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 16 ---

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 1.05 ARG 1 -0.69 PRO 261

ASN 108 0.93 PRO 2 -0.67 ASN 50

ASN 108 0.63 GLY 3 -0.68 ILE 49

PRO 5 0.75 LEU 4 -0.64 ILE 49

LEU 4 0.75 PRO 5 -0.36 ILE 49

ARG 1 0.72 VAL 6 -0.33 ILE 49

ARG 1 1.05 GLU 7 -0.19 GLY 26

ARG 1 1.05 TYR 8 -0.19 ILE 130

ARG 1 0.91 LEU 9 -0.23 TYR 134

ARG 1 0.80 GLN 10 -0.25 ASN 187

ARG 1 0.67 VAL 11 -0.28 TYR 134

ARG 1 0.60 PRO 12 -0.30 ARG 186

ARG 1 0.49 SER 13 -0.32 ALA 183

ARG 1 0.46 ALA 14 -0.36 ALA 183

ARG 1 0.36 SER 15 -0.38 ALA 183

ARG 1 0.38 MET 16 -0.32 ALA 183

ARG 1 0.45 GLY 17 -0.34 TYR 79

ARG 1 0.52 ARG 18 -0.27 ALA 183

ARG 1 0.61 ASP 19 -0.28 ASN 187

ARG 1 0.57 ILE 20 -0.28 TRP 93

ARG 1 0.65 LYS 21 -0.25 ASN 187

ARG 1 0.60 VAL 22 -0.24 ILE 130

ARG 1 0.60 GLN 23 -0.18 ILE 130

ARG 1 0.58 PHE 24 -0.20 GLN 59

PRO 2 0.46 GLN 25 -0.25 GLN 59

LEU 4 0.50 GLY 26 -0.42 GLN 59

LEU 4 0.56 GLY 27 -0.44 GLN 59

LEU 4 0.47 GLY 28 -0.29 GLN 59

PRO 2 0.43 PRO 29 -0.21 GLN 59

ASP 214 0.36 HIS 30 -0.19 GLN 59

ASP 214 0.34 ALA 31 -0.19 GLN 59

ASP 214 0.35 VAL 32 -0.22 GLU 56

ASP 214 0.25 TYR 33 -0.16 ALA 128

GLY 37 0.28 LEU 34 -0.16 ALA 128

GLY 37 0.24 LEU 35 -0.17 GLY 3

GLY 37 0.34 ASP 36 -0.25 GLY 3

ASP 36 0.34 GLY 37 -0.23 GLY 3

MET 164 0.22 LEU 38 -0.22 GLY 3

GLY 46 0.38 ARG 39 -0.25 GLY 3

GLY 46 0.28 ALA 40 -0.27 GLY 3

GLY 86 0.33 GLN 41 -0.35 GLY 3

GLY 86 0.33 ASP 42 -0.30 GLY 3

ARG 1 0.39 ASP 43 -0.37 GLY 3

ARG 1 0.31 TYR 44 -0.40 GLY 3

GLY 86 0.25 ASN 45 -0.35 GLY 3

ARG 39 0.38 GLY 46 -0.44 GLY 3

ARG 39 0.30 TRP 47 -0.39 GLY 3

ASN 219 0.27 ASP 48 -0.55 LEU 4

ASN 219 0.32 ILE 49 -0.68 GLY 3

ASN 219 0.43 ASN 50 -0.67 PRO 2

ASN 219 0.38 THR 51 -0.63 ARG 1

ASN 219 0.34 PRO 52 -0.61 ARG 1

ASP 214 0.37 ALA 53 -0.33 ARG 1

GLU 55 0.62 PHE 54 -0.22 TYR 58

PHE 54 0.62 GLU 55 -0.29 ARG 1

ASP 214 0.56 GLU 56 -0.36 ARG 1

ASP 214 0.55 TYR 57 -0.26 GLU 56

ASP 214 0.51 TYR 58 -0.22 PHE 54

ASP 214 0.63 GLN 59 -0.44 GLY 27

ASP 214 0.62 SER 60 -0.18 GLU 55

ASP 214 0.52 GLY 61 -0.20 GLN 59

ASP 214 0.46 LEU 62 -0.21 GLN 59

ASP 214 0.39 SER 63 -0.31 GLN 59

ASP 214 0.35 VAL 64 -0.21 GLN 59

PRO 2 0.27 ILE 65 -0.16 GLN 59

ARG 1 0.23 MET 66 -0.20 ALA 128

ARG 1 0.31 PRO 67 -0.23 ILE 130

ARG 1 0.34 VAL 68 -0.22 PRO 189

GLY 86 0.25 GLY 69 -0.20 GLY 3

LEU 34 0.20 GLY 70 -0.20 PRO 189

GLY 46 0.28 GLN 71 -0.19 GLY 3

ASP 36 0.26 SER 72 -0.20 ASN 150

ALA 118 0.21 SER 73 -0.21 ASN 150

GLY 120 0.24 PHE 74 -0.26 ASN 150

ALA 118 0.23 TYR 75 -0.28 PRO 189

ALA 118 0.20 THR 76 -0.36 ASN 187

ALA 118 0.18 ASP 77 -0.36 ASN 187

ALA 118 0.17 TRP 78 -0.29 ASP 243

ALA 118 0.16 TYR 79 -0.34 SER 15

ARG 1 0.19 GLN 80 -0.27 GLY 17

ARG 1 0.23 PRO 81 -0.23 ASP 243

GLY 46 0.22 SER 82 -0.23 ASP 243

GLY 46 0.22 GLN 83 -0.22 ASP 243

GLN 41 0.25 SER 84 -0.20 ASP 243

GLN 41 0.31 ASN 85 -0.18 ASP 243

GLN 41 0.33 GLY 86 -0.18 ASP 243

ARG 1 0.30 GLN 87 -0.19 ASP 243

ARG 1 0.33 ASN 88 -0.20 ASP 243

ARG 1 0.31 TYR 89 -0.22 ASP 243

ARG 1 0.26 THR 90 -0.25 GLY 17

ARG 1 0.22 TYR 91 -0.25 ASN 187

ARG 1 0.22 LYS 92 -0.35 ASN 187

ARG 1 0.19 TRP 93 -0.31 ASN 187

GLN 138 0.19 GLU 94 -0.37 ASN 187

PRO 2 0.26 THR 95 -0.42 ARG 186

ARG 1 0.31 PHE 96 -0.35 ASN 187

PRO 2 0.24 LEU 97 -0.32 ILE 130

PRO 2 0.25 THR 98 -0.45 TYR 134

PRO 2 0.37 ARG 99 -0.49 TYR 134

PRO 2 0.45 GLU 100 -0.37 TYR 134

PRO 2 0.47 MET 101 -0.36 TYR 134

PRO 2 0.46 PRO 102 -0.39 TYR 134

PRO 2 0.57 ALA 103 -0.41 TYR 134

PRO 2 0.68 TRP 104 -0.35 TYR 134

PRO 2 0.67 LEU 105 -0.29 TYR 134

PRO 2 0.65 GLN 106 -0.29 TYR 134

PRO 2 0.78 ALA 107 -0.30 TYR 134

PRO 2 0.93 ASN 108 -0.27 TYR 134

PRO 2 0.84 LYS 109 -0.21 TYR 134

PRO 2 0.70 GLY 110 -0.19 TYR 134

PRO 2 0.54 VAL 111 -0.18 TYR 134

PRO 2 0.43 SER 112 -0.17 TYR 134

PRO 2 0.39 PRO 113 -0.26 TYR 134

PRO 2 0.28 THR 114 -0.17 PRO 136

ASP 214 0.30 GLY 115 -0.17 GLU 56

ASP 214 0.31 ASN 116 -0.19 GLU 56

ASP 214 0.32 ALA 117 -0.22 GLU 56

ASP 214 0.26 ALA 118 -0.19 GLU 56

ASP 214 0.27 VAL 119 -0.18 ARG 1

GLY 37 0.29 GLY 120 -0.20 ARG 1

ILE 160 0.27 LEU 121 -0.27 ARG 1

ILE 160 0.35 SER 122 -0.27 PRO 2

ILE 160 0.30 MET 123 -0.21 LEU 149

GLY 120 0.28 SER 124 -0.18 GLY 3

ILE 160 0.24 GLY 125 -0.22 ARG 1

ASN 187 0.18 GLY 126 -0.20 PRO 67

MET 175 0.19 SER 127 -0.26 PRO 189

ALA 142 0.26 ALA 128 -0.21 PRO 67

ASP 214 0.20 LEU 129 -0.25 THR 98

GLY 280 0.15 ILE 130 -0.35 THR 98

ASP 214 0.16 LEU 131 -0.32 THR 98

ASP 214 0.22 ALA 132 -0.26 PRO 102

GLY 280 0.20 ALA 133 -0.35 ARG 99

ASP 214 0.17 TYR 134 -0.49 ARG 99

ASP 214 0.19 TYR 135 -0.34 ALA 103

ASP 214 0.24 PRO 136 -0.26 ALA 103

ASP 214 0.24 GLN 137 -0.22 ALA 198

ASP 214 0.24 GLN 138 -0.21 PRO 113

ASP 214 0.26 PHE 139 -0.16 GLU 56

ASP 214 0.31 PRO 140 -0.15 GLU 56

ASP 214 0.36 TYR 141 -0.16 GLU 56

ASP 214 0.31 ALA 142 -0.17 GLU 56

ASP 214 0.33 ALA 143 -0.23 ARG 1

ASP 214 0.24 SER 144 -0.27 ARG 1

LEU 159 0.26 LEU 145 -0.35 ARG 1

LEU 159 0.30 SER 146 -0.34 ARG 1

SER 144 0.24 GLY 147 -0.25 ARG 1

PRO 157 0.22 PHE 148 -0.21 ARG 1

GLY 280 0.14 LEU 149 -0.23 PHE 74

GLY 280 0.13 ASN 150 -0.31 ALA 242

PHE 148 0.20 PRO 151 -0.32 ALA 242

SER 146 0.11 SER 152 -0.45 ALA 242

PRO 254 0.12 GLU 153 -0.51 ALA 242

THR 229 0.22 SER 154 -0.47 ALA 242

LEU 228 0.25 TRP 155 -0.38 ALA 242

THR 229 0.23 TRP 156 -0.32 ALA 242

SER 122 0.25 PRO 157 -0.33 ALA 242

SER 122 0.27 THR 158 -0.29 ALA 242

SER 122 0.33 LEU 159 -0.23 ALA 242

SER 122 0.35 ILE 160 -0.23 ALA 242

SER 122 0.27 GLY 161 -0.24 ALA 242

SER 122 0.30 LEU 162 -0.20 ALA 242

SER 122 0.31 ALA 163 -0.18 ALA 242

SER 122 0.25 MET 164 -0.19 ALA 242

ASN 50 0.26 ASN 165 -0.18 ALA 242

ASN 50 0.31 ASP 166 -0.17 GLY 3

ASN 50 0.32 SER 167 -0.19 GLY 3

GLY 46 0.31 GLY 168 -0.17 GLY 3

ASN 50 0.27 GLY 169 -0.17 ASP 243

GLY 46 0.24 TYR 170 -0.20 ASP 243

GLY 46 0.22 ASN 171 -0.24 ALA 242

MET 123 0.25 ALA 172 -0.28 ASP 243

MET 123 0.21 ASN 173 -0.31 ASP 243

GLY 120 0.18 SER 174 -0.28 ASP 243

GLY 120 0.20 MET 175 -0.27 ASP 243

SER 127 0.17 TRP 176 -0.34 ASP 243

SER 122 0.19 GLY 177 -0.35 ASP 243

SER 122 0.22 PRO 178 -0.38 ASP 243

SER 122 0.22 SER 179 -0.44 ASP 243

SER 122 0.17 SER 180 -0.50 ASP 243

SER 122 0.17 ASP 181 -0.46 ASP 243

SER 122 0.11 PRO 182 -0.51 ASP 243

GLY 126 0.14 ALA 183 -0.41 ASP 243

GLY 126 0.17 TRP 184 -0.43 ASP 243

GLY 280 0.13 LYS 185 -0.50 ASP 243

GLY 280 0.13 ARG 186 -0.45 ASP 243

GLY 126 0.18 ASN 187 -0.42 THR 95

GLY 280 0.15 ASP 188 -0.36 ASP 243

GLY 280 0.17 PRO 189 -0.34 THR 95

GLY 280 0.17 MET 190 -0.35 ALA 242

GLY 280 0.16 VAL 191 -0.54 ASP 243

GLY 280 0.19 GLN 192 -0.47 ILE 193

ASP 214 0.24 ILE 193 -0.47 GLN 192

GLY 280 0.27 PRO 194 -0.41 GLY 244

GLY 280 0.25 ARG 195 -0.38 ARG 99

ASP 214 0.29 LEU 196 -0.38 GLY 245

GLY 280 0.37 VAL 197 -0.35 GLY 245

GLY 280 0.35 ALA 198 -0.33 ARG 99

GLY 280 0.36 ASN 199 -0.24 ALA 103

GLY 280 0.47 ASN 200 -0.19 ARG 246

GLY 280 0.35 THR 201 -0.16 GLN 137

ASP 214 0.43 ARG 202 -0.15 GLN 137

ASP 214 0.39 ILE 203 -0.19 ARG 1

ASP 214 0.45 TRP 204 -0.26 ARG 1

ASP 214 0.36 VAL 205 -0.31 ARG 1

ASP 214 0.38 TYR 206 -0.38 ARG 1

LEU 159 0.25 CYS 207 -0.39 ARG 1

LEU 159 0.24 GLY 208 -0.44 ARG 1

LEU 159 0.22 ASN 209 -0.41 ARG 1

LEU 159 0.19 GLY 210 -0.38 ARG 1

GLN 59 0.20 THR 211 -0.40 ARG 1

GLN 59 0.27 PRO 212 -0.44 PRO 2

ALA 269 0.50 SER 213 -0.52 ARG 1

ALA 269 0.81 ASP 214 -0.62 ASP 218

GLU 265 0.52 LEU 215 -0.62 ARG 1

ALA 269 0.34 GLY 216 -0.57 PRO 2

PRO 261 0.49 GLY 217 -0.44 PRO 2

PRO 261 0.31 ASP 218 -0.62 ASP 214

ASN 50 0.43 ASN 219 -0.50 ASP 214

ASN 50 0.35 ILE 220 -0.38 ASP 214

ASN 50 0.31 PRO 221 -0.32 ASP 214

SER 259 0.37 ALA 222 -0.35 PRO 2

SER 259 0.24 LYS 223 -0.34 PRO 2

SER 259 0.18 PHE 224 -0.30 PRO 2

LEU 159 0.33 LEU 225 -0.32 PRO 2

LEU 159 0.29 GLU 226 -0.34 PRO 2

LEU 159 0.21 GLY 227 -0.32 PRO 2

LEU 159 0.26 LEU 228 -0.30 THR 232

LEU 159 0.27 THR 229 -0.30 ARG 1

LEU 159 0.19 LEU 230 -0.33 ARG 1

PRO 254 0.20 ARG 231 -0.30 LEU 228

PRO 254 0.16 THR 232 -0.30 LEU 228

ASP 214 0.19 ASN 233 -0.29 ARG 1

ASP 214 0.25 GLN 234 -0.28 ARG 1

PRO 254 0.19 THR 235 -0.27 LEU 228

ASP 214 0.22 PHE 236 -0.24 THR 95

ASP 214 0.36 ARG 237 -0.22 ARG 1

ASP 214 0.33 ASP 238 -0.27 GLU 153

ASP 214 0.28 THR 239 -0.46 GLU 153

ASP 214 0.33 TYR 240 -0.33 VAL 191

ASP 214 0.48 ALA 241 -0.35 VAL 191

ASP 214 0.39 ALA 242 -0.51 GLU 153

GLY 280 0.38 ASP 243 -0.54 VAL 191

GLY 280 0.44 GLY 244 -0.45 PRO 182

GLY 280 0.42 GLY 245 -0.42 VAL 191

HIS 276 0.61 ARG 246 -0.26 PRO 182

HIS 276 0.53 ASN 247 -0.12 ARG 237

ASP 214 0.49 GLY 248 -0.16 ARG 1

ASP 214 0.58 VAL 249 -0.23 ARG 1

ASP 214 0.54 PHE 250 -0.28 ARG 1

ASP 214 0.58 ASN 251 -0.36 ARG 1

ASP 214 0.46 PHE 252 -0.38 ARG 1

ASP 214 0.46 PRO 253 -0.49 ARG 1

ALA 241 0.31 PRO 254 -0.50 ARG 1

PHE 252 0.29 ASN 255 -0.52 ARG 1

ALA 241 0.23 GLY 256 -0.51 ARG 1

LEU 159 0.22 THR 257 -0.43 ARG 1

LEU 159 0.28 HIS 258 -0.41 PRO 2

ALA 222 0.37 SER 259 -0.50 PRO 2

ASN 219 0.37 TRP 260 -0.53 ARG 1

GLY 217 0.49 PRO 261 -0.69 ARG 1

GLY 217 0.34 TYR 262 -0.59 ARG 1

GLY 217 0.27 TRP 263 -0.51 ARG 1

ASP 214 0.39 ASN 264 -0.62 ARG 1

ASP 214 0.65 GLU 265 -0.67 ARG 1

ASP 214 0.57 GLN 266 -0.51 ARG 1

ASP 214 0.53 LEU 267 -0.43 ARG 1

ASP 214 0.71 VAL 268 -0.52 ARG 1

ASP 214 0.81 ALA 269 -0.48 ARG 1

ASP 214 0.64 MET 270 -0.36 ARG 1

ASP 214 0.64 LYS 271 -0.33 ARG 1

ASP 214 0.68 ALA 272 -0.31 ARG 1

ASP 214 0.61 ASP 273 -0.25 ARG 1

ASP 214 0.52 ILE 274 -0.22 GLU 56

ASP 214 0.53 GLN 275 -0.27 GLU 56

ARG 246 0.61 HIS 276 -0.23 GLU 56

ARG 246 0.47 VAL 277 -0.18 GLU 56

ASP 214 0.42 LEU 278 -0.21 GLU 56

ASP 214 0.43 ASN 279 -0.23 GLU 56

ARG 246 0.53 GLY 280 -0.24 GLU 56

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 16 ---

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

* EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *