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 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
GLU 7 0.38 ARG 1 -0.75 LEU 215

GLU 7 0.36 PRO 2 -0.67 GLY 216

GLY 27 0.27 GLY 3 -0.51 GLY 216

GLY 27 0.29 LEU 4 -0.45 GLY 216

PRO 2 0.34 PRO 5 -0.36 ASN 219

ARG 1 0.33 VAL 6 -0.39 ASN 219

ARG 1 0.38 GLU 7 -0.36 ASN 219

ARG 1 0.33 TYR 8 -0.39 ASN 219

ARG 1 0.30 LEU 9 -0.36 ASN 219

ARG 1 0.26 GLN 10 -0.37 ASN 219

PRO 2 0.23 VAL 11 -0.34 ASN 219

PRO 182 0.23 PRO 12 -0.32 ASN 219

TYR 79 0.26 SER 13 -0.31 ASN 219

TYR 79 0.33 ALA 14 -0.27 ASN 219

TYR 79 0.36 SER 15 -0.27 PRO 221

TYR 79 0.30 MET 16 -0.29 PRO 221

TYR 79 0.32 GLY 17 -0.28 ASN 219

TYR 79 0.23 ARG 18 -0.32 ASN 219

ARG 1 0.22 ASP 19 -0.35 ASN 219

LYS 21 0.24 ILE 20 -0.38 ASN 219

ILE 20 0.24 LYS 21 -0.39 ASN 219

ARG 1 0.19 VAL 22 -0.37 ASN 219

ARG 1 0.19 GLN 23 -0.38 ASN 219

ARG 1 0.21 PHE 24 -0.33 ASN 219

PRO 2 0.20 GLN 25 -0.31 ASN 219

LEU 4 0.25 GLY 26 -0.26 ASN 219

LEU 4 0.29 GLY 27 -0.21 ASN 219

GLY 3 0.23 GLY 28 -0.18 ASN 219

GLY 3 0.22 PRO 29 -0.18 ASN 219

LEU 4 0.17 HIS 30 -0.17 PRO 221

LEU 4 0.17 ALA 31 -0.19 ASN 219

PRO 182 0.11 VAL 32 -0.21 PRO 221

PRO 182 0.12 TYR 33 -0.25 PRO 221

GLN 87 0.09 LEU 34 -0.29 ASN 219

GLN 87 0.10 LEU 35 -0.33 PRO 221

GLN 87 0.13 ASP 36 -0.41 PRO 221

LEU 121 0.13 GLY 37 -0.51 PRO 221

GLY 147 0.20 LEU 38 -0.64 PRO 221

GLN 87 0.19 ARG 39 -0.60 ASN 219

GLN 87 0.20 ALA 40 -0.49 ASN 219

ASN 88 0.25 GLN 41 -0.54 ASN 219

ASN 88 0.32 ASP 42 -0.47 ASN 219

ASN 88 0.30 ASP 43 -0.50 ASN 219

ASN 88 0.23 TYR 44 -0.51 ASN 219

ASN 88 0.18 ASN 45 -0.47 ASN 219

GLN 87 0.17 GLY 46 -0.54 ASN 219

GLN 87 0.15 TRP 47 -0.42 ASN 219

ASN 88 0.17 ASP 48 -0.44 ASN 219

ASN 88 0.18 ILE 49 -0.52 ASN 219

ASN 88 0.15 ASN 50 -0.55 GLY 217

ASN 88 0.14 THR 51 -0.52 ARG 1

ASN 88 0.16 PRO 52 -0.56 ARG 1

ASN 88 0.13 ALA 53 -0.42 PRO 261

GLU 55 0.33 PHE 54 -0.33 PRO 261

PHE 54 0.33 GLU 55 -0.34 LEU 215

ASN 88 0.12 GLU 56 -0.29 GLU 265

ASN 88 0.10 TYR 57 -0.23 PRO 261

GLY 61 0.12 TYR 58 -0.26 PRO 261

GLY 3 0.19 GLN 59 -0.19 GLY 217

GLY 3 0.13 SER 60 -0.14 ASN 219

GLY 3 0.19 GLY 61 -0.15 ASN 219

LEU 4 0.17 LEU 62 -0.17 ASN 219

LEU 4 0.20 SER 63 -0.22 ASN 219

PRO 182 0.12 VAL 64 -0.27 ASN 219

PRO 182 0.14 ILE 65 -0.29 ASN 219

ASN 88 0.13 MET 66 -0.36 ASN 219

LYS 92 0.14 PRO 67 -0.37 ASN 219

ASN 88 0.20 VAL 68 -0.43 ASN 219

ASN 88 0.21 GLY 69 -0.42 ASN 219

GLN 87 0.15 GLY 70 -0.41 PRO 221

GLN 87 0.19 GLN 71 -0.45 PRO 221

GLY 147 0.15 SER 72 -0.53 PRO 221

LEU 149 0.09 SER 73 -0.46 PRO 221

LEU 149 0.11 PHE 74 -0.46 PRO 221

ALA 183 0.10 TYR 75 -0.39 PRO 221

ALA 183 0.19 THR 76 -0.37 PRO 221

ALA 183 0.24 ASP 77 -0.34 PRO 221

GLY 177 0.22 TRP 78 -0.37 PRO 221

SER 15 0.36 TYR 79 -0.36 PRO 221

GLY 17 0.26 GLN 80 -0.33 PRO 221

ASP 42 0.18 PRO 81 -0.31 PRO 221

ASP 42 0.11 SER 82 -0.34 PRO 221

ASP 42 0.09 GLN 83 -0.32 ILE 220

ARG 231 0.12 SER 84 -0.33 ILE 220

ARG 231 0.14 ASN 85 -0.31 ILE 220

GLN 41 0.18 GLY 86 -0.25 ILE 220

ASP 42 0.29 GLN 87 -0.26 ILE 220

ASP 42 0.32 ASN 88 -0.23 ILE 220

ASP 42 0.26 TYR 89 -0.26 ILE 220

GLY 17 0.23 THR 90 -0.30 PRO 221

LYS 21 0.17 TYR 91 -0.34 PRO 221

GLY 177 0.21 LYS 92 -0.31 PRO 221

ALA 183 0.21 TRP 93 -0.34 PRO 221

ALA 183 0.28 GLU 94 -0.31 PRO 221

ALA 183 0.37 THR 95 -0.29 PRO 221

PRO 182 0.27 PHE 96 -0.31 PRO 221

PRO 182 0.25 LEU 97 -0.29 PRO 221

PRO 182 0.32 THR 98 -0.25 PRO 221

PRO 182 0.38 ARG 99 -0.24 PRO 221

PRO 182 0.32 GLU 100 -0.27 PRO 221

PRO 182 0.26 MET 101 -0.29 ASN 219

PRO 182 0.29 PRO 102 -0.24 ASN 219

PRO 182 0.33 ALA 103 -0.24 ASN 219

PRO 182 0.28 TRP 104 -0.27 ASN 219

PRO 182 0.24 LEU 105 -0.27 ASN 219

PRO 182 0.27 GLN 106 -0.23 ASN 219

PRO 182 0.28 ALA 107 -0.24 ASN 219

PRO 2 0.27 ASN 108 -0.27 ASN 219

PRO 2 0.29 LYS 109 -0.26 ASN 219

PRO 2 0.25 GLY 110 -0.22 ASN 219

PRO 5 0.23 VAL 111 -0.22 ASN 219

PRO 182 0.23 SER 112 -0.19 PRO 221

PRO 182 0.27 PRO 113 -0.20 PRO 221

TYR 134 0.23 THR 114 -0.18 PRO 221

PRO 182 0.17 GLY 115 -0.15 PRO 221

GLY 26 0.16 ASN 116 -0.18 PRO 221

GLY 26 0.10 ALA 117 -0.17 PRO 221

PRO 182 0.09 ALA 118 -0.21 PRO 221

SER 167 0.08 VAL 119 -0.21 PRO 221

SER 167 0.11 GLY 120 -0.27 PRO 221

SER 167 0.17 LEU 121 -0.29 PRO 221

SER 167 0.23 SER 122 -0.38 PRO 221

SER 167 0.23 MET 123 -0.50 PRO 221

SER 167 0.14 SER 124 -0.38 PRO 221

SER 167 0.18 GLY 125 -0.28 PRO 221

ASP 166 0.18 GLY 126 -0.30 PRO 221

ASP 166 0.12 SER 127 -0.32 PRO 221

GLU 153 0.10 ALA 128 -0.25 PRO 221

GLU 153 0.14 LEU 129 -0.22 PRO 221

LEU 131 0.20 ILE 130 -0.26 PRO 221

ILE 130 0.20 LEU 131 -0.25 PRO 221

GLU 153 0.19 ALA 132 -0.19 PRO 221

GLU 153 0.23 ALA 133 -0.20 PRO 221

TYR 135 0.33 TYR 134 -0.23 PRO 221

TYR 134 0.33 TYR 135 -0.21 PRO 221

GLU 153 0.20 PRO 136 -0.16 PRO 221

TYR 134 0.22 GLN 137 -0.16 PRO 221

TYR 134 0.23 GLN 138 -0.19 PRO 221

GLY 26 0.16 PHE 139 -0.17 PRO 221

GLU 153 0.15 PRO 140 -0.13 PRO 221

PRO 253 0.15 TYR 141 -0.12 PRO 221

PRO 253 0.13 ALA 142 -0.15 PRO 221

ASP 166 0.12 ALA 143 -0.13 PRO 221

SER 167 0.16 SER 144 -0.18 ARG 1

SER 167 0.18 LEU 145 -0.25 ARG 1

SER 167 0.22 SER 146 -0.28 ARG 1

SER 167 0.28 GLY 147 -0.24 SER 146

ALA 163 0.34 PHE 148 -0.31 PRO 221

ALA 163 0.27 LEU 149 -0.27 PRO 221

ALA 163 0.25 ASN 150 -0.33 LEU 225

ALA 163 0.19 PRO 151 -0.50 PRO 221

TRP 155 0.23 SER 152 -0.46 PRO 221

VAL 191 0.41 GLU 153 -0.48 LEU 225

VAL 191 0.31 SER 154 -0.62 PHE 224

VAL 191 0.28 TRP 155 -0.75 PHE 224

VAL 191 0.21 TRP 156 -0.68 LEU 225

VAL 191 0.16 PRO 157 -0.68 PRO 221

ASN 173 0.15 THR 158 -0.76 PRO 221

ASN 150 0.17 LEU 159 -0.94 PRO 221

ASN 150 0.19 ILE 160 -0.82 PRO 221

ASN 150 0.14 GLY 161 -0.70 PRO 221

THR 232 0.20 LEU 162 -0.79 PRO 221

PHE 148 0.34 ALA 163 -0.85 PRO 221

PHE 148 0.25 MET 164 -0.63 PRO 221

THR 232 0.21 ASN 165 -0.51 ILE 220

LEU 228 0.33 ASP 166 -0.54 ILE 220

LEU 228 0.29 SER 167 -0.51 ILE 220

LEU 228 0.22 GLY 168 -0.39 ILE 220

ARG 231 0.19 GLY 169 -0.40 ILE 220

THR 232 0.15 TYR 170 -0.43 PRO 221

GLY 161 0.13 ASN 171 -0.47 PRO 221

SER 15 0.11 ALA 172 -0.54 PRO 221

SER 15 0.16 ASN 173 -0.47 PRO 221

SER 15 0.16 SER 174 -0.41 PRO 221

TRP 78 0.18 MET 175 -0.44 PRO 221

THR 95 0.25 TRP 176 -0.45 PRO 221

SER 15 0.27 GLY 177 -0.45 PRO 221

SER 15 0.22 PRO 178 -0.51 PRO 221

THR 95 0.22 SER 179 -0.55 PRO 221

ARG 99 0.27 SER 180 -0.48 PRO 221

THR 95 0.32 ASP 181 -0.45 PRO 221

ARG 99 0.38 PRO 182 -0.39 PRO 221

THR 95 0.37 ALA 183 -0.40 PRO 221

THR 95 0.26 TRP 184 -0.46 PRO 221

SER 154 0.27 LYS 185 -0.38 PRO 221

ARG 99 0.27 ARG 186 -0.35 PRO 221

ARG 99 0.22 ASN 187 -0.37 PRO 221

GLU 153 0.26 ASP 188 -0.35 PRO 221

GLU 153 0.23 PRO 189 -0.25 PRO 221

GLU 153 0.28 MET 190 -0.20 PRO 221

GLU 153 0.41 VAL 191 -0.23 PRO 221

GLU 153 0.29 GLN 192 -0.22 PRO 221

GLU 153 0.25 ILE 193 -0.15 TYR 79

GLU 153 0.24 PRO 194 -0.18 TYR 79

GLU 153 0.23 ARG 195 -0.19 TYR 79

GLU 153 0.19 LEU 196 -0.15 TYR 79

GLU 153 0.18 VAL 197 -0.15 TYR 79

GLU 153 0.18 ALA 198 -0.18 TYR 79

GLU 153 0.17 ASN 199 -0.16 TYR 79

PRO 253 0.19 ASN 200 -0.13 TYR 79

PRO 253 0.18 THR 201 -0.11 TYR 79

PRO 253 0.22 ARG 202 -0.09 TYR 79

PRO 253 0.20 ILE 203 -0.10 ARG 1

PRO 253 0.21 TRP 204 -0.16 ARG 1

ASP 166 0.17 VAL 205 -0.21 ARG 1

SER 213 0.18 TYR 206 -0.28 ARG 1

ASP 166 0.18 CYS 207 -0.32 ARG 1

LYS 223 0.20 GLY 208 -0.40 ARG 1

PHE 252 0.34 ASN 209 -0.40 ARG 1

LYS 223 0.26 GLY 210 -0.48 TRP 155

PHE 252 0.30 THR 211 -0.48 ARG 1

PHE 252 0.24 PRO 212 -0.56 ARG 1

PHE 250 0.28 SER 213 -0.61 ARG 1

ALA 269 0.29 ASP 214 -0.71 ARG 1

ALA 269 0.20 LEU 215 -0.75 ARG 1

ALA 269 0.13 GLY 216 -0.73 ARG 1

PHE 252 0.10 GLY 217 -0.64 ARG 1

PHE 252 0.18 ASP 218 -0.61 ARG 1

THR 211 0.19 ASN 219 -0.66 LEU 159

GLY 210 0.21 ILE 220 -0.79 LEU 159

GLY 227 0.14 PRO 221 -0.94 LEU 159

PHE 252 0.08 ALA 222 -0.70 LEU 159

GLY 210 0.26 LYS 223 -0.61 LEU 159

GLY 227 0.24 PHE 224 -0.75 TRP 155

ASP 166 0.17 LEU 225 -0.68 TRP 155

ASP 166 0.15 GLU 226 -0.49 TRP 155

PHE 224 0.24 GLY 227 -0.45 TRP 155

ASP 166 0.33 LEU 228 -0.57 SER 154

ASP 166 0.32 THR 229 -0.38 SER 154

ASP 166 0.25 LEU 230 -0.29 ARG 1

ASP 166 0.30 ARG 231 -0.26 ARG 1

ALA 163 0.31 THR 232 -0.22 ARG 1

ASP 166 0.25 ASN 233 -0.22 ARG 1

ASP 166 0.24 GLN 234 -0.23 ARG 1

ALA 163 0.25 THR 235 -0.19 ARG 1

ALA 163 0.23 PHE 236 -0.17 ARG 1

ASN 209 0.20 ARG 237 -0.18 ARG 1

ASP 166 0.20 ASP 238 -0.17 ARG 1

ALA 163 0.20 THR 239 -0.14 ARG 1

GLU 153 0.17 TYR 240 -0.12 ARG 1

PRO 254 0.24 ALA 241 -0.13 ARG 1

PRO 254 0.19 ALA 242 -0.12 ARG 1

GLU 153 0.18 ASP 243 -0.13 TYR 79

PRO 254 0.22 GLY 244 -0.13 TYR 79

PRO 254 0.22 GLY 245 -0.13 TYR 79

PRO 253 0.31 ARG 246 -0.11 TYR 79

PRO 253 0.27 ASN 247 -0.10 TYR 79

PRO 253 0.30 GLY 248 -0.12 ARG 1

PRO 253 0.33 VAL 249 -0.18 ARG 1

PRO 253 0.38 PHE 250 -0.23 ARG 1

PRO 253 0.35 ASN 251 -0.30 ARG 1

ASN 209 0.34 PHE 252 -0.34 ARG 1

PHE 250 0.38 PRO 253 -0.40 ARG 1

PHE 250 0.30 PRO 254 -0.44 ARG 1

PHE 252 0.32 ASN 255 -0.47 ARG 1

PHE 250 0.23 GLY 256 -0.49 ARG 1

PHE 250 0.16 THR 257 -0.46 ARG 1

PHE 250 0.08 HIS 258 -0.44 LEU 159

GLY 86 0.09 SER 259 -0.44 GLY 217

GLN 87 0.09 TRP 260 -0.47 ARG 1

ALA 269 0.09 PRO 261 -0.64 ARG 1

ALA 269 0.13 TYR 262 -0.50 ARG 1

GLN 87 0.10 TRP 263 -0.37 ARG 1

ASN 50 0.13 ASN 264 -0.44 ARG 1

ALA 269 0.21 GLU 265 -0.47 ARG 1

ASP 214 0.17 GLN 266 -0.33 ARG 1

ASN 50 0.14 LEU 267 -0.24 ARG 1

ASN 50 0.14 VAL 268 -0.26 ARG 1

ASP 214 0.29 ALA 269 -0.25 ARG 1

ASP 214 0.22 MET 270 -0.17 ARG 1

ASP 214 0.16 LYS 271 -0.11 ARG 1

ASP 214 0.23 ALA 272 -0.09 VAL 249

ASP 214 0.25 ASP 273 -0.08 ARG 1

ASP 214 0.17 ILE 274 -0.08 PRO 221

ASP 214 0.15 GLN 275 -0.07 PRO 221

ASP 214 0.22 HIS 276 -0.08 ARG 99

ASP 214 0.19 VAL 277 -0.09 ARG 99

ASN 199 0.14 LEU 278 -0.10 ARG 99

GLY 3 0.15 ASN 279 -0.10 SER 112

ASP 214 0.18 GLY 280 -0.11 ARG 99

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 10 ---

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

* EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *