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 13 ---

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
PRO 5 0.17 ARG 1 -1.02 ASP 214

GLY 3 0.54 PRO 2 -0.89 ASP 214

PRO 2 0.54 GLY 3 -0.75 ASP 214

GLY 27 0.24 LEU 4 -0.65 ASP 214

PRO 221 0.24 PRO 5 -0.55 ASP 214

PRO 221 0.29 VAL 6 -0.54 ASP 214

PRO 221 0.32 GLU 7 -0.49 ASP 214

PRO 221 0.38 TYR 8 -0.46 ASP 214

PRO 221 0.36 LEU 9 -0.41 ASP 214

PRO 221 0.37 GLN 10 -0.37 ASP 214

PRO 221 0.35 VAL 11 -0.32 ASP 214

PRO 221 0.33 PRO 12 -0.29 ASP 214

PRO 221 0.31 SER 13 -0.27 ASP 214

PRO 221 0.28 ALA 14 -0.24 ASP 214

PRO 221 0.27 SER 15 -0.24 PRO 2

PRO 221 0.30 MET 16 -0.29 PRO 2

PRO 221 0.30 GLY 17 -0.28 PRO 2

PRO 221 0.32 ARG 18 -0.33 PRO 2

PRO 221 0.36 ASP 19 -0.33 ASP 214

PRO 221 0.40 ILE 20 -0.35 PRO 2

PRO 221 0.43 LYS 21 -0.39 ASP 214

PRO 221 0.40 VAL 22 -0.39 ASP 214

PRO 221 0.39 GLN 23 -0.45 ASP 214

PRO 221 0.32 PHE 24 -0.43 ASP 214

PRO 221 0.28 GLN 25 -0.44 ASP 214

PRO 221 0.25 GLY 26 -0.38 ASP 214

GLY 3 0.32 GLY 27 -0.35 ASP 214

GLY 3 0.27 GLY 28 -0.31 PRO 253

GLY 3 0.22 PRO 29 -0.25 PRO 253

PRO 221 0.20 HIS 30 -0.25 PRO 253

PRO 221 0.24 ALA 31 -0.25 PRO 253

PRO 221 0.25 VAL 32 -0.26 PRO 253

PRO 221 0.31 TYR 33 -0.23 ASP 214

PRO 221 0.36 LEU 34 -0.29 PRO 261

PRO 221 0.41 LEU 35 -0.28 PRO 261

PRO 221 0.54 ASP 36 -0.33 PRO 261

PRO 221 0.64 GLY 37 -0.32 PRO 2

PRO 221 0.70 LEU 38 -0.31 PRO 2

PRO 221 0.78 ARG 39 -0.39 GLY 216

PRO 221 0.63 ALA 40 -0.40 PRO 2

PRO 221 0.63 GLN 41 -0.47 PRO 2

PRO 221 0.53 ASP 42 -0.44 PRO 2

PRO 221 0.55 ASP 43 -0.54 PRO 2

PRO 221 0.54 TYR 44 -0.58 PRO 2

PRO 221 0.55 ASN 45 -0.48 PRO 2

PRO 221 0.60 GLY 46 -0.51 PRO 2

PRO 221 0.46 TRP 47 -0.53 PRO 261

PRO 221 0.44 ASP 48 -0.58 ASP 214

PRO 221 0.53 ILE 49 -0.73 PRO 2

PRO 221 0.48 ASN 50 -0.74 LEU 215

PRO 221 0.34 THR 51 -0.73 LEU 215

PRO 221 0.28 PRO 52 -0.73 ASP 214

PRO 221 0.26 ALA 53 -0.56 ASP 214

PRO 221 0.27 PHE 54 -0.56 ASP 214

PRO 221 0.21 GLU 55 -0.62 ASP 214

PRO 221 0.18 GLU 56 -0.52 PRO 253

PRO 221 0.20 TYR 57 -0.46 PRO 253

PRO 2 0.31 TYR 58 -0.48 ASP 214

PRO 2 0.45 GLN 59 -0.45 PRO 254

PRO 2 0.32 SER 60 -0.45 PRO 253

PRO 2 0.31 GLY 61 -0.38 PRO 253

GLY 3 0.21 LEU 62 -0.34 PRO 253

PRO 221 0.24 SER 63 -0.32 ASP 214

PRO 221 0.28 VAL 64 -0.36 ASP 214

PRO 221 0.33 ILE 65 -0.34 ASP 214

PRO 221 0.41 MET 66 -0.37 ASP 214

PRO 221 0.42 PRO 67 -0.34 ASP 214

PRO 221 0.49 VAL 68 -0.40 PRO 2

PRO 221 0.50 GLY 69 -0.38 PRO 2

PRO 221 0.48 GLY 70 -0.32 PRO 2

PRO 221 0.53 GLN 71 -0.33 GLY 216

PRO 221 0.52 SER 72 -0.29 PRO 2

PRO 221 0.43 SER 73 -0.27 PRO 2

PRO 221 0.40 PHE 74 -0.24 PRO 2

PRO 221 0.38 TYR 75 -0.24 PRO 2

PRO 221 0.33 THR 76 -0.21 PRO 2

PHE 224 0.31 ASP 77 -0.21 PRO 2

PHE 224 0.34 TRP 78 -0.23 PRO 2

PHE 224 0.32 TYR 79 -0.22 PRO 2

PHE 224 0.32 GLN 80 -0.24 PRO 2

PHE 224 0.32 PRO 81 -0.28 PRO 2

PHE 224 0.36 SER 82 -0.27 PRO 2

PHE 224 0.35 GLN 83 -0.26 PRO 2

PHE 224 0.35 SER 84 -0.26 PRO 2

PHE 224 0.32 ASN 85 -0.29 PRO 2

PHE 224 0.27 GLY 86 -0.31 PRO 2

PHE 224 0.27 GLN 87 -0.34 PRO 2

GLY 17 0.26 ASN 88 -0.34 PRO 2

PHE 224 0.28 TYR 89 -0.31 PRO 2

PHE 224 0.30 THR 90 -0.28 PRO 2

PRO 221 0.34 TYR 91 -0.28 PRO 2

PRO 221 0.31 LYS 92 -0.25 PRO 2

PRO 221 0.34 TRP 93 -0.24 PRO 2

PRO 221 0.30 GLU 94 -0.19 PRO 2

PRO 221 0.28 THR 95 -0.18 PRO 2

PRO 221 0.31 PHE 96 -0.21 ASP 214

PRO 221 0.31 LEU 97 -0.20 PRO 261

PRO 221 0.26 THR 98 -0.16 PRO 261

PRO 221 0.26 ARG 99 -0.16 ASP 214

PRO 221 0.28 GLU 100 -0.22 ASP 214

PRO 221 0.31 MET 101 -0.24 ASP 214

PRO 221 0.27 PRO 102 -0.21 ASP 214

PRO 221 0.25 ALA 103 -0.21 ASP 214

PRO 221 0.28 TRP 104 -0.26 ASP 214

PRO 221 0.27 LEU 105 -0.28 ASP 214

PRO 221 0.24 GLN 106 -0.24 ASP 214

PRO 221 0.24 ALA 107 -0.26 ASP 214

PRO 221 0.25 ASN 108 -0.31 ASP 214

PRO 221 0.25 LYS 109 -0.32 ASP 214

PRO 221 0.22 GLY 110 -0.27 ASP 214

PRO 221 0.23 VAL 111 -0.25 ASP 214

PRO 221 0.21 SER 112 -0.19 ASP 214

PRO 221 0.22 PRO 113 -0.16 ASP 214

PRO 221 0.19 THR 114 -0.12 PRO 253

PRO 221 0.17 GLY 115 -0.16 PRO 253

PRO 221 0.20 ASN 116 -0.18 PRO 253

PRO 221 0.21 ALA 117 -0.19 PRO 253

PRO 221 0.25 ALA 118 -0.14 PRO 261

PRO 221 0.26 VAL 119 -0.18 ARG 1

PRO 221 0.32 GLY 120 -0.21 PRO 2

PRO 221 0.35 LEU 121 -0.25 PRO 2

PRO 221 0.38 SER 122 -0.25 PRO 2

PRO 221 0.45 MET 123 -0.25 PRO 2

PRO 221 0.38 SER 124 -0.23 PRO 2

PRO 221 0.25 GLY 125 -0.20 PRO 2

PRO 221 0.22 GLY 126 -0.18 PRO 2

PRO 221 0.28 SER 127 -0.18 PRO 2

PRO 221 0.25 ALA 128 -0.15 PRO 2

PRO 221 0.17 LEU 129 -0.14 ARG 1

PRO 221 0.19 ILE 130 -0.13 PRO 2

PRO 221 0.22 LEU 131 -0.11 PRO 2

PRO 221 0.18 ALA 132 -0.12 GLU 153

PRO 221 0.15 ALA 133 -0.15 GLU 153

PRO 221 0.16 TYR 134 -0.17 PRO 182

PRO 221 0.18 TYR 135 -0.14 PRO 182

PRO 221 0.15 PRO 136 -0.14 PRO 182

PRO 221 0.16 GLN 137 -0.12 PRO 182

PRO 221 0.20 GLN 138 -0.09 PRO 261

PRO 221 0.19 PHE 139 -0.10 PRO 182

PRO 221 0.15 PRO 140 -0.13 GLU 153

PRO 221 0.15 TYR 141 -0.12 GLU 153

PRO 221 0.17 ALA 142 -0.13 ARG 1

PRO 221 0.17 ALA 143 -0.19 ARG 1

PRO 221 0.17 SER 144 -0.21 ARG 1

PRO 221 0.17 LEU 145 -0.27 ARG 1

SER 213 0.20 SER 146 -0.27 ARG 1

GLY 126 0.20 GLY 147 -0.22 PRO 2

ASN 209 0.26 PHE 148 -0.20 PRO 2

PRO 254 0.28 LEU 149 -0.18 PRO 2

PRO 254 0.34 ASN 150 -0.20 TRP 156

THR 229 0.36 PRO 151 -0.19 ILE 160

PRO 254 0.35 SER 152 -0.25 VAL 191

PRO 254 0.41 GLU 153 -0.39 VAL 191

LEU 228 0.52 SER 154 -0.30 VAL 191

LEU 228 0.56 TRP 155 -0.26 VAL 191

LEU 228 0.49 TRP 156 -0.22 VAL 191

PHE 224 0.49 PRO 157 -0.22 VAL 191

PHE 224 0.54 THR 158 -0.19 VAL 191

PHE 224 0.68 LEU 159 -0.19 PRO 2

PHE 224 0.61 ILE 160 -0.20 PRO 2

PHE 224 0.59 GLY 161 -0.20 PRO 2

PHE 224 0.66 LEU 162 -0.20 PRO 2

PHE 224 0.70 ALA 163 -0.23 PRO 2

PHE 224 0.54 MET 164 -0.25 PRO 2

PHE 224 0.49 ASN 165 -0.25 PRO 2

ILE 220 0.50 ASP 166 -0.25 PRO 2

PRO 221 0.56 SER 167 -0.32 GLY 216

PRO 221 0.43 GLY 168 -0.34 GLY 216

PHE 224 0.39 GLY 169 -0.27 PRO 2

PHE 224 0.42 TYR 170 -0.27 PRO 2

PHE 224 0.45 ASN 171 -0.24 PRO 2

PHE 224 0.47 ALA 172 -0.22 PRO 2

PHE 224 0.43 ASN 173 -0.21 PRO 2

PHE 224 0.39 SER 174 -0.23 PRO 2

PHE 224 0.39 MET 175 -0.23 PRO 2

PHE 224 0.37 TRP 176 -0.20 PRO 2

PHE 224 0.37 GLY 177 -0.20 PRO 2

PHE 224 0.39 PRO 178 -0.18 PRO 2

PHE 224 0.40 SER 179 -0.17 PRO 2

LEU 228 0.36 SER 180 -0.16 PRO 2

PHE 224 0.33 ASP 181 -0.17 PRO 2

PRO 254 0.28 PRO 182 -0.17 TYR 134

PHE 224 0.28 ALA 183 -0.17 PRO 2

PHE 224 0.32 TRP 184 -0.17 PRO 2

PRO 254 0.30 LYS 185 -0.16 PRO 157

PRO 254 0.24 ARG 186 -0.15 PRO 2

PHE 224 0.24 ASN 187 -0.17 PRO 2

THR 232 0.28 ASP 188 -0.17 PRO 157

PRO 254 0.25 PRO 189 -0.23 GLU 153

PRO 254 0.32 MET 190 -0.30 GLU 153

PRO 254 0.32 VAL 191 -0.39 GLU 153

PRO 254 0.24 GLN 192 -0.27 GLU 153

PRO 254 0.24 ILE 193 -0.29 GLU 153

PRO 254 0.22 PRO 194 -0.30 GLU 153

SER 213 0.19 ARG 195 -0.24 GLU 153

SER 213 0.19 LEU 196 -0.21 GLU 153

SER 213 0.22 VAL 197 -0.23 GLU 153

SER 213 0.19 ALA 198 -0.22 GLU 153

SER 213 0.16 ASN 199 -0.18 GLU 153

SER 213 0.17 ASN 200 -0.18 GLU 153

SER 213 0.15 THR 201 -0.17 GLU 153

SER 213 0.14 ARG 202 -0.15 GLU 153

SER 213 0.17 ILE 203 -0.14 ARG 231

SER 213 0.18 TRP 204 -0.19 ARG 1

SER 213 0.23 VAL 205 -0.24 ARG 1

SER 213 0.27 TYR 206 -0.31 ARG 1

SER 213 0.32 CYS 207 -0.33 ARG 1

SER 213 0.42 GLY 208 -0.40 ARG 1

SER 154 0.47 ASN 209 -0.40 ARG 1

GLY 227 0.50 GLY 210 -0.38 ARG 1

GLY 227 0.49 THR 211 -0.50 ARG 1

SER 154 0.31 PRO 212 -0.60 ARG 1

PRO 253 0.58 SER 213 -0.80 ARG 1

PRO 253 0.43 ASP 214 -1.02 ARG 1

PHE 252 0.35 LEU 215 -0.93 ARG 1

PHE 252 0.25 GLY 216 -0.73 ARG 1

PRO 261 0.26 GLY 217 -0.44 PRO 2

TRP 155 0.22 ASP 218 -0.40 PRO 2

ILE 49 0.34 ASN 219 -0.21 PRO 2

ALA 163 0.57 ILE 220 -0.17 GLY 210

ARG 39 0.78 PRO 221 -0.21 LEU 228

GLY 37 0.40 ALA 222 -0.20 PRO 2

LEU 159 0.41 LYS 223 -0.25 PRO 2

ALA 163 0.70 PHE 224 -0.30 GLY 227

ILE 160 0.47 LEU 225 -0.21 ARG 231

TRP 155 0.36 GLU 226 -0.26 ARG 1

GLY 210 0.50 GLY 227 -0.30 PHE 224

TRP 155 0.56 LEU 228 -0.32 ARG 231

PRO 151 0.36 THR 229 -0.23 ARG 1

ASN 209 0.43 LEU 230 -0.28 ARG 1

PRO 254 0.53 ARG 231 -0.32 LEU 228

PRO 254 0.44 THR 232 -0.24 LEU 228

PRO 254 0.38 ASN 233 -0.24 LEU 228

PRO 254 0.52 GLN 234 -0.24 LEU 228

PRO 254 0.48 THR 235 -0.26 LEU 228

PRO 254 0.37 PHE 236 -0.19 ARG 1

SER 213 0.38 ARG 237 -0.20 GLY 248

PRO 254 0.41 ASP 238 -0.21 LEU 228

PRO 254 0.36 THR 239 -0.24 GLU 153

SER 213 0.31 TYR 240 -0.23 GLU 153

SER 213 0.36 ALA 241 -0.18 GLU 153

SER 213 0.34 ALA 242 -0.24 GLU 153

SER 213 0.29 ASP 243 -0.30 GLU 153

SER 213 0.29 GLY 244 -0.24 GLU 153

SER 213 0.28 GLY 245 -0.22 GLU 153

ASP 214 0.30 ARG 246 -0.17 GLU 153

ASP 214 0.23 ASN 247 -0.17 GLU 153

SER 213 0.26 GLY 248 -0.20 ARG 237

ASP 214 0.28 VAL 249 -0.29 ASP 273

SER 213 0.36 PHE 250 -0.24 ARG 231

SER 213 0.42 ASN 251 -0.37 ALA 269

SER 213 0.53 PHE 252 -0.34 ARG 1

SER 213 0.58 PRO 253 -0.66 ALA 269

ARG 231 0.53 PRO 254 -0.57 ARG 1

SER 213 0.53 ASN 255 -0.62 ARG 1

SER 213 0.39 GLY 256 -0.57 ARG 1

SER 154 0.22 THR 257 -0.42 ARG 1

ALA 222 0.27 HIS 258 -0.32 PRO 2

ALA 222 0.34 SER 259 -0.40 PRO 2

PRO 221 0.35 TRP 260 -0.50 PRO 261

GLY 217 0.26 PRO 261 -0.68 ARG 1

ASN 251 0.21 TYR 262 -0.57 ARG 1

PRO 221 0.21 TRP 263 -0.39 ARG 1

PRO 221 0.22 ASN 264 -0.48 ARG 1

ARG 246 0.14 GLU 265 -0.57 ARG 1

ARG 246 0.13 GLN 266 -0.47 PRO 253

PRO 221 0.19 LEU 267 -0.44 PRO 253

PRO 221 0.14 VAL 268 -0.58 PRO 253

ASN 264 0.12 ALA 269 -0.66 PRO 253

PRO 221 0.11 MET 270 -0.48 PRO 253

PRO 221 0.15 LYS 271 -0.48 PRO 253

PRO 2 0.14 ALA 272 -0.48 PRO 253

THR 51 0.10 ASP 273 -0.38 PRO 253

PRO 221 0.14 ILE 274 -0.32 PRO 253

PRO 2 0.19 GLN 275 -0.35 PRO 253

PRO 2 0.18 HIS 276 -0.32 PRO 253

GLY 3 0.13 VAL 277 -0.24 PRO 253

GLY 3 0.16 LEU 278 -0.23 PRO 253

PRO 2 0.23 ASN 279 -0.27 PRO 253

PRO 2 0.23 GLY 280 -0.25 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.

*** 1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 240220092131172147

--- normal mode 13 ---

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

* 1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *