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 13 ---

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 0.37 ARG 1 -1.00 TYR 44

ASP 214 0.33 PRO 2 -1.25 TYR 8

GLY 86 0.33 GLY 3 -0.46 GLU 7

GLY 86 0.43 LEU 4 -0.33 PRO 5

GLY 86 0.49 PRO 5 -0.33 LEU 4

GLY 86 0.53 VAL 6 -0.70 PRO 2

GLY 86 0.57 GLU 7 -1.01 PRO 2

GLY 86 0.66 TYR 8 -1.25 PRO 2

GLY 86 0.59 LEU 9 -1.03 PRO 2

GLY 86 0.62 GLN 10 -0.96 PRO 2

ASN 88 0.49 VAL 11 -0.81 PRO 2

ASN 88 0.44 PRO 12 -0.74 PRO 2

TRP 104 0.32 SER 13 -0.66 PRO 2

ALA 103 0.25 ALA 14 -0.60 PRO 2

TYR 79 0.26 SER 15 -0.54 PRO 2

GLN 80 0.30 MET 16 -0.54 PRO 2

TYR 89 0.45 GLY 17 -0.60 PRO 2

ASN 88 0.52 ARG 18 -0.67 PRO 2

ASN 88 0.61 ASP 19 -0.78 PRO 2

ASN 88 0.57 ILE 20 -0.81 PRO 2

GLY 86 0.70 LYS 21 -0.98 PRO 2

GLY 86 0.57 VAL 22 -0.91 PRO 2

GLY 86 0.57 GLN 23 -0.95 PRO 2

GLY 86 0.49 PHE 24 -0.76 PRO 2

GLY 86 0.46 GLN 25 -0.51 PRO 2

GLY 86 0.42 GLY 26 -0.35 PRO 2

GLY 86 0.38 GLY 27 -0.28 LEU 4

GLY 86 0.34 GLY 28 -0.26 PRO 5

GLY 86 0.31 PRO 29 -0.30 PRO 2

GLY 86 0.28 HIS 30 -0.29 PRO 2

GLY 86 0.30 ALA 31 -0.37 PRO 2

GLY 86 0.29 VAL 32 -0.36 PRO 2

GLY 86 0.28 TYR 33 -0.48 PRO 2

GLY 86 0.30 LEU 34 -0.47 ARG 1

GLY 86 0.24 LEU 35 -0.49 ARG 1

GLN 71 0.30 ASP 36 -0.50 ARG 1

GLY 120 0.20 GLY 37 -0.39 ARG 1

TRP 156 0.19 LEU 38 -0.35 ARG 1

GLY 46 0.34 ARG 39 -0.37 ARG 1

GLY 168 0.41 ALA 40 -0.49 ARG 1

GLY 168 0.74 GLN 41 -0.65 ARG 1

GLY 86 0.84 ASP 42 -0.72 ARG 1

GLY 86 0.84 ASP 43 -0.95 ARG 1

GLY 86 0.66 TYR 44 -1.00 ARG 1

GLY 86 0.52 ASN 45 -0.80 ARG 1

GLY 168 0.44 GLY 46 -0.61 ARG 1

GLY 86 0.38 TRP 47 -0.54 ARG 1

GLY 86 0.46 ASP 48 -0.78 ARG 1

GLY 86 0.48 ILE 49 -0.70 ARG 1

GLY 86 0.38 ASN 50 -0.38 ARG 1

GLY 86 0.35 THR 51 -0.23 ARG 1

GLY 86 0.35 PRO 52 -0.10 ARG 1

GLY 86 0.35 ALA 53 -0.23 ARG 1

GLY 86 0.39 PHE 54 -0.32 GLU 55

GLY 86 0.32 GLU 55 -0.32 PHE 54

GLY 86 0.32 GLU 56 -0.10 GLN 59

GLY 86 0.33 TYR 57 -0.06 VAL 268

GLY 86 0.37 TYR 58 -0.09 GLU 56

GLY 86 0.36 GLN 59 -0.11 VAL 268

GLY 86 0.31 SER 60 -0.12 VAL 249

GLY 86 0.31 GLY 61 -0.17 PRO 5

GLY 86 0.33 LEU 62 -0.20 PRO 5

GLY 86 0.37 SER 63 -0.35 PRO 2

GLY 86 0.39 VAL 64 -0.44 PRO 2

GLY 86 0.40 ILE 65 -0.61 PRO 2

GLY 86 0.45 MET 66 -0.70 ARG 1

GLY 86 0.45 PRO 67 -0.71 PRO 2

GLY 86 0.60 VAL 68 -0.79 ARG 1

GLY 86 0.53 GLY 69 -0.61 PRO 2

MET 66 0.30 GLY 70 -0.50 PRO 2

ALA 40 0.39 GLN 71 -0.38 PRO 2

VAL 68 0.23 SER 72 -0.34 PRO 2

GLY 70 0.23 SER 73 -0.38 PRO 2

PRO 157 0.15 PHE 74 -0.37 PRO 2

ALA 183 0.15 TYR 75 -0.45 PRO 2

ALA 183 0.21 THR 76 -0.41 PRO 2

ASP 181 0.20 ASP 77 -0.41 PRO 2

LYS 21 0.23 TRP 78 -0.35 PRO 2

GLY 17 0.34 TYR 79 -0.32 ARG 186

GLY 17 0.40 GLN 80 -0.28 PRO 2

LYS 21 0.45 PRO 81 -0.26 PRO 2

ASP 42 0.51 SER 82 -0.22 MET 175

ASP 42 0.54 GLN 83 -0.22 GLY 86

ASP 42 0.61 SER 84 -0.21 ASN 173

ASP 42 0.80 ASN 85 -0.16 ASN 173

ASP 42 0.84 GLY 86 -0.22 GLN 83

ASP 42 0.73 GLN 87 -0.18 PRO 2

LYS 21 0.64 ASN 88 -0.20 PRO 2

ASP 19 0.53 TYR 89 -0.33 PRO 2

GLY 17 0.39 THR 90 -0.36 PRO 2

LYS 21 0.33 TYR 91 -0.41 PRO 2

MET 101 0.24 LYS 92 -0.46 PRO 2

HIS 30 0.20 TRP 93 -0.51 PRO 2

ALA 183 0.17 GLU 94 -0.48 PRO 2

PRO 113 0.20 THR 95 -0.51 PRO 2

SER 112 0.22 PHE 96 -0.58 PRO 2

HIS 30 0.21 LEU 97 -0.57 PRO 2

THR 114 0.25 THR 98 -0.51 PRO 2

PRO 113 0.29 ARG 99 -0.52 PRO 2

ALA 103 0.27 GLU 100 -0.61 PRO 2

GLY 86 0.31 MET 101 -0.65 PRO 2

SER 112 0.28 PRO 102 -0.56 PRO 2

SER 13 0.30 ALA 103 -0.54 PRO 2

ASN 88 0.34 TRP 104 -0.62 PRO 2

GLY 86 0.36 LEU 105 -0.61 PRO 2

GLY 86 0.30 GLN 106 -0.50 PRO 2

GLY 86 0.32 ALA 107 -0.52 PRO 2

GLY 86 0.39 ASN 108 -0.59 PRO 2

GLY 86 0.39 LYS 109 -0.54 PRO 2

GLY 86 0.34 GLY 110 -0.42 PRO 2

GLY 86 0.33 VAL 111 -0.46 PRO 2

PRO 102 0.28 SER 112 -0.39 PRO 2

ARG 99 0.29 PRO 113 -0.45 PRO 2

THR 98 0.25 THR 114 -0.37 PRO 2

THR 98 0.19 GLY 115 -0.35 ASN 200

GLY 86 0.21 ASN 116 -0.35 PRO 2

GLY 86 0.18 ALA 117 -0.32 PRO 2

GLY 86 0.17 ALA 118 -0.38 PRO 2

GLY 86 0.17 VAL 119 -0.33 PRO 2

GLY 37 0.20 GLY 120 -0.34 PRO 2

ARG 39 0.19 LEU 121 -0.29 ARG 1

ARG 39 0.20 SER 122 -0.27 ARG 1

PRO 151 0.16 MET 123 -0.32 PRO 2

GLY 37 0.12 SER 124 -0.37 PRO 2

GLY 37 0.14 GLY 125 -0.30 PRO 2

GLY 37 0.10 GLY 126 -0.30 PRO 2

GLY 37 0.09 SER 127 -0.37 PRO 2

GLY 37 0.10 ALA 128 -0.37 PRO 2

GLY 37 0.09 LEU 129 -0.31 PRO 2

GLY 37 0.07 ILE 130 -0.34 PRO 2

LEU 278 0.09 LEU 131 -0.40 PRO 2

GLY 37 0.07 ALA 132 -0.34 PRO 2

GLY 37 0.06 ALA 133 -0.32 PRO 2

VAL 277 0.07 TYR 134 -0.37 PRO 2

GLY 280 0.12 TYR 135 -0.38 PRO 2

VAL 277 0.11 PRO 136 -0.33 PRO 2

GLY 280 0.18 GLN 137 -0.41 ASN 199

GLY 280 0.18 GLN 138 -0.39 PRO 2

VAL 277 0.14 PHE 139 -0.36 PRO 2

VAL 277 0.11 PRO 140 -0.31 THR 201

GLY 37 0.10 TYR 141 -0.25 PRO 2

GLY 37 0.12 ALA 142 -0.27 PRO 2

GLY 37 0.13 ALA 143 -0.23 PRO 2

ARG 39 0.14 SER 144 -0.23 PRO 2

ARG 39 0.18 LEU 145 -0.18 PRO 2

ARG 39 0.18 SER 146 -0.16 PRO 2

ARG 39 0.17 GLY 147 -0.23 PRO 2

LEU 149 0.15 PHE 148 -0.23 PRO 2

PHE 148 0.15 LEU 149 -0.23 PRO 2

ARG 39 0.13 ASN 150 -0.27 TRP 184

ARG 39 0.16 PRO 151 -0.27 THR 232

LYS 185 0.15 SER 152 -0.32 THR 235

ARG 39 0.15 GLU 153 -0.36 THR 235

LYS 185 0.16 SER 154 -0.38 ARG 231

ASP 43 0.18 TRP 155 -0.38 ARG 231

ARG 39 0.20 TRP 156 -0.29 ARG 231

GLN 41 0.21 PRO 157 -0.24 ARG 231

ASP 43 0.22 THR 158 -0.29 LEU 228

ASP 43 0.20 LEU 159 -0.33 LEU 228

GLN 41 0.22 ILE 160 -0.23 LEU 228

GLN 41 0.29 GLY 161 -0.22 LEU 228

ASP 43 0.27 LEU 162 -0.23 LEU 228

ASP 43 0.24 ALA 163 -0.22 ARG 1

GLN 41 0.35 MET 164 -0.23 PRO 2

GLN 41 0.42 ASN 165 -0.18 PRO 2

GLN 41 0.38 ASP 166 -0.16 PRO 2

GLN 41 0.45 SER 167 -0.21 PRO 2

GLN 41 0.74 GLY 168 -0.17 PRO 2

GLN 41 0.58 GLY 169 -0.15 PRO 2

ASP 42 0.49 TYR 170 -0.22 PRO 2

ASP 42 0.42 ASN 171 -0.20 PRO 2

ASP 42 0.30 ALA 172 -0.23 PRO 2

ASP 43 0.29 ASN 173 -0.26 ASP 243

ASP 42 0.33 SER 174 -0.25 ASP 243

LYS 21 0.26 MET 175 -0.28 PRO 2

LYS 21 0.19 TRP 176 -0.29 ASP 243

GLY 17 0.26 GLY 177 -0.30 ASP 243

ASP 43 0.22 PRO 178 -0.31 ALA 242

ASP 43 0.19 SER 179 -0.32 THR 239

GLY 17 0.19 SER 180 -0.41 ALA 242

ASP 77 0.20 ASP 181 -0.38 ASP 243

THR 76 0.18 PRO 182 -0.44 ASP 243

THR 76 0.21 ALA 183 -0.34 ASP 243

THR 76 0.14 TRP 184 -0.34 MET 190

SER 154 0.16 LYS 185 -0.38 ASP 243

SER 154 0.12 ARG 186 -0.33 ASP 243

SER 152 0.13 ASN 187 -0.31 PRO 2

GLU 153 0.12 ASP 188 -0.30 MET 190

GLN 192 0.11 PRO 189 -0.27 PRO 2

PHE 148 0.10 MET 190 -0.36 LYS 185

MET 123 0.09 VAL 191 -0.37 PRO 182

PRO 189 0.11 GLN 192 -0.36 ILE 193

SER 146 0.12 ILE 193 -0.36 GLN 192

SER 146 0.10 PRO 194 -0.36 PRO 182

SER 144 0.09 ARG 195 -0.30 TYR 79

SER 144 0.12 LEU 196 -0.29 GLN 137

VAL 205 0.16 VAL 197 -0.31 GLN 137

VAL 205 0.12 ALA 198 -0.37 GLN 137

ILE 203 0.12 ASN 199 -0.41 GLN 137

ILE 203 0.14 ASN 200 -0.35 GLY 115

ASN 199 0.11 THR 201 -0.31 PRO 140

GLY 37 0.09 ARG 202 -0.21 GLY 115

ASN 200 0.14 ILE 203 -0.19 VAL 277

GLY 248 0.16 TRP 204 -0.16 LEU 149

ARG 246 0.18 VAL 205 -0.16 LEU 149

ALA 241 0.19 TYR 206 -0.16 SER 154

ALA 241 0.19 CYS 207 -0.20 TRP 155

ALA 241 0.19 GLY 208 -0.21 TRP 155

ALA 241 0.19 ASN 209 -0.27 TRP 155

ALA 241 0.16 GLY 210 -0.22 TRP 155

ALA 241 0.15 THR 211 -0.21 TRP 155

ARG 39 0.17 PRO 212 -0.14 TRP 155

ARG 1 0.25 SER 213 -0.15 TRP 155

ARG 1 0.37 ASP 214 -0.13 ALA 269

ARG 1 0.29 LEU 215 -0.11 ALA 269

ASN 50 0.26 GLY 216 -0.08 ALA 269

GLY 168 0.25 GLY 217 -0.08 ALA 269

GLY 168 0.22 ASP 218 -0.08 ALA 269

GLY 168 0.23 ASN 219 -0.07 ALA 269

GLY 168 0.15 ILE 220 -0.07 TRP 155

SER 167 0.16 PRO 221 -0.11 ARG 1

ARG 39 0.21 ALA 222 -0.08 ARG 1

ARG 39 0.15 LYS 223 -0.15 TRP 155

ALA 241 0.14 PHE 224 -0.22 LEU 159

ARG 231 0.14 LEU 225 -0.21 LEU 159

ALA 241 0.16 GLU 226 -0.21 LEU 159

ARG 231 0.18 GLY 227 -0.27 TRP 155

ARG 231 0.17 LEU 228 -0.35 TRP 155

ARG 39 0.15 THR 229 -0.27 TRP 155

ALA 241 0.18 LEU 230 -0.31 TRP 155

GLY 227 0.18 ARG 231 -0.38 SER 154

LEU 228 0.15 THR 232 -0.29 SER 154

ALA 241 0.15 ASN 233 -0.27 THR 232

ALA 241 0.19 GLN 234 -0.32 SER 154

GLY 227 0.16 THR 235 -0.36 GLU 153

SER 146 0.13 PHE 236 -0.31 SER 180

ALA 241 0.17 ARG 237 -0.29 SER 180

GLN 234 0.19 ASP 238 -0.35 SER 180

LEU 230 0.15 THR 239 -0.40 SER 180

SER 146 0.14 TYR 240 -0.34 PRO 182

PHE 252 0.22 ALA 241 -0.34 PRO 182

ASP 238 0.17 ALA 242 -0.42 PRO 182

ASN 251 0.15 ASP 243 -0.44 PRO 182

ASN 251 0.19 GLY 244 -0.37 PRO 182

GLY 244 0.19 GLY 245 -0.33 PRO 182

VAL 249 0.29 ARG 246 -0.29 GLY 280

VAL 249 0.11 ASN 247 -0.28 VAL 277

VAL 249 0.26 GLY 248 -0.25 VAL 277

ARG 246 0.29 VAL 249 -0.28 HIS 276

ARG 246 0.24 PHE 250 -0.22 SER 154

ARG 246 0.23 ASN 251 -0.22 ASP 273

ALA 241 0.22 PHE 252 -0.25 SER 154

ALA 241 0.19 PRO 253 -0.22 TRP 155

ALA 241 0.18 PRO 254 -0.25 TRP 155

ALA 241 0.16 ASN 255 -0.21 TRP 155

ARG 39 0.17 GLY 256 -0.16 TRP 155

ARG 39 0.19 THR 257 -0.12 TRP 155

ARG 39 0.24 HIS 258 -0.10 ARG 1

ARG 39 0.23 SER 259 -0.12 ARG 1

GLY 168 0.27 TRP 260 -0.14 ARG 1

GLY 86 0.26 PRO 261 -0.05 ALA 269

ARG 39 0.19 TYR 262 -0.11 ALA 269

ARG 39 0.21 TRP 263 -0.09 PRO 2

GLY 86 0.24 ASN 264 -0.05 GLN 59

GLY 86 0.21 GLU 265 -0.11 ALA 269

ARG 246 0.17 GLN 266 -0.11 ALA 269

GLY 86 0.22 LEU 267 -0.08 PRO 2

GLY 86 0.23 VAL 268 -0.11 GLN 59

GLY 86 0.17 ALA 269 -0.14 GLY 256

GLY 86 0.17 MET 270 -0.15 ASN 251

GLY 86 0.22 LYS 271 -0.13 ASN 251

GLY 86 0.20 ALA 272 -0.18 ASN 251

GLY 86 0.16 ASP 273 -0.24 VAL 249

GLY 86 0.19 ILE 274 -0.19 VAL 249

GLY 86 0.22 GLN 275 -0.21 VAL 249

GLY 86 0.18 HIS 276 -0.28 VAL 249

GLN 137 0.17 VAL 277 -0.28 ASN 247

GLY 86 0.20 LEU 278 -0.24 ASN 247

GLY 86 0.23 ASN 279 -0.24 ASN 247

ARG 99 0.19 GLY 280 -0.29 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 13 ---

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

* EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *