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 7 ---

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
GLN 59 0.10 ARG 1 -0.40 ILE 49

GLY 3 0.19 PRO 2 -0.36 ILE 49

PRO 2 0.19 GLY 3 -0.19 ASP 43

GLY 27 0.12 LEU 4 -0.14 ASP 214

GLY 27 0.08 PRO 5 -0.11 ASP 214

ASN 200 0.05 VAL 6 -0.12 PRO 2

ASN 219 0.11 GLU 7 -0.13 PRO 2

ASN 219 0.17 TYR 8 -0.20 PRO 2

ASN 219 0.19 LEU 9 -0.14 PRO 2

ASN 219 0.24 GLN 10 -0.16 GLY 168

PRO 221 0.25 VAL 11 -0.13 GLY 168

PRO 221 0.28 PRO 12 -0.13 GLY 168

PRO 221 0.34 SER 13 -0.11 ASN 88

PRO 221 0.35 ALA 14 -0.13 ASN 88

PRO 221 0.39 SER 15 -0.14 ASN 88

PRO 221 0.44 MET 16 -0.14 ASN 88

PRO 221 0.40 GLY 17 -0.17 ASN 88

PRO 221 0.38 ARG 18 -0.14 GLY 86

ASN 219 0.32 ASP 19 -0.16 GLY 168

ASN 219 0.32 ILE 20 -0.17 GLY 168

ASN 219 0.28 LYS 21 -0.19 PRO 2

ASN 219 0.22 VAL 22 -0.17 PRO 2

ASN 219 0.16 GLN 23 -0.21 PRO 2

ASN 219 0.11 PHE 24 -0.12 PRO 2

ASN 200 0.06 GLN 25 -0.10 ASP 214

GLY 3 0.09 GLY 26 -0.14 ASP 214

GLY 3 0.14 GLY 27 -0.19 ASP 214

GLY 3 0.12 GLY 28 -0.20 ASP 214

ASN 199 0.10 PRO 29 -0.17 ASP 214

ASN 199 0.11 HIS 30 -0.18 ASP 214

PRO 221 0.09 ALA 31 -0.15 ASP 214

PRO 221 0.09 VAL 32 -0.14 ASP 214

PRO 221 0.15 TYR 33 -0.10 ARG 1

PRO 221 0.15 LEU 34 -0.15 ARG 1

PRO 221 0.24 LEU 35 -0.18 ARG 1

ASN 219 0.31 ASP 36 -0.21 ARG 1

ALA 222 0.42 GLY 37 -0.23 LEU 159

ALA 222 0.72 LEU 38 -0.27 LEU 159

ASN 219 0.75 ARG 39 -0.28 LEU 159

ASN 219 0.55 ALA 40 -0.25 PRO 2

ASN 219 0.54 GLN 41 -0.28 PRO 2

ASN 219 0.47 ASP 42 -0.29 PRO 2

ASN 219 0.36 ASP 43 -0.34 PRO 2

ASN 219 0.29 TYR 44 -0.35 PRO 2

ASN 219 0.26 ASN 45 -0.29 PRO 2

GLY 217 0.29 GLY 46 -0.28 ARG 1

GLY 217 0.14 TRP 47 -0.29 ARG 1

GLY 216 0.11 ASP 48 -0.38 ARG 1

GLY 216 0.21 ILE 49 -0.40 ARG 1

LEU 215 0.22 ASN 50 -0.37 ARG 1

GLN 87 0.12 THR 51 -0.32 ARG 1

GLN 87 0.09 PRO 52 -0.30 ARG 1

GLN 87 0.07 ALA 53 -0.18 ARG 1

ASP 273 0.06 PHE 54 -0.13 ASP 214

ASP 273 0.08 GLU 55 -0.20 ASP 214

LYS 271 0.11 GLU 56 -0.28 ASP 214

ILE 274 0.11 TYR 57 -0.25 ASP 214

GLN 275 0.11 TYR 58 -0.25 ASP 214

GLY 3 0.16 GLN 59 -0.27 ASP 214

GLN 275 0.15 SER 60 -0.30 ASP 214

GLY 3 0.14 GLY 61 -0.26 ASP 214

ASN 200 0.11 LEU 62 -0.22 ASP 214

ASN 199 0.08 SER 63 -0.16 ASP 214

PRO 221 0.07 VAL 64 -0.12 ASP 214

PRO 221 0.13 ILE 65 -0.11 PRO 2

ASN 219 0.18 MET 66 -0.18 PRO 2

ASN 219 0.26 PRO 67 -0.19 PRO 2

ASN 219 0.33 VAL 68 -0.24 PRO 2

ASN 219 0.46 GLY 69 -0.23 PRO 2

PRO 221 0.53 GLY 70 -0.20 PRO 2

PRO 221 0.70 GLN 71 -0.22 PRO 2

PRO 221 0.78 SER 72 -0.19 PRO 2

PRO 221 0.60 SER 73 -0.18 PRO 2

PRO 221 0.50 PHE 74 -0.17 PRO 2

PRO 221 0.42 TYR 75 -0.15 PRO 2

PRO 221 0.42 THR 76 -0.13 PRO 2

PRO 221 0.44 ASP 77 -0.18 TYR 134

PRO 221 0.51 TRP 78 -0.15 TYR 134

PRO 221 0.49 TYR 79 -0.17 TYR 134

PRO 221 0.55 GLN 80 -0.15 TYR 134

PRO 221 0.62 PRO 81 -0.12 TYR 134

PRO 221 0.73 SER 82 -0.14 PRO 2

PRO 221 0.73 GLN 83 -0.13 PRO 2

PRO 221 0.84 SER 84 -0.15 PRO 2

PRO 221 0.85 ASN 85 -0.16 PRO 2

ILE 220 0.74 GLY 86 -0.15 GLY 17

PRO 221 0.71 GLN 87 -0.16 GLY 17

PRO 221 0.61 ASN 88 -0.17 GLY 17

PRO 221 0.56 TYR 89 -0.13 MET 16

PRO 221 0.54 THR 90 -0.14 TYR 134

PRO 221 0.53 TYR 91 -0.13 PRO 2

PRO 221 0.44 LYS 92 -0.14 TYR 134

PRO 221 0.41 TRP 93 -0.13 PRO 2

PRO 221 0.35 GLU 94 -0.11 LYS 92

PRO 221 0.33 THR 95 -0.12 TYR 135

PRO 221 0.32 PHE 96 -0.10 PRO 2

PRO 221 0.28 LEU 97 -0.10 PRO 2

PRO 221 0.25 THR 98 -0.11 THR 95

PRO 221 0.26 ARG 99 -0.12 THR 114

PRO 221 0.27 GLU 100 -0.11 PRO 113

PRO 221 0.24 MET 101 -0.09 GLY 168

PRO 221 0.20 PRO 102 -0.09 ALA 14

PRO 221 0.20 ALA 103 -0.13 ALA 14

PRO 221 0.20 TRP 104 -0.10 ALA 14

PRO 221 0.16 LEU 105 -0.08 GLY 168

PRO 221 0.15 GLN 106 -0.09 ASN 279

PRO 221 0.15 ALA 107 -0.09 ASN 88

PRO 221 0.14 ASN 108 -0.08 GLY 168

PRO 221 0.11 LYS 109 -0.09 ASP 214

PRO 221 0.10 GLY 110 -0.12 ASP 214

PRO 221 0.11 VAL 111 -0.12 ASP 214

PRO 221 0.12 SER 112 -0.12 ASP 214

PRO 221 0.16 PRO 113 -0.12 ARG 99

PRO 221 0.13 THR 114 -0.12 ARG 99

ASN 199 0.12 GLY 115 -0.16 ASP 214

PRO 221 0.11 ASN 116 -0.14 ASP 214

PRO 221 0.10 ALA 117 -0.14 ASP 214

PRO 221 0.15 ALA 118 -0.09 GLN 266

PRO 221 0.12 VAL 119 -0.11 ARG 1

PRO 221 0.19 GLY 120 -0.16 ARG 1

SER 167 0.22 LEU 121 -0.19 ARG 1

SER 167 0.31 SER 122 -0.21 ARG 1

PRO 221 0.44 MET 123 -0.20 TRP 156

PRO 221 0.32 SER 124 -0.17 ARG 1

PRO 221 0.21 GLY 125 -0.16 ARG 1

PRO 221 0.25 GLY 126 -0.15 ARG 1

PRO 221 0.29 SER 127 -0.14 ARG 1

PRO 221 0.21 ALA 128 -0.12 ARG 1

PRO 221 0.18 LEU 129 -0.10 VAL 205

PRO 221 0.23 ILE 130 -0.10 TYR 79

PRO 221 0.23 LEU 131 -0.12 ASP 77

PRO 221 0.17 ALA 132 -0.10 ILE 203

PRO 221 0.17 ALA 133 -0.13 TYR 79

PRO 221 0.19 TYR 134 -0.18 ASP 77

PRO 221 0.19 TYR 135 -0.13 ASP 77

PRO 221 0.15 PRO 136 -0.15 THR 201

PRO 221 0.13 GLN 137 -0.12 PRO 253

PRO 221 0.16 GLN 138 -0.12 ARG 99

PRO 221 0.15 PHE 139 -0.11 ASP 214

ASN 199 0.13 PRO 140 -0.14 ASP 214

SER 60 0.10 TYR 141 -0.15 ASP 214

ALA 163 0.13 ALA 142 -0.12 ASP 214

ASP 166 0.16 ALA 143 -0.12 ASP 214

ASP 166 0.20 SER 144 -0.13 ARG 1

ASP 166 0.28 LEU 145 -0.15 ARG 1

ALA 163 0.39 SER 146 -0.17 ARG 1

ALA 163 0.31 GLY 147 -0.19 ARG 1

ALA 163 0.28 PHE 148 -0.19 ARG 1

ALA 163 0.21 LEU 149 -0.15 ARG 1

PRO 221 0.16 ASN 150 -0.16 ARG 1

PRO 221 0.27 PRO 151 -0.18 ARG 1

PRO 221 0.23 SER 152 -0.16 ARG 1

VAL 191 0.17 GLU 153 -0.16 ARG 1

VAL 191 0.13 SER 154 -0.18 ARG 1

PHE 224 0.22 TRP 155 -0.21 ARG 39

PHE 224 0.28 TRP 156 -0.23 GLY 37

PRO 221 0.41 PRO 157 -0.19 ARG 39

PHE 224 0.49 THR 158 -0.21 ARG 39

PHE 224 0.62 LEU 159 -0.28 ARG 39

LEU 225 0.67 ILE 160 -0.27 ARG 39

PRO 221 0.82 GLY 161 -0.19 PRO 2

PRO 221 1.01 LEU 162 -0.20 PRO 2

PRO 221 1.20 ALA 163 -0.23 ARG 39

PRO 221 1.11 MET 164 -0.20 PRO 2

PRO 221 1.20 ASN 165 -0.19 PRO 2

PRO 221 1.56 ASP 166 -0.21 PRO 2

PRO 221 1.35 SER 167 -0.22 PRO 2

PRO 221 1.10 GLY 168 -0.22 PRO 2

PRO 221 1.08 GLY 169 -0.19 PRO 2

PRO 221 0.95 TYR 170 -0.18 PRO 2

PRO 221 0.83 ASN 171 -0.16 PRO 2

PRO 221 0.70 ALA 172 -0.16 PRO 2

PRO 221 0.61 ASN 173 -0.14 PRO 2

PRO 221 0.63 SER 174 -0.13 PRO 2

PRO 221 0.58 MET 175 -0.14 PRO 2

PRO 221 0.48 TRP 176 -0.13 PRO 2

PRO 221 0.48 GLY 177 -0.12 PRO 2

PRO 221 0.43 PRO 178 -0.13 PRO 2

PRO 221 0.35 SER 179 -0.15 PRO 2

PRO 221 0.28 SER 180 -0.12 PRO 2

PRO 221 0.33 ASP 181 -0.11 PRO 2

PRO 221 0.28 PRO 182 -0.15 PRO 194

PRO 221 0.33 ALA 183 -0.13 PRO 194

PRO 221 0.32 TRP 184 -0.13 ARG 1

PRO 221 0.23 LYS 185 -0.12 MET 190

PRO 221 0.25 ARG 186 -0.14 TYR 79

PRO 221 0.29 ASN 187 -0.12 ARG 1

PRO 221 0.22 ASP 188 -0.13 ARG 1

PRO 221 0.16 PRO 189 -0.12 ARG 1

ALA 163 0.13 MET 190 -0.12 LYS 185

GLU 153 0.17 VAL 191 -0.14 PRO 182

PRO 221 0.15 GLN 192 -0.15 ILE 193

PRO 221 0.11 ILE 193 -0.15 GLN 192

GLY 280 0.11 PRO 194 -0.15 TYR 79

PRO 221 0.13 ARG 195 -0.16 TYR 79

GLY 280 0.12 LEU 196 -0.12 TYR 79

GLY 280 0.14 VAL 197 -0.13 PRO 253

GLY 280 0.16 ALA 198 -0.15 TYR 79

GLY 280 0.17 ASN 199 -0.14 TYR 79

GLY 280 0.19 ASN 200 -0.15 PRO 253

VAL 277 0.14 THR 201 -0.15 PRO 136

ALA 163 0.13 ARG 202 -0.17 PRO 253

ALA 163 0.16 ILE 203 -0.15 PRO 253

ASP 166 0.19 TRP 204 -0.17 PRO 253

ALA 163 0.24 VAL 205 -0.11 ASP 214

ASP 166 0.32 TYR 206 -0.12 ASP 214

ALA 163 0.42 CYS 207 -0.13 ARG 1

ASP 166 0.52 GLY 208 -0.13 ALA 269

ASP 166 0.61 ASN 209 -0.22 PHE 252

ASP 166 0.76 GLY 210 -0.16 ARG 1

ASP 166 0.73 THR 211 -0.21 ALA 269

ASP 166 0.72 PRO 212 -0.25 ALA 269

ASP 166 0.59 SER 213 -0.34 ALA 269

ASP 166 0.56 ASP 214 -0.39 ALA 269

ASP 166 0.52 LEU 215 -0.31 ALA 269

ASP 166 0.65 GLY 216 -0.22 ALA 269

SER 167 0.81 GLY 217 -0.20 ARG 1

ASP 166 0.91 ASP 218 -0.18 ALA 269

ASP 166 1.14 ASN 219 -0.19 ARG 1

ASP 166 1.33 ILE 220 -0.18 ARG 1

ASP 166 1.56 PRO 221 -0.22 ARG 1

ASP 166 1.12 ALA 222 -0.23 ARG 1

ASP 166 1.01 LYS 223 -0.19 ARG 1

ALA 163 1.08 PHE 224 -0.20 ARG 1

ALA 163 1.10 LEU 225 -0.23 ARG 1

ALA 163 0.77 GLU 226 -0.19 ARG 1

ALA 163 0.68 GLY 227 -0.16 ARG 1

ALA 163 0.66 LEU 228 -0.20 ARG 1

ALA 163 0.56 THR 229 -0.18 ARG 1

ALA 163 0.46 LEU 230 -0.14 ARG 1

ALA 163 0.38 ARG 231 -0.13 ARG 1

ALA 163 0.33 THR 232 -0.14 ARG 1

ALA 163 0.32 ASN 233 -0.12 ARG 1

ALA 163 0.29 GLN 234 -0.13 ASN 209

ALA 163 0.25 THR 235 -0.09 ARG 1

ALA 163 0.22 PHE 236 -0.11 VAL 191

ALA 163 0.22 ARG 237 -0.12 ASN 209

ALA 163 0.20 ASP 238 -0.12 ASN 209

ALA 163 0.17 THR 239 -0.13 PRO 182

ALA 163 0.16 TYR 240 -0.12 PRO 253

ALA 163 0.16 ALA 241 -0.15 PRO 254

ALA 163 0.14 ALA 242 -0.13 PRO 182

ALA 163 0.12 ASP 243 -0.14 PRO 182

GLY 280 0.14 GLY 244 -0.13 PRO 254

GLY 280 0.13 GLY 245 -0.16 PRO 253

HIS 276 0.15 ARG 246 -0.19 PRO 253

HIS 276 0.15 ASN 247 -0.19 PRO 253

ALA 163 0.17 GLY 248 -0.21 PRO 253

ASP 166 0.20 VAL 249 -0.24 PRO 253

ASP 166 0.25 PHE 250 -0.27 PRO 253

ASP 166 0.30 ASN 251 -0.26 PRO 253

ASP 166 0.37 PHE 252 -0.22 ASN 209

ASP 166 0.43 PRO 253 -0.27 PHE 250

ASP 166 0.51 PRO 254 -0.20 PHE 250

ASP 166 0.56 ASN 255 -0.24 ALA 269

ASP 166 0.59 GLY 256 -0.24 ALA 269

ASP 166 0.70 THR 257 -0.20 ARG 1

SER 167 0.73 HIS 258 -0.23 ARG 1

SER 167 0.60 SER 259 -0.26 ARG 1

ARG 39 0.43 TRP 260 -0.30 ARG 1

ARG 39 0.38 PRO 261 -0.24 ARG 1

ASP 166 0.40 TYR 262 -0.19 ARG 1

SER 167 0.30 TRP 263 -0.19 ARG 1

ARG 39 0.23 ASN 264 -0.19 ARG 1

ASP 166 0.28 GLU 265 -0.26 ASP 214

ASP 166 0.24 GLN 266 -0.22 ASP 214

ASP 166 0.18 LEU 267 -0.20 ASP 214

ASP 166 0.17 VAL 268 -0.32 ASP 214

ASP 166 0.19 ALA 269 -0.39 ASP 214

ASP 166 0.17 MET 270 -0.29 ASP 214

ASP 166 0.13 LYS 271 -0.31 ASP 214

ASP 273 0.15 ALA 272 -0.36 ASP 214

ALA 272 0.15 ASP 273 -0.31 ASP 214

SER 60 0.12 ILE 274 -0.25 ASP 214

SER 60 0.15 GLN 275 -0.28 ASP 214

ASN 200 0.16 HIS 276 -0.29 ASP 214

ASN 200 0.17 VAL 277 -0.24 ASP 214

ASN 200 0.15 LEU 278 -0.22 ASP 214

ASN 200 0.17 ASN 279 -0.24 ASP 214

ASN 200 0.19 GLY 280 -0.25 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.

*** EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 24021912402138273

--- normal mode 7 ---

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

* EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *