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 14 ---

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 0.50 ARG 1 -0.92 THR 51

ASN 108 0.50 PRO 2 -0.88 ASN 50

LYS 109 0.53 GLY 3 -0.63 ASN 50

LYS 109 0.54 LEU 4 -0.51 PRO 52

LYS 109 0.57 PRO 5 -0.27 ILE 49

ARG 1 0.40 VAL 6 -0.22 ILE 49

ARG 1 0.50 GLU 7 -0.17 GLY 26

ASN 219 0.45 TYR 8 -0.13 PHE 24

ASN 219 0.44 LEU 9 -0.11 ASP 43

ASN 219 0.42 GLN 10 -0.13 LYS 21

ASN 219 0.41 VAL 11 -0.12 ASP 42

ASN 219 0.37 PRO 12 -0.14 ASP 42

ASN 219 0.37 SER 13 -0.13 ASP 42

ASN 219 0.33 ALA 14 -0.12 GLY 17

ASN 219 0.34 SER 15 -0.09 ALA 40

ASN 219 0.36 MET 16 -0.11 ALA 40

TYR 89 0.41 GLY 17 -0.12 ALA 14

ASN 88 0.40 ARG 18 -0.17 ASP 42

ASN 219 0.40 ASP 19 -0.18 ASP 42

ASN 219 0.45 ILE 20 -0.19 ASP 42

ASN 219 0.50 LYS 21 -0.13 GLN 10

ASN 219 0.50 VAL 22 -0.10 LEU 105

ASN 219 0.49 GLN 23 -0.10 GLY 37

ASN 219 0.43 PHE 24 -0.13 TYR 8

ASN 219 0.35 GLN 25 -0.12 GLU 7

LYS 109 0.44 GLY 26 -0.17 GLU 7

LEU 4 0.47 GLY 27 -0.10 ARG 246

GLY 3 0.41 GLY 28 -0.12 TYR 8

GLY 3 0.37 PRO 29 -0.12 TYR 8

ASN 219 0.30 HIS 30 -0.11 ALA 163

ASN 219 0.35 ALA 31 -0.12 ALA 163

ASN 219 0.38 VAL 32 -0.15 ARG 1

ASN 219 0.43 TYR 33 -0.15 GLY 37

ASN 219 0.50 LEU 34 -0.27 ARG 1

PRO 221 0.57 LEU 35 -0.29 ARG 1

PRO 221 0.69 ASP 36 -0.41 GLY 37

PRO 221 0.93 GLY 37 -0.49 PRO 2

PRO 221 0.89 LEU 38 -0.46 PRO 2

PRO 221 0.91 ARG 39 -0.52 PRO 2

PRO 221 0.82 ALA 40 -0.40 PRO 2

ASN 219 0.77 GLN 41 -0.38 PRO 2

ASN 219 0.66 ASP 42 -0.23 PRO 2

ASN 219 0.66 ASP 43 -0.30 GLY 3

ASN 219 0.67 TYR 44 -0.35 GLY 3

ASN 219 0.66 ASN 45 -0.38 PRO 2

ASN 219 0.77 GLY 46 -0.55 PRO 2

ASN 219 0.61 TRP 47 -0.54 PRO 2

ASN 219 0.58 ASP 48 -0.56 PRO 2

ASN 219 0.70 ILE 49 -0.75 PRO 2

ASN 219 0.69 ASN 50 -0.88 PRO 2

ASN 219 0.47 THR 51 -0.92 ARG 1

ASN 219 0.37 PRO 52 -0.86 ARG 1

ASN 219 0.36 ALA 53 -0.52 ARG 1

GLU 55 0.46 PHE 54 -0.22 GLY 37

PHE 54 0.46 GLU 55 -0.35 ARG 1

ASN 219 0.24 GLU 56 -0.46 ALA 269

ASN 219 0.27 TYR 57 -0.25 ARG 246

GLY 27 0.30 TYR 58 -0.21 ARG 246

GLY 3 0.32 GLN 59 -0.20 ARG 246

ASN 219 0.24 SER 60 -0.23 ARG 246

GLY 3 0.31 GLY 61 -0.14 ARG 246

ASN 219 0.30 LEU 62 -0.13 ALA 163

ASN 219 0.35 SER 63 -0.10 TYR 8

ASN 219 0.40 VAL 64 -0.13 GLY 37

ASN 219 0.45 ILE 65 -0.12 GLY 37

ASN 219 0.52 MET 66 -0.15 GLY 37

ASN 219 0.54 PRO 67 -0.10 ALA 40

ASN 219 0.60 VAL 68 -0.16 PRO 2

ASN 219 0.62 GLY 69 -0.20 ALA 40

PRO 221 0.60 GLY 70 -0.20 PRO 2

PRO 221 0.67 GLN 71 -0.30 PRO 2

PRO 221 0.61 SER 72 -0.33 PRO 2

PRO 221 0.56 SER 73 -0.22 PRO 2

PRO 221 0.58 PHE 74 -0.25 PRO 2

PRO 221 0.54 TYR 75 -0.16 ARG 1

PRO 221 0.46 THR 76 -0.15 GLY 280

PRO 221 0.39 ASP 77 -0.13 GLY 280

PRO 221 0.35 TRP 78 -0.12 GLY 280

PRO 221 0.28 TYR 79 -0.15 THR 232

GLY 17 0.28 GLN 80 -0.16 ARG 231

GLY 17 0.33 PRO 81 -0.18 THR 229

ILE 220 0.27 SER 82 -0.23 THR 229

GLY 17 0.27 GLN 83 -0.29 THR 158

GLY 17 0.21 SER 84 -0.33 LEU 228

ILE 220 0.28 ASN 85 -0.26 LEU 228

LYS 21 0.32 GLY 86 -0.21 LEU 228

ASN 219 0.33 GLN 87 -0.17 THR 229

GLY 17 0.40 ASN 88 -0.15 LEU 228

GLY 17 0.41 TYR 89 -0.10 THR 229

ASN 219 0.33 THR 90 -0.10 THR 232

PRO 221 0.40 TYR 91 -0.08 GLY 280

PRO 221 0.40 LYS 92 -0.09 GLY 280

PRO 221 0.46 TRP 93 -0.10 GLY 280

PRO 221 0.44 GLU 94 -0.14 GLY 280

PRO 221 0.39 THR 95 -0.11 GLY 280

PRO 221 0.41 PHE 96 -0.09 GLY 280

PRO 221 0.43 LEU 97 -0.11 GLY 280

PRO 221 0.39 THR 98 -0.14 GLY 280

PRO 221 0.36 ARG 99 -0.11 GLY 280

ASN 219 0.36 GLU 100 -0.08 ASP 42

ASN 219 0.39 MET 101 -0.09 ASP 42

ASN 219 0.36 PRO 102 -0.09 GLY 280

ASN 219 0.34 ALA 103 -0.08 ASP 42

PRO 5 0.37 TRP 104 -0.10 GLN 10

PRO 5 0.41 LEU 105 -0.12 GLN 10

GLY 3 0.40 GLN 106 -0.09 GLN 10

GLY 3 0.44 ALA 107 -0.08 ASP 43

GLY 3 0.51 ASN 108 -0.10 ASP 43

PRO 5 0.57 LYS 109 -0.12 TYR 8

GLY 3 0.52 GLY 110 -0.09 TYR 8

GLY 26 0.40 VAL 111 -0.10 TYR 8

GLY 3 0.32 SER 112 -0.10 GLY 280

PRO 221 0.32 PRO 113 -0.13 GLY 280

PRO 221 0.30 THR 114 -0.18 GLY 280

PRO 221 0.29 GLY 115 -0.24 GLY 280

PRO 221 0.33 ASN 116 -0.15 GLY 280

PRO 221 0.34 ALA 117 -0.19 ARG 1

PRO 221 0.40 ALA 118 -0.24 ARG 1

PRO 221 0.41 VAL 119 -0.37 ARG 1

PRO 221 0.50 GLY 120 -0.41 ARG 1

PRO 221 0.55 LEU 121 -0.51 ARG 1

PRO 221 0.65 SER 122 -0.57 ALA 163

PRO 221 0.71 MET 123 -0.41 ALA 163

PRO 221 0.61 SER 124 -0.36 ARG 1

PRO 221 0.49 GLY 125 -0.42 ARG 1

PRO 221 0.46 GLY 126 -0.34 ARG 1

PRO 221 0.48 SER 127 -0.27 ARG 1

PRO 221 0.45 ALA 128 -0.28 ARG 1

PRO 221 0.37 LEU 129 -0.30 ARG 1

PRO 221 0.39 ILE 130 -0.22 ARG 1

PRO 221 0.40 LEU 131 -0.19 GLY 280

PRO 221 0.34 ALA 132 -0.24 GLY 280

PRO 221 0.32 ALA 133 -0.28 GLY 280

PRO 221 0.33 TYR 134 -0.27 GLY 280

PRO 221 0.33 TYR 135 -0.26 GLY 280

PRO 221 0.30 PRO 136 -0.32 GLY 280

PRO 221 0.29 GLN 137 -0.31 GLY 280

PRO 221 0.32 GLN 138 -0.24 GLY 280

PRO 221 0.32 PHE 139 -0.23 GLY 280

PRO 221 0.27 PRO 140 -0.30 GLY 280

PRO 221 0.27 TYR 141 -0.26 ARG 1

PRO 221 0.32 ALA 142 -0.31 ARG 1

PRO 221 0.32 ALA 143 -0.43 ARG 1

PRO 221 0.36 SER 144 -0.47 ARG 1

ALA 222 0.33 LEU 145 -0.55 ARG 1

ALA 222 0.33 SER 146 -0.55 ARG 1

PRO 221 0.43 GLY 147 -0.48 ARG 1

PRO 221 0.41 PHE 148 -0.49 ALA 163

PRO 221 0.35 LEU 149 -0.39 ARG 1

PRO 221 0.32 ASN 150 -0.33 ARG 1

PRO 221 0.39 PRO 151 -0.32 ASN 150

PRO 221 0.31 SER 152 -0.26 ARG 1

PRO 221 0.26 GLU 153 -0.29 ARG 1

PRO 221 0.20 SER 154 -0.35 ARG 231

PRO 221 0.22 TRP 155 -0.39 ARG 231

PRO 221 0.35 TRP 156 -0.37 ARG 231

PRO 221 0.29 PRO 157 -0.35 ASN 173

PRO 221 0.19 THR 158 -0.38 ARG 231

PRO 221 0.27 LEU 159 -0.52 LEU 228

PRO 221 0.38 ILE 160 -0.47 PHE 148

SER 179 0.32 GLY 161 -0.46 THR 229

SER 179 0.26 LEU 162 -0.63 LEU 228

ILE 220 0.32 ALA 163 -0.57 THR 229

ILE 220 0.37 MET 164 -0.44 SER 122

ILE 220 0.22 ASN 165 -0.43 THR 229

ILE 220 0.27 ASP 166 -0.48 LEU 225

ILE 220 0.52 SER 167 -0.46 PRO 2

ILE 220 0.47 GLY 168 -0.34 PRO 2

ILE 220 0.29 GLY 169 -0.33 THR 229

ILE 220 0.32 TYR 170 -0.31 THR 229

ILE 220 0.23 ASN 171 -0.36 THR 229

PRO 221 0.26 ALA 172 -0.38 PHE 148

PRO 221 0.19 ASN 173 -0.35 PRO 157

ILE 220 0.23 SER 174 -0.25 ARG 231

PRO 221 0.34 MET 175 -0.19 THR 232

PRO 221 0.31 TRP 176 -0.21 THR 232

PRO 221 0.24 GLY 177 -0.24 ARG 231

GLY 161 0.27 PRO 178 -0.29 ARG 231

GLY 161 0.32 SER 179 -0.30 ARG 231

GLY 161 0.24 SER 180 -0.27 ARG 231

PRO 221 0.24 ASP 181 -0.21 ARG 231

PRO 221 0.26 PRO 182 -0.20 GLY 280

PRO 221 0.31 ALA 183 -0.18 GLY 280

PRO 221 0.32 TRP 184 -0.21 ARG 1

PRO 221 0.31 LYS 185 -0.22 ARG 1

PRO 221 0.33 ARG 186 -0.21 GLY 280

PRO 221 0.39 ASN 187 -0.22 ARG 1

PRO 221 0.36 ASP 188 -0.27 ARG 1

PRO 221 0.32 PRO 189 -0.31 ARG 1

PRO 221 0.25 MET 190 -0.33 ARG 1

PRO 221 0.25 VAL 191 -0.27 ARG 1

PRO 221 0.27 GLN 192 -0.25 ARG 1

PRO 221 0.22 ILE 193 -0.29 ARG 1

GLY 244 0.22 PRO 194 -0.26 GLY 280

GLY 244 0.26 ARG 195 -0.29 GLY 280

GLY 245 0.29 LEU 196 -0.28 GLY 280

TYR 135 0.23 VAL 197 -0.30 HIS 276

TYR 135 0.26 ALA 198 -0.34 GLY 280

GLY 245 0.24 ASN 199 -0.40 GLY 280

GLN 137 0.26 ASN 200 -0.38 HIS 276

PRO 221 0.23 THR 201 -0.30 HIS 276

PRO 140 0.23 ARG 202 -0.33 ARG 1

PRO 221 0.22 ILE 203 -0.38 ARG 1

PRO 221 0.21 TRP 204 -0.47 ARG 1

ALA 222 0.19 VAL 205 -0.51 ARG 1

ALA 222 0.18 TYR 206 -0.57 ARG 1

ASP 273 0.14 CYS 207 -0.57 ARG 1

ASP 273 0.16 GLY 208 -0.59 ARG 1

SER 259 0.22 ASN 209 -0.50 ARG 1

SER 259 0.30 GLY 210 -0.51 ARG 1

SER 259 0.34 THR 211 -0.49 ARG 1

SER 259 0.39 PRO 212 -0.55 ARG 1

ASN 50 0.28 SER 213 -0.60 ARG 1

ASN 50 0.39 ASP 214 -0.61 ARG 1

ASN 50 0.37 LEU 215 -0.75 ARG 1

ASN 50 0.53 GLY 216 -0.63 ARG 1

TRP 260 0.66 GLY 217 -0.53 PRO 2

ASN 50 0.58 ASP 218 -0.46 PRO 2

ALA 40 0.82 ASN 219 -0.35 PRO 2

ARG 39 0.85 ILE 220 -0.33 PRO 2

GLY 37 0.93 PRO 221 -0.38 PRO 2

GLY 37 0.69 ALA 222 -0.48 PRO 2

GLY 37 0.45 LYS 223 -0.45 PRO 2

GLY 37 0.43 PHE 224 -0.42 PRO 2

GLY 37 0.37 LEU 225 -0.57 LEU 162

GLY 37 0.21 GLU 226 -0.53 LEU 162

GLY 37 0.18 GLY 227 -0.50 LEU 162

GLY 37 0.14 LEU 228 -0.63 LEU 162

LEU 225 0.12 THR 229 -0.60 LEU 162

ASP 273 0.11 LEU 230 -0.49 LEU 162

PHE 250 0.15 ARG 231 -0.48 LEU 162

LEU 225 0.12 THR 232 -0.43 LEU 162

ARG 231 0.12 ASN 233 -0.46 ARG 1

PHE 250 0.14 GLN 234 -0.45 ARG 1

GLN 137 0.10 THR 235 -0.41 ARG 1

PRO 221 0.12 PHE 236 -0.40 ARG 1

GLN 137 0.17 ARG 237 -0.43 ARG 1

GLN 137 0.15 ASP 238 -0.40 ARG 1

ARG 99 0.12 THR 239 -0.36 ARG 1

GLY 245 0.17 TYR 240 -0.36 ARG 1

GLN 137 0.19 ALA 241 -0.43 PRO 254

GLN 137 0.16 ALA 242 -0.39 PRO 254

ARG 195 0.18 ASP 243 -0.32 ARG 1

ARG 195 0.26 GLY 244 -0.35 PRO 254

LEU 196 0.29 GLY 245 -0.34 ARG 1

ASN 200 0.25 ARG 246 -0.42 ARG 1

GLN 137 0.20 ASN 247 -0.38 ARG 1

GLN 137 0.16 GLY 248 -0.44 ARG 1

GLY 115 0.16 VAL 249 -0.50 ARG 1

ARG 231 0.15 PHE 250 -0.53 ARG 1

ASP 273 0.17 ASN 251 -0.58 ARG 1

ASP 273 0.14 PHE 252 -0.57 ARG 1

SER 259 0.16 PRO 253 -0.56 ARG 1

SER 259 0.22 PRO 254 -0.49 ARG 1

SER 259 0.23 ASN 255 -0.56 ARG 1

SER 259 0.33 GLY 256 -0.61 ARG 1

SER 259 0.39 THR 257 -0.60 ARG 1

ALA 222 0.43 HIS 258 -0.59 ARG 1

GLY 217 0.62 SER 259 -0.71 ARG 1

GLY 217 0.66 TRP 260 -0.80 ARG 1

GLY 217 0.38 PRO 261 -0.91 ARG 1

GLY 217 0.24 TYR 262 -0.79 ARG 1

GLY 217 0.33 TRP 263 -0.72 ARG 1

GLY 217 0.35 ASN 264 -0.85 ARG 1

LYS 271 0.25 GLU 265 -0.88 ARG 1

MET 270 0.24 GLN 266 -0.71 ARG 1

GLY 217 0.31 LEU 267 -0.59 ARG 1

GLY 217 0.26 VAL 268 -0.64 ARG 1

GLN 266 0.23 ALA 269 -0.63 ARG 1

GLN 266 0.24 MET 270 -0.50 ARG 1

GLY 217 0.27 LYS 271 -0.39 ARG 1

GLY 217 0.23 ALA 272 -0.43 ASP 273

ALA 222 0.22 ASP 273 -0.43 ALA 272

PRO 221 0.25 ILE 274 -0.28 ARG 1

GLY 217 0.24 GLN 275 -0.27 ASN 200

GLY 217 0.21 HIS 276 -0.38 ASN 200

PRO 221 0.22 VAL 277 -0.34 ASN 200

PRO 221 0.24 LEU 278 -0.23 ASN 199

GLY 3 0.23 ASN 279 -0.26 ASN 199

GLY 3 0.21 GLY 280 -0.40 ASN 199

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 14 ---

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

* EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *