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

* 1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *

CA distance fluctuations for 240220092131172147

--- 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
TYR 8 0.41 ARG 1 -0.21 LEU 215

GLU 7 0.41 PRO 2 -0.18 ASP 214

ASN 88 0.07 GLY 3 -0.16 ASP 214

GLY 27 0.09 LEU 4 -0.15 ASP 214

PRO 2 0.25 PRO 5 -0.12 ASP 214

PRO 2 0.38 VAL 6 -0.11 LEU 159

PRO 2 0.41 GLU 7 -0.11 LEU 159

ARG 1 0.41 TYR 8 -0.12 LEU 159

PRO 2 0.32 LEU 9 -0.14 GLY 168

ARG 1 0.29 GLN 10 -0.17 GLY 168

ARG 1 0.24 VAL 11 -0.15 GLY 168

ASN 219 0.24 PRO 12 -0.15 GLY 168

PRO 221 0.29 SER 13 -0.13 GLY 168

PRO 221 0.31 ALA 14 -0.16 ASN 88

PRO 221 0.36 SER 15 -0.17 ASN 88

PRO 221 0.39 MET 16 -0.16 ASN 88

ASN 219 0.36 GLY 17 -0.18 ASN 88

ASN 219 0.35 ARG 18 -0.17 GLY 168

ASN 219 0.28 ASP 19 -0.19 GLY 168

ASN 219 0.28 ILE 20 -0.19 GLY 168

ARG 1 0.31 LYS 21 -0.17 GLY 168

ARG 1 0.30 VAL 22 -0.12 GLY 168

ARG 1 0.35 GLN 23 -0.13 LEU 159

ARG 1 0.27 PHE 24 -0.10 LEU 159

PRO 2 0.20 GLN 25 -0.11 ASP 214

PRO 2 0.14 GLY 26 -0.14 ASP 214

ASN 200 0.09 GLY 27 -0.19 ASP 214

ASN 199 0.11 GLY 28 -0.19 ASP 214

ASN 199 0.11 PRO 29 -0.17 ASP 214

ASN 199 0.11 HIS 30 -0.17 ASP 214

PRO 2 0.10 ALA 31 -0.14 ASP 214

GLY 37 0.09 VAL 32 -0.13 ASP 214

ARG 1 0.12 TYR 33 -0.09 GLN 266

GLY 37 0.12 LEU 34 -0.09 LEU 159

ASN 219 0.19 LEU 35 -0.12 LEU 159

GLY 217 0.27 ASP 36 -0.18 LEU 159

GLY 217 0.38 GLY 37 -0.26 LEU 159

ALA 222 0.67 LEU 38 -0.29 LEU 159

ASN 219 0.71 ARG 39 -0.30 LEU 159

ASN 219 0.51 ALA 40 -0.23 LEU 159

ASN 219 0.47 GLN 41 -0.23 LEU 159

ASN 219 0.42 ASP 42 -0.21 SER 167

ARG 1 0.32 ASP 43 -0.20 ALA 163

ARG 1 0.34 TYR 44 -0.19 LEU 159

ARG 1 0.26 ASN 45 -0.19 LEU 159

GLY 217 0.26 GLY 46 -0.21 LEU 159

GLN 87 0.18 TRP 47 -0.15 LEU 159

ARG 1 0.24 ASP 48 -0.16 LEU 159

ARG 1 0.23 ILE 49 -0.20 LEU 159

GLN 87 0.22 ASN 50 -0.17 LEU 159

GLN 87 0.18 THR 51 -0.22 TRP 260

GLN 87 0.14 PRO 52 -0.18 TRP 260

GLN 87 0.12 ALA 53 -0.17 TRP 260

GLN 87 0.08 PHE 54 -0.14 ASP 214

GLN 87 0.09 GLU 55 -0.20 ASP 214

ARG 39 0.11 GLU 56 -0.26 ASP 214

ARG 39 0.08 TYR 57 -0.24 ASP 214

ASN 200 0.08 TYR 58 -0.24 ASP 214

ASN 200 0.09 GLN 59 -0.26 ASP 214

ASN 200 0.10 SER 60 -0.28 ASP 214

ASN 200 0.11 GLY 61 -0.25 ASP 214

ASN 200 0.10 LEU 62 -0.21 ASP 214

PRO 2 0.11 SER 63 -0.16 ASP 214

ARG 1 0.13 VAL 64 -0.12 ASP 214

ARG 1 0.18 ILE 65 -0.08 LEU 159

ARG 1 0.22 MET 66 -0.12 LEU 159

ARG 1 0.23 PRO 67 -0.12 LEU 159

ASN 219 0.28 VAL 68 -0.15 LEU 159

ASN 219 0.42 GLY 69 -0.14 LEU 159

ASN 219 0.47 GLY 70 -0.13 ILE 160

ASN 219 0.63 GLN 71 -0.16 ILE 160

PRO 221 0.73 SER 72 -0.19 ILE 160

PRO 221 0.56 SER 73 -0.10 ILE 160

PRO 221 0.47 PHE 74 -0.10 ALA 40

PRO 221 0.38 TYR 75 -0.07 ILE 130

PRO 221 0.40 THR 76 -0.12 TYR 134

PRO 221 0.42 ASP 77 -0.21 TYR 134

PRO 221 0.49 TRP 78 -0.18 TYR 134

PRO 221 0.48 TYR 79 -0.21 TYR 134

PRO 221 0.55 GLN 80 -0.18 TYR 134

PRO 221 0.61 PRO 81 -0.15 TYR 134

PRO 221 0.72 SER 82 -0.11 TYR 134

PRO 221 0.73 GLN 83 -0.10 TYR 134

PRO 221 0.84 SER 84 -0.11 ARG 18

ASN 219 0.84 ASN 85 -0.15 ARG 18

ASN 219 0.75 GLY 86 -0.17 GLY 17

ASN 219 0.69 GLN 87 -0.18 GLY 17

ASN 219 0.60 ASN 88 -0.18 GLY 17

PRO 221 0.52 TYR 89 -0.16 ASN 88

PRO 221 0.52 THR 90 -0.16 TYR 134

PRO 221 0.50 TYR 91 -0.13 TYR 134

PRO 221 0.41 LYS 92 -0.16 TYR 134

PRO 221 0.36 TRP 93 -0.10 GLY 168

PRO 221 0.32 GLU 94 -0.13 LYS 92

PRO 221 0.30 THR 95 -0.14 LYS 92

PRO 221 0.28 PHE 96 -0.10 TYR 89

PRO 221 0.24 LEU 97 -0.09 LYS 92

PRO 221 0.22 THR 98 -0.13 THR 95

PRO 221 0.23 ARG 99 -0.16 PRO 113

PRO 221 0.23 GLU 100 -0.14 PRO 113

PRO 221 0.19 MET 101 -0.10 SER 13

PRO 221 0.16 PRO 102 -0.11 GLU 100

PRO 221 0.17 ALA 103 -0.15 ALA 14

PRO 2 0.18 TRP 104 -0.12 ALA 14

PRO 2 0.17 LEU 105 -0.09 ALA 14

PRO 2 0.14 GLN 106 -0.11 ALA 14

PRO 2 0.15 ALA 107 -0.10 ALA 14

PRO 2 0.18 ASN 108 -0.09 GLY 168

PRO 2 0.17 LYS 109 -0.10 GLY 27

PRO 2 0.13 GLY 110 -0.12 ASP 214

PRO 2 0.14 VAL 111 -0.12 ASP 214

PRO 2 0.11 SER 112 -0.12 ASP 214

PRO 221 0.13 PRO 113 -0.16 ARG 99

PRO 221 0.11 THR 114 -0.16 ARG 99

ASN 199 0.13 GLY 115 -0.15 ASP 214

ASN 199 0.10 ASN 116 -0.14 ASP 214

GLY 37 0.10 ALA 117 -0.14 ASP 214

GLY 37 0.12 ALA 118 -0.09 GLN 266

GLY 37 0.14 VAL 119 -0.08 GLN 266

GLY 37 0.18 GLY 120 -0.09 TRP 156

SER 167 0.25 LEU 121 -0.15 GLY 147

SER 167 0.34 SER 122 -0.16 TRP 156

ALA 222 0.41 MET 123 -0.19 TRP 156

PRO 221 0.27 SER 124 -0.13 TRP 156

ASP 166 0.19 GLY 125 -0.10 GLY 46

PRO 221 0.23 GLY 126 -0.08 GLY 46

PRO 221 0.26 SER 127 -0.06 ALA 40

PRO 221 0.18 ALA 128 -0.06 GLN 266

PRO 221 0.16 LEU 129 -0.11 VAL 205

PRO 221 0.21 ILE 130 -0.13 TYR 79

PRO 221 0.21 LEU 131 -0.15 ASP 77

PRO 221 0.16 ALA 132 -0.12 ASP 77

PRO 221 0.16 ALA 133 -0.16 TYR 79

PRO 221 0.18 TYR 134 -0.21 TYR 79

PRO 221 0.17 TYR 135 -0.16 ASP 77

PRO 221 0.13 PRO 136 -0.14 THR 201

PRO 221 0.12 GLN 137 -0.12 SER 15

PRO 221 0.13 GLN 138 -0.13 ARG 99

PRO 221 0.12 PHE 139 -0.11 THR 95

ASN 199 0.13 PRO 140 -0.14 ASP 214

ASP 166 0.11 TYR 141 -0.14 ASP 214

ASP 166 0.13 ALA 142 -0.11 ASP 214

ASP 166 0.18 ALA 143 -0.11 ASP 214

ASP 166 0.22 SER 144 -0.07 GLN 266

ASP 166 0.31 LEU 145 -0.07 LEU 228

ASP 166 0.41 SER 146 -0.11 LEU 228

ALA 163 0.29 GLY 147 -0.15 LEU 121

ALA 163 0.26 PHE 148 -0.15 SER 122

ALA 163 0.20 LEU 149 -0.11 GLY 46

PRO 221 0.17 ASN 150 -0.12 GLY 46

PRO 221 0.29 PRO 151 -0.16 GLY 37

PRO 221 0.24 SER 152 -0.13 ARG 39

VAL 191 0.18 GLU 153 -0.14 ARG 39

VAL 191 0.14 SER 154 -0.17 ARG 39

PHE 224 0.20 TRP 155 -0.21 ARG 39

PRO 221 0.27 TRP 156 -0.22 GLY 37

PRO 221 0.43 PRO 157 -0.19 ARG 39

PRO 221 0.50 THR 158 -0.22 ARG 39

PHE 224 0.59 LEU 159 -0.30 ARG 39

PRO 221 0.69 ILE 160 -0.27 ARG 39

PRO 221 0.86 GLY 161 -0.15 ARG 39

PRO 221 1.10 LEU 162 -0.18 ARG 39

PRO 221 1.27 ALA 163 -0.27 ARG 39

PRO 221 1.13 MET 164 -0.14 ASP 43

PRO 221 1.25 ASN 165 -0.12 ASP 19

PRO 221 1.61 ASP 166 -0.17 ASP 43

PRO 221 1.26 SER 167 -0.21 ASP 42

ASN 219 1.04 GLY 168 -0.19 ASP 19

PRO 221 1.07 GLY 169 -0.14 ASP 19

PRO 221 0.95 TYR 170 -0.12 ASP 19

PRO 221 0.85 ASN 171 -0.08 PRO 178

PRO 221 0.72 ALA 172 -0.09 SER 179

PRO 221 0.63 ASN 173 -0.09 ALA 183

PRO 221 0.64 SER 174 -0.12 TYR 134

PRO 221 0.58 MET 175 -0.11 TYR 134

PRO 221 0.48 TRP 176 -0.14 ARG 186

PRO 221 0.49 GLY 177 -0.11 PRO 194

PRO 221 0.45 PRO 178 -0.11 ASN 165

PRO 221 0.37 SER 179 -0.14 GLY 161

PRO 221 0.29 SER 180 -0.10 GLY 161

PRO 221 0.33 ASP 181 -0.12 PRO 194

PRO 221 0.28 PRO 182 -0.18 PRO 194

PRO 221 0.33 ALA 183 -0.16 PRO 194

PRO 221 0.32 TRP 184 -0.10 MET 190

PRO 221 0.23 LYS 185 -0.15 MET 190

PRO 221 0.24 ARG 186 -0.17 TYR 79

PRO 221 0.28 ASN 187 -0.12 TYR 79

PRO 221 0.22 ASP 188 -0.09 ALA 40

PRO 221 0.16 PRO 189 -0.10 VAL 205

PRO 221 0.13 MET 190 -0.15 LYS 185

GLU 153 0.18 VAL 191 -0.18 PRO 182

PRO 221 0.15 GLN 192 -0.17 ILE 193

PRO 221 0.11 ILE 193 -0.17 GLN 192

GLU 153 0.11 PRO 194 -0.18 PRO 182

PRO 221 0.13 ARG 195 -0.19 TYR 79

PRO 221 0.11 LEU 196 -0.15 TYR 79

GLY 280 0.12 VAL 197 -0.15 TYR 79

GLY 280 0.13 ALA 198 -0.18 TYR 79

ASN 279 0.14 ASN 199 -0.17 TYR 79

GLY 280 0.16 ASN 200 -0.14 PRO 253

VAL 277 0.11 THR 201 -0.14 PRO 136

ASP 166 0.14 ARG 202 -0.16 ASP 214

ASP 166 0.17 ILE 203 -0.14 PRO 253

ASP 166 0.21 TRP 204 -0.16 ASP 214

ASP 166 0.26 VAL 205 -0.11 ASP 214

ASP 166 0.34 TYR 206 -0.11 ASP 214

ASP 166 0.44 CYS 207 -0.08 THR 257

ASP 166 0.55 GLY 208 -0.12 ALA 269

ASP 166 0.63 ASN 209 -0.20 PHE 252

ASP 166 0.80 GLY 210 -0.14 ALA 269

ASP 166 0.76 THR 211 -0.19 ALA 269

ASP 166 0.76 PRO 212 -0.24 ALA 269

ASP 166 0.63 SER 213 -0.32 ALA 269

ASP 166 0.61 ASP 214 -0.37 ALA 269

ASP 166 0.57 LEU 215 -0.30 ALA 269

ASP 166 0.70 GLY 216 -0.21 ALA 269

ASP 166 0.87 GLY 217 -0.16 ALA 269

ASP 166 0.99 ASP 218 -0.16 ALA 269

ASP 166 1.25 ASN 219 -0.13 ALA 269

ASP 166 1.38 ILE 220 -0.12 ALA 269

ASP 166 1.61 PRO 221 -0.15 THR 51

ASP 166 1.21 ALA 222 -0.16 PRO 261

ASP 166 1.04 LYS 223 -0.13 ALA 269

ALA 163 1.04 PHE 224 -0.13 GLY 227

ALA 163 1.06 LEU 225 -0.17 ASN 50

ALA 163 0.75 GLU 226 -0.12 THR 51

ALA 163 0.64 GLY 227 -0.13 PHE 224

ALA 163 0.57 LEU 228 -0.14 ASN 50

ALA 163 0.53 THR 229 -0.11 LEU 228

ALA 163 0.45 LEU 230 -0.08 LYS 223

ALA 163 0.36 ARG 231 -0.11 GLY 227

ALA 163 0.31 THR 232 -0.08 ILE 49

ALA 163 0.31 ASN 233 -0.08 VAL 191

ASP 166 0.29 GLN 234 -0.14 ASN 209

ALA 163 0.24 THR 235 -0.11 PRO 182

ALA 163 0.21 PHE 236 -0.12 VAL 191

ASP 166 0.22 ARG 237 -0.13 PRO 253

ASP 166 0.20 ASP 238 -0.13 PRO 182

ALA 163 0.16 THR 239 -0.16 PRO 182

ALA 163 0.15 TYR 240 -0.14 PRO 182

ASP 166 0.16 ALA 241 -0.15 PRO 254

ALA 163 0.14 ALA 242 -0.16 PRO 182

ALA 163 0.11 ASP 243 -0.17 PRO 182

GLY 280 0.13 GLY 244 -0.14 PRO 182

ASP 166 0.13 GLY 245 -0.16 PRO 253

ASP 166 0.14 ARG 246 -0.19 PRO 253

ASP 166 0.15 ASN 247 -0.18 PRO 253

ASP 166 0.18 GLY 248 -0.21 PRO 253

ASP 166 0.22 VAL 249 -0.23 PRO 253

ASP 166 0.27 PHE 250 -0.26 PRO 253

ASP 166 0.33 ASN 251 -0.25 PRO 253

ASP 166 0.40 PHE 252 -0.21 ASN 255

ASP 166 0.46 PRO 253 -0.26 PHE 250

ASP 166 0.53 PRO 254 -0.20 PHE 250

ASP 166 0.58 ASN 255 -0.23 ALA 269

ASP 166 0.63 GLY 256 -0.23 ALA 269

ASP 166 0.74 THR 257 -0.17 ALA 269

SER 167 0.77 HIS 258 -0.15 SER 259

SER 167 0.67 SER 259 -0.16 LEU 225

ARG 39 0.49 TRP 260 -0.22 THR 51

SER 167 0.44 PRO 261 -0.19 GLU 56

ASP 166 0.44 TYR 262 -0.19 VAL 268

SER 167 0.35 TRP 263 -0.13 HIS 258

ARG 39 0.28 ASN 264 -0.16 ALA 53

ASP 166 0.32 GLU 265 -0.25 VAL 268

ASP 166 0.27 GLN 266 -0.21 ASP 214

ASP 166 0.21 LEU 267 -0.20 ASP 214

ASP 166 0.20 VAL 268 -0.31 ASP 214

ASP 166 0.22 ALA 269 -0.37 ASP 214

ASP 166 0.19 MET 270 -0.28 ASP 214

ASP 166 0.15 LYS 271 -0.29 ASP 214

ASP 166 0.14 ALA 272 -0.34 ASP 214

ASP 166 0.15 ASP 273 -0.30 ASP 214

ASP 166 0.13 ILE 274 -0.24 ASP 214

ASN 200 0.11 GLN 275 -0.26 ASP 214

ARG 246 0.14 HIS 276 -0.28 ASP 214

ASN 200 0.15 VAL 277 -0.23 ASP 214

ASN 200 0.14 LEU 278 -0.21 ASP 214

ASN 200 0.15 ASN 279 -0.23 ASP 214

ASN 200 0.16 GLY 280 -0.24 ASP 214

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.

*** 1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 240220092131172147

--- normal mode 8 ---

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

* 1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *