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

* 1DQZ *

CA distance fluctuations for 240228060125923889

--- normal mode 11 ---

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 0.48 ARG 1 -0.97 ASN 108

ASP 214 0.53 PRO 2 -1.07 PRO 12

GLU 55 0.51 GLY 3 -0.50 ASN 108

GLU 55 0.55 LEU 4 -0.39 LYS 109

ASP 214 0.20 PRO 5 -0.51 LYS 109

ASP 214 0.17 VAL 6 -0.28 PHE 24

ASP 214 0.13 GLU 7 -0.54 PRO 2

ASP 214 0.12 TYR 8 -0.64 PRO 2

ASP 214 0.09 LEU 9 -0.84 PRO 2

LEU 105 0.10 GLN 10 -0.98 PRO 2

ASP 42 0.08 VAL 11 -1.00 PRO 2

ASP 42 0.08 PRO 12 -1.07 PRO 2

GLY 216 0.07 SER 13 -0.96 PRO 2

GLY 216 0.07 ALA 14 -0.99 PRO 2

GLY 216 0.07 SER 15 -0.87 PRO 2

GLY 216 0.08 MET 16 -0.85 PRO 2

GLY 216 0.08 GLY 17 -0.95 PRO 2

ASP 42 0.09 ARG 18 -0.97 PRO 2

ASP 42 0.09 ASP 19 -0.98 PRO 2

ASP 42 0.10 ILE 20 -0.82 PRO 2

GLN 10 0.09 LYS 21 -0.73 PRO 2

LEU 215 0.09 VAL 22 -0.63 PRO 2

LEU 215 0.11 GLN 23 -0.48 PRO 2

LEU 215 0.10 PHE 24 -0.45 PRO 2

LEU 215 0.12 GLN 25 -0.38 PRO 5

ASP 214 0.09 GLY 26 -0.44 PRO 5

PRO 254 0.09 GLY 27 -0.40 PRO 5

SER 63 0.08 GLY 28 -0.32 PRO 5

GLN 10 0.07 PRO 29 -0.35 PRO 2

ALA 31 0.08 HIS 30 -0.29 PRO 2

HIS 30 0.08 ALA 31 -0.30 PRO 5

GLY 37 0.06 VAL 32 -0.22 PRO 5

GLY 37 0.06 TYR 33 -0.31 PRO 2

GLY 37 0.10 LEU 34 -0.22 PRO 2

GLY 37 0.08 LEU 35 -0.28 PRO 2

GLY 37 0.15 ASP 36 -0.24 PRO 2

PRO 261 0.15 GLY 37 -0.20 LEU 225

GLY 216 0.19 LEU 38 -0.22 PRO 2

GLY 46 0.21 ARG 39 -0.23 LEU 225

GLY 46 0.14 ALA 40 -0.29 PRO 2

GLY 168 0.11 GLN 41 -0.34 PRO 2

ILE 20 0.10 ASP 42 -0.48 PRO 2

ASP 214 0.11 ASP 43 -0.43 PRO 2

ASP 214 0.12 TYR 44 -0.33 PRO 2

LEU 215 0.12 ASN 45 -0.28 PRO 2

ARG 39 0.21 GLY 46 -0.17 PRO 221

LEU 4 0.18 TRP 47 -0.11 PRO 221

LEU 4 0.20 ASP 48 -0.11 PRO 221

LEU 4 0.20 ILE 49 -0.15 PRO 221

LEU 4 0.25 ASN 50 -0.14 PRO 221

LEU 4 0.32 THR 51 -0.08 PRO 221

LEU 4 0.43 PRO 52 -0.07 ALA 53

LEU 4 0.28 ALA 53 -0.07 PRO 52

LEU 4 0.31 PHE 54 -0.20 GLU 55

LEU 4 0.55 GLU 55 -0.20 PHE 54

GLY 3 0.42 GLU 56 -0.06 SER 60

GLY 3 0.25 TYR 57 -0.13 PRO 5

GLY 3 0.29 TYR 58 -0.16 PRO 5

GLY 3 0.23 GLN 59 -0.17 PRO 5

GLY 3 0.20 SER 60 -0.15 PRO 5

PRO 254 0.10 GLY 61 -0.19 PRO 5

PRO 254 0.09 LEU 62 -0.24 PRO 5

GLY 28 0.08 SER 63 -0.35 PRO 5

LEU 215 0.07 VAL 64 -0.26 PRO 5

LEU 215 0.07 ILE 65 -0.38 PRO 2

LEU 215 0.09 MET 66 -0.36 PRO 2

LEU 215 0.08 PRO 67 -0.50 PRO 2

LEU 215 0.09 VAL 68 -0.50 PRO 2

GLY 216 0.10 GLY 69 -0.50 PRO 2

GLY 216 0.11 GLY 70 -0.49 PRO 2

GLY 216 0.14 GLN 71 -0.39 PRO 2

GLY 216 0.16 SER 72 -0.35 PRO 2

GLY 216 0.13 SER 73 -0.44 PRO 2

GLY 217 0.12 PHE 74 -0.37 PRO 2

GLY 216 0.09 TYR 75 -0.46 PRO 2

GLY 216 0.09 THR 76 -0.50 PRO 2

GLY 216 0.09 ASP 77 -0.59 PRO 2

GLY 217 0.11 TRP 78 -0.57 PRO 2

GLY 217 0.11 TYR 79 -0.59 PRO 2

GLY 217 0.11 GLN 80 -0.62 PRO 2

GLY 216 0.12 PRO 81 -0.62 PRO 2

GLY 216 0.14 SER 82 -0.52 PRO 2

GLY 217 0.15 GLN 83 -0.50 PRO 2

GLY 216 0.16 SER 84 -0.44 PRO 2

GLY 216 0.15 ASN 85 -0.46 PRO 2

GLY 216 0.13 GLY 86 -0.55 PRO 2

GLY 216 0.11 GLN 87 -0.60 PRO 2

GLY 216 0.09 ASN 88 -0.71 PRO 2

GLY 216 0.09 TYR 89 -0.74 PRO 2

GLY 216 0.10 THR 90 -0.70 PRO 2

GLY 216 0.10 TYR 91 -0.65 PRO 2

GLY 216 0.08 LYS 92 -0.68 PRO 2

GLY 216 0.08 TRP 93 -0.62 PRO 2

GLY 216 0.07 GLU 94 -0.58 PRO 2

TYR 135 0.07 THR 95 -0.69 PRO 2

GLY 216 0.07 PHE 96 -0.73 PRO 2

GLY 216 0.06 LEU 97 -0.62 PRO 2

GLN 138 0.06 THR 98 -0.62 PRO 2

GLN 138 0.08 ARG 99 -0.75 PRO 2

GLN 138 0.07 GLU 100 -0.86 PRO 2

ASP 42 0.06 MET 101 -0.79 PRO 2

ALA 103 0.07 PRO 102 -0.72 PRO 2

PRO 102 0.07 ALA 103 -0.85 PRO 2

GLN 10 0.08 TRP 104 -0.96 PRO 2

GLN 10 0.10 LEU 105 -0.81 PRO 2

GLN 10 0.08 GLN 106 -0.78 PRO 2

GLN 10 0.08 ALA 107 -0.96 PRO 2

GLN 10 0.09 ASN 108 -1.00 PRO 2

GLN 10 0.08 LYS 109 -0.78 PRO 2

GLN 10 0.07 GLY 110 -0.68 ARG 1

GLN 10 0.07 VAL 111 -0.57 PRO 2

GLN 10 0.07 SER 112 -0.52 PRO 2

ALA 103 0.07 PRO 113 -0.57 PRO 2

GLY 115 0.09 THR 114 -0.44 PRO 2

THR 114 0.09 GLY 115 -0.31 PRO 2

ALA 103 0.05 ASN 116 -0.29 PRO 2

ALA 103 0.05 ALA 117 -0.21 PRO 2

GLY 37 0.05 ALA 118 -0.25 PRO 2

ILE 160 0.07 VAL 119 -0.14 PRO 2

ILE 160 0.09 GLY 120 -0.16 PRO 2

ILE 160 0.15 LEU 121 -0.09 PRO 2

ILE 160 0.23 SER 122 -0.13 GLY 37

ILE 160 0.16 MET 123 -0.20 PRO 2

PRO 261 0.09 SER 124 -0.24 PRO 2

ILE 160 0.09 GLY 125 -0.15 PRO 2

ASN 187 0.07 GLY 126 -0.21 PRO 2

GLY 216 0.06 SER 127 -0.30 PRO 2

LEU 267 0.04 ALA 128 -0.26 PRO 2

GLU 56 0.04 LEU 129 -0.23 PRO 2

SER 259 0.05 ILE 130 -0.32 PRO 2

SER 15 0.05 LEU 131 -0.38 PRO 2

SER 15 0.05 ALA 132 -0.31 PRO 2

ASP 77 0.05 ALA 133 -0.31 PRO 2

ASP 77 0.07 TYR 134 -0.41 PRO 2

SER 15 0.07 TYR 135 -0.43 PRO 2

ASN 200 0.06 PRO 136 -0.34 PRO 2

ARG 99 0.08 GLN 137 -0.38 PRO 2

ARG 99 0.08 GLN 138 -0.43 PRO 2

ARG 99 0.07 PHE 139 -0.31 PRO 2

ARG 99 0.06 PRO 140 -0.22 PRO 2

ARG 99 0.05 TYR 141 -0.15 PRO 5

GLY 3 0.05 ALA 142 -0.15 PRO 2

GLY 3 0.11 ALA 143 -0.09 PRO 5

GLY 3 0.11 SER 144 -0.07 PRO 5

GLY 3 0.16 LEU 145 -0.06 GLN 41

LEU 159 0.16 SER 146 -0.09 GLN 41

SER 146 0.14 GLY 147 -0.12 MET 123

PRO 151 0.19 PHE 148 -0.14 LEU 38

PRO 221 0.11 LEU 149 -0.14 PRO 2

PRO 221 0.16 ASN 150 -0.16 PRO 2

PRO 221 0.22 PRO 151 -0.21 PRO 2

PRO 221 0.23 SER 152 -0.24 PRO 2

PRO 221 0.26 GLU 153 -0.18 PRO 2

PRO 221 0.33 SER 154 -0.14 PRO 2

PRO 221 0.41 TRP 155 -0.13 PRO 2

PRO 221 0.35 TRP 156 -0.16 PRO 2

PRO 221 0.35 PRO 157 -0.23 PRO 2

PRO 221 0.44 THR 158 -0.19 PRO 2

PRO 221 0.50 LEU 159 -0.14 PRO 2

PRO 221 0.35 ILE 160 -0.20 PRO 2

PRO 221 0.32 GLY 161 -0.26 PRO 2

PRO 221 0.41 LEU 162 -0.19 PRO 2

GLY 217 0.31 ALA 163 -0.21 LEU 228

GLY 217 0.24 MET 164 -0.27 PRO 2

GLY 217 0.24 ASN 165 -0.28 PRO 2

GLY 217 0.28 ASP 166 -0.22 LEU 228

GLY 216 0.22 SER 167 -0.24 PRO 2

GLY 216 0.18 GLY 168 -0.33 PRO 2

GLY 216 0.19 GLY 169 -0.34 PRO 2

GLY 217 0.18 TYR 170 -0.39 PRO 2

GLY 217 0.19 ASN 171 -0.39 PRO 2

GLY 217 0.20 ALA 172 -0.37 PRO 2

PRO 221 0.20 ASN 173 -0.41 PRO 2

GLY 217 0.15 SER 174 -0.49 PRO 2

GLY 217 0.15 MET 175 -0.48 PRO 2

PRO 221 0.16 TRP 176 -0.44 PRO 2

PRO 221 0.20 GLY 177 -0.44 PRO 2

PRO 221 0.27 PRO 178 -0.36 PRO 2

PRO 221 0.29 SER 179 -0.31 PRO 2

PRO 221 0.26 SER 180 -0.33 PRO 2

PRO 221 0.21 ASP 181 -0.40 PRO 2

PRO 221 0.18 PRO 182 -0.41 PRO 2

PRO 221 0.15 ALA 183 -0.43 PRO 2

PRO 221 0.19 TRP 184 -0.34 PRO 2

PRO 221 0.16 LYS 185 -0.31 PRO 2

PRO 221 0.12 ARG 186 -0.37 PRO 2

PRO 221 0.11 ASN 187 -0.35 PRO 2

PRO 221 0.13 ASP 188 -0.27 PRO 2

PRO 221 0.08 PRO 189 -0.22 PRO 2

PRO 221 0.09 MET 190 -0.16 PRO 2

PRO 221 0.11 VAL 191 -0.22 PRO 2

PRO 221 0.08 GLN 192 -0.25 PRO 2

PRO 221 0.06 ILE 193 -0.18 PRO 2

PRO 221 0.05 PRO 194 -0.20 PRO 2

TYR 79 0.05 ARG 195 -0.26 PRO 2

SER 15 0.04 LEU 196 -0.20 PRO 2

SER 15 0.04 VAL 197 -0.15 PRO 2

SER 15 0.06 ALA 198 -0.21 PRO 2

SER 15 0.06 ASN 199 -0.23 PRO 2

PRO 136 0.06 ASN 200 -0.14 PRO 2

ARG 99 0.05 THR 201 -0.15 PRO 2

GLY 3 0.07 ARG 202 -0.11 PRO 5

GLY 3 0.10 ILE 203 -0.09 PRO 5

GLY 3 0.15 TRP 204 -0.11 ASP 214

GLY 3 0.16 VAL 205 -0.09 ASP 214

GLY 3 0.21 TYR 206 -0.10 ASP 214

GLY 3 0.21 CYS 207 -0.08 SER 213

GLY 3 0.26 GLY 208 -0.10 SER 213

GLY 3 0.26 ASN 209 -0.09 GLN 234

GLY 3 0.24 GLY 210 -0.08 GLN 41

PRO 2 0.30 THR 211 -0.07 PHE 252

PRO 2 0.34 PRO 212 -0.10 PHE 252

PRO 2 0.45 SER 213 -0.17 PRO 253

PRO 2 0.53 ASP 214 -0.18 ASN 251

PRO 2 0.45 LEU 215 -0.15 ASN 251

GLY 3 0.37 GLY 216 -0.11 ASN 251

LEU 162 0.32 GLY 217 -0.10 PRO 261

LEU 159 0.30 ASP 218 -0.08 ASN 251

LEU 159 0.37 ASN 219 -0.09 PRO 261

LEU 159 0.37 ILE 220 -0.13 GLN 41

LEU 159 0.50 PRO 221 -0.20 GLN 41

LEU 159 0.41 ALA 222 -0.14 SER 259

LEU 159 0.28 LYS 223 -0.11 GLN 41

TRP 155 0.32 PHE 224 -0.20 ARG 39

LEU 159 0.34 LEU 225 -0.23 ARG 39

LEU 159 0.21 GLU 226 -0.14 ARG 39

GLY 3 0.18 GLY 227 -0.17 ARG 39

SER 154 0.23 LEU 228 -0.23 SER 167

SER 154 0.16 THR 229 -0.17 SER 167

GLY 3 0.17 LEU 230 -0.13 SER 167

GLY 3 0.15 ARG 231 -0.16 ALA 163

GLY 3 0.12 THR 232 -0.15 ALA 163

GLY 3 0.14 ASN 233 -0.11 SER 167

GLY 3 0.16 GLN 234 -0.13 PRO 254

GLY 3 0.12 THR 235 -0.12 ALA 163

GLY 3 0.10 PHE 236 -0.10 ALA 163

GLY 3 0.14 ARG 237 -0.13 PRO 254

GLY 3 0.13 ASP 238 -0.13 PRO 254

GLY 3 0.09 THR 239 -0.11 GLU 153

GLY 3 0.09 TYR 240 -0.10 PRO 254

GLY 3 0.11 ALA 241 -0.13 PRO 254

GLY 3 0.09 ALA 242 -0.12 PRO 254

GLY 3 0.06 ASP 243 -0.10 GLU 153

GLY 3 0.07 GLY 244 -0.11 ASP 214

GLY 3 0.08 GLY 245 -0.12 ASP 214

GLY 3 0.10 ARG 246 -0.14 ASP 214

GLY 3 0.10 ASN 247 -0.13 ASP 214

GLY 3 0.13 GLY 248 -0.14 ASP 214

GLY 3 0.19 VAL 249 -0.16 ASP 214

GLY 3 0.20 PHE 250 -0.16 ASP 214

GLY 3 0.26 ASN 251 -0.18 ASP 214

GLY 3 0.26 PHE 252 -0.18 PRO 253

GLY 3 0.33 PRO 253 -0.18 PHE 252

PRO 2 0.36 PRO 254 -0.13 ASP 238

PRO 2 0.35 ASN 255 -0.14 SER 213

GLY 3 0.31 GLY 256 -0.12 PHE 252

LEU 159 0.25 THR 257 -0.09 GLY 208

LEU 159 0.31 HIS 258 -0.09 GLN 41

LEU 159 0.30 SER 259 -0.14 ALA 222

GLY 3 0.24 TRP 260 -0.11 PRO 221

GLY 3 0.36 PRO 261 -0.10 GLY 217

GLY 3 0.32 TYR 262 -0.09 VAL 249

GLY 3 0.25 TRP 263 -0.06 TRP 260

GLY 3 0.32 ASN 264 -0.07 LEU 267

GLY 3 0.38 GLU 265 -0.12 ALA 269

GLY 3 0.31 GLN 266 -0.08 LEU 215

GLY 3 0.26 LEU 267 -0.07 ASN 264

GLY 3 0.36 VAL 268 -0.07 THR 51

GLY 3 0.34 ALA 269 -0.14 LEU 215

GLY 3 0.25 MET 270 -0.10 ASP 214

GLY 3 0.25 LYS 271 -0.08 THR 51

GLY 3 0.25 ALA 272 -0.09 ASP 214

GLY 3 0.19 ASP 273 -0.12 ASP 214

GLY 3 0.14 ILE 274 -0.11 PRO 5

GLY 3 0.14 GLN 275 -0.12 PRO 5

GLY 3 0.13 HIS 276 -0.11 PRO 5

GLY 3 0.08 VAL 277 -0.13 PRO 5

SER 112 0.06 LEU 278 -0.17 PRO 5

SER 112 0.05 ASN 279 -0.16 PRO 5

GLY 3 0.07 GLY 280 -0.12 PRO 5

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 ***

CA distance fluctuations for 240228060125923889

--- normal mode 11 ---

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

* 1DQZ *