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 9 ---

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 124 0.43 PRO 1 -0.51 SER 161

GLY 124 0.50 LEU 2 -0.56 PRO 162

GLY 124 0.28 ILE 3 -0.40 PRO 162

ARG 125 0.28 ASN 4 -0.46 PRO 162

ARG 125 0.29 SER 5 -0.49 PRO 162

ASP 68 0.35 ARG 6 -0.53 PRO 162

ASP 68 0.30 THR 7 -0.41 THR 166

ALA 343 0.22 GLY 8 -0.30 PRO 162

ARG 336 0.24 SER 9 -0.27 PRO 162

ARG 336 0.26 ILE 10 -0.21 PRO 162

ARG 336 0.23 TYR 11 -0.21 PRO 162

HIS 332 0.26 ILE 12 -0.21 PRO 1

HIS 332 0.25 VAL 13 -0.21 PRO 1

GLU 328 0.27 LYS 14 -0.22 PRO 1

LYS 14 0.23 PRO 15 -0.23 PRO 1

LEU 29 0.20 LYS 16 -0.21 PRO 1

THR 26 0.19 MET 17 -0.18 PRO 1

PHE 25 0.17 HIS 18 -0.14 PRO 1

THR 87 0.11 GLY 19 -0.09 PRO 1

ARG 6 0.12 PRO 20 -0.08 LYS 14

PRO 323 0.16 ALA 21 -0.10 PRO 1

PRO 323 0.21 GLU 22 -0.15 PRO 1

PRO 329 0.21 VAL 23 -0.11 PRO 1

PRO 329 0.22 ALA 24 -0.12 PHE 25

PRO 329 0.32 PHE 25 -0.15 PRO 1

PRO 329 0.35 THR 26 -0.18 PRO 1

PRO 329 0.30 CYS 27 -0.11 PRO 1

PRO 329 0.34 GLU 28 -0.13 PRO 1

PRO 329 0.44 LEU 29 -0.21 PRO 1

PRO 329 0.39 PHE 30 -0.19 PRO 1

PRO 329 0.36 SER 31 -0.13 ARG 125

ARG 333 0.43 ARG 32 -0.19 PRO 1

ARG 336 0.47 VAL 33 -0.25 PRO 1

ARG 336 0.42 GLU 34 -0.19 ILE 3

ARG 336 0.43 ASP 35 -0.16 PRO 1

ARG 336 0.50 VAL 36 -0.24 PRO 1

ARG 336 0.49 LEU 37 -0.26 PRO 1

ARG 336 0.43 GLY 38 -0.17 PRO 1

ARG 336 0.39 LEU 39 -0.14 ARG 125

ARG 336 0.34 PRO 40 -0.20 ARG 125

ARG 336 0.32 GLN 41 -0.20 ARG 125

ARG 336 0.29 ASN 42 -0.22 ARG 125

ARG 336 0.30 THR 43 -0.18 PRO 162

ARG 336 0.31 MET 44 -0.15 PRO 162

ARG 336 0.25 LYS 45 -0.17 PRO 162

HIS 332 0.24 ILE 46 -0.13 PRO 162

HIS 332 0.20 GLY 47 -0.12 PRO 162

HIS 332 0.18 ILE 48 -0.08 PRO 1

GLU 328 0.16 MET 49 -0.14 PRO 1

GLU 328 0.11 ASP 50 -0.10 PRO 1

LEU 29 0.11 GLU 51 -0.16 PRO 1

LEU 29 0.13 GLU 52 -0.14 PRO 1

LEU 29 0.10 ARG 53 -0.11 PRO 1

LEU 29 0.10 ARG 54 -0.10 PRO 1

PRO 329 0.08 THR 55 -0.08 PRO 1

HIS 332 0.06 THR 56 -0.05 PRO 1

ARG 6 0.07 VAL 57 -0.03 ILE 3

ARG 6 0.10 ASN 58 -0.04 PRO 162

ARG 6 0.10 LEU 59 -0.04 SER 102

ARG 6 0.15 LYS 60 -0.08 ALA 67

ARG 6 0.17 ALA 61 -0.05 ALA 24

ARG 6 0.14 CYS 62 -0.06 PRO 162

ARG 6 0.19 ILE 63 -0.07 ALA 67

ARG 6 0.23 LYS 64 -0.10 GLU 28

ARG 6 0.20 ALA 65 -0.10 GLU 28

ARG 6 0.21 ALA 66 -0.10 CYS 27

ARG 6 0.31 ALA 67 -0.16 ALA 120

ARG 6 0.35 ASP 68 -0.18 GLY 121

ARG 6 0.27 ARG 69 -0.14 ARG 125

ARG 6 0.23 VAL 70 -0.12 GLN 127

LEU 2 0.21 VAL 71 -0.16 ASN 42

HIS 332 0.17 PHE 72 -0.12 ALA 165

HIS 332 0.15 ILE 73 -0.11 VAL 70

GLY 235 0.15 ASN 74 -0.08 THR 7

GLY 235 0.13 THR 75 -0.10 ASN 4

GLY 235 0.13 GLY 76 -0.17 PRO 1

GLY 235 0.08 PHE 77 -0.16 PRO 1

LEU 29 0.10 LEU 78 -0.22 PRO 1

LEU 29 0.14 ASP 79 -0.21 PRO 1

LEU 29 0.12 ARG 80 -0.16 PRO 1

LEU 29 0.12 THR 81 -0.17 PRO 1

LEU 29 0.17 GLY 82 -0.20 PRO 1

LEU 29 0.17 ASP 83 -0.17 PRO 1

LEU 29 0.14 GLU 84 -0.15 PRO 1

LEU 29 0.17 ILE 85 -0.16 PRO 1

LEU 29 0.21 HIS 86 -0.17 PRO 1

LEU 29 0.19 THR 87 -0.14 PRO 1

LEU 29 0.16 SER 88 -0.13 PRO 1

LEU 29 0.20 MET 89 -0.15 PRO 1

LEU 29 0.18 GLU 90 -0.13 PRO 1

LEU 29 0.15 ALA 91 -0.12 PRO 1

LEU 29 0.15 GLY 92 -0.13 PRO 1

LEU 29 0.15 PRO 93 -0.15 PRO 1

LEU 29 0.13 MET 94 -0.15 PRO 1

LEU 29 0.11 VAL 95 -0.16 PRO 1

VAL 36 0.11 ARG 96 -0.18 PRO 1

VAL 36 0.10 LYS 97 -0.20 PRO 1

VAL 245 0.08 GLY 98 -0.20 PRO 1

VAL 245 0.08 THR 99 -0.18 ALA 148

LEU 29 0.08 MET 100 -0.16 PRO 1

LEU 247 0.09 LYS 101 -0.18 ALA 148

MET 135 0.09 SER 102 -0.20 ALA 152

MET 135 0.08 GLN 103 -0.14 ALA 152

LEU 138 0.09 PRO 104 -0.13 ARG 189

ASP 141 0.07 TRP 105 -0.11 PRO 199

ASP 141 0.08 ILE 106 -0.11 GLU 110

ASP 141 0.11 LEU 107 -0.14 SER 102

ASP 141 0.09 ALA 108 -0.11 PRO 104

GLY 235 0.07 TYR 109 -0.08 PRO 199

GLY 235 0.09 GLU 110 -0.12 SER 102

THR 145 0.10 ASP 111 -0.12 SER 102

GLY 235 0.08 HIS 112 -0.09 PRO 104

GLY 235 0.10 ASN 113 -0.09 SER 102

LEU 2 0.14 VAL 114 -0.11 SER 102

LEU 2 0.16 ASP 115 -0.10 ASP 68

LEU 2 0.16 ALA 116 -0.11 ALA 67

LEU 2 0.19 GLY 117 -0.13 ALA 67

LEU 2 0.25 LEU 118 -0.13 ASP 68

LEU 2 0.24 ALA 119 -0.12 ASP 68

LEU 2 0.25 ALA 120 -0.16 ALA 67

LEU 2 0.32 GLY 121 -0.18 ASP 68

LEU 2 0.32 PHE 122 -0.17 ASP 68

LEU 2 0.38 SER 123 -0.16 ASN 42

LEU 2 0.50 GLY 124 -0.18 ASN 42

LEU 2 0.47 ARG 125 -0.22 ASN 42

LEU 2 0.33 ALA 126 -0.18 ASN 42

LEU 2 0.24 GLN 127 -0.15 ASN 42

LEU 2 0.15 VAL 128 -0.11 ASN 42

GLY 235 0.16 GLY 129 -0.15 THR 7

GLY 235 0.15 LYS 130 -0.14 THR 7

GLY 235 0.15 GLY 131 -0.16 ASN 4

CYS 236 0.15 MET 132 -0.23 PRO 1

CYS 236 0.12 TRP 133 -0.26 PRO 1

LEU 107 0.09 THR 134 -0.31 PRO 1

SER 102 0.09 MET 135 -0.32 PRO 1

LEU 107 0.07 THR 136 -0.39 PRO 1

LEU 107 0.07 GLU 137 -0.38 PRO 1

LEU 107 0.09 LEU 138 -0.30 PRO 1

LEU 107 0.07 MET 139 -0.31 ARG 6

LEU 107 0.08 ALA 140 -0.28 ARG 6

LEU 107 0.11 ASP 141 -0.24 ARG 6

LEU 107 0.09 MET 142 -0.25 ARG 6

VAL 234 0.09 VAL 143 -0.26 ARG 6

ARG 189 0.08 GLU 144 -0.21 ARG 6

ARG 189 0.10 THR 145 -0.19 THR 7

GLY 235 0.10 LYS 146 -0.21 THR 7

GLY 235 0.10 ILE 147 -0.21 THR 7

GLY 235 0.08 ALA 148 -0.18 GLY 98

GLY 235 0.11 GLN 149 -0.17 LYS 101

GLY 235 0.12 PRO 150 -0.18 THR 7

PRO 1 0.13 ARG 151 -0.18 SER 102

LEU 2 0.12 ALA 152 -0.20 SER 102

LEU 2 0.18 GLY 153 -0.16 SER 102

GLY 235 0.14 ALA 154 -0.15 THR 7

LEU 2 0.21 SER 155 -0.19 THR 7

GLY 235 0.18 THR 156 -0.24 THR 7

GLY 235 0.18 ALA 157 -0.24 THR 7

GLY 235 0.22 TRP 158 -0.27 ARG 6

CYS 236 0.21 VAL 159 -0.32 ARG 6

CYS 236 0.26 PRO 160 -0.43 PRO 1

VAL 234 0.24 SER 161 -0.51 PRO 1

VAL 234 0.24 PRO 162 -0.56 LEU 2

VAL 234 0.18 THR 163 -0.48 ARG 6

VAL 234 0.16 ALA 164 -0.40 ARG 6

VAL 234 0.20 ALA 165 -0.45 ARG 6

VAL 234 0.17 THR 166 -0.48 ARG 6

VAL 234 0.14 LEU 167 -0.39 ARG 6

VAL 234 0.15 HIS 168 -0.33 ARG 6

VAL 234 0.16 ALA 169 -0.37 ARG 6

VAL 234 0.13 LEU 170 -0.32 THR 7

VAL 234 0.12 HIS 171 -0.27 THR 7

PRO 1 0.19 TYR 172 -0.29 THR 7

PRO 1 0.25 HIS 173 -0.29 THR 7

PRO 1 0.20 GLN 174 -0.24 THR 7

PRO 1 0.23 VAL 175 -0.20 THR 7

PRO 1 0.32 ASP 176 -0.18 THR 7

PRO 1 0.28 VAL 177 -0.17 THR 7

LEU 2 0.36 ALA 178 -0.14 PRO 40

PRO 1 0.34 ALA 179 -0.13 SER 102

PRO 1 0.26 VAL 180 -0.15 SER 102

LEU 2 0.28 GLN 181 -0.13 SER 102

LEU 2 0.31 GLN 182 -0.12 PRO 40

LEU 2 0.26 GLY 183 -0.13 GLU 203

LEU 2 0.22 LEU 184 -0.13 SER 102

LEU 2 0.26 ALA 185 -0.11 PRO 40

LEU 2 0.23 GLY 186 -0.10 PRO 40

LEU 2 0.19 LYS 187 -0.11 GLU 203

LEU 2 0.15 ARG 188 -0.11 GLU 203

LEU 2 0.11 ARG 189 -0.13 GLU 203

THR 145 0.09 ALA 190 -0.12 LYS 202

THR 145 0.08 THR 191 -0.09 LYS 202

ASP 141 0.06 ILE 192 -0.06 ALA 67

ASP 141 0.07 GLU 193 -0.08 ALA 91

ASP 141 0.08 GLN 194 -0.12 THR 197

ASP 141 0.06 LEU 195 -0.06 PRO 199

LEU 29 0.06 LEU 196 -0.06 GLN 321

LEU 29 0.07 THR 197 -0.12 GLN 194

LEU 29 0.09 ILE 198 -0.10 PRO 1

LEU 29 0.09 PRO 199 -0.12 PRO 1

LEU 29 0.11 LEU 200 -0.12 PRO 1

LEU 29 0.10 ALA 201 -0.13 PRO 1

LEU 29 0.09 LYS 202 -0.13 ARG 189

VAL 36 0.09 GLU 203 -0.14 ALA 152

VAL 36 0.12 LEU 204 -0.14 PRO 1

VAL 36 0.11 ALA 205 -0.15 PRO 1

VAL 36 0.11 TRP 206 -0.16 PRO 1

VAL 36 0.11 ALA 207 -0.17 PRO 1

VAL 36 0.13 PRO 208 -0.18 PRO 1

VAL 36 0.12 ASP 209 -0.20 PRO 1

VAL 36 0.11 GLU 210 -0.20 PRO 1

VAL 36 0.14 ILE 211 -0.19 PRO 1

VAL 36 0.15 ARG 212 -0.21 PRO 1

VAL 36 0.13 GLU 213 -0.22 PRO 1

VAL 36 0.13 GLU 214 -0.22 PRO 1

VAL 36 0.16 VAL 215 -0.22 PRO 1

VAL 36 0.16 ASP 216 -0.24 PRO 1

VAL 36 0.14 ASN 217 -0.26 PRO 1

VAL 36 0.16 ASN 218 -0.25 PRO 1

VAL 36 0.19 CYS 219 -0.26 PRO 1

VAL 36 0.17 GLN 220 -0.28 PRO 1

VAL 36 0.17 SER 221 -0.29 PRO 1

VAL 36 0.21 ILE 222 -0.28 PRO 1

VAL 36 0.22 LEU 223 -0.29 PRO 1

VAL 36 0.19 GLY 224 -0.32 PRO 1

VAL 36 0.21 TYR 225 -0.33 PRO 1

VAL 36 0.26 VAL 226 -0.31 PRO 1

VAL 36 0.26 VAL 227 -0.32 PRO 1

VAL 36 0.25 ARG 228 -0.36 PRO 1

VAL 36 0.29 TRP 229 -0.34 PRO 1

VAL 36 0.34 VAL 230 -0.31 PRO 1

VAL 36 0.32 ASP 231 -0.32 PRO 1

LEU 37 0.30 GLN 232 -0.36 PRO 1

LEU 37 0.33 GLY 233 -0.36 PRO 1

LEU 37 0.25 VAL 234 -0.41 PRO 1

LEU 37 0.24 GLY 235 -0.39 PRO 1

PRO 160 0.26 CYS 236 -0.42 PRO 1

SER 161 0.22 SER 237 -0.42 PRO 1

SER 161 0.18 LYS 238 -0.42 PRO 1

SER 161 0.13 VAL 239 -0.37 PRO 1

VAL 36 0.11 PRO 240 -0.35 PRO 1

VAL 36 0.11 ASP 241 -0.31 PRO 1

VAL 36 0.12 ILE 242 -0.29 PRO 1

VAL 36 0.09 HIS 243 -0.29 PRO 1

VAL 36 0.09 ASP 244 -0.32 PRO 1

GLY 98 0.08 VAL 245 -0.33 PRO 1

LYS 101 0.08 ALA 246 -0.37 PRO 1

LYS 101 0.09 LEU 247 -0.36 PRO 1

PRO 160 0.09 MET 248 -0.39 PRO 1

VAL 36 0.13 GLU 249 -0.36 PRO 1

VAL 33 0.16 ASP 250 -0.35 PRO 1

VAL 33 0.22 ARG 251 -0.31 PRO 1

VAL 33 0.16 ALA 252 -0.28 PRO 1

VAL 33 0.14 THR 253 -0.29 PRO 1

VAL 33 0.20 LEU 254 -0.28 PRO 1

LEU 29 0.21 ARG 255 -0.25 PRO 1

LEU 29 0.16 ILE 256 -0.23 PRO 1

VAL 36 0.17 SER 257 -0.24 PRO 1

VAL 36 0.22 SER 258 -0.23 PRO 1

LEU 29 0.21 GLN 259 -0.21 PRO 1

LEU 29 0.17 LEU 260 -0.20 PRO 1

VAL 36 0.19 LEU 261 -0.21 PRO 1

VAL 36 0.22 ALA 262 -0.19 PRO 1

LEU 29 0.20 ASN 263 -0.17 PRO 1

VAL 36 0.18 TRP 264 -0.18 PRO 1

VAL 36 0.21 LEU 265 -0.18 PRO 1

VAL 36 0.21 ARG 266 -0.16 PRO 1

VAL 36 0.18 HIS 267 -0.15 PRO 1

VAL 36 0.18 GLY 268 -0.16 PRO 1

VAL 36 0.17 VAL 269 -0.17 PRO 1

VAL 36 0.19 ILE 270 -0.18 PRO 1

VAL 36 0.22 THR 271 -0.18 PRO 1

VAL 36 0.24 SER 272 -0.19 PRO 1

VAL 36 0.23 ALA 273 -0.19 PRO 1

VAL 36 0.21 ASP 274 -0.20 PRO 1

VAL 36 0.22 VAL 275 -0.21 PRO 1

VAL 36 0.24 ARG 276 -0.22 PRO 1

VAL 36 0.22 ALA 277 -0.22 PRO 1

VAL 36 0.20 SER 278 -0.23 PRO 1

VAL 36 0.22 LEU 279 -0.24 PRO 1

VAL 36 0.22 GLU 280 -0.24 PRO 1

VAL 36 0.19 ARG 281 -0.25 PRO 1

VAL 36 0.19 MET 282 -0.26 PRO 1

VAL 36 0.21 ALA 283 -0.27 PRO 1

VAL 36 0.19 PRO 284 -0.28 PRO 1

VAL 36 0.17 LEU 285 -0.29 PRO 1

VAL 36 0.18 VAL 286 -0.31 PRO 1

VAL 36 0.19 ASP 287 -0.31 PRO 1

VAL 36 0.16 ARG 288 -0.31 PRO 1

VAL 36 0.14 GLN 289 -0.33 PRO 1

VAL 36 0.17 ASN 290 -0.35 PRO 1

VAL 36 0.16 ALA 291 -0.34 PRO 1

PRO 162 0.16 GLY 292 -0.36 PRO 1

PRO 162 0.19 ASP 293 -0.38 PRO 1

PRO 162 0.20 VAL 294 -0.36 PRO 1

LEU 37 0.23 ALA 295 -0.36 PRO 1

VAL 36 0.23 TYR 296 -0.34 PRO 1

VAL 36 0.26 ARG 297 -0.31 PRO 1

VAL 36 0.24 PRO 298 -0.29 PRO 1

VAL 36 0.26 MET 299 -0.27 PRO 1

VAL 36 0.24 ALA 300 -0.26 PRO 1

VAL 36 0.25 PRO 301 -0.25 PRO 1

VAL 36 0.28 ASN 302 -0.24 PRO 1

VAL 36 0.28 PHE 303 -0.24 PRO 1

VAL 36 0.31 ASP 304 -0.22 PRO 1

VAL 36 0.33 ASP 305 -0.23 PRO 1

VAL 36 0.32 SER 306 -0.25 PRO 1

VAL 36 0.35 ILE 307 -0.25 PRO 1

VAL 36 0.31 ALA 308 -0.27 PRO 1

VAL 36 0.29 PHE 309 -0.26 PRO 1

VAL 36 0.32 LEU 310 -0.24 PRO 1

VAL 36 0.33 ALA 311 -0.25 PRO 1

VAL 36 0.28 ALA 312 -0.26 PRO 1

VAL 36 0.28 GLN 313 -0.23 PRO 1

VAL 36 0.32 GLU 314 -0.22 PRO 1

VAL 36 0.29 LEU 315 -0.23 PRO 1

VAL 36 0.26 ILE 316 -0.22 PRO 1

VAL 36 0.28 LEU 317 -0.20 PRO 1

VAL 36 0.31 SER 318 -0.20 PRO 1

LEU 29 0.27 GLY 319 -0.21 PRO 1

LEU 29 0.26 ALA 320 -0.18 PRO 1

LEU 29 0.30 GLN 321 -0.18 PRO 1

LEU 29 0.34 GLN 322 -0.19 PRO 1

LEU 29 0.36 PRO 323 -0.19 PRO 1

LEU 29 0.29 ASN 324 -0.19 PRO 1

LEU 29 0.27 GLY 325 -0.21 PRO 1

LEU 29 0.31 TYR 326 -0.24 PRO 1

VAL 33 0.32 THR 327 -0.25 PRO 1

VAL 33 0.40 GLU 328 -0.26 PRO 1

VAL 33 0.45 PRO 329 -0.22 PRO 1

VAL 36 0.40 ILE 330 -0.23 PRO 1

VAL 36 0.38 LEU 331 -0.26 PRO 1

VAL 33 0.46 HIS 332 -0.25 PRO 1

VAL 36 0.48 ARG 333 -0.23 PRO 1

VAL 36 0.42 ARG 334 -0.25 PRO 1

VAL 36 0.43 ARG 335 -0.27 PRO 1

VAL 36 0.50 ARG 336 -0.24 PRO 1

VAL 36 0.46 GLU 337 -0.23 PRO 1

VAL 36 0.41 PHE 338 -0.26 PRO 1

LEU 37 0.46 LYS 339 -0.25 PRO 1

VAL 36 0.48 ALA 340 -0.22 PRO 1

VAL 36 0.43 ARG 341 -0.22 PRO 1

LEU 37 0.41 ALA 342 -0.24 PRO 1

LEU 37 0.46 ALA 343 -0.21 PRO 1

LEU 37 0.44 GLU 344 -0.19 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 9 ---

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

* EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *