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 15 ---

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 0.42 ARG 1 -1.15 THR 51

GLY 110 0.49 PRO 2 -1.07 ASN 50

GLY 110 0.65 GLY 3 -0.68 ILE 49

LYS 109 0.62 LEU 4 -0.50 ILE 49

LYS 109 0.62 PRO 5 -0.24 ILE 49

GLY 86 0.33 VAL 6 -0.17 ILE 49

GLY 86 0.42 GLU 7 -0.20 GLY 26

GLY 86 0.50 TYR 8 -0.14 PHE 24

GLY 86 0.46 LEU 9 -0.09 ASN 116

ASN 88 0.54 GLN 10 -0.11 MET 101

ASN 88 0.43 VAL 11 -0.09 ASP 43

ASN 88 0.43 PRO 12 -0.11 ASP 43

ASN 88 0.33 SER 13 -0.14 ASP 42

ASN 219 0.27 ALA 14 -0.13 GLY 17

ASN 219 0.28 SER 15 -0.10 ASP 42

ASN 219 0.30 MET 16 -0.12 GLY 70

ASN 88 0.50 GLY 17 -0.13 ALA 14

ASN 88 0.57 ARG 18 -0.20 ASP 42

ASN 88 0.58 ASP 19 -0.15 ASP 42

ASN 88 0.50 ILE 20 -0.16 ASP 42

GLY 86 0.54 LYS 21 -0.16 PRO 2

ASN 219 0.45 VAL 22 -0.11 PRO 2

ASN 219 0.45 GLN 23 -0.17 PRO 2

ASN 219 0.39 PHE 24 -0.14 TYR 8

LEU 4 0.34 GLN 25 -0.16 GLU 7

LEU 4 0.49 GLY 26 -0.20 GLU 7

LEU 4 0.56 GLY 27 -0.19 ARG 246

GLY 3 0.53 GLY 28 -0.18 ASN 200

GLY 3 0.47 PRO 29 -0.15 ASN 200

GLY 3 0.32 HIS 30 -0.18 ASN 200

ASN 219 0.30 ALA 31 -0.16 ASN 200

ASN 219 0.33 VAL 32 -0.21 ARG 1

ASN 219 0.37 TYR 33 -0.25 ARG 1

ASN 219 0.43 LEU 34 -0.41 ARG 1

ASN 219 0.45 LEU 35 -0.45 ARG 1

ASN 219 0.56 ASP 36 -0.56 ARG 1

PRO 221 0.67 GLY 37 -0.63 ARG 1

PRO 221 0.70 LEU 38 -0.59 PRO 2

ASN 219 0.77 ARG 39 -0.67 PRO 2

ASN 219 0.72 ALA 40 -0.59 PRO 2

ASN 219 0.69 GLN 41 -0.63 PRO 2

ASN 219 0.59 ASP 42 -0.48 PRO 2

ASN 219 0.61 ASP 43 -0.55 PRO 2

ASN 219 0.61 TYR 44 -0.60 PRO 2

ASN 219 0.58 ASN 45 -0.59 PRO 2

ASN 219 0.68 GLY 46 -0.76 PRO 2

ASN 219 0.53 TRP 47 -0.76 ARG 1

ASN 219 0.51 ASP 48 -0.73 PRO 2

ASN 219 0.62 ILE 49 -1.00 PRO 2

GLY 217 0.65 ASN 50 -1.15 ARG 1

GLY 217 0.42 THR 51 -1.15 ARG 1

ASN 219 0.29 PRO 52 -0.92 ARG 1

GLY 217 0.33 ALA 53 -0.59 ARG 1

ASN 219 0.29 PHE 54 -0.26 ARG 1

LYS 109 0.19 GLU 55 -0.30 ARG 1

GLY 217 0.21 GLU 56 -0.39 ARG 1

GLY 217 0.23 TYR 57 -0.28 ARG 246

GLY 27 0.31 TYR 58 -0.24 ARG 246

GLY 3 0.44 GLN 59 -0.24 ARG 246

GLY 3 0.28 SER 60 -0.28 ARG 246

GLY 3 0.42 GLY 61 -0.22 ARG 246

GLY 3 0.29 LEU 62 -0.21 ASN 200

LEU 4 0.32 SER 63 -0.17 ASN 200

ASN 219 0.36 VAL 64 -0.16 ASN 200

ASN 219 0.39 ILE 65 -0.12 TYR 8

ASN 219 0.46 MET 66 -0.27 PRO 2

ASN 219 0.47 PRO 67 -0.24 PRO 2

ASN 219 0.53 VAL 68 -0.37 PRO 2

ASN 219 0.54 GLY 69 -0.39 PRO 2

ASN 219 0.50 GLY 70 -0.37 PRO 2

ASN 219 0.56 GLN 71 -0.45 PRO 2

PRO 221 0.49 SER 72 -0.46 PRO 2

PRO 221 0.42 SER 73 -0.35 PRO 2

PRO 221 0.44 PHE 74 -0.38 ARG 1

PRO 221 0.40 TYR 75 -0.31 ARG 1

PRO 221 0.34 THR 76 -0.26 ARG 1

PRO 221 0.29 ASP 77 -0.18 PRO 2

ASN 219 0.27 TRP 78 -0.20 PRO 2

ASN 219 0.23 TYR 79 -0.17 PRO 2

GLY 17 0.33 GLN 80 -0.16 THR 232

GLY 17 0.39 PRO 81 -0.17 LEU 228

LYS 21 0.35 SER 82 -0.22 PRO 2

LYS 21 0.36 GLN 83 -0.27 THR 158

ASP 42 0.39 SER 84 -0.30 LEU 228

ASP 42 0.52 ASN 85 -0.22 PRO 2

ASP 43 0.56 GLY 86 -0.18 THR 158

LYS 21 0.53 GLN 87 -0.16 LEU 228

ASP 19 0.58 ASN 88 -0.14 LEU 228

GLY 17 0.49 TYR 89 -0.10 LEU 228

GLY 17 0.33 THR 90 -0.13 PRO 2

ASN 219 0.33 TYR 91 -0.18 PRO 2

ASN 219 0.32 LYS 92 -0.14 PRO 2

ASN 219 0.36 TRP 93 -0.18 PRO 2

PRO 221 0.32 GLU 94 -0.17 ARG 1

ASN 219 0.30 THR 95 -0.08 ARG 1

ASN 219 0.33 PHE 96 -0.08 ASP 42

ASN 219 0.34 LEU 97 -0.11 ARG 1

ASN 219 0.30 THR 98 -0.07 PRO 182

ASN 219 0.29 ARG 99 -0.07 ASP 42

ASN 219 0.31 GLU 100 -0.08 ASP 42

ASN 219 0.34 MET 101 -0.11 GLN 10

ASN 219 0.31 PRO 102 -0.10 GLN 10

GLY 3 0.35 ALA 103 -0.06 GLN 10

PRO 5 0.40 TRP 104 -0.08 GLN 10

PRO 5 0.43 LEU 105 -0.10 GLN 10

GLY 3 0.49 GLN 106 -0.12 PRO 113

GLY 3 0.53 ALA 107 -0.09 GLN 137

GLY 3 0.59 ASN 108 -0.09 PRO 113

GLY 3 0.63 LYS 109 -0.13 VAL 111

GLY 3 0.65 GLY 110 -0.13 ASN 199

GLY 3 0.46 VAL 111 -0.13 TYR 8

GLY 3 0.40 SER 112 -0.13 ASN 199

GLY 3 0.30 PRO 113 -0.12 GLN 106

GLY 3 0.25 THR 114 -0.14 TYR 134

ASN 219 0.23 GLY 115 -0.21 ASN 199

ASN 219 0.27 ASN 116 -0.16 ASN 199

ASN 219 0.27 ALA 117 -0.26 ARG 1

ASN 219 0.30 ALA 118 -0.34 ARG 1

ASN 219 0.31 VAL 119 -0.48 ARG 1

PRO 221 0.37 GLY 120 -0.55 ARG 1

PRO 221 0.40 LEU 121 -0.66 ARG 1

PRO 221 0.49 SER 122 -0.63 ARG 1

PRO 221 0.55 MET 123 -0.55 ARG 1

PRO 221 0.45 SER 124 -0.51 ARG 1

PRO 221 0.37 GLY 125 -0.55 ARG 1

PRO 221 0.36 GLY 126 -0.46 ARG 1

PRO 221 0.37 SER 127 -0.40 ARG 1

PRO 221 0.33 ALA 128 -0.40 ARG 1

PRO 221 0.29 LEU 129 -0.40 ARG 1

PRO 221 0.30 ILE 130 -0.33 ARG 1

PRO 221 0.30 LEU 131 -0.27 ARG 1

PRO 221 0.26 ALA 132 -0.28 ARG 1

PRO 221 0.25 ALA 133 -0.28 ARG 1

PRO 221 0.26 TYR 134 -0.21 ARG 1

PRO 221 0.25 TYR 135 -0.20 TYR 134

PRO 221 0.23 PRO 136 -0.22 GLY 280

PRO 221 0.22 GLN 137 -0.19 TYR 134

PRO 221 0.24 GLN 138 -0.15 TYR 134

PRO 221 0.24 PHE 139 -0.20 ARG 1

PRO 221 0.20 PRO 140 -0.23 ASN 199

PRO 221 0.20 TYR 141 -0.32 ARG 1

PRO 221 0.24 ALA 142 -0.39 ARG 1

PRO 221 0.24 ALA 143 -0.52 ARG 1

PRO 221 0.27 SER 144 -0.57 ARG 1

ALA 222 0.23 LEU 145 -0.66 ARG 1

ALA 222 0.25 SER 146 -0.65 ARG 1

PRO 221 0.36 GLY 147 -0.60 ARG 1

PRO 221 0.37 PHE 148 -0.53 ARG 1

PRO 221 0.31 LEU 149 -0.48 ARG 1

PRO 221 0.30 ASN 150 -0.43 ARG 1

PRO 221 0.36 PRO 151 -0.40 ARG 1

PRO 221 0.29 SER 152 -0.36 ARG 1

PRO 221 0.25 GLU 153 -0.38 ARG 1

PRO 221 0.22 SER 154 -0.37 ARG 231

PRO 221 0.26 TRP 155 -0.39 ARG 231

PRO 221 0.36 TRP 156 -0.39 ARG 1

PRO 221 0.30 PRO 157 -0.36 ARG 1

PRO 221 0.24 THR 158 -0.38 PRO 2

PRO 221 0.34 LEU 159 -0.45 LEU 228

PRO 221 0.40 ILE 160 -0.42 ARG 1

SER 179 0.32 GLY 161 -0.42 PRO 2

SER 179 0.27 LEU 162 -0.52 LEU 228

PRO 221 0.31 ALA 163 -0.54 PRO 2

PRO 221 0.33 MET 164 -0.47 PRO 2

ASP 42 0.25 ASN 165 -0.46 PRO 2

ILE 220 0.27 ASP 166 -0.56 PRO 2

ASN 219 0.48 SER 167 -0.56 PRO 2

ASN 219 0.46 GLY 168 -0.44 PRO 2

ASP 42 0.37 GLY 169 -0.38 PRO 2

ASP 42 0.32 TYR 170 -0.36 PRO 2

ASP 42 0.28 ASN 171 -0.32 LEU 228

PRO 221 0.24 ALA 172 -0.33 PRO 2

ASP 42 0.20 ASN 173 -0.34 PRO 157

LYS 21 0.23 SER 174 -0.23 THR 232

PRO 221 0.28 MET 175 -0.25 PRO 2

PRO 221 0.26 TRP 176 -0.26 ARG 1

PRO 221 0.22 GLY 177 -0.23 ARG 231

GLY 161 0.26 PRO 178 -0.28 ARG 231

GLY 161 0.32 SER 179 -0.30 ARG 231

GLY 161 0.23 SER 180 -0.28 ARG 231

PRO 221 0.22 ASP 181 -0.24 ARG 1

PRO 221 0.24 PRO 182 -0.25 ARG 1

PRO 221 0.27 ALA 183 -0.26 ARG 1

PRO 221 0.29 TRP 184 -0.31 ARG 1

PRO 221 0.27 LYS 185 -0.31 ARG 1

PRO 221 0.28 ARG 186 -0.28 ARG 1

PRO 221 0.32 ASN 187 -0.33 ARG 1

PRO 221 0.31 ASP 188 -0.37 ARG 1

PRO 221 0.28 PRO 189 -0.41 ARG 1

PRO 221 0.24 MET 190 -0.41 ARG 1

PRO 221 0.23 VAL 191 -0.35 ARG 1

PRO 221 0.24 GLN 192 -0.34 ARG 1

PRO 221 0.21 ILE 193 -0.36 ARG 1

PRO 221 0.19 PRO 194 -0.31 ARG 1

PRO 221 0.21 ARG 195 -0.31 GLY 280

PRO 221 0.21 LEU 196 -0.33 ARG 1

GLY 245 0.17 VAL 197 -0.37 GLY 280

PRO 221 0.17 ALA 198 -0.40 GLY 280

PRO 221 0.19 ASN 199 -0.43 GLY 280

ARG 246 0.18 ASN 200 -0.48 GLY 280

PRO 221 0.18 THR 201 -0.34 VAL 277

GLN 137 0.15 ARG 202 -0.37 ARG 1

PRO 221 0.17 ILE 203 -0.43 ARG 1

PRO 221 0.16 TRP 204 -0.51 ARG 1

PRO 221 0.16 VAL 205 -0.56 ARG 1

ALA 222 0.13 TYR 206 -0.63 ARG 1

ASP 273 0.10 CYS 207 -0.64 ARG 1

SER 259 0.15 GLY 208 -0.64 ARG 1

SER 259 0.22 ASN 209 -0.56 ARG 1

SER 259 0.29 GLY 210 -0.58 ARG 1

SER 259 0.32 THR 211 -0.54 ARG 1

ASN 50 0.39 PRO 212 -0.58 ARG 1

ASN 50 0.35 SER 213 -0.58 ARG 1

ASN 50 0.50 ASP 214 -0.52 ARG 1

ASN 50 0.48 LEU 215 -0.72 ARG 1

ASN 50 0.61 GLY 216 -0.67 ARG 1

ASN 50 0.65 GLY 217 -0.62 ARG 1

ASN 50 0.59 ASP 218 -0.51 ARG 1

ARG 39 0.77 ASN 219 -0.48 PRO 2

ARG 39 0.71 ILE 220 -0.46 PRO 2

ARG 39 0.75 PRO 221 -0.53 PRO 2

GLY 37 0.54 ALA 222 -0.61 ARG 1

ARG 39 0.37 LYS 223 -0.55 ARG 1

ARG 39 0.29 PHE 224 -0.53 ARG 1

GLY 147 0.24 LEU 225 -0.58 ARG 1

GLY 37 0.15 GLU 226 -0.61 ARG 1

GLY 37 0.13 GLY 227 -0.54 ARG 1

THR 232 0.13 LEU 228 -0.52 LEU 162

LEU 225 0.14 THR 229 -0.56 ARG 1

ARG 231 0.09 LEU 230 -0.55 ARG 1

ASN 233 0.13 ARG 231 -0.48 ARG 1

LEU 225 0.15 THR 232 -0.51 ARG 1

ARG 231 0.13 ASN 233 -0.52 ARG 1

GLY 248 0.08 GLN 234 -0.50 ARG 1

LEU 225 0.11 THR 235 -0.46 ARG 1

PRO 221 0.15 PHE 236 -0.46 ARG 1

GLY 245 0.09 ARG 237 -0.47 ARG 1

ARG 246 0.10 ASP 238 -0.44 ARG 1

PRO 221 0.11 THR 239 -0.41 ARG 1

GLY 245 0.15 TYR 240 -0.41 ARG 1

ASN 200 0.09 ALA 241 -0.43 ARG 1

ARG 195 0.07 ALA 242 -0.39 ARG 1

PRO 221 0.12 ASP 243 -0.36 ARG 1

ARG 195 0.17 GLY 244 -0.37 ARG 1

LEU 196 0.20 GLY 245 -0.37 ARG 1

ASN 200 0.18 ARG 246 -0.42 ARG 1

PRO 136 0.11 ASN 247 -0.39 ARG 1

PRO 221 0.11 GLY 248 -0.46 ARG 1

GLN 137 0.11 VAL 249 -0.51 ARG 1

ARG 231 0.12 PHE 250 -0.55 ARG 1

ASP 273 0.10 ASN 251 -0.59 ARG 1

ASP 273 0.09 PHE 252 -0.59 ARG 1

SER 259 0.16 PRO 253 -0.55 ARG 1

SER 259 0.22 PRO 254 -0.48 ARG 1

SER 259 0.22 ASN 255 -0.57 ARG 1

SER 259 0.32 GLY 256 -0.66 ARG 1

SER 259 0.39 THR 257 -0.70 ARG 1

GLY 37 0.28 HIS 258 -0.73 ARG 1

GLY 217 0.58 SER 259 -0.89 ARG 1

GLY 217 0.64 TRP 260 -1.02 ARG 1

TRP 47 0.35 PRO 261 -1.03 ARG 1

LEU 34 0.22 TYR 262 -0.87 ARG 1

GLY 217 0.29 TRP 263 -0.85 ARG 1

GLY 217 0.32 ASN 264 -0.95 ARG 1

LYS 271 0.23 GLU 265 -0.88 ARG 1

LYS 271 0.21 GLN 266 -0.74 ARG 1

GLY 217 0.27 LEU 267 -0.65 ARG 1

GLY 217 0.22 VAL 268 -0.63 ARG 1

GLN 266 0.20 ALA 269 -0.60 ARG 1

GLN 266 0.20 MET 270 -0.50 ARG 1

GLY 217 0.24 LYS 271 -0.37 ARG 1

GLU 265 0.20 ALA 272 -0.41 ARG 246

GLN 266 0.18 ASP 273 -0.39 ALA 272

GLY 217 0.21 ILE 274 -0.30 ARG 202

GLY 217 0.21 GLN 275 -0.34 ASN 200

GLY 217 0.18 HIS 276 -0.43 ASN 200

PRO 221 0.16 VAL 277 -0.45 ASN 200

ASN 219 0.20 LEU 278 -0.35 ASN 200

GLY 3 0.31 ASN 279 -0.36 ASN 200

GLY 3 0.29 GLY 280 -0.48 ASN 200

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 15 ---

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

* 1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *