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 7 ---

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
GLN 59 0.38 ARG 1 -1.51 ASP 43

GLN 59 0.35 PRO 2 -1.28 ASP 43

GLN 59 0.46 GLY 3 -0.45 ASP 43

PRO 5 0.18 LEU 4 -0.18 TYR 44

LEU 4 0.18 PRO 5 -0.15 PRO 2

PRO 52 0.09 VAL 6 -0.39 PRO 2

THR 51 0.06 GLU 7 -0.62 PRO 2

ILE 49 0.06 TYR 8 -0.90 PRO 2

ASN 219 0.06 LEU 9 -0.86 PRO 2

ASN 219 0.07 GLN 10 -0.96 PRO 2

ASN 219 0.06 VAL 11 -0.82 PRO 2

PRO 221 0.06 PRO 12 -0.82 PRO 2

PRO 221 0.06 SER 13 -0.79 PRO 2

PRO 221 0.06 ALA 14 -0.75 PRO 2

PRO 221 0.06 SER 15 -0.74 ARG 1

PRO 221 0.07 MET 16 -0.85 ARG 1

PRO 221 0.07 GLY 17 -0.88 PRO 2

PRO 221 0.08 ARG 18 -0.98 PRO 2

ASN 219 0.07 ASP 19 -0.99 PRO 2

ASN 219 0.08 ILE 20 -0.99 ARG 1

ASN 219 0.07 LYS 21 -1.06 ARG 1

ASN 219 0.06 VAL 22 -0.86 ARG 1

ILE 49 0.05 GLN 23 -0.77 ARG 1

THR 51 0.04 PHE 24 -0.51 ARG 1

LEU 4 0.09 GLN 25 -0.26 PRO 2

GLY 3 0.21 GLY 26 -0.14 PRO 2

GLY 3 0.35 GLY 27 -0.07 GLY 26

GLY 3 0.30 GLY 28 -0.05 VAL 6

GLY 3 0.22 PRO 29 -0.05 PRO 2

GLY 3 0.18 HIS 30 -0.07 PRO 2

GLY 3 0.12 ALA 31 -0.16 ARG 1

GLU 56 0.10 VAL 32 -0.20 ARG 1

GLU 56 0.07 TYR 33 -0.38 ARG 1

GLU 56 0.06 LEU 34 -0.44 ARG 1

PRO 221 0.05 LEU 35 -0.57 ARG 1

ASN 219 0.07 ASP 36 -0.69 ARG 1

PRO 221 0.09 GLY 37 -0.67 ARG 1

PRO 221 0.12 LEU 38 -0.75 ARG 1

PRO 221 0.14 ARG 39 -0.88 ARG 1

PRO 221 0.11 ALA 40 -0.96 ARG 1

ASN 219 0.12 GLN 41 -1.19 ARG 1

ASN 219 0.11 ASP 42 -1.36 ARG 1

ASN 219 0.10 ASP 43 -1.51 ARG 1

ASN 219 0.09 TYR 44 -1.19 ARG 1

ASN 219 0.07 ASN 45 -0.92 ARG 1

GLY 217 0.09 GLY 46 -0.77 ARG 1

PRO 261 0.05 TRP 47 -0.54 ARG 1

TYR 8 0.05 ASP 48 -0.63 ARG 1

TYR 8 0.06 ILE 49 -0.74 ARG 1

PRO 261 0.08 ASN 50 -0.49 ARG 1

VAL 6 0.08 THR 51 -0.25 ARG 1

VAL 6 0.09 PRO 52 -0.18 GLY 3

GLU 56 0.06 ALA 53 -0.12 ARG 1

VAL 6 0.05 PHE 54 -0.12 ARG 1

ARG 1 0.16 GLU 55 -0.16 PRO 52

ARG 1 0.22 GLU 56 -0.10 PRO 52

GLY 3 0.17 TYR 57 -0.07 PHE 54

GLY 3 0.31 TYR 58 -0.10 PHE 54

GLY 3 0.46 GLN 59 -0.08 GLY 26

GLY 3 0.32 SER 60 -0.06 ASP 214

GLY 3 0.35 GLY 61 -0.05 ASP 214

GLY 3 0.24 LEU 62 -0.05 VAL 6

GLY 3 0.17 SER 63 -0.11 PRO 2

GLU 56 0.08 VAL 64 -0.25 ARG 1

GLU 56 0.05 ILE 65 -0.46 ARG 1

ASN 219 0.05 MET 66 -0.65 ARG 1

ASN 219 0.06 PRO 67 -0.81 ARG 1

ASN 219 0.08 VAL 68 -1.04 ARG 1

PRO 221 0.09 GLY 69 -1.08 ARG 1

PRO 221 0.09 GLY 70 -0.94 ARG 1

PRO 221 0.11 GLN 71 -0.95 ARG 1

PRO 221 0.10 SER 72 -0.81 ARG 1

PRO 221 0.08 SER 73 -0.78 ARG 1

PRO 221 0.07 PHE 74 -0.65 ARG 1

PRO 221 0.06 TYR 75 -0.67 ARG 1

PRO 221 0.05 THR 76 -0.63 ARG 1

PRO 221 0.05 ASP 77 -0.65 ARG 1

PRO 221 0.05 TRP 78 -0.70 ARG 1

PRO 221 0.04 TYR 79 -0.67 ARG 1

PRO 221 0.05 GLN 80 -0.74 ARG 1

PRO 221 0.06 PRO 81 -0.84 ARG 1

PRO 221 0.07 SER 82 -0.85 ARG 1

PRO 221 0.06 GLN 83 -0.82 ARG 1

ILE 220 0.07 SER 84 -0.85 ARG 1

PRO 221 0.08 ASN 85 -0.96 ARG 1

ILE 220 0.07 GLY 86 -0.99 ARG 1

PRO 221 0.08 GLN 87 -1.00 ARG 1

PRO 221 0.07 ASN 88 -0.96 ARG 1

PRO 221 0.07 TYR 89 -0.91 ARG 1

PRO 221 0.06 THR 90 -0.83 ARG 1

PRO 221 0.07 TYR 91 -0.83 ARG 1

PRO 221 0.06 LYS 92 -0.74 ARG 1

PRO 221 0.06 TRP 93 -0.73 ARG 1

PRO 221 0.05 GLU 94 -0.60 ARG 1

PRO 221 0.05 THR 95 -0.60 ARG 1

PRO 221 0.05 PHE 96 -0.67 ARG 1

PRO 221 0.05 LEU 97 -0.58 ARG 1

GLU 56 0.05 THR 98 -0.48 ARG 1

PRO 221 0.04 ARG 99 -0.50 ARG 1

PRO 221 0.05 GLU 100 -0.59 ARG 1

PRO 221 0.05 MET 101 -0.59 ARG 1

GLU 56 0.05 PRO 102 -0.44 ARG 1

PRO 221 0.04 ALA 103 -0.45 PRO 2

PRO 221 0.04 TRP 104 -0.53 PRO 2

LEU 4 0.05 LEU 105 -0.44 PRO 2

GLY 3 0.09 GLN 106 -0.33 PRO 2

GLY 3 0.07 ALA 107 -0.37 PRO 2

LEU 4 0.06 ASN 108 -0.42 PRO 2

GLY 3 0.11 LYS 109 -0.32 PRO 2

GLY 3 0.18 GLY 110 -0.20 PRO 2

GLY 3 0.14 VAL 111 -0.22 PRO 2

GLY 3 0.14 SER 112 -0.19 PRO 2

GLY 3 0.08 PRO 113 -0.28 PRO 2

GLY 3 0.10 THR 114 -0.19 ARG 1

GLY 3 0.13 GLY 115 -0.11 PRO 2

GLY 3 0.10 ASN 116 -0.16 ARG 1

GLU 56 0.10 ALA 117 -0.17 ARG 1

GLU 56 0.08 ALA 118 -0.29 ARG 1

GLU 56 0.08 VAL 119 -0.29 ARG 1

GLU 56 0.05 GLY 120 -0.40 ARG 1

GLN 41 0.04 LEU 121 -0.41 ARG 1

ALA 222 0.05 SER 122 -0.46 ARG 1

PRO 221 0.07 MET 123 -0.56 ARG 1

PRO 221 0.05 SER 124 -0.53 ARG 1

GLU 56 0.04 GLY 125 -0.39 ARG 1

GLU 56 0.04 GLY 126 -0.40 ARG 1

PRO 221 0.04 SER 127 -0.47 ARG 1

GLU 56 0.06 ALA 128 -0.37 ARG 1

GLU 56 0.06 LEU 129 -0.30 ARG 1

GLU 56 0.05 ILE 130 -0.37 ARG 1

GLU 56 0.05 LEU 131 -0.38 ARG 1

GLU 56 0.07 ALA 132 -0.27 ARG 1

GLU 56 0.06 ALA 133 -0.27 ARG 1

GLU 56 0.05 TYR 134 -0.32 ARG 1

GLU 56 0.06 TYR 135 -0.30 ARG 1

GLU 56 0.07 PRO 136 -0.21 ARG 1

GLY 3 0.08 GLN 137 -0.18 ARG 1

GLU 56 0.07 GLN 138 -0.25 ARG 1

GLU 56 0.08 PHE 139 -0.22 ARG 1

GLY 3 0.09 PRO 140 -0.11 ARG 1

GLU 56 0.10 TYR 141 -0.10 ARG 1

GLU 56 0.09 ALA 142 -0.18 ARG 1

GLU 56 0.09 ALA 143 -0.17 ARG 1

GLU 56 0.06 SER 144 -0.25 ARG 1

GLU 56 0.04 LEU 145 -0.24 ARG 1

GLN 41 0.04 SER 146 -0.27 ARG 1

MET 123 0.03 GLY 147 -0.35 ARG 1

ALA 163 0.03 PHE 148 -0.39 ARG 1

GLU 56 0.03 LEU 149 -0.33 ARG 1

ALA 163 0.03 ASN 150 -0.35 ARG 1

ALA 172 0.02 PRO 151 -0.44 ARG 1

VAL 191 0.03 SER 152 -0.42 ARG 1

VAL 191 0.04 GLU 153 -0.37 ARG 1

THR 239 0.03 SER 154 -0.38 ARG 1

THR 239 0.03 TRP 155 -0.43 ARG 1

THR 235 0.03 TRP 156 -0.46 ARG 1

VAL 191 0.02 PRO 157 -0.52 ARG 1

SER 84 0.02 THR 158 -0.54 ARG 1

LEU 228 0.04 LEU 159 -0.54 ARG 1

PHE 224 0.05 ILE 160 -0.59 ARG 1

PHE 224 0.05 GLY 161 -0.64 ARG 1

PHE 224 0.07 LEU 162 -0.65 ARG 1

PHE 224 0.11 ALA 163 -0.67 ARG 1

PRO 221 0.10 MET 164 -0.75 ARG 1

PRO 221 0.10 ASN 165 -0.78 ARG 1

PRO 221 0.14 ASP 166 -0.78 ARG 1

PRO 221 0.15 SER 167 -0.86 ARG 1

PRO 221 0.12 GLY 168 -0.96 ARG 1

PRO 221 0.10 GLY 169 -0.89 ARG 1

PRO 221 0.09 TYR 170 -0.85 ARG 1

PRO 221 0.06 ASN 171 -0.76 ARG 1

PRO 221 0.05 ALA 172 -0.68 ARG 1

PRO 221 0.04 ASN 173 -0.65 ARG 1

PRO 221 0.05 SER 174 -0.72 ARG 1

PRO 221 0.05 MET 175 -0.69 ARG 1

PRO 221 0.03 TRP 176 -0.60 ARG 1

GLN 137 0.03 GLY 177 -0.59 ARG 1

GLN 137 0.03 PRO 178 -0.55 ARG 1

ARG 195 0.03 SER 179 -0.50 ARG 1

GLY 280 0.03 SER 180 -0.46 ARG 1

GLN 137 0.03 ASP 181 -0.49 ARG 1

GLY 280 0.04 PRO 182 -0.44 ARG 1

TYR 135 0.04 ALA 183 -0.49 ARG 1

GLY 280 0.03 TRP 184 -0.48 ARG 1

GLY 280 0.04 LYS 185 -0.40 ARG 1

GLY 280 0.04 ARG 186 -0.41 ARG 1

GLY 280 0.03 ASN 187 -0.44 ARG 1

GLU 56 0.03 ASP 188 -0.38 ARG 1

GLU 56 0.05 PRO 189 -0.31 ARG 1

GLU 56 0.05 MET 190 -0.26 ARG 1

GLU 56 0.04 VAL 191 -0.28 ARG 1

GLU 56 0.05 GLN 192 -0.27 ARG 1

GLU 56 0.06 ILE 193 -0.20 ARG 1

GLU 56 0.06 PRO 194 -0.17 ARG 1

GLU 56 0.06 ARG 195 -0.20 ARG 1

GLU 56 0.07 LEU 196 -0.16 ARG 1

GLU 56 0.07 VAL 197 -0.10 ARG 1

GLY 280 0.07 ALA 198 -0.11 ARG 1

GLY 280 0.08 ASN 199 -0.11 ARG 1

GLY 3 0.10 ASN 200 -0.04 PRO 2

GLU 56 0.09 THR 201 -0.08 ARG 1

GLU 56 0.10 ARG 202 -0.04 PRO 140

GLU 56 0.09 ILE 203 -0.07 ARG 1

GLU 56 0.10 TRP 204 -0.05 ARG 1

GLU 56 0.07 VAL 205 -0.10 ARG 1

GLU 56 0.06 TYR 206 -0.09 ARG 1

GLN 41 0.04 CYS 207 -0.13 ARG 1

GLN 41 0.05 GLY 208 -0.10 ARG 1

GLN 41 0.06 ASN 209 -0.10 ARG 1

GLN 41 0.07 GLY 210 -0.16 ARG 1

GLN 41 0.07 THR 211 -0.08 GLY 3

GLN 41 0.08 PRO 212 -0.10 GLY 3

ARG 1 0.07 SER 213 -0.07 GLY 3

ARG 1 0.14 ASP 214 -0.08 GLY 3

ASN 50 0.07 LEU 215 -0.10 GLY 3

GLN 41 0.08 GLY 216 -0.14 GLY 3

GLN 41 0.10 GLY 217 -0.20 ARG 1

GLN 41 0.11 ASP 218 -0.19 ARG 1

GLN 41 0.12 ASN 219 -0.30 ARG 1

SER 167 0.13 ILE 220 -0.32 ARG 1

SER 167 0.15 PRO 221 -0.41 ARG 1

ARG 39 0.12 ALA 222 -0.35 ARG 1

SER 167 0.09 LYS 223 -0.26 ARG 1

ASP 166 0.11 PHE 224 -0.32 ARG 1

ALA 163 0.10 LEU 225 -0.36 ARG 1

SER 167 0.07 GLU 226 -0.27 ARG 1

ASP 166 0.07 GLY 227 -0.22 ARG 1

ALA 163 0.08 LEU 228 -0.29 ARG 1

ALA 163 0.06 THR 229 -0.28 ARG 1

ALA 163 0.05 LEU 230 -0.18 ARG 1

ALA 163 0.05 ARG 231 -0.18 ARG 1

ALA 163 0.05 THR 232 -0.23 ARG 1

GLU 56 0.04 ASN 233 -0.18 ARG 1

GLU 56 0.04 GLN 234 -0.11 ARG 1

GLU 56 0.04 THR 235 -0.15 ARG 1

GLU 56 0.05 PHE 236 -0.16 ARG 1

GLU 56 0.06 ARG 237 -0.08 ARG 1

GLU 56 0.06 ASP 238 -0.07 ARG 1

GLU 56 0.05 THR 239 -0.11 ARG 1

GLU 56 0.06 TYR 240 -0.09 ARG 1

GLU 56 0.07 ALA 241 -0.02 PRO 2

GLU 56 0.06 ALA 242 -0.05 ARG 1

GLU 56 0.06 ASP 243 -0.08 ARG 1

GLU 56 0.07 GLY 244 -0.03 GLN 137

GLU 56 0.08 GLY 245 -0.03 GLN 137

GLY 3 0.10 ARG 246 -0.03 GLN 137

GLY 3 0.10 ASN 247 -0.04 GLN 137

GLU 56 0.09 GLY 248 -0.04 PRO 253

GLU 56 0.10 VAL 249 -0.04 PRO 253

GLU 56 0.08 PHE 250 -0.05 PRO 253

GLU 56 0.07 ASN 251 -0.05 PRO 253

GLU 56 0.05 PHE 252 -0.04 ASN 209

ARG 1 0.08 PRO 253 -0.05 ASP 273

ARG 1 0.07 PRO 254 -0.04 ASP 273

GLN 41 0.05 ASN 255 -0.05 ASP 273

GLN 41 0.06 GLY 256 -0.07 GLY 3

GLN 41 0.07 THR 257 -0.18 ARG 1

GLN 41 0.08 HIS 258 -0.30 ARG 1

GLN 41 0.08 SER 259 -0.32 ARG 1

GLY 46 0.07 TRP 260 -0.31 ARG 1

ASN 50 0.08 PRO 261 -0.14 GLY 3

GLY 46 0.05 TYR 262 -0.09 GLY 3

GLY 46 0.04 TRP 263 -0.17 ARG 1

GLY 46 0.04 ASN 264 -0.08 GLY 3

ARG 1 0.10 GLU 265 -0.06 ALA 269

GLU 56 0.07 GLN 266 -0.04 ALA 272

GLU 56 0.10 LEU 267 -0.05 LYS 271

ARG 1 0.19 VAL 268 -0.06 ASP 214

ARG 1 0.24 ALA 269 -0.07 ASP 214

ARG 1 0.14 MET 270 -0.05 ASP 214

ARG 1 0.20 LYS 271 -0.06 ASP 214

ARG 1 0.31 ALA 272 -0.07 ASP 214

ARG 1 0.21 ASP 273 -0.06 ASP 214

GLY 3 0.16 ILE 274 -0.05 ASP 214

GLY 3 0.22 GLN 275 -0.06 ASP 214

ARG 1 0.23 HIS 276 -0.06 ASP 214

GLY 3 0.18 VAL 277 -0.05 ASP 214

GLY 3 0.19 LEU 278 -0.04 ASP 214

GLY 3 0.24 ASN 279 -0.05 ASP 214

GLY 3 0.23 GLY 280 -0.05 ASP 214

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 7 ---

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

* 1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *