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

* EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *

CA distance fluctuations for 24021912402138273

--- 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
GLY 3 0.20 ARG 1 -0.99 TYR 44

GLY 3 0.21 PRO 2 -1.01 ASP 43

GLN 59 0.24 GLY 3 -0.53 ASP 43

ASN 219 0.18 LEU 4 -0.37 TYR 44

ASN 219 0.23 PRO 5 -0.24 GLY 86

ASN 219 0.27 VAL 6 -0.32 PRO 2

ASN 219 0.29 GLU 7 -0.39 PRO 2

ASN 219 0.30 TYR 8 -0.58 PRO 2

PRO 221 0.28 LEU 9 -0.46 PRO 2

PRO 221 0.28 GLN 10 -0.47 PRO 2

PRO 221 0.24 VAL 11 -0.39 PRO 2

PRO 221 0.21 PRO 12 -0.37 PRO 2

PRO 221 0.17 SER 13 -0.38 PRO 2

PRO 221 0.13 ALA 14 -0.34 PRO 2

ALA 103 0.15 SER 15 -0.37 PRO 2

GLY 168 0.13 MET 16 -0.46 PRO 2

PRO 221 0.15 GLY 17 -0.44 PRO 2

PRO 221 0.22 ARG 18 -0.49 PRO 2

PRO 221 0.25 ASP 19 -0.49 PRO 2

PRO 221 0.27 ILE 20 -0.55 PRO 2

PRO 221 0.31 LYS 21 -0.62 PRO 2

PRO 221 0.28 VAL 22 -0.54 PRO 2

PRO 221 0.29 GLN 23 -0.58 PRO 2

ASN 219 0.25 PHE 24 -0.36 PRO 2

ASN 219 0.22 GLN 25 -0.19 GLY 86

ASN 219 0.18 GLY 26 -0.13 GLY 86

TYR 58 0.22 GLY 27 -0.13 ARG 39

GLY 3 0.17 GLY 28 -0.10 ARG 39

TYR 58 0.13 PRO 29 -0.08 GLU 7

TYR 58 0.13 HIS 30 -0.10 GLY 37

ASN 219 0.13 ALA 31 -0.13 ARG 1

ASN 219 0.14 VAL 32 -0.19 ARG 1

PRO 221 0.16 TYR 33 -0.29 ARG 1

PRO 221 0.21 LEU 34 -0.38 ARG 1

PRO 221 0.22 LEU 35 -0.45 ARG 1

PRO 221 0.31 ASP 36 -0.57 ARG 1

LEU 225 0.36 GLY 37 -0.58 ARG 1

LEU 228 0.29 LEU 38 -0.60 ARG 1

PRO 221 0.37 ARG 39 -0.76 ARG 1

PRO 221 0.43 ALA 40 -0.76 ARG 1

PRO 221 0.50 GLN 41 -0.84 PRO 2

PRO 221 0.42 ASP 42 -0.86 PRO 2

PRO 221 0.45 ASP 43 -1.01 PRO 2

PRO 221 0.44 TYR 44 -0.99 ARG 1

PRO 221 0.39 ASN 45 -0.82 ARG 1

PRO 221 0.45 GLY 46 -0.75 ARG 1

PRO 221 0.32 TRP 47 -0.62 ARG 1

ASN 219 0.34 ASP 48 -0.85 ARG 1

ASN 219 0.41 ILE 49 -0.97 ARG 1

ASN 219 0.41 ASN 50 -0.62 ARG 1

ASN 219 0.30 THR 51 -0.44 ARG 1

ASN 219 0.25 PRO 52 -0.36 ARG 39

ASN 219 0.24 ALA 53 -0.34 ARG 39

ASN 219 0.23 PHE 54 -0.28 ARG 39

ASN 219 0.18 GLU 55 -0.33 ARG 39

ASN 219 0.17 GLU 56 -0.26 ARG 39

ASN 219 0.14 TYR 57 -0.24 ARG 39

GLY 27 0.22 TYR 58 -0.24 ARG 39

GLY 3 0.24 GLN 59 -0.20 ARG 39

GLY 3 0.17 SER 60 -0.18 ARG 39

GLY 3 0.19 GLY 61 -0.14 ARG 39

TYR 58 0.14 LEU 62 -0.14 ARG 39

ASN 219 0.16 SER 63 -0.12 ARG 39

ASN 219 0.19 VAL 64 -0.22 ARG 1

PRO 221 0.21 ILE 65 -0.33 PRO 2

PRO 221 0.26 MET 66 -0.49 ARG 1

PRO 221 0.27 PRO 67 -0.54 PRO 2

PRO 221 0.34 VAL 68 -0.70 PRO 2

PRO 221 0.32 GLY 69 -0.72 PRO 2

PRO 221 0.21 GLY 70 -0.62 PRO 2

LEU 228 0.22 GLN 71 -0.69 ARG 1

LEU 228 0.18 SER 72 -0.59 ARG 1

LEU 228 0.13 SER 73 -0.53 PRO 2

LEU 228 0.11 PHE 74 -0.45 ARG 1

LEU 228 0.09 TYR 75 -0.43 PRO 2

THR 114 0.11 THR 76 -0.39 PRO 2

THR 114 0.17 ASP 77 -0.39 PRO 2

THR 114 0.13 TRP 78 -0.44 PRO 2

TYR 135 0.19 TYR 79 -0.41 PRO 2

THR 114 0.14 GLN 80 -0.48 PRO 2

THR 95 0.11 PRO 81 -0.55 PRO 2

THR 95 0.08 SER 82 -0.59 PRO 2

TYR 134 0.08 GLN 83 -0.59 PRO 2

VAL 191 0.09 SER 84 -0.64 PRO 2

LEU 228 0.12 ASN 85 -0.72 PRO 2

LEU 228 0.10 GLY 86 -0.74 PRO 2

LEU 228 0.10 GLN 87 -0.70 PRO 2

SER 15 0.13 ASN 88 -0.64 PRO 2

SER 15 0.14 TYR 89 -0.57 PRO 2

THR 95 0.12 THR 90 -0.51 PRO 2

GLY 168 0.10 TYR 91 -0.52 PRO 2

THR 95 0.16 LYS 92 -0.43 PRO 2

PRO 221 0.10 TRP 93 -0.43 PRO 2

ASP 77 0.14 GLU 94 -0.34 PRO 2

LYS 92 0.16 THR 95 -0.32 PRO 2

PRO 221 0.12 PHE 96 -0.36 PRO 2

PRO 221 0.12 LEU 97 -0.33 PRO 2

PRO 113 0.17 THR 98 -0.25 PRO 2

PRO 113 0.19 ARG 99 -0.24 PRO 2

ALA 103 0.15 GLU 100 -0.28 PRO 2

PRO 221 0.16 MET 101 -0.29 PRO 2

PRO 221 0.13 PRO 102 -0.20 PRO 2

GLU 100 0.15 ALA 103 -0.18 ALA 198

PRO 221 0.16 TRP 104 -0.20 PRO 2

PRO 221 0.17 LEU 105 -0.18 PRO 2

ASN 219 0.14 GLN 106 -0.14 ALA 198

ASN 219 0.15 ALA 107 -0.15 ALA 198

ASN 219 0.18 ASN 108 -0.12 ALA 198

ASN 219 0.18 LYS 109 -0.09 ALA 198

GLY 26 0.17 GLY 110 -0.10 ALA 198

ASN 219 0.14 VAL 111 -0.09 ASN 200

ARG 99 0.17 SER 112 -0.13 ASN 200

ARG 99 0.19 PRO 113 -0.15 ASN 200

TYR 79 0.17 THR 114 -0.18 ASN 200

GLN 138 0.17 GLY 115 -0.14 ASN 247

TYR 79 0.11 ASN 116 -0.12 ARG 1

ASN 219 0.09 ALA 117 -0.16 ARG 1

PRO 221 0.10 ALA 118 -0.23 ARG 1

PRO 221 0.12 VAL 119 -0.27 ARG 1

PRO 221 0.13 GLY 120 -0.33 ARG 1

LEU 225 0.15 LEU 121 -0.35 ARG 1

LEU 228 0.21 SER 122 -0.35 ARG 1

LEU 228 0.20 MET 123 -0.42 ARG 1

LEU 228 0.13 SER 124 -0.40 ARG 1

GLN 41 0.12 GLY 125 -0.30 ARG 1

GLN 41 0.09 GLY 126 -0.28 ARG 1

GLN 41 0.05 SER 127 -0.32 ARG 1

TYR 79 0.06 ALA 128 -0.27 ARG 1

ALA 142 0.11 LEU 129 -0.22 ARG 1

ALA 183 0.12 ILE 130 -0.24 ARG 1

TYR 79 0.14 LEU 131 -0.25 ARG 1

PRO 182 0.15 ALA 132 -0.19 ARG 1

PRO 182 0.19 ALA 133 -0.18 ARG 1

PRO 182 0.21 TYR 134 -0.20 PRO 2

TYR 79 0.19 TYR 135 -0.18 PRO 2

GLY 280 0.21 PRO 136 -0.16 ALA 198

GLY 280 0.20 GLN 137 -0.22 ASN 200

GLY 115 0.17 GLN 138 -0.15 ALA 103

PRO 182 0.14 PHE 139 -0.16 ARG 1

GLY 280 0.17 PRO 140 -0.16 THR 114

ALA 133 0.14 TYR 141 -0.12 THR 114

LEU 129 0.11 ALA 142 -0.17 ARG 1

GLN 192 0.06 ALA 143 -0.18 ARG 1

GLN 41 0.10 SER 144 -0.22 ARG 1

GLN 41 0.12 LEU 145 -0.22 ARG 1

GLN 41 0.18 SER 146 -0.22 ARG 1

GLN 41 0.17 GLY 147 -0.27 ARG 1

LEU 38 0.15 PHE 148 -0.28 ARG 1

GLN 41 0.11 LEU 149 -0.23 ARG 1

ALA 163 0.14 ASN 150 -0.24 LEU 225

ALA 163 0.12 PRO 151 -0.31 ARG 1

VAL 191 0.18 SER 152 -0.32 PRO 221

THR 239 0.23 GLU 153 -0.38 PRO 221

THR 239 0.20 SER 154 -0.50 PRO 221

THR 239 0.18 TRP 155 -0.60 PRO 221

THR 239 0.15 TRP 156 -0.51 PRO 221

VAL 191 0.14 PRO 157 -0.47 PRO 221

ASP 243 0.13 THR 158 -0.59 PRO 221

THR 239 0.12 LEU 159 -0.67 PRO 221

ASN 150 0.12 ILE 160 -0.46 ARG 1

VAL 191 0.11 GLY 161 -0.49 ARG 1

ASN 85 0.11 LEU 162 -0.55 PRO 221

LEU 228 0.18 ALA 163 -0.56 ARG 1

LEU 228 0.15 MET 164 -0.58 ARG 1

LEU 228 0.12 ASN 165 -0.61 PRO 2

LEU 228 0.20 ASP 166 -0.65 ARG 1

LEU 228 0.24 SER 167 -0.70 ARG 1

LEU 228 0.19 GLY 168 -0.74 PRO 2

LEU 228 0.14 GLY 169 -0.68 PRO 2

LEU 228 0.11 TYR 170 -0.62 PRO 2

VAL 191 0.09 ASN 171 -0.56 PRO 2

VAL 191 0.12 ALA 172 -0.49 PRO 2

ARG 195 0.12 ASN 173 -0.46 PRO 2

TYR 134 0.12 SER 174 -0.49 PRO 2

TYR 135 0.11 MET 175 -0.46 PRO 2

TYR 134 0.16 TRP 176 -0.39 PRO 2

TYR 134 0.16 GLY 177 -0.40 PRO 2

ARG 195 0.15 PRO 178 -0.39 PRO 2

PRO 194 0.17 SER 179 -0.40 PRO 221

PRO 194 0.20 SER 180 -0.35 PRO 221

ARG 195 0.19 ASP 181 -0.32 PRO 2

ARG 195 0.25 PRO 182 -0.28 PRO 2

ARG 186 0.21 ALA 183 -0.32 PRO 2

ARG 195 0.17 TRP 184 -0.32 PRO 2

ARG 195 0.19 LYS 185 -0.26 PRO 2

ALA 183 0.21 ARG 186 -0.26 PRO 2

GLY 280 0.11 ASN 187 -0.28 PRO 2

ALA 172 0.11 ASP 188 -0.25 ARG 1

GLU 153 0.11 PRO 189 -0.21 ARG 1

GLU 153 0.21 MET 190 -0.18 ARG 1

GLU 153 0.19 VAL 191 -0.19 PRO 2

PRO 182 0.17 GLN 192 -0.17 PRO 2

GLU 153 0.18 ILE 193 -0.14 ARG 1

PRO 182 0.22 PRO 194 -0.13 ARG 99

PRO 182 0.25 ARG 195 -0.15 ARG 99

PRO 182 0.19 LEU 196 -0.13 ALA 103

PRO 182 0.19 VAL 197 -0.18 GLN 137

PRO 182 0.22 ALA 198 -0.20 GLN 137

PRO 182 0.21 ASN 199 -0.22 GLN 137

HIS 276 0.18 ASN 200 -0.22 GLN 137

PRO 182 0.18 THR 201 -0.17 GLN 137

PRO 182 0.13 ARG 202 -0.15 THR 114

GLN 192 0.14 ILE 203 -0.12 THR 114

GLY 248 0.09 TRP 204 -0.11 ARG 1

GLN 41 0.09 VAL 205 -0.13 ARG 1

GLN 41 0.10 TYR 206 -0.13 LEU 159

GLN 41 0.15 CYS 207 -0.15 LEU 159

SER 259 0.20 GLY 208 -0.19 LEU 159

SER 259 0.20 ASN 209 -0.17 LEU 159

SER 259 0.25 GLY 210 -0.28 LEU 159

SER 259 0.22 THR 211 -0.26 LEU 159

SER 259 0.20 PRO 212 -0.32 LEU 159

VAL 6 0.13 SER 213 -0.31 LEU 162

VAL 6 0.16 ASP 214 -0.35 ASP 166

ALA 53 0.18 LEU 215 -0.39 ASP 166

ASN 50 0.21 GLY 216 -0.44 ASP 166

ASN 50 0.35 GLY 217 -0.49 LEU 162

ASN 50 0.31 ASP 218 -0.44 LEU 162

ASN 50 0.41 ASN 219 -0.51 LEU 159

GLN 41 0.42 ILE 220 -0.50 TRP 155

GLN 41 0.50 PRO 221 -0.67 LEU 159

GLY 46 0.40 ALA 222 -0.60 LEU 159

GLN 41 0.32 LYS 223 -0.42 LEU 159

GLN 41 0.38 PHE 224 -0.50 TRP 155

GLN 41 0.37 LEU 225 -0.51 LEU 159

GLN 41 0.27 GLU 226 -0.32 LEU 159

GLN 41 0.28 GLY 227 -0.26 SER 154

ARG 39 0.33 LEU 228 -0.34 SER 154

GLN 41 0.23 THR 229 -0.21 SER 154

GLN 41 0.20 LEU 230 -0.12 ARG 1

GLN 41 0.20 ARG 231 -0.16 LEU 228

GLN 41 0.17 THR 232 -0.19 LEU 228

GLN 41 0.15 ASN 233 -0.14 ARG 1

GLN 41 0.14 GLN 234 -0.13 LEU 228

GLU 153 0.16 THR 235 -0.16 LEU 228

GLU 153 0.17 PHE 236 -0.13 ARG 1

GLU 153 0.14 ARG 237 -0.12 GLN 137

GLU 153 0.19 ASP 238 -0.12 LEU 228

GLU 153 0.23 THR 239 -0.13 LEU 228

GLU 153 0.20 TYR 240 -0.13 GLN 137

GLU 153 0.18 ALA 241 -0.14 GLN 137

GLU 153 0.21 ALA 242 -0.13 GLN 137

GLU 153 0.22 ASP 243 -0.14 GLN 137

GLU 153 0.17 GLY 244 -0.17 GLN 137

GLU 153 0.16 GLY 245 -0.18 GLN 137

PRO 182 0.13 ARG 246 -0.16 GLN 137

PRO 182 0.14 ASN 247 -0.15 THR 114

GLN 192 0.12 GLY 248 -0.12 THR 114

GLN 266 0.10 VAL 249 -0.13 VAL 277

GLN 266 0.09 PHE 250 -0.10 LEU 230

SER 259 0.11 ASN 251 -0.12 ASP 273

SER 259 0.14 PHE 252 -0.11 ASN 209

SER 259 0.13 PRO 253 -0.12 ASP 273

SER 259 0.14 PRO 254 -0.12 LEU 162

SER 259 0.16 ASN 255 -0.20 LEU 159

SER 259 0.23 GLY 256 -0.27 LEU 159

SER 259 0.36 THR 257 -0.37 LEU 159

GLY 46 0.28 HIS 258 -0.45 LEU 159

THR 257 0.36 SER 259 -0.53 ALA 163

ALA 222 0.28 TRP 260 -0.43 ASP 166

GLY 217 0.22 PRO 261 -0.40 ASP 166

ALA 53 0.14 TYR 262 -0.33 ALA 163

ALA 222 0.14 TRP 263 -0.30 ALA 163

GLY 217 0.18 ASN 264 -0.31 ASP 166

GLY 217 0.13 GLU 265 -0.28 ASP 166

VAL 249 0.10 GLN 266 -0.21 ASP 166

ASN 219 0.12 LEU 267 -0.22 GLY 37

GLY 217 0.12 VAL 268 -0.22 ASP 166

ARG 246 0.11 ALA 269 -0.19 ASP 166

ARG 202 0.11 MET 270 -0.16 GLY 37

ARG 202 0.11 LYS 271 -0.18 ARG 39

ASP 273 0.14 ALA 272 -0.15 ARG 39

ALA 272 0.14 ASP 273 -0.12 GLY 37

ASN 200 0.12 ILE 274 -0.13 GLY 37

PRO 136 0.13 GLN 275 -0.12 GLY 37

ASN 200 0.18 HIS 276 -0.12 PRO 253

ASN 199 0.17 VAL 277 -0.13 VAL 249

PRO 136 0.17 LEU 278 -0.09 VAL 249

GLN 137 0.19 ASN 279 -0.09 GLY 37

PRO 136 0.21 GLY 280 -0.10 PRO 253

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_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 24021912402138273

--- normal mode 8 ---

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

* EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *