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

* 1DQZ *

CA distance fluctuations for 240228060125923889

--- 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
GLY 3 0.22 ARG 1 -1.01 LYS 109

GLY 3 0.43 PRO 2 -0.82 ASN 108

PRO 2 0.43 GLY 3 -0.34 ASN 219

PRO 2 0.13 LEU 4 -0.38 ASN 219

PRO 182 0.05 PRO 5 -0.41 ASN 219

GLU 55 0.07 VAL 6 -0.47 ASN 219

GLU 55 0.09 GLU 7 -0.70 PRO 2

GLU 55 0.11 TYR 8 -0.62 PRO 2

PRO 182 0.10 LEU 9 -0.68 PRO 2

SER 15 0.11 GLN 10 -0.62 PRO 2

PRO 182 0.14 VAL 11 -0.56 PRO 2

PRO 182 0.16 PRO 12 -0.52 PRO 2

TYR 79 0.20 SER 13 -0.44 ARG 1

TYR 79 0.27 ALA 14 -0.43 ARG 1

TYR 79 0.28 SER 15 -0.36 ARG 1

ASP 42 0.25 MET 16 -0.36 PRO 221

ASP 42 0.24 GLY 17 -0.37 PRO 2

ASP 43 0.28 ARG 18 -0.40 PRO 2

ASP 43 0.15 ASP 19 -0.47 PRO 2

ASP 43 0.16 ILE 20 -0.48 PRO 221

ILE 20 0.16 LYS 21 -0.51 PRO 221

GLN 23 0.11 VAL 22 -0.50 PRO 221

ILE 20 0.11 GLN 23 -0.50 PRO 221

PRO 182 0.11 PHE 24 -0.51 ARG 1

PRO 182 0.09 GLN 25 -0.47 ARG 1

PRO 182 0.13 GLY 26 -0.69 ARG 1

ASN 199 0.13 GLY 27 -0.58 ARG 1

PRO 182 0.17 GLY 28 -0.63 ARG 1

PRO 182 0.20 PRO 29 -0.66 ARG 1

PRO 182 0.20 HIS 30 -0.52 ARG 1

PRO 182 0.17 ALA 31 -0.46 ARG 1

PRO 182 0.13 VAL 32 -0.35 ARG 1

PRO 182 0.13 TYR 33 -0.37 PRO 221

ASN 88 0.09 LEU 34 -0.43 PRO 221

ASN 88 0.10 LEU 35 -0.47 PRO 221

ASN 88 0.15 ASP 36 -0.61 PRO 221

GLN 87 0.16 GLY 37 -0.71 PRO 221

GLN 87 0.18 LEU 38 -0.84 PRO 221

GLN 87 0.26 ARG 39 -0.97 PRO 221

ASN 88 0.23 ALA 40 -0.75 PRO 221

ASN 88 0.30 GLN 41 -0.75 PRO 221

ASN 88 0.32 ASP 42 -0.63 PRO 221

ARG 18 0.28 ASP 43 -0.64 ILE 220

ARG 18 0.21 TYR 44 -0.64 ASN 219

ASN 88 0.18 ASN 45 -0.64 PRO 221

ASN 88 0.19 GLY 46 -0.70 PRO 221

ASN 88 0.16 TRP 47 -0.54 ASN 219

ASN 88 0.16 ASP 48 -0.58 ASN 219

ASN 88 0.19 ILE 49 -0.71 ASN 219

ASN 88 0.17 ASN 50 -0.68 ASN 219

PRO 2 0.15 THR 51 -0.53 GLY 217

PRO 2 0.26 PRO 52 -0.42 GLY 217

PRO 2 0.14 ALA 53 -0.40 ASN 219

GLU 55 0.11 PHE 54 -0.40 ASN 219

PRO 2 0.37 GLU 55 -0.36 ASN 219

PRO 2 0.30 GLU 56 -0.28 GLY 217

PRO 2 0.15 TYR 57 -0.29 PRO 221

PRO 2 0.18 TYR 58 -0.32 ASN 219

GLY 3 0.17 GLN 59 -0.26 ASN 219

ASN 200 0.17 SER 60 -0.23 ARG 1

ASN 199 0.18 GLY 61 -0.38 ARG 1

ASN 199 0.16 LEU 62 -0.42 ARG 1

PRO 182 0.14 SER 63 -0.51 ARG 1

PRO 182 0.11 VAL 64 -0.39 ARG 1

PRO 182 0.12 ILE 65 -0.44 ARG 1

ARG 18 0.09 MET 66 -0.50 PRO 221

LYS 92 0.11 PRO 67 -0.51 PRO 221

ARG 18 0.17 VAL 68 -0.59 PRO 221

ASN 88 0.22 GLY 69 -0.59 PRO 221

ASN 88 0.18 GLY 70 -0.57 PRO 221

GLN 87 0.23 GLN 71 -0.64 PRO 221

GLN 87 0.16 SER 72 -0.68 PRO 221

GLN 87 0.10 SER 73 -0.57 PRO 221

SER 127 0.11 PHE 74 -0.55 PRO 221

ALA 183 0.08 TYR 75 -0.49 PRO 221

ALA 183 0.15 THR 76 -0.44 PRO 221

GLY 177 0.20 ASP 77 -0.41 PRO 221

GLY 177 0.18 TRP 78 -0.43 PRO 221

SER 15 0.28 TYR 79 -0.40 PRO 221

ALA 14 0.18 GLN 80 -0.39 PRO 221

ASP 42 0.12 PRO 81 -0.39 ILE 220

ARG 39 0.05 SER 82 -0.44 ILE 220

LEU 162 0.06 GLN 83 -0.43 ILE 220

PHE 148 0.09 SER 84 -0.44 ILE 220

GLY 147 0.11 ASN 85 -0.43 ILE 220

ARG 39 0.16 GLY 86 -0.37 ILE 220

ARG 39 0.26 GLN 87 -0.35 ILE 220

ASP 42 0.32 ASN 88 -0.31 ILE 220

ASP 42 0.29 TYR 89 -0.33 ILE 220

ASP 42 0.22 THR 90 -0.37 PRO 221

ASP 42 0.18 TYR 91 -0.42 PRO 221

TYR 79 0.20 LYS 92 -0.39 PRO 221

PRO 182 0.16 TRP 93 -0.43 PRO 221

ALA 183 0.25 GLU 94 -0.38 PRO 221

PRO 182 0.32 THR 95 -0.37 ARG 1

PRO 182 0.23 PHE 96 -0.40 ARG 1

PRO 182 0.23 LEU 97 -0.40 ARG 1

PRO 182 0.32 THR 98 -0.41 ARG 1

PRO 182 0.34 ARG 99 -0.46 ARG 1

PRO 182 0.27 GLU 100 -0.50 ARG 1

PRO 182 0.23 MET 101 -0.53 ARG 1

PRO 182 0.28 PRO 102 -0.57 ARG 1

PRO 182 0.31 ALA 103 -0.64 ARG 1

PRO 182 0.25 TRP 104 -0.70 ARG 1

PRO 182 0.22 LEU 105 -0.75 ARG 1

PRO 182 0.27 GLN 106 -0.79 ARG 1

PRO 182 0.26 ALA 107 -0.88 ARG 1

PRO 182 0.21 ASN 108 -0.98 ARG 1

PRO 182 0.19 LYS 109 -1.01 ARG 1

PRO 182 0.22 GLY 110 -0.94 ARG 1

PRO 182 0.22 VAL 111 -0.74 ARG 1

PRO 182 0.26 SER 112 -0.64 ARG 1

PRO 182 0.30 PRO 113 -0.57 ARG 1

PRO 182 0.29 THR 114 -0.48 ARG 1

PRO 182 0.24 GLY 115 -0.41 ARG 1

PRO 182 0.20 ASN 116 -0.39 ARG 1

PRO 182 0.15 ALA 117 -0.31 ARG 1

PRO 182 0.13 ALA 118 -0.30 PRO 221

PRO 253 0.10 VAL 119 -0.29 PRO 221

SER 167 0.10 GLY 120 -0.37 PRO 221

SER 167 0.17 LEU 121 -0.37 PRO 221

SER 167 0.23 SER 122 -0.44 PRO 221

SER 167 0.24 MET 123 -0.57 PRO 221

SER 167 0.14 SER 124 -0.46 PRO 221

SER 167 0.18 GLY 125 -0.32 PRO 221

ALA 163 0.22 GLY 126 -0.31 PRO 221

ALA 163 0.14 SER 127 -0.37 PRO 221

ALA 163 0.11 ALA 128 -0.31 PRO 221

GLU 153 0.15 LEU 129 -0.24 PRO 221

LEU 131 0.19 ILE 130 -0.29 PRO 221

PRO 182 0.23 LEU 131 -0.30 PRO 221

PRO 182 0.21 ALA 132 -0.27 ARG 1

GLU 153 0.23 ALA 133 -0.23 ARG 1

TYR 135 0.35 TYR 134 -0.26 PRO 221

TYR 134 0.35 TYR 135 -0.31 ARG 1

TYR 134 0.28 PRO 136 -0.30 ARG 1

PRO 182 0.29 GLN 137 -0.35 ARG 1

PRO 182 0.28 GLN 138 -0.39 ARG 1

PRO 182 0.23 PHE 139 -0.33 ARG 1

PRO 182 0.20 PRO 140 -0.29 ARG 1

PRO 253 0.17 TYR 141 -0.25 ARG 1

PRO 253 0.14 ALA 142 -0.23 ARG 1

PRO 253 0.14 ALA 143 -0.18 ARG 1

SER 167 0.16 SER 144 -0.20 PRO 221

SER 167 0.17 LEU 145 -0.17 PRO 221

SER 167 0.20 SER 146 -0.21 PRO 151

ALA 163 0.25 GLY 147 -0.24 PRO 221

ALA 163 0.35 PHE 148 -0.32 PRO 151

ALA 163 0.27 LEU 149 -0.22 PRO 221

TRP 156 0.25 ASN 150 -0.27 LEU 225

ILE 160 0.21 PRO 151 -0.45 LEU 225

VAL 191 0.23 SER 152 -0.40 LEU 225

VAL 191 0.43 GLU 153 -0.42 LEU 225

VAL 191 0.32 SER 154 -0.55 LEU 228

VAL 191 0.29 TRP 155 -0.66 PHE 224

ASN 150 0.25 TRP 156 -0.58 PHE 224

SER 152 0.22 PRO 157 -0.60 PHE 224

VAL 191 0.19 THR 158 -0.68 PHE 224

ASN 150 0.20 LEU 159 -0.80 PHE 224

ASN 150 0.21 ILE 160 -0.78 PRO 221

PRO 151 0.18 GLY 161 -0.71 PRO 221

ASN 150 0.19 LEU 162 -0.81 ILE 220

PHE 148 0.35 ALA 163 -0.93 PRO 221

PHE 148 0.24 MET 164 -0.74 PRO 221

PHE 148 0.22 ASN 165 -0.66 ILE 220

PHE 148 0.30 ASP 166 -0.76 ILE 220

PHE 148 0.26 SER 167 -0.71 ILE 220

PHE 148 0.17 GLY 168 -0.57 ILE 220

PHE 148 0.19 GLY 169 -0.56 ILE 220

PHE 148 0.14 TYR 170 -0.55 ILE 220

PRO 151 0.09 ASN 171 -0.54 ILE 220

THR 95 0.09 ALA 172 -0.58 PRO 221

THR 95 0.13 ASN 173 -0.51 PRO 221

SER 15 0.12 SER 174 -0.46 PRO 221

TRP 78 0.17 MET 175 -0.49 PRO 221

THR 95 0.22 TRP 176 -0.47 PRO 221

THR 95 0.24 GLY 177 -0.47 PRO 221

THR 95 0.18 PRO 178 -0.52 PRO 221

LYS 185 0.23 SER 179 -0.52 PRO 221

ARG 99 0.24 SER 180 -0.45 PRO 221

ARG 99 0.29 ASP 181 -0.44 PRO 221

ARG 99 0.34 PRO 182 -0.38 PRO 221

THR 95 0.30 ALA 183 -0.40 PRO 221

TYR 135 0.21 TRP 184 -0.44 PRO 221

SER 179 0.23 LYS 185 -0.34 PRO 221

TYR 135 0.25 ARG 186 -0.34 PRO 221

LEU 131 0.23 ASN 187 -0.36 PRO 221

GLU 153 0.23 ASP 188 -0.32 PRO 221

GLU 153 0.23 PRO 189 -0.24 PRO 221

GLU 153 0.30 MET 190 -0.17 VAL 191

GLU 153 0.43 VAL 191 -0.20 PRO 221

GLU 153 0.30 GLN 192 -0.20 PRO 221

GLU 153 0.28 ILE 193 -0.17 ARG 1

GLU 153 0.28 PRO 194 -0.18 ARG 1

GLU 153 0.25 ARG 195 -0.20 ARG 1

GLU 153 0.22 LEU 196 -0.19 ARG 1

GLY 280 0.22 VAL 197 -0.18 ARG 1

GLY 280 0.24 ALA 198 -0.19 ARG 1

GLY 280 0.25 ASN 199 -0.21 ARG 1

GLY 280 0.28 ASN 200 -0.19 ARG 1

VAL 277 0.20 THR 201 -0.21 ARG 1

PRO 253 0.22 ARG 202 -0.19 ARG 1

PRO 253 0.19 ILE 203 -0.17 ARG 1

PRO 253 0.24 TRP 204 -0.13 ARG 1

ASP 166 0.15 VAL 205 -0.12 ARG 1

ASN 209 0.17 TYR 206 -0.11 SER 154

LYS 223 0.17 CYS 207 -0.21 SER 154

LYS 223 0.26 GLY 208 -0.29 SER 154

PHE 252 0.45 ASN 209 -0.48 GLY 227

LYS 223 0.39 GLY 210 -0.61 GLY 227

PHE 252 0.29 THR 211 -0.48 TRP 155

ASN 255 0.22 PRO 212 -0.41 TRP 155

ALA 269 0.29 SER 213 -0.35 TRP 155

PRO 2 0.25 ASP 214 -0.29 TRP 155

PRO 2 0.20 LEU 215 -0.26 TRP 155

PRO 2 0.07 GLY 216 -0.31 THR 51

ALA 222 0.09 GLY 217 -0.61 ASN 50

ASN 255 0.17 ASP 218 -0.53 ASN 50

GLY 210 0.27 ASN 219 -0.72 ARG 39

GLY 210 0.31 ILE 220 -0.85 ALA 163

GLY 227 0.22 PRO 221 -0.97 ARG 39

PHE 252 0.09 ALA 222 -0.56 ARG 39

GLY 210 0.39 LYS 223 -0.59 LEU 159

GLY 227 0.34 PHE 224 -0.80 LEU 159

GLY 227 0.19 LEU 225 -0.63 LEU 159

PHE 250 0.14 GLU 226 -0.44 TRP 155

PHE 224 0.34 GLY 227 -0.61 GLY 210

THR 229 0.23 LEU 228 -0.55 SER 154

ASP 166 0.25 THR 229 -0.39 SER 154

GLY 227 0.31 LEU 230 -0.32 PRO 254

GLY 227 0.23 ARG 231 -0.33 PRO 254

ALA 163 0.26 THR 232 -0.24 PRO 254

ALA 163 0.22 ASN 233 -0.17 SER 180

GLY 227 0.27 GLN 234 -0.16 SER 180

ALA 163 0.23 THR 235 -0.18 PRO 182

ALA 163 0.22 PHE 236 -0.14 PRO 182

GLY 227 0.20 ARG 237 -0.11 ARG 1

GLY 227 0.21 ASP 238 -0.12 PRO 182

TRP 155 0.25 THR 239 -0.13 ARG 1

TRP 155 0.20 TYR 240 -0.14 ARG 1

ASN 209 0.18 ALA 241 -0.12 ARG 1

TRP 155 0.22 ALA 242 -0.12 ARG 1

SER 154 0.23 ASP 243 -0.14 ARG 1

GLY 280 0.19 GLY 244 -0.13 ARG 1

GLY 280 0.19 GLY 245 -0.14 ARG 1

PRO 253 0.24 ARG 246 -0.13 ARG 1

PRO 253 0.25 ASN 247 -0.14 ARG 1

PRO 253 0.28 GLY 248 -0.13 ARG 1

PRO 253 0.33 VAL 249 -0.09 ARG 1

PRO 253 0.33 PHE 250 -0.09 VAL 205

PRO 253 0.37 ASN 251 -0.09 SER 154

ASN 209 0.45 PHE 252 -0.17 SER 154

ASN 251 0.37 PRO 253 -0.26 SER 154

VAL 249 0.25 PRO 254 -0.37 SER 154

ASN 251 0.27 ASN 255 -0.35 TRP 155

PHE 250 0.18 GLY 256 -0.33 TRP 155

PHE 250 0.14 THR 257 -0.42 SER 259

SER 167 0.05 HIS 258 -0.36 SER 259

GLN 87 0.14 SER 259 -0.45 ALA 222

ASN 88 0.13 TRP 260 -0.45 GLY 217

ASN 88 0.13 PRO 261 -0.29 GLY 217

ASN 88 0.12 TYR 262 -0.21 TRP 155

GLN 87 0.12 TRP 263 -0.20 PRO 221

ASN 88 0.14 ASN 264 -0.25 GLY 217

SER 213 0.20 GLU 265 -0.15 SER 154

SER 213 0.20 GLN 266 -0.11 SER 154

SER 213 0.13 LEU 267 -0.19 PRO 221

PRO 2 0.23 VAL 268 -0.13 GLY 217

SER 213 0.29 ALA 269 -0.07 SER 154

PRO 253 0.25 MET 270 -0.09 PRO 221

PRO 253 0.20 LYS 271 -0.14 PRO 221

PRO 253 0.25 ALA 272 -0.10 ARG 1

PRO 253 0.28 ASP 273 -0.13 ARG 1

PRO 253 0.21 ILE 274 -0.21 ARG 1

PRO 253 0.20 GLN 275 -0.24 ARG 1

PRO 253 0.24 HIS 276 -0.22 ARG 1

ASN 200 0.26 VAL 277 -0.25 ARG 1

ASN 200 0.23 LEU 278 -0.34 ARG 1

ASN 200 0.25 ASN 279 -0.37 ARG 1

ASN 200 0.28 GLY 280 -0.30 ARG 1

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 13 ---

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

* 1DQZ *