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

* 1DQZ *

CA distance fluctuations for 240228060125923889

--- normal mode 14 ---

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 0.23 ARG 1 -1.01 ASN 108

GLY 3 0.44 PRO 2 -0.87 GLU 7

PRO 2 0.44 GLY 3 -0.64 ASP 214

GLN 59 0.11 LEU 4 -0.68 ASP 214

ASP 43 0.06 PRO 5 -0.64 ASP 214

ASP 43 0.07 VAL 6 -0.66 ASP 214

GLY 26 0.09 GLU 7 -0.87 PRO 2

GLY 168 0.12 TYR 8 -0.84 PRO 2

GLY 168 0.15 LEU 9 -0.87 PRO 2

GLY 168 0.19 GLN 10 -0.78 PRO 2

GLY 168 0.17 VAL 11 -0.72 ARG 1

ARG 18 0.24 PRO 12 -0.66 ARG 1

TRP 104 0.18 SER 13 -0.56 ARG 1

ALA 107 0.20 ALA 14 -0.53 ARG 1

ALA 103 0.17 SER 15 -0.47 ARG 1

TRP 104 0.15 MET 16 -0.46 ARG 1

ALA 107 0.16 GLY 17 -0.50 ARG 1

PRO 12 0.24 ARG 18 -0.55 PRO 2

GLY 168 0.21 ASP 19 -0.61 PRO 2

GLY 168 0.22 ILE 20 -0.57 PRO 2

GLY 70 0.21 LYS 21 -0.61 PRO 2

GLY 70 0.16 VAL 22 -0.58 PRO 2

GLY 69 0.11 GLN 23 -0.54 PRO 2

GLY 69 0.08 PHE 24 -0.58 ARG 1

ASP 43 0.09 GLN 25 -0.56 LEU 215

GLU 7 0.09 GLY 26 -0.56 ARG 1

GLN 59 0.11 GLY 27 -0.47 ASP 214

GLN 59 0.11 GLY 28 -0.39 ASP 214

GLN 138 0.11 PRO 29 -0.46 ARG 1

GLN 59 0.13 HIS 30 -0.37 ARG 1

GLN 59 0.13 ALA 31 -0.37 ARG 1

TYR 58 0.13 VAL 32 -0.32 PRO 261

TYR 58 0.10 TYR 33 -0.35 ARG 1

GLU 55 0.09 LEU 34 -0.41 PRO 261

PRO 221 0.13 LEU 35 -0.33 PRO 261

PRO 221 0.18 ASP 36 -0.36 PRO 261

PRO 221 0.24 GLY 37 -0.31 PRO 261

PHE 224 0.25 LEU 38 -0.30 GLY 216

PRO 221 0.22 ARG 39 -0.42 GLY 216

PRO 221 0.19 ALA 40 -0.44 GLY 216

PRO 221 0.21 GLN 41 -0.44 GLY 216

PRO 221 0.18 ASP 42 -0.41 GLY 216

PRO 221 0.17 ASP 43 -0.47 LEU 215

PRO 221 0.14 TYR 44 -0.54 LEU 215

PRO 221 0.17 ASN 45 -0.49 LEU 215

PRO 221 0.16 GLY 46 -0.56 GLY 216

ILE 49 0.14 TRP 47 -0.64 PRO 261

ALA 53 0.16 ASP 48 -0.72 LEU 215

TRP 47 0.14 ILE 49 -0.70 LEU 215

LEU 267 0.16 ASN 50 -0.85 GLY 216

VAL 268 0.18 THR 51 -0.93 LEU 215

LYS 271 0.19 PRO 52 -0.98 LEU 215

ASP 48 0.16 ALA 53 -0.76 LEU 215

GLU 55 0.14 PHE 54 -0.71 LEU 215

PRO 2 0.25 GLU 55 -0.78 ASP 214

PRO 2 0.22 GLU 56 -0.70 SER 213

GLN 275 0.15 TYR 57 -0.56 SER 213

PRO 2 0.18 TYR 58 -0.62 ASP 214

PRO 2 0.25 GLN 59 -0.56 SER 213

GLN 275 0.17 SER 60 -0.49 PRO 254

GLN 59 0.20 GLY 61 -0.42 PRO 254

GLN 59 0.15 LEU 62 -0.38 ASP 214

GLN 59 0.12 SER 63 -0.44 ASP 214

TYR 58 0.10 VAL 64 -0.48 LEU 215

GLN 59 0.08 ILE 65 -0.45 ARG 1

PRO 221 0.10 MET 66 -0.47 LEU 215

GLN 71 0.13 PRO 67 -0.43 ARG 1

GLY 69 0.17 VAL 68 -0.43 LEU 215

LYS 21 0.20 GLY 69 -0.39 GLY 216

LYS 21 0.21 GLY 70 -0.34 GLY 216

LYS 21 0.21 GLN 71 -0.37 GLY 216

PHE 224 0.23 SER 72 -0.28 GLY 216

PHE 224 0.22 SER 73 -0.26 ARG 1

PHE 224 0.23 PHE 74 -0.24 ARG 1

PHE 224 0.19 TYR 75 -0.30 ARG 1

PHE 224 0.20 THR 76 -0.29 ARG 1

PHE 224 0.19 ASP 77 -0.33 ARG 1

PHE 224 0.21 TRP 78 -0.30 ARG 1

PHE 224 0.19 TYR 79 -0.29 ARG 1

THR 158 0.21 GLN 80 -0.30 ARG 1

THR 158 0.20 PRO 81 -0.31 ARG 1

THR 158 0.21 SER 82 -0.27 ARG 1

THR 158 0.23 GLN 83 -0.25 ARG 1

PHE 224 0.20 SER 84 -0.23 GLY 216

ASP 19 0.17 ASN 85 -0.30 GLY 216

ASP 19 0.14 GLY 86 -0.32 GLY 216

ASP 19 0.16 GLN 87 -0.34 GLY 216

THR 158 0.15 ASN 88 -0.39 ASP 42

THR 158 0.16 TYR 89 -0.37 ARG 1

THR 158 0.18 THR 90 -0.36 ARG 1

PHE 224 0.17 TYR 91 -0.35 ARG 1

PHE 224 0.16 LYS 92 -0.38 ARG 1

PHE 224 0.16 TRP 93 -0.38 ARG 1

PHE 224 0.16 GLU 94 -0.36 ARG 1

ALA 183 0.15 THR 95 -0.42 ARG 1

MET 101 0.15 PHE 96 -0.47 ARG 1

PHE 224 0.11 LEU 97 -0.44 ARG 1

PRO 113 0.15 THR 98 -0.43 ARG 1

ALA 103 0.16 ARG 99 -0.49 ARG 1

ALA 103 0.23 GLU 100 -0.57 ARG 1

TRP 93 0.15 MET 101 -0.60 ARG 1

LYS 92 0.11 PRO 102 -0.57 ARG 1

GLU 100 0.23 ALA 103 -0.65 ARG 1

ALA 14 0.20 TRP 104 -0.76 ARG 1

ALA 14 0.13 LEU 105 -0.76 ARG 1

GLU 100 0.16 GLN 106 -0.73 ARG 1

ALA 14 0.20 ALA 107 -0.85 ARG 1

ALA 14 0.18 ASN 108 -1.01 ARG 1

ALA 14 0.13 LYS 109 -0.93 ARG 1

ALA 14 0.13 GLY 110 -0.75 ARG 1

ARG 99 0.11 VAL 111 -0.62 ARG 1

ARG 99 0.13 SER 112 -0.52 ARG 1

THR 98 0.15 PRO 113 -0.50 ARG 1

TYR 135 0.14 THR 114 -0.40 ARG 1

GLN 59 0.14 GLY 115 -0.32 ARG 1

GLN 59 0.14 ASN 116 -0.32 ARG 1

TYR 58 0.13 ALA 117 -0.26 ARG 1

TYR 58 0.10 ALA 118 -0.27 ARG 1

PRO 52 0.10 VAL 119 -0.22 ARG 1

PRO 221 0.11 GLY 120 -0.22 PRO 261

PRO 221 0.12 LEU 121 -0.19 PRO 261

LEU 225 0.21 SER 122 -0.15 ARG 1

LEU 225 0.27 MET 123 -0.18 ARG 1

LEU 225 0.18 SER 124 -0.21 ARG 1

LEU 225 0.13 GLY 125 -0.18 ARG 1

ASN 209 0.17 GLY 126 -0.19 ARG 1

PHE 224 0.17 SER 127 -0.24 ARG 1

LEU 225 0.12 ALA 128 -0.24 ARG 1

ASN 209 0.12 LEU 129 -0.21 ARG 1

ASN 209 0.14 ILE 130 -0.24 ARG 1

PHE 224 0.12 LEU 131 -0.28 ARG 1

TYR 58 0.10 ALA 132 -0.25 ARG 1

ASN 209 0.13 ALA 133 -0.23 ARG 1

TYR 135 0.15 TYR 134 -0.27 ARG 1

TYR 134 0.15 TYR 135 -0.31 ARG 1

ASN 279 0.13 PRO 136 -0.27 ARG 1

ASN 279 0.14 GLN 137 -0.30 ARG 1

GLY 115 0.13 GLN 138 -0.35 ARG 1

SER 60 0.13 PHE 139 -0.28 ARG 1

SER 60 0.14 PRO 140 -0.23 ARG 1

GLU 56 0.13 TYR 141 -0.20 ARG 1

PRO 52 0.11 ALA 142 -0.20 ARG 1

ASN 50 0.10 ALA 143 -0.18 ARG 1

ASN 50 0.08 SER 144 -0.17 ARG 1

ASN 50 0.07 LEU 145 -0.15 ARG 1

SER 213 0.14 SER 146 -0.14 ARG 1

ASN 209 0.16 GLY 147 -0.16 ARG 1

ASN 209 0.25 PHE 148 -0.15 ARG 1

ASN 209 0.28 LEU 149 -0.16 ARG 1

ASN 209 0.33 ASN 150 -0.17 THR 239

ASN 209 0.30 PRO 151 -0.16 ARG 1

ASN 209 0.30 SER 152 -0.18 PRO 157

PRO 254 0.36 GLU 153 -0.24 ASP 243

PRO 254 0.36 SER 154 -0.24 ALA 242

THR 211 0.31 TRP 155 -0.22 ALA 242

PRO 157 0.30 TRP 156 -0.20 THR 239

ASN 173 0.32 PRO 157 -0.18 SER 152

ASN 173 0.38 THR 158 -0.17 ALA 242

PHE 224 0.37 LEU 159 -0.16 THR 239

PHE 224 0.35 ILE 160 -0.15 PRO 151

PHE 224 0.34 GLY 161 -0.20 SER 179

PHE 224 0.37 LEU 162 -0.13 SER 179

PHE 224 0.37 ALA 163 -0.16 GLY 217

PHE 224 0.29 MET 164 -0.21 GLY 216

PHE 224 0.26 ASN 165 -0.21 GLY 216

PHE 224 0.24 ASP 166 -0.25 GLY 217

PHE 224 0.18 SER 167 -0.34 GLY 216

ILE 20 0.22 GLY 168 -0.36 GLY 216

PHE 224 0.19 GLY 169 -0.28 GLY 216

PHE 224 0.22 TYR 170 -0.25 GLY 216

THR 158 0.27 ASN 171 -0.21 ARG 1

THR 158 0.30 ALA 172 -0.20 ARG 1

THR 158 0.38 ASN 173 -0.21 ARG 1

THR 158 0.27 SER 174 -0.25 ARG 1

PHE 224 0.24 MET 175 -0.25 ARG 1

PHE 224 0.24 TRP 176 -0.23 ARG 1

PHE 224 0.23 GLY 177 -0.22 ARG 1

TRP 155 0.25 PRO 178 -0.20 ARG 1

LEU 228 0.26 SER 179 -0.20 GLY 161

PRO 254 0.27 SER 180 -0.18 ARG 1

PRO 254 0.23 ASP 181 -0.20 ARG 1

PRO 254 0.23 PRO 182 -0.21 ARG 1

ASN 209 0.20 ALA 183 -0.22 ARG 1

ASN 209 0.25 TRP 184 -0.20 ARG 1

PRO 254 0.27 LYS 185 -0.20 ARG 1

PRO 254 0.21 ARG 186 -0.22 ARG 1

ASN 209 0.20 ASN 187 -0.22 ARG 1

ASN 209 0.25 ASP 188 -0.20 ARG 1

PRO 254 0.24 PRO 189 -0.19 ARG 1

PRO 254 0.32 MET 190 -0.18 GLU 153

PRO 254 0.31 VAL 191 -0.18 ARG 1

PRO 254 0.25 GLN 192 -0.19 ARG 1

PRO 254 0.26 ILE 193 -0.17 GLU 153

PRO 254 0.25 PRO 194 -0.16 GLU 153

PRO 254 0.19 ARG 195 -0.19 ARG 1

PRO 254 0.17 LEU 196 -0.18 ARG 1

PRO 254 0.20 VAL 197 -0.14 ARG 1

PRO 254 0.17 ALA 198 -0.16 ARG 1

VAL 277 0.17 ASN 199 -0.18 ARG 1

HIS 276 0.17 ASN 200 -0.14 ARG 1

GLU 56 0.12 THR 201 -0.17 ARG 1

GLU 56 0.14 ARG 202 -0.14 ARG 1

LEU 215 0.12 ILE 203 -0.15 ARG 1

LEU 215 0.16 TRP 204 -0.16 ARG 231

LEU 215 0.19 VAL 205 -0.18 ARG 231

LEU 215 0.25 TYR 206 -0.22 MET 270

SER 213 0.26 CYS 207 -0.28 ALA 269

GLY 256 0.36 GLY 208 -0.40 ALA 269

ARG 231 0.50 ASN 209 -0.43 ALA 269

GLY 227 0.55 GLY 210 -0.35 GLU 265

GLY 227 0.44 THR 211 -0.49 GLU 56

GLN 234 0.29 PRO 212 -0.58 PRO 52

PRO 253 0.49 SER 213 -0.76 PRO 52

PRO 253 0.45 ASP 214 -0.88 PRO 52

PHE 252 0.44 LEU 215 -0.98 PRO 52

PHE 252 0.32 GLY 216 -0.85 ASN 50

ASN 251 0.21 GLY 217 -0.57 ASN 50

GLY 227 0.20 ASP 218 -0.41 ASN 50

GLY 227 0.11 ASN 219 -0.22 PRO 52

ALA 163 0.20 ILE 220 -0.15 GLU 56

GLY 37 0.24 PRO 221 -0.12 LEU 228

HIS 258 0.09 ALA 222 -0.12 GLU 56

GLY 227 0.23 LYS 223 -0.25 GLU 56

ALA 163 0.37 PHE 224 -0.18 ALA 269

MET 123 0.27 LEU 225 -0.15 LEU 228

PRO 151 0.21 GLU 226 -0.22 ALA 269

GLY 210 0.55 GLY 227 -0.25 ALA 269

SER 154 0.31 LEU 228 -0.21 ALA 269

ASN 209 0.34 THR 229 -0.18 ALA 269

ASN 209 0.49 LEU 230 -0.25 ALA 269

PRO 254 0.50 ARG 231 -0.23 PHE 250

PRO 254 0.41 THR 232 -0.18 THR 235

PRO 254 0.38 ASN 233 -0.20 ARG 231

PRO 254 0.55 GLN 234 -0.21 PHE 250

PRO 254 0.51 THR 235 -0.18 THR 232

PRO 254 0.40 PHE 236 -0.15 TRP 156

PRO 254 0.41 ARG 237 -0.16 GLY 248

PRO 254 0.48 ASP 238 -0.14 TRP 155

PRO 254 0.41 THR 239 -0.23 SER 154

PRO 254 0.33 TYR 240 -0.18 GLU 153

PRO 254 0.38 ALA 241 -0.18 SER 154

PRO 254 0.39 ALA 242 -0.24 SER 154

PRO 254 0.32 ASP 243 -0.24 GLU 153

PRO 254 0.28 GLY 244 -0.19 GLU 153

ASP 214 0.27 GLY 245 -0.17 GLU 153

ASP 214 0.29 ARG 246 -0.14 GLU 153

ASP 214 0.22 ASN 247 -0.12 ARG 231

LEU 215 0.25 GLY 248 -0.16 ARG 237

LEU 215 0.29 VAL 249 -0.23 ASP 273

LEU 215 0.36 PHE 250 -0.23 ARG 231

LEU 215 0.41 ASN 251 -0.35 ALA 269

SER 213 0.46 PHE 252 -0.35 ALA 269

SER 213 0.49 PRO 253 -0.70 ALA 269

GLN 234 0.55 PRO 254 -0.61 ALA 269

SER 213 0.48 ASN 255 -0.60 GLU 265

GLY 208 0.36 GLY 256 -0.56 GLU 265

GLY 208 0.18 THR 257 -0.32 ALA 53

ASN 251 0.10 HIS 258 -0.19 ALA 53

ASN 251 0.12 SER 259 -0.27 ARG 39

TRP 263 0.13 TRP 260 -0.47 PRO 261

ASN 251 0.17 PRO 261 -0.85 THR 51

ASN 251 0.24 TYR 262 -0.52 ALA 53

TRP 260 0.13 TRP 263 -0.38 GLY 256

ARG 246 0.11 ASN 264 -0.48 ALA 53

ARG 246 0.15 GLU 265 -0.60 ASN 255

GLY 248 0.16 GLN 266 -0.47 PRO 253

THR 51 0.17 LEU 267 -0.44 PRO 253

THR 51 0.18 VAL 268 -0.58 PRO 253

ARG 246 0.15 ALA 269 -0.70 PRO 253

THR 51 0.15 MET 270 -0.51 PRO 253

GLU 56 0.19 LYS 271 -0.51 PRO 253

PRO 2 0.17 ALA 272 -0.51 PRO 253

GLU 56 0.16 ASP 273 -0.41 PRO 253

GLU 56 0.17 ILE 274 -0.35 PRO 253

SER 60 0.17 GLN 275 -0.39 PRO 253

ASN 200 0.17 HIS 276 -0.35 PRO 253

ASN 199 0.17 VAL 277 -0.26 PRO 253

SER 60 0.16 LEU 278 -0.26 PRO 253

ASN 199 0.17 ASN 279 -0.30 PRO 253

ASN 199 0.17 GLY 280 -0.29 PRO 253

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 14 ---

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

* 1DQZ *