA 154 -0.70 LEU 2

SER 102 0.10 SER 155 -0.75 LEU 2

SER 102 0.10 THR 156 -0.88 LEU 2

GLY 98 0.12 ALA 157 -0.95 LEU 2

GLY 98 0.10 TRP 158 -0.97 LEU 2

GLY 98 0.12 VAL 159 -1.12 PRO 1

GLY 98 0.09 PRO 160 -1.08 PRO 1

GLY 98 0.10 SER 161 -1.27 PRO 1

GLY 98 0.10 PRO 162 -1.49 PRO 1

GLY 98 0.14 THR 163 -1.64 PRO 1

GLY 98 0.17 ALA 164 -1.46 PRO 1

GLY 98 0.14 ALA 165 -1.48 PRO 1

GLY 98 0.16 THR 166 -1.68 PRO 1

GLY 98 0.20 LEU 167 -1.48 PRO 1

GLY 98 0.20 HIS 168 -1.30 PRO 1

SER 102 0.17 ALA 169 -1.35 LEU 2

SER 102 0.21 LEU 170 -1.23 PRO 1

SER 102 0.24 HIS 171 -1.08 PRO 1

SER 102 0.19 TYR 172 -1.03 LEU 2

SER 102 0.19 HIS 173 -1.00 LEU 2

SER 102 0.24 GLN 174 -0.94 PRO 1

SER 102 0.22 VAL 175 -0.83 PRO 1

SER 102 0.17 ASP 176 -0.71 LEU 2

SER 102 0.15 VAL 177 -0.68 LEU 2

SER 102 0.11 ALA 178 -0.53 LEU 2

SER 102 0.12 ALA 179 -0.51 LEU 2

LEU 107 0.13 VAL 180 -0.56 PRO 1

SER 102 0.08 GLN 181 -0.47 LEU 2

GLU 203 0.07 GLN 182 -0.39 PRO 1

GLU 203 0.07 GLY 183 -0.43 PRO 1

GLU 203 0.06 LEU 184 -0.43 PRO 1

GLU 203 0.04 ALA 185 -0.34 PRO 1

THR 7 0.07 GLY 186 -0.29 PRO 1

GLU 90 0.04 LYS 187 -0.36 PRO 1

GLN 174 0.05 ARG 188 -0.36 PRO 1

VAL 175 0.09 ARG 189 -0.42 PRO 1

ALA 148 0.11 ALA 190 -0.41 PRO 1

ALA 148 0.12 THR 191 -0.36 PRO 1

ALA 148 0.12 ILE 192 -0.33 PRO 1

ALA 148 0.14 GLU 193 -0.34 PRO 1

ALA 148 0.18 GLN 194 -0.39 PRO 1

ALA 148 0.17 LEU 195 -0.39 PRO 1

ALA 148 0.16 LEU 196 -0.36 PRO 1

ALA 148 0.20 THR 197 -0.39 PRO 1

THR 145 0.21 ILE 198 -0.40 PRO 1

THR 145 0.27 PRO 199 -0.43 PRO 1

THR 145 0.25 LEU 200 -0.41 PRO 1

THR 145 0.28 ALA 201 -0.42 PRO 1

GLU 144 0.29 LYS 202 -0.39 PRO 1

GLU 144 0.30 GLU 203 -0.39 PRO 1

GLU 144 0.27 LEU 204 -0.39 PRO 1

GLU 144 0.28 ALA 205 -0.39 PRO 1

GLU 144 0.29 TRP 206 -0.42 PRO 1

ASP 141 0.29 ALA 207 -0.41 PRO 1

ASP 141 0.25 PRO 208 -0.42 PRO 1

ASP 141 0.28 ASP 209 -0.44 PRO 1

ASP 141 0.31 GLU 210 -0.46 PRO 1

ASP 141 0.26 ILE 211 -0.45 PRO 1

ASP 141 0.24 ARG 212 -0.46 PRO 1

ASP 141 0.28 GLU 213 -0.49 PRO 1

ASP 141 0.27 GLU 214 -0.50 PRO 1

ASP 141 0.21 VAL 215 -0.49 PRO 1

ASP 141 0.19 ASP 216 -0.52 PRO 1

ASP 141 0.22 ASN 217 -0.55 PRO 1

ASP 141 0.19 ASN 218 -0.54 PRO 1

ASP 141 0.14 CYS 219 -0.53 PRO 1

ASP 141 0.11 GLN 220 -0.57 PRO 1

ASP 141 0.11 SER 221 -0.61 PRO 1

LEU 29 0.09 ILE 222 -0.56 PRO 1

LEU 29 0.09 LEU 223 -0.56 PRO 1

LEU 29 0.10 GLY 224 -0.62 PRO 1

LEU 29 0.12 TYR 225 -0.63 PRO 1

LEU 29 0.12 VAL 226 -0.57 PRO 1

LEU 29 0.12 VAL 227 -0.57 PRO 1

LEU 29 0.14 ARG 228 -0.62 PRO 1

LEU 29 0.15 TRP 229 -0.59 PRO 1

LEU 29 0.14 VAL 230 -0.52 PRO 1

LEU 29 0.14 ASP 231 -0.53 PRO 1

LEU 29 0.16 GLN 232 -0.59 PRO 1

LEU 29 0.18 GLY 233 -0.58 PRO 1

LEU 29 0.18 VAL 234 -0.68 PRO 1

LEU 29 0.17 GLY 235 -0.68 PRO 1

LEU 29 0.16 CYS 236 -0.77 PRO 1

LEU 29 0.14 SER 237 -0.78 PRO 1

LEU 29 0.13 LYS 238 -0.81 PRO 1

LEU 29 0.11 VAL 239 -0.73 PRO 1

LEU 29 0.10 PRO 240 -0.72 PRO 1

LEU 138 0.12 ASP 241 -0.68 PRO 1

LEU 138 0.13 ILE 242 -0.62 PRO 1

LEU 138 0.15 HIS 243 -0.65 PRO 1

THR 163 0.09 ASP 244 -0.69 PRO 1

GLU 137 0.16 VAL 245 -0.75 PRO 1

LEU 29 0.10 ALA 246 -0.81 PRO 1

LEU 29 0.10 LEU 247 -0.81 PRO 1

LEU 29 0.11 MET 248 -0.82 PRO 1

LEU 29 0.12 GLU 249 -0.73 PRO 1

LEU 29 0.14 ASP 250 -0.68 PRO 1

PHE 25 0.13 ARG 251 -0.60 PRO 1

PHE 25 0.11 ALA 252 -0.60 PRO 1

ASP 141 0.10 THR 253 -0.62 PRO 1

PHE 25 0.10 LEU 254 -0.57 PRO 1

THR 145 0.11 ARG 255 -0.52 PRO 1

THR 145 0.17 ILE 256 -0.53 PRO 1

ASP 141 0.16 SER 257 -0.53 PRO 1

THR 145 0.13 SER 258 -0.49 PRO 1

THR 145 0.16 GLN 259 -0.46 PRO 1

THR 145 0.20 LEU 260 -0.47 PRO 1

THR 145 0.18 LEU 261 -0.45 PRO 1

THR 145 0.16 ALA 262 -0.42 PRO 1

THR 145 0.18 ASN 263 -0.41 PRO 1

THR 145 0.20 TRP 264 -0.41 PRO 1

THR 145 0.17 LEU 265 -0.39 PRO 1

THR 145 0.16 ARG 266 -0.37 PRO 1

THR 145 0.18 HIS 267 -0.37 PRO 1

GLU 144 0.18 GLY 268 -0.37 PRO 1

GLU 144 0.21 VAL 269 -0.40 PRO 1

ASP 141 0.19 ILE 270 -0.41 PRO 1

ASP 141 0.16 THR 271 -0.39 PRO 1

ASP 141 0.13 SER 272 -0.39 PRO 1

ASP 141 0.13 ALA 273 -0.40 PRO 1

ASP 141 0.16 ASP 274 -0.42 PRO 1

ASP 141 0.14 VAL 275 -0.44 PRO 1

ASP 141 0.11 ARG 276 -0.43 PRO 1

ASP 141 0.13 ALA 277 -0.44 PRO 1

ASP 141 0.14 SER 278 -0.47 PRO 1

ASP 141 0.11 LEU 279 -0.48 PRO 1

ASP 141 0.09 GLU 280 -0.47 PRO 1

ASP 141 0.11 ARG 281 -0.49 PRO 1

ASP 141 0.10 MET 282 -0.53 PRO 1

LEU 29 0.08 ALA 283 -0.52 PRO 1

LEU 29 0.08 PRO 284 -0.53 PRO 1

LEU 29 0.08 LEU 285 -0.56 PRO 1

LEU 29 0.09 VAL 286 -0.59 PRO 1

LEU 29 0.10 ASP 287 -0.57 PRO 1

LEU 29 0.10 ARG 288 -0.58 PRO 1

LEU 29 0.10 GLN 289 -0.64 PRO 1

LEU 29 0.11 ASN 290 -0.64 PRO 1

LEU 29 0.11 ALA 291 -0.60 PRO 1

LEU 29 0.12 GLY 292 -0.65 PRO 1

LEU 29 0.13 ASP 293 -0.65 PRO 1

LEU 29 0.13 VAL 294 -0.59 PRO 1

LEU 29 0.14 ALA 295 -0.58 PRO 1

LEU 29 0.13 TYR 296 -0.58 PRO 1

LEU 29 0.11 ARG 297 -0.53 PRO 1

LEU 29 0.10 PRO 298 -0.52 PRO 1

LEU 29 0.09 MET 299 -0.50 PRO 1

LEU 29 0.08 ALA 300 -0.48 PRO 1

LEU 29 0.08 PRO 301 -0.45 PRO 1

LEU 29 0.07 ASN 302 -0.43 PRO 1

PHE 25 0.07 PHE 303 -0.44 PRO 1

PHE 25 0.07 ASP 304 -0.40 PRO 1

PHE 25 0.08 ASP 305 -0.41 PRO 1

PHE 25 0.09 SER 306 -0.45 PRO 1

PHE 25 0.10 ILE 307 -0.44 PRO 1

PHE 25 0.10 ALA 308 -0.49 PRO 1

PHE 25 0.08 PHE 309 -0.48 PRO 1

PHE 25 0.08 LEU 310 -0.44 PRO 1

PHE 25 0.09 ALA 311 -0.45 PRO 1

PHE 25 0.08 ALA 312 -0.48 PRO 1

ASP 141 0.08 GLN 313 -0.45 PRO 1

THR 145 0.08 GLU 314 -0.42 PRO 1

THR 145 0.08 LEU 315 -0.45 PRO 1

THR 145 0.11 ILE 316 -0.44 PRO 1

THR 145 0.11 LEU 317 -0.40 PRO 1

THR 145 0.10 SER 318 -0.38 PRO 1

THR 145 0.11 GLY 319 -0.41 PRO 1

THR 145 0.13 ALA 320 -0.37 PRO 1

THR 145 0.10 GLN 321 -0.34 PRO 1

THR 145 0.09 GLN 322 -0.36 PRO 1

LEU 196 0.08 PRO 323 -0.33 PRO 1

THR 145 0.10 ASN 324 -0.35 PRO 1

THR 145 0.11 GLY 325 -0.40 PRO 1

PHE 25 0.09 TYR 326 -0.43 PRO 1

PHE 25 0.11 THR 327 -0.46 PRO 1

PHE 25 0.14 GLU 328 -0.44 PRO 1

PHE 25 0.13 PRO 329 -0.38 PRO 1

PHE 25 0.11 ILE 330 -0.41 PRO 1

PHE 25 0.13 LEU 331 -0.46 PRO 1

PHE 25 0.15 HIS 332 -0.42 PRO 1

PHE 25 0.13 ARG 333 -0.38 PRO 1

PHE 25 0.12 ARG 334 -0.42 PRO 1

PHE 25 0.14 ARG 335 -0.44 PRO 1

PHE 25 0.14 ARG 336 -0.38 PRO 1

PHE 25 0.12 GLU 337 -0.38 PRO 1

PHE 25 0.12 PHE 338 -0.42 PRO 1

PHE 25 0.14 LYS 339 -0.41 PRO 1

PHE 25 0.13 ALA 340 -0.35 PRO 1

PHE 25 0.12 ARG 341 -0.37 PRO 1

LEU 29 0.12 ALA 342 -0.40 PRO 1

ARG 32 0.12 ALA 343 -0.36 PRO 1

PHE 25 0.12 GLU 344 -0.34 PRO 1

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).
Last modification: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 ***

CA distance fluctuations for 24021912332929451

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.

* EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *