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 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
GLU 7 0.67 ARG 1 -0.65 PRO 52

GLU 7 0.64 PRO 2 -0.56 ASN 219

LYS 109 0.50 GLY 3 -0.45 ASN 219

LYS 109 0.49 LEU 4 -0.41 PRO 52

PRO 2 0.57 PRO 5 -0.29 ARG 246

ARG 1 0.60 VAL 6 -0.29 ARG 246

ARG 1 0.67 GLU 7 -0.29 ARG 246

ARG 1 0.56 TYR 8 -0.24 ASN 200

ARG 1 0.47 LEU 9 -0.26 ASN 200

ARG 1 0.38 GLN 10 -0.22 ASN 200

PRO 2 0.35 VAL 11 -0.22 ASN 200

PRO 2 0.30 PRO 12 -0.18 ASN 200

PRO 2 0.23 SER 13 -0.16 PRO 221

PRO 2 0.22 ALA 14 -0.14 PRO 221

PRO 2 0.16 SER 15 -0.15 PRO 221

ARG 1 0.15 MET 16 -0.15 PRO 221

ARG 1 0.18 GLY 17 -0.13 ILE 220

ARG 1 0.20 ARG 18 -0.14 ILE 220

ARG 1 0.27 ASP 19 -0.14 PRO 221

ARG 1 0.25 ILE 20 -0.17 PRO 221

ARG 1 0.31 LYS 21 -0.19 PRO 221

ARG 1 0.32 VAL 22 -0.22 ASN 200

ARG 1 0.35 GLN 23 -0.24 ARG 246

ARG 1 0.40 PHE 24 -0.30 ARG 246

PRO 2 0.33 GLN 25 -0.33 ARG 246

GLY 110 0.44 GLY 26 -0.36 ARG 246

LEU 4 0.32 GLY 27 -0.42 ARG 246

GLY 3 0.26 GLY 28 -0.45 ARG 246

GLY 3 0.25 PRO 29 -0.44 ARG 246

ARG 99 0.20 HIS 30 -0.48 ARG 246

ARG 99 0.17 ALA 31 -0.40 ARG 246

TYR 33 0.21 VAL 32 -0.36 ARG 246

VAL 32 0.21 TYR 33 -0.28 ALA 118

GLY 37 0.23 LEU 34 -0.28 PRO 221

LYS 271 0.21 LEU 35 -0.33 PRO 221

GLY 37 0.32 ASP 36 -0.39 PRO 221

ASP 36 0.32 GLY 37 -0.51 PRO 221

SER 122 0.24 LEU 38 -0.39 PRO 221

SER 259 0.34 ARG 39 -0.36 PRO 221

GLY 168 0.23 ALA 40 -0.39 PRO 221

GLY 168 0.34 GLN 41 -0.28 PRO 221

GLY 168 0.29 ASP 42 -0.23 PRO 221

GLY 168 0.26 ASP 43 -0.22 ILE 220

GLY 168 0.24 TYR 44 -0.26 PRO 221

GLY 168 0.23 ASN 45 -0.32 PRO 221

ARG 39 0.28 GLY 46 -0.39 PRO 221

ARG 39 0.26 TRP 47 -0.35 PRO 221

ASP 166 0.22 ASP 48 -0.31 PRO 221

ASP 166 0.24 ILE 49 -0.36 GLY 3

ASP 166 0.25 ASN 50 -0.47 PRO 2

ASP 166 0.21 THR 51 -0.54 ARG 1

ASP 166 0.20 PRO 52 -0.65 ARG 1

ASP 166 0.18 ALA 53 -0.33 ASN 219

GLU 55 0.46 PHE 54 -0.32 ARG 246

PHE 54 0.46 GLU 55 -0.38 ARG 1

ASP 166 0.16 GLU 56 -0.41 VAL 268

ASP 166 0.16 TYR 57 -0.39 ARG 246

GLY 110 0.23 TYR 58 -0.36 ARG 246

GLY 27 0.27 GLN 59 -0.40 ARG 246

ASP 166 0.15 SER 60 -0.46 ARG 246

ARG 99 0.16 GLY 61 -0.46 ARG 246

ARG 99 0.17 LEU 62 -0.45 ARG 246

LEU 4 0.21 SER 63 -0.41 ARG 246

GLU 55 0.18 VAL 64 -0.35 ARG 246

GLU 55 0.19 ILE 65 -0.28 ARG 246

GLY 168 0.20 MET 66 -0.26 PRO 221

GLY 168 0.19 PRO 67 -0.25 PRO 221

GLY 168 0.24 VAL 68 -0.25 PRO 221

GLY 168 0.23 GLY 69 -0.27 PRO 221

LYS 271 0.16 GLY 70 -0.27 PRO 221

VAL 68 0.19 GLN 71 -0.28 PRO 221

THR 239 0.23 SER 72 -0.22 PRO 221

ALA 242 0.19 SER 73 -0.22 PRO 221

SER 127 0.25 PHE 74 -0.24 PRO 221

ALA 118 0.20 TYR 75 -0.24 PRO 221

LEU 131 0.23 THR 76 -0.18 PRO 221

LEU 131 0.22 ASP 77 -0.16 ASP 181

ASP 243 0.27 TRP 78 -0.15 GLY 161

ASP 243 0.31 TYR 79 -0.13 SER 15

ALA 242 0.28 GLN 80 -0.11 ASN 165

ALA 242 0.27 PRO 81 -0.07 ILE 220

ALA 242 0.29 SER 82 -0.08 ASP 166

ALA 242 0.31 GLN 83 -0.07 ASP 166

ALA 242 0.31 SER 84 -0.06 ASP 166

ALA 242 0.26 ASN 85 -0.05 ILE 220

ALA 242 0.24 GLY 86 -0.07 ILE 220

ALA 242 0.22 GLN 87 -0.12 ILE 220

ALA 242 0.21 ASN 88 -0.10 ILE 220

ALA 242 0.19 TYR 89 -0.12 ILE 220

ALA 242 0.21 THR 90 -0.12 ILE 220

ALA 242 0.18 TYR 91 -0.16 PRO 221

THR 114 0.18 LYS 92 -0.17 PRO 221

THR 114 0.17 TRP 93 -0.21 PRO 221

THR 114 0.19 GLU 94 -0.23 ALA 183

THR 114 0.23 THR 95 -0.28 ALA 183

PRO 2 0.17 PHE 96 -0.20 ALA 183

THR 114 0.21 LEU 97 -0.21 PRO 221

THR 114 0.30 THR 98 -0.26 TYR 134

PRO 113 0.28 ARG 99 -0.28 ALA 183

PRO 2 0.27 GLU 100 -0.21 ALA 183

PRO 2 0.29 MET 101 -0.26 ASN 199

PRO 2 0.30 PRO 102 -0.37 ASN 199

PRO 2 0.36 ALA 103 -0.38 ASN 199

PRO 2 0.41 TRP 104 -0.34 ASN 200

PRO 2 0.43 LEU 105 -0.38 ASN 200

PRO 2 0.42 GLN 106 -0.44 ASN 200

PRO 2 0.49 ALA 107 -0.41 ASN 200

PRO 2 0.58 ASN 108 -0.38 ASN 200

PRO 2 0.56 LYS 109 -0.40 ASN 200

PRO 2 0.49 GLY 110 -0.45 ASN 200

GLY 26 0.36 VAL 111 -0.45 ASN 200

PRO 2 0.28 SER 112 -0.52 ASN 200

ARG 99 0.28 PRO 113 -0.45 ASN 199

THR 98 0.30 THR 114 -0.58 ASN 200

GLN 138 0.20 GLY 115 -0.62 ASN 200

THR 98 0.18 ASN 116 -0.45 ASN 200

GLN 275 0.22 ALA 117 -0.36 TYR 141

TYR 75 0.20 ALA 118 -0.28 TYR 33

LYS 271 0.23 VAL 119 -0.25 PRO 221

GLY 37 0.28 GLY 120 -0.29 PRO 221

ALA 163 0.27 LEU 121 -0.34 PRO 221

ALA 163 0.35 SER 122 -0.35 PRO 221

MET 164 0.25 MET 123 -0.32 PRO 221

SER 144 0.21 SER 124 -0.31 PRO 221

SER 144 0.24 GLY 125 -0.25 PRO 221

GLY 248 0.24 GLY 126 -0.18 PRO 221

PHE 74 0.25 SER 127 -0.21 PRO 221

ALA 142 0.32 ALA 128 -0.23 PRO 221

ALA 172 0.20 LEU 129 -0.24 PRO 102

TRP 78 0.24 ILE 130 -0.24 PRO 102

THR 76 0.23 LEU 131 -0.26 PRO 102

ASP 77 0.18 ALA 132 -0.31 PRO 102

THR 201 0.23 ALA 133 -0.29 PRO 102

ASP 77 0.22 TYR 134 -0.32 ALA 103

VAL 277 0.16 TYR 135 -0.36 PRO 102

PRO 140 0.18 PRO 136 -0.37 THR 114

VAL 277 0.17 GLN 137 -0.62 ASN 199

GLY 115 0.20 GLN 138 -0.42 ASN 199

VAL 277 0.19 PHE 139 -0.34 VAL 197

PRO 136 0.18 PRO 140 -0.56 THR 201

ALA 128 0.18 TYR 141 -0.36 ALA 117

ALA 128 0.32 ALA 142 -0.27 VAL 32

ALA 163 0.22 ALA 143 -0.25 ARG 1

ALA 163 0.26 SER 144 -0.25 ARG 1

ALA 163 0.31 LEU 145 -0.29 ARG 1

ALA 163 0.37 SER 146 -0.27 ARG 1

ALA 163 0.35 GLY 147 -0.21 ARG 1

ALA 163 0.38 PHE 148 -0.17 ARG 1

ALA 172 0.34 LEU 149 -0.18 ARG 1

THR 239 0.42 ASN 150 -0.17 THR 98

THR 239 0.43 PRO 151 -0.19 THR 98

ALA 242 0.51 SER 152 -0.26 LYS 185

ALA 242 0.55 GLU 153 -0.27 LYS 185

ALA 242 0.50 SER 154 -0.24 LYS 185

ALA 242 0.43 TRP 155 -0.21 LYS 185

ALA 242 0.43 TRP 156 -0.16 THR 98

ALA 242 0.41 PRO 157 -0.17 THR 76

ALA 242 0.38 THR 158 -0.17 SER 179

ALA 242 0.38 LEU 159 -0.09 THR 95

THR 239 0.37 ILE 160 -0.10 THR 76

ALA 242 0.35 GLY 161 -0.23 ALA 172

ALA 222 0.42 LEU 162 -0.19 PRO 178

HIS 258 0.43 ALA 163 -0.10 PRO 178

PHE 148 0.32 MET 164 -0.10 MET 175

HIS 258 0.34 ASN 165 -0.17 ALA 172

SER 259 0.43 ASP 166 -0.11 ALA 172

SER 259 0.37 SER 167 -0.13 ILE 220

GLN 41 0.34 GLY 168 -0.13 ILE 220

GLY 216 0.28 GLY 169 -0.08 SER 82

ALA 242 0.30 TYR 170 -0.09 GLN 80

ALA 242 0.34 ASN 171 -0.17 ASN 165

ALA 242 0.39 ALA 172 -0.23 GLY 161

ALA 242 0.39 ASN 173 -0.16 LEU 162

ALA 242 0.34 SER 174 -0.14 ASN 165

ALA 242 0.31 MET 175 -0.20 GLY 161

ASP 243 0.37 TRP 176 -0.19 GLY 161

ALA 242 0.39 GLY 177 -0.20 GLY 161

ALA 242 0.43 PRO 178 -0.19 LEU 162

ALA 242 0.48 SER 179 -0.17 ARG 99

ALA 242 0.52 SER 180 -0.20 ARG 99

ASP 243 0.45 ASP 181 -0.22 ARG 99

ASP 243 0.48 PRO 182 -0.27 ARG 99

ASP 243 0.39 ALA 183 -0.28 ARG 99

ASP 243 0.46 TRP 184 -0.23 ARG 99

ASP 243 0.48 LYS 185 -0.27 GLU 153

ASP 243 0.35 ARG 186 -0.25 ARG 99

GLY 245 0.30 ASN 187 -0.22 THR 98

TYR 240 0.36 ASP 188 -0.21 THR 98

ALA 172 0.32 PRO 189 -0.21 PRO 102

TYR 240 0.40 MET 190 -0.21 GLN 137

ASP 243 0.48 VAL 191 -0.20 ALA 103

ILE 193 0.37 GLN 192 -0.24 GLN 137

LYS 185 0.42 ILE 193 -0.33 GLN 137

LYS 185 0.40 PRO 194 -0.38 GLN 137

ARG 186 0.32 ARG 195 -0.42 GLN 137

LYS 185 0.26 LEU 196 -0.43 GLN 137

LYS 185 0.32 VAL 197 -0.49 GLY 115

LYS 185 0.29 ALA 198 -0.53 GLN 137

ARG 186 0.22 ASN 199 -0.62 GLN 137

LYS 185 0.25 ASN 200 -0.62 GLY 115

ALA 133 0.23 THR 201 -0.56 PRO 140

ALA 172 0.19 ARG 202 -0.42 ALA 241

ALA 163 0.23 ILE 203 -0.35 ALA 241

ALA 163 0.25 TRP 204 -0.34 ALA 241

ALA 163 0.30 VAL 205 -0.31 ARG 1

ALA 163 0.31 TYR 206 -0.35 ARG 1

ALA 163 0.32 CYS 207 -0.33 ARG 1

ALA 163 0.29 GLY 208 -0.35 ARG 1

LEU 162 0.22 ASN 209 -0.33 ARG 1

LEU 162 0.26 GLY 210 -0.37 ARG 1

LEU 162 0.22 THR 211 -0.39 ARG 1

ASP 166 0.27 PRO 212 -0.45 ARG 1

ASP 166 0.29 SER 213 -0.45 ARG 1

ASP 166 0.36 ASP 214 -0.50 ARG 1

ASP 166 0.35 LEU 215 -0.58 ARG 1

ASP 166 0.41 GLY 216 -0.55 ARG 1

ASP 166 0.41 GLY 217 -0.57 ARG 1

ASP 214 0.35 ASP 218 -0.52 ARG 1

LEU 162 0.28 ASN 219 -0.56 PRO 2

ARG 231 0.28 ILE 220 -0.50 PRO 2

LEU 162 0.31 PRO 221 -0.51 GLY 37

LEU 162 0.42 ALA 222 -0.48 SER 259

LEU 162 0.29 LYS 223 -0.40 ARG 1

ARG 231 0.36 PHE 224 -0.36 ARG 1

LEU 162 0.41 LEU 225 -0.30 ARG 1

LEU 162 0.35 GLU 226 -0.31 ARG 1

PHE 224 0.32 GLY 227 -0.30 ARG 1

ARG 231 0.43 LEU 228 -0.26 ARG 1

ALA 163 0.39 THR 229 -0.23 ARG 1

ALA 163 0.31 LEU 230 -0.27 ARG 1

LEU 228 0.43 ARG 231 -0.26 ARG 1

ALA 163 0.36 THR 232 -0.22 ARG 1

ALA 163 0.35 ASN 233 -0.26 ARG 1

ALA 163 0.31 GLN 234 -0.28 ARG 1

LEU 159 0.38 THR 235 -0.23 ARG 1

PRO 151 0.34 PHE 236 -0.24 ARG 1

ALA 163 0.30 ARG 237 -0.30 ARG 1

GLU 153 0.37 ASP 238 -0.30 VAL 277

GLU 153 0.52 THR 239 -0.31 VAL 277

SER 152 0.42 TYR 240 -0.38 VAL 277

GLU 153 0.42 ALA 241 -0.54 VAL 277

GLU 153 0.55 ALA 242 -0.46 VAL 277

SER 180 0.50 ASP 243 -0.46 VAL 277

SER 180 0.42 GLY 244 -0.57 GLY 280

VAL 191 0.44 GLY 245 -0.60 VAL 277

VAL 191 0.34 ARG 246 -0.75 VAL 277

LYS 185 0.25 ASN 247 -0.70 VAL 277

ALA 163 0.27 GLY 248 -0.48 VAL 277

ALA 163 0.26 VAL 249 -0.41 ALA 241

ALA 163 0.29 PHE 250 -0.36 ARG 1

ALA 163 0.27 ASN 251 -0.38 ARG 1

ALA 163 0.26 PHE 252 -0.36 ARG 1

ALA 163 0.23 PRO 253 -0.34 ARG 1

ASP 166 0.19 PRO 254 -0.32 ARG 1

ASP 166 0.23 ASN 255 -0.36 ARG 1

ASP 166 0.29 GLY 256 -0.40 ARG 1

ASP 166 0.34 THR 257 -0.41 ARG 1

ALA 163 0.43 HIS 258 -0.37 ARG 1

ASP 166 0.43 SER 259 -0.48 ALA 222

ASP 166 0.35 TRP 260 -0.48 ARG 1

ASP 166 0.32 PRO 261 -0.60 ARG 1

ASP 166 0.31 TYR 262 -0.50 ARG 1

ASP 166 0.29 TRP 263 -0.42 ARG 1

ASP 166 0.26 ASN 264 -0.53 ARG 1

ASP 166 0.26 GLU 265 -0.56 ARG 1

ASP 166 0.24 GLN 266 -0.44 ARG 1

ARG 39 0.24 LEU 267 -0.38 ARG 1

ASP 166 0.20 VAL 268 -0.47 ARG 1

ASP 166 0.22 ALA 269 -0.45 ARG 1

ALA 163 0.22 MET 270 -0.41 ALA 241

GLY 37 0.24 LYS 271 -0.45 ARG 246

GLY 37 0.21 ALA 272 -0.52 ARG 246

ALA 163 0.21 ASP 273 -0.55 ARG 246

VAL 119 0.23 ILE 274 -0.53 ARG 246

ALA 117 0.22 GLN 275 -0.58 ARG 246

ALA 117 0.20 HIS 276 -0.71 ARG 246

PHE 139 0.19 VAL 277 -0.75 ARG 246

ALA 117 0.21 LEU 278 -0.60 ARG 246

THR 98 0.19 ASN 279 -0.60 ARG 246

GLN 138 0.17 GLY 280 -0.69 ARG 246

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 15 ---

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

* EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *