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 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
ASP 214 0.27 ARG 1 -0.53 PHE 54

GLN 59 0.49 PRO 2 -1.11 ASP 43

GLN 59 0.36 GLY 3 -0.50 GLU 7

GLU 55 0.39 LEU 4 -0.40 GLU 7

ASP 214 0.24 PRO 5 -0.36 LEU 4

ASP 214 0.24 VAL 6 -0.36 LEU 4

ASP 214 0.20 GLU 7 -0.55 PRO 2

ASP 214 0.19 TYR 8 -0.83 PRO 2

GLY 216 0.16 LEU 9 -0.75 PRO 2

GLY 216 0.16 GLN 10 -0.84 PRO 2

GLY 216 0.14 VAL 11 -0.70 PRO 2

GLY 216 0.13 PRO 12 -0.69 PRO 2

GLY 216 0.13 SER 13 -0.67 PRO 2

ASN 219 0.11 ALA 14 -0.64 PRO 2

ASN 219 0.11 SER 15 -0.63 PRO 2

ASN 219 0.12 MET 16 -0.73 PRO 2

ASN 219 0.12 GLY 17 -0.76 PRO 2

GLY 216 0.13 ARG 18 -0.85 PRO 2

GLY 216 0.15 ASP 19 -0.86 PRO 2

ASP 42 0.16 ILE 20 -0.84 PRO 2

GLY 216 0.17 LYS 21 -0.89 PRO 2

GLY 216 0.16 VAL 22 -0.71 PRO 2

GLY 216 0.18 GLN 23 -0.63 PRO 2

GLY 216 0.16 PHE 24 -0.40 PRO 2

LEU 215 0.17 GLN 25 -0.31 ARG 1

LEU 215 0.13 GLY 26 -0.23 ARG 1

PRO 2 0.18 GLY 27 -0.24 ARG 1

PRO 2 0.16 GLY 28 -0.20 ARG 1

PRO 261 0.06 PRO 29 -0.19 ARG 1

ALA 31 0.06 HIS 30 -0.21 ARG 1

PRO 261 0.07 ALA 31 -0.26 ARG 1

PRO 261 0.07 VAL 32 -0.27 ARG 1

PRO 261 0.09 TYR 33 -0.28 ARG 1

PRO 261 0.12 LEU 34 -0.30 PRO 2

GLY 217 0.12 LEU 35 -0.41 PRO 2

GLY 217 0.16 ASP 36 -0.48 PRO 2

GLY 217 0.19 GLY 37 -0.45 PRO 2

ASN 219 0.24 LEU 38 -0.50 PRO 2

ASN 219 0.22 ARG 39 -0.59 PRO 2

GLY 216 0.17 ALA 40 -0.67 PRO 2

GLY 216 0.19 GLN 41 -0.84 PRO 2

GLY 216 0.17 ASP 42 -0.99 PRO 2

ASP 214 0.19 ASP 43 -1.11 PRO 2

GLY 216 0.21 TYR 44 -0.90 PRO 2

GLY 216 0.19 ASN 45 -0.68 PRO 2

GLY 216 0.23 GLY 46 -0.56 PRO 2

PRO 261 0.22 TRP 47 -0.39 PRO 2

GLY 216 0.24 ASP 48 -0.48 PRO 2

GLY 216 0.27 ILE 49 -0.55 PRO 2

GLY 216 0.33 ASN 50 -0.36 PRO 2

PRO 261 0.38 THR 51 -0.28 ARG 1

LEU 215 0.33 PRO 52 -0.40 ARG 1

PRO 261 0.26 ALA 53 -0.41 ARG 1

LEU 215 0.22 PHE 54 -0.53 ARG 1

LEU 4 0.39 GLU 55 -0.37 ARG 1

GLY 3 0.30 GLU 56 -0.25 ARG 1

PRO 2 0.21 TYR 57 -0.33 ARG 1

PRO 2 0.34 TYR 58 -0.35 ARG 1

PRO 2 0.49 GLN 59 -0.23 ARG 1

PRO 2 0.38 SER 60 -0.23 ARG 1

PRO 2 0.32 GLY 61 -0.20 ARG 1

PRO 2 0.15 LEU 62 -0.24 ARG 1

PRO 261 0.10 SER 63 -0.28 ARG 1

PRO 261 0.13 VAL 64 -0.33 ARG 1

GLY 216 0.12 ILE 65 -0.33 PRO 2

GLY 216 0.15 MET 66 -0.49 PRO 2

GLY 216 0.15 PRO 67 -0.63 PRO 2

GLY 216 0.17 VAL 68 -0.79 PRO 2

GLY 216 0.15 GLY 69 -0.81 PRO 2

ASN 219 0.15 GLY 70 -0.70 PRO 2

ASN 219 0.17 GLN 71 -0.68 PRO 2

ASN 219 0.22 SER 72 -0.57 PRO 2

ASN 219 0.18 SER 73 -0.58 PRO 2

ASN 219 0.18 PHE 74 -0.46 PRO 2

ASN 219 0.14 TYR 75 -0.50 PRO 2

ASN 219 0.15 THR 76 -0.48 PRO 2

ASN 219 0.14 ASP 77 -0.52 PRO 2

ASN 219 0.16 TRP 78 -0.56 PRO 2

PRO 221 0.17 TYR 79 -0.55 PRO 2

ASN 219 0.16 GLN 80 -0.62 PRO 2

ASN 219 0.15 PRO 81 -0.70 PRO 2

ASN 219 0.17 SER 82 -0.67 PRO 2

ASN 219 0.17 GLN 83 -0.66 PRO 2

ASN 219 0.17 SER 84 -0.65 PRO 2

ASN 219 0.15 ASN 85 -0.73 PRO 2

ASN 219 0.11 GLY 86 -0.81 PRO 2

ASN 219 0.11 GLN 87 -0.83 PRO 2

ASN 219 0.10 ASN 88 -0.85 PRO 2

ASN 219 0.11 TYR 89 -0.80 PRO 2

ASN 219 0.13 THR 90 -0.70 PRO 2

ASN 219 0.14 TYR 91 -0.68 PRO 2

ASN 219 0.12 LYS 92 -0.61 PRO 2

ASN 219 0.13 TRP 93 -0.57 PRO 2

ASN 219 0.11 GLU 94 -0.47 PRO 2

ASN 219 0.11 THR 95 -0.48 PRO 2

ASN 219 0.12 PHE 96 -0.54 PRO 2

ASN 219 0.10 LEU 97 -0.45 PRO 2

ASN 219 0.09 THR 98 -0.37 PRO 2

ASN 219 0.09 ARG 99 -0.40 PRO 2

GLY 217 0.10 GLU 100 -0.48 PRO 2

GLY 216 0.11 MET 101 -0.47 PRO 2

GLY 216 0.09 PRO 102 -0.34 PRO 2

GLY 216 0.09 ALA 103 -0.34 PRO 2

GLY 216 0.11 TRP 104 -0.41 PRO 2

GLY 216 0.11 LEU 105 -0.33 PRO 2

GLY 216 0.09 GLN 106 -0.22 PRO 2

GLY 216 0.10 ALA 107 -0.26 PRO 2

GLY 216 0.12 ASN 108 -0.30 PRO 2

GLY 216 0.11 LYS 109 -0.22 LEU 4

GLY 216 0.09 GLY 110 -0.18 ARG 1

GLY 216 0.08 VAL 111 -0.21 ARG 1

PRO 261 0.06 SER 112 -0.19 ARG 1

ALA 14 0.07 PRO 113 -0.20 ARG 1

ARG 99 0.08 THR 114 -0.19 ARG 1

ARG 99 0.07 GLY 115 -0.19 ARG 1

ALA 14 0.05 ASN 116 -0.22 ARG 1

ALA 14 0.05 ALA 117 -0.22 ARG 1

GLY 217 0.05 ALA 118 -0.22 ARG 1

LEU 159 0.06 VAL 119 -0.22 ARG 1

GLY 217 0.09 GLY 120 -0.26 PRO 2

LEU 159 0.13 LEU 121 -0.27 PRO 2

ILE 160 0.19 SER 122 -0.30 PRO 2

ASN 219 0.19 MET 123 -0.38 PRO 2

GLY 217 0.13 SER 124 -0.36 PRO 2

GLY 217 0.10 GLY 125 -0.25 PRO 2

PRO 221 0.13 GLY 126 -0.27 PRO 2

PRO 221 0.12 SER 127 -0.33 PRO 2

PRO 221 0.08 ALA 128 -0.25 PRO 2

PRO 221 0.09 LEU 129 -0.19 PRO 2

PRO 221 0.11 ILE 130 -0.26 PRO 2

ASP 77 0.09 LEU 131 -0.27 PRO 2

ASP 77 0.07 ALA 132 -0.18 ARG 1

TYR 79 0.10 ALA 133 -0.18 PRO 2

ASP 77 0.13 TYR 134 -0.23 PRO 2

THR 90 0.10 TYR 135 -0.21 PRO 2

THR 90 0.08 PRO 136 -0.17 ARG 1

SER 15 0.08 GLN 137 -0.18 ARG 1

ARG 99 0.08 GLN 138 -0.20 ARG 1

THR 95 0.07 PHE 139 -0.20 ARG 1

SER 15 0.06 PRO 140 -0.18 ARG 1

ALA 14 0.05 TYR 141 -0.18 ARG 1

TYR 79 0.05 ALA 142 -0.18 ARG 1

SER 60 0.07 ALA 143 -0.16 ARG 1

LEU 267 0.09 SER 144 -0.14 ARG 1

GLY 147 0.16 LEU 145 -0.13 PRO 2

GLY 147 0.19 SER 146 -0.16 PRO 2

SER 146 0.19 GLY 147 -0.21 PRO 2

PRO 151 0.20 PHE 148 -0.25 PRO 2

PRO 221 0.16 LEU 149 -0.21 PRO 2

PRO 221 0.22 ASN 150 -0.23 PRO 2

PRO 221 0.32 PRO 151 -0.28 PRO 2

PRO 221 0.31 SER 152 -0.28 PRO 2

PRO 221 0.34 GLU 153 -0.24 PRO 2

PRO 221 0.43 SER 154 -0.22 PRO 2

PRO 221 0.54 TRP 155 -0.25 PRO 2

PRO 221 0.49 TRP 156 -0.28 PRO 2

PRO 221 0.46 PRO 157 -0.33 PRO 2

PRO 221 0.54 THR 158 -0.33 PRO 2

PRO 221 0.65 LEU 159 -0.31 PRO 2

PRO 221 0.49 ILE 160 -0.37 PRO 2

PRO 221 0.42 GLY 161 -0.43 PRO 2

PRO 221 0.50 LEU 162 -0.40 PRO 2

PRO 221 0.44 ALA 163 -0.41 PRO 2

ASN 219 0.30 MET 164 -0.50 PRO 2

ASN 219 0.28 ASN 165 -0.53 PRO 2

ASN 219 0.30 ASP 166 -0.50 PRO 2

ASN 219 0.25 SER 167 -0.56 PRO 2

ASN 219 0.18 GLY 168 -0.66 PRO 2

ASN 219 0.21 GLY 169 -0.63 PRO 2

ASN 219 0.22 TYR 170 -0.61 PRO 2

ASN 219 0.24 ASN 171 -0.55 PRO 2

PRO 221 0.30 ALA 172 -0.48 PRO 2

PRO 221 0.27 ASN 173 -0.48 PRO 2

PRO 221 0.20 SER 174 -0.56 PRO 2

PRO 221 0.21 MET 175 -0.53 PRO 2

PRO 221 0.24 TRP 176 -0.46 PRO 2

PRO 221 0.27 GLY 177 -0.46 PRO 2

PRO 221 0.33 PRO 178 -0.40 PRO 2

PRO 221 0.37 SER 179 -0.34 PRO 2

PRO 221 0.33 SER 180 -0.33 PRO 2

PRO 221 0.29 ASP 181 -0.37 PRO 2

PRO 221 0.25 PRO 182 -0.35 PRO 2

PRO 221 0.23 ALA 183 -0.38 PRO 2

PRO 221 0.28 TRP 184 -0.34 PRO 2

PRO 221 0.24 LYS 185 -0.28 PRO 2

PRO 221 0.19 ARG 186 -0.30 PRO 2

PRO 221 0.20 ASN 187 -0.32 PRO 2

PRO 221 0.20 ASP 188 -0.26 PRO 2

PRO 221 0.14 PRO 189 -0.20 PRO 2

PRO 221 0.13 MET 190 -0.16 GLU 153

PRO 221 0.15 VAL 191 -0.22 GLU 153

PRO 221 0.13 GLN 192 -0.18 PRO 2

PRO 221 0.09 ILE 193 -0.13 GLU 153

TYR 79 0.10 PRO 194 -0.13 GLU 153

TYR 79 0.12 ARG 195 -0.13 ARG 1

TYR 79 0.09 LEU 196 -0.13 ARG 1

TYR 79 0.09 VAL 197 -0.12 PRO 253

TYR 79 0.11 ALA 198 -0.12 ARG 1

TYR 79 0.10 ASN 199 -0.14 ARG 1

TYR 79 0.08 ASN 200 -0.13 SER 213

TYR 79 0.07 THR 201 -0.14 ARG 1

GLY 3 0.08 ARG 202 -0.14 SER 213

SER 60 0.08 ILE 203 -0.13 SER 213

GLY 3 0.10 TRP 204 -0.15 SER 213

LEU 267 0.13 VAL 205 -0.13 SER 213

LEU 267 0.14 TYR 206 -0.15 SER 213

PRO 52 0.14 CYS 207 -0.10 SER 213

PRO 52 0.18 GLY 208 -0.12 SER 213

TRP 155 0.19 ASN 209 -0.14 GLN 234

TRP 155 0.27 GLY 210 -0.11 PHE 252

TRP 155 0.24 THR 211 -0.17 PHE 252

LEU 159 0.24 PRO 212 -0.17 PHE 252

LEU 4 0.26 SER 213 -0.24 ASN 251

LEU 4 0.32 ASP 214 -0.21 ASN 251

PRO 52 0.33 LEU 215 -0.15 ALA 269

ASN 50 0.33 GLY 216 -0.12 ASN 251

LEU 159 0.33 GLY 217 -0.10 ASN 251

LEU 159 0.35 ASP 218 -0.12 PHE 252

LEU 159 0.45 ASN 219 -0.18 PRO 2

LEU 159 0.48 ILE 220 -0.22 PRO 2

LEU 159 0.65 PRO 221 -0.31 PRO 2

LEU 159 0.49 ALA 222 -0.24 PRO 2

TRP 155 0.37 LYS 223 -0.16 PRO 2

TRP 155 0.47 PHE 224 -0.23 PRO 2

TRP 155 0.46 LEU 225 -0.26 PRO 2

TRP 155 0.31 GLU 226 -0.16 PRO 2

SER 154 0.26 GLY 227 -0.19 ASP 166

SER 154 0.34 LEU 228 -0.28 ASP 166

SER 154 0.23 THR 229 -0.21 ASP 166

SER 154 0.15 LEU 230 -0.17 ASP 166

ALA 269 0.11 ARG 231 -0.20 ASP 166

SER 180 0.10 THR 232 -0.21 ALA 163

VAL 268 0.11 ASN 233 -0.15 ASP 166

ALA 269 0.12 GLN 234 -0.15 ASP 166

ALA 269 0.09 THR 235 -0.16 ALA 163

VAL 268 0.09 PHE 236 -0.14 ALA 163

ALA 272 0.11 ARG 237 -0.17 PRO 254

ALA 272 0.11 ASP 238 -0.17 PRO 254

ALA 272 0.08 THR 239 -0.13 PRO 254

ALA 272 0.08 TYR 240 -0.14 PRO 254

ALA 272 0.10 ALA 241 -0.19 PRO 254

ALA 272 0.08 ALA 242 -0.17 PRO 254

TYR 79 0.07 ASP 243 -0.14 PRO 254

TYR 79 0.07 GLY 244 -0.17 PRO 254

GLY 3 0.08 GLY 245 -0.17 PRO 254

GLY 3 0.11 ARG 246 -0.21 PRO 253

GLY 3 0.11 ASN 247 -0.18 ASP 214

GLY 3 0.11 GLY 248 -0.19 SER 213

ALA 272 0.16 VAL 249 -0.21 SER 213

GLY 3 0.15 PHE 250 -0.24 PRO 253

ALA 269 0.20 ASN 251 -0.24 SER 213

GLY 3 0.18 PHE 252 -0.24 ASN 255

GLY 3 0.23 PRO 253 -0.24 PHE 252

GLY 3 0.24 PRO 254 -0.20 ARG 246

GLY 3 0.22 ASN 255 -0.24 PHE 252

PRO 52 0.22 GLY 256 -0.17 ASN 251

LEU 159 0.26 THR 257 -0.12 ASN 251

LEU 159 0.31 HIS 258 -0.18 PRO 2

LEU 159 0.29 SER 259 -0.20 PRO 2

LEU 159 0.23 TRP 260 -0.19 PRO 2

THR 51 0.38 PRO 261 -0.10 ALA 269

PRO 52 0.24 TYR 262 -0.10 ALA 269

LEU 159 0.18 TRP 263 -0.12 ARG 1

PRO 52 0.22 ASN 264 -0.12 ARG 1

PRO 52 0.27 GLU 265 -0.17 ALA 269

GLY 3 0.18 GLN 266 -0.10 ASP 214

ASN 251 0.14 LEU 267 -0.18 ARG 1

GLY 3 0.23 VAL 268 -0.14 ARG 1

PRO 2 0.25 ALA 269 -0.19 ASP 214

GLY 3 0.19 MET 270 -0.14 ASP 214

PRO 2 0.23 LYS 271 -0.18 ARG 1

PRO 2 0.32 ALA 272 -0.15 ASP 214

PRO 2 0.23 ASP 273 -0.17 ASP 214

PRO 2 0.16 ILE 274 -0.18 ARG 1

PRO 2 0.25 GLN 275 -0.18 ARG 1

PRO 2 0.26 HIS 276 -0.15 ARG 1

PRO 2 0.16 VAL 277 -0.16 ARG 1

PRO 2 0.13 LEU 278 -0.18 ARG 1

PRO 2 0.22 ASN 279 -0.17 ARG 1

PRO 2 0.25 GLY 280 -0.15 ARG 1

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 10 ---

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

* 1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *