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

* *

CA distance fluctuations for 2404260151392809221

--- normal mode 16 ---

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
LEU 289 0.61 SER 95 -0.98 ASP 207

LYS 164 0.42 SER 96 -1.28 ASP 207

PHE 212 0.80 VAL 97 -0.89 ASP 208

PHE 212 0.57 PRO 98 -1.27 ASP 207

PHE 212 0.59 SER 99 -1.27 ASP 208

PHE 212 0.48 GLN 100 -1.29 ASP 208

ASN 131 0.39 LYS 101 -1.64 ASP 208

THR 211 0.49 THR 102 -1.52 ASP 208

THR 211 0.65 TYR 103 -1.45 ASP 208

THR 211 0.65 GLN 104 -1.22 ASP 208

THR 211 0.77 GLY 105 -1.19 ASP 208

ASN 210 0.81 SER 106 -1.12 ARG 209

ASN 210 0.79 TYR 107 -1.02 ARG 209

ASN 210 0.73 GLY 108 -1.00 ASP 208

ASN 210 0.63 PHE 109 -0.99 ASP 208

ASN 210 0.56 ARG 110 -0.98 SER 166

ASN 210 0.56 ARG 110 -0.98 SER 166

ASN 210 0.48 LEU 111 -0.88 SER 166

ASN 210 0.47 GLY 112 -0.76 SER 166

GLY 226 0.53 PHE 113 -0.60 SER 166

GLY 226 0.76 LEU 114 -0.50 SER 166

GLY 226 0.77 HIS 115 -0.45 SER 166

GLY 226 0.79 SER 116 -0.33 SER 166

GLY 226 0.72 GLY 117 -0.32 ASP 208

GLY 226 0.62 THR 118 -0.28 ASP 208

GLY 226 0.64 ALA 119 -0.20 LYS 164

GLY 226 0.57 LYS 120 -0.16 LYS 164

GLY 226 0.60 SER 121 -0.14 LYS 164

GLY 226 0.62 VAL 122 -0.18 LYS 164

GLY 226 0.62 VAL 122 -0.18 LYS 164

GLY 226 0.49 THR 123 -0.28 VAL 225

GLY 226 0.48 CYS 124 -0.27 VAL 225

GLY 226 0.48 CYS 124 -0.27 VAL 225

GLY 226 0.54 THR 125 -0.32 ASP 208

GLY 226 0.46 TYR 126 -0.45 ASP 208

GLY 226 0.45 SER 127 -0.53 ASP 208

SER 95 0.42 PRO 128 -0.63 ASP 208

SER 95 0.49 ALA 129 -0.66 ASP 208

SER 95 0.51 LEU 130 -0.67 ASP 208

SER 95 0.45 ASN 131 -0.72 ASP 208

SER 95 0.41 LYS 132 -0.58 ASP 208

GLY 262 0.42 MET 133 -0.42 ASP 208

GLY 262 0.42 MET 133 -0.42 ASP 208

GLY 226 0.38 PHE 134 -0.31 ASP 208

SER 261 0.41 CYS 135 -0.29 VAL 225

SER 261 0.42 GLN 136 -0.33 VAL 225

SER 261 0.46 LEU 137 -0.37 VAL 225

ASP 186 0.57 ALA 138 -0.45 VAL 225

ASP 186 0.57 LYS 139 -0.46 VAL 225

ASP 186 0.57 LYS 139 -0.46 VAL 225

ASP 186 0.45 THR 140 -0.53 VAL 225

SER 261 0.43 CYS 141 -0.41 VAL 225

SER 261 0.43 CYS 141 -0.41 VAL 225

GLY 226 0.50 PRO 142 -0.48 SER 166

GLY 226 0.41 VAL 143 -0.62 SER 166

ASN 210 0.47 GLN 144 -0.72 SER 166

ASN 210 0.55 LEU 145 -0.79 SER 166

ASN 210 0.63 TRP 146 -0.81 SER 166

ASN 210 0.72 VAL 147 -0.86 ARG 209

ASN 210 0.81 ASP 148 -0.99 ARG 209

ASN 210 0.87 SER 149 -1.02 ARG 209

ASN 210 0.84 THR 150 -0.92 ARG 209

ASN 210 0.79 PRO 151 -0.90 ARG 209

THR 211 0.83 PRO 152 -0.87 ARG 209

THR 211 0.76 PRO 153 -0.73 ARG 209

THR 211 0.85 GLY 154 -0.68 ARG 209

THR 211 0.88 THR 155 -0.71 ARG 209

THR 211 0.77 ARG 156 -0.64 ASP 207

THR 211 0.72 VAL 157 -0.62 SER 166

GLY 262 0.98 ARG 158 -0.58 SER 166

GLY 262 0.78 ALA 159 -0.74 ILE 232

GLY 262 0.68 MET 160 -0.52 ILE 232

SER 261 0.53 ALA 161 -0.46 ASP 208

PHE 212 0.47 ILE 162 -0.60 ASP 208

PHE 212 0.44 TYR 163 -0.59 ASP 208

PRO 98 0.57 LYS 164 -0.71 ASP 208

GLY 244 0.59 GLN 165 -0.82 ASP 208

GLY 244 0.76 SER 166 -1.50 THR 102

GLY 244 1.19 GLN 167 -1.01 ASP 208

GLY 244 0.93 HIS 168 -0.65 GLN 100

GLY 244 0.52 MET 169 -1.05 GLN 100

GLY 244 0.52 MET 169 -1.05 GLN 100

PHE 212 0.84 THR 170 -0.54 ASP 208

PHE 212 0.64 GLU 171 -0.72 ARG 249

SER 261 0.67 VAL 172 -0.39 THR 211

SER 261 0.56 VAL 173 -0.31 SER 96

ASP 207 0.71 ARG 174 -0.42 SER 96

ASP 207 0.71 ARG 174 -0.42 SER 96

ASP 207 0.68 ARG 175 -0.54 PHE 212

GLN 167 0.86 CYS 176 -0.60 THR 211

GLN 167 0.92 PRO 177 -0.73 PHE 212

GLN 167 0.90 HIS 178 -0.68 PHE 212

GLN 167 0.73 HIS 179 -0.72 PHE 212

ASP 207 0.71 GLU 180 -0.98 PHE 212

ASP 207 0.71 GLU 180 -0.98 PHE 212

GLN 167 0.69 ARG 181 -1.04 PHE 212

GLN 167 0.71 ARG 181 -1.02 PHE 212

GLN 167 0.65 CYS 182 -0.90 PHE 212

GLN 167 0.52 SER 183 -0.91 PHE 212

GLN 167 0.46 ASP 184 -0.77 PHE 212

ALA 138 0.46 SER 185 -0.89 PHE 212

ALA 138 0.57 ASP 186 -0.76 PHE 212

GLY 199 0.52 GLY 187 -0.93 PHE 212

GLY 199 0.48 LEU 188 -0.79 PHE 212

SER 261 0.55 ALA 189 -0.79 PHE 212

ASP 207 0.62 PRO 190 -1.15 PHE 212

ASP 207 0.75 PRO 191 -1.15 PHE 212

ASP 207 0.90 GLN 192 -1.05 PHE 212

ASP 207 0.72 HIS 193 -0.67 PHE 212

SER 261 0.58 LEU 194 -0.40 VAL 225

SER 261 0.64 ILE 195 -0.44 VAL 225

SER 261 0.65 ARG 196 -0.50 VAL 225

SER 261 0.64 VAL 197 -0.58 VAL 225

SER 261 0.56 GLU 198 -0.68 VAL 225

GLY 187 0.52 GLY 199 -0.99 VAL 225

SER 261 0.49 ASN 200 -0.91 VAL 225

SER 261 0.58 LEU 201 -0.74 VAL 225

SER 261 0.69 ARG 202 -0.71 VAL 225

SER 261 0.77 VAL 203 -0.63 VAL 225

SER 261 0.92 GLU 204 -0.59 SER 96

SER 261 0.79 TYR 205 -0.82 SER 96

SER 261 0.78 LEU 206 -0.87 SER 96

GLN 192 0.90 ASP 207 -1.28 SER 96

ARG 181 0.55 ASP 208 -1.64 LYS 101

ARG 181 0.60 ARG 209 -1.11 SER 106

ARG 181 0.61 ARG 209 -1.12 SER 106

SER 149 0.87 ASN 210 -0.39 GLY 244

ASN 263 1.55 THR 211 -0.72 GLY 244

THR 170 0.84 PHE 212 -1.15 PRO 191

SER 261 0.91 ARG 213 -0.76 SER 96

SER 261 0.74 HIS 214 -0.81 SER 96

SER 261 0.91 SER 215 -0.56 SER 96

SER 261 0.90 VAL 216 -0.51 ILE 232

SER 261 1.02 VAL 217 -0.53 GLU 224

SER 261 1.02 VAL 217 -0.53 GLU 224

SER 261 0.64 VAL 218 -0.52 VAL 225

THR 211 0.65 PRO 219 -0.49 ARG 209

THR 211 0.65 TYR 220 -0.60 ARG 209

ASN 210 0.63 GLU 221 -0.61 ARG 209

ASN 210 0.71 PRO 222 -0.69 ARG 209

ASN 210 0.69 PRO 223 -0.65 ARG 209

ASN 210 0.65 GLU 224 -0.77 ASN 200

ASN 210 0.65 GLU 224 -0.78 ASN 200

ASN 210 0.65 GLU 224 -0.76 ASN 200

ASN 210 0.71 VAL 225 -0.99 GLY 199

SER 116 0.79 GLY 226 -0.61 ARG 209

ASN 210 0.65 SER 227 -0.58 ARG 209

ASN 210 0.69 ASP 228 -0.68 ARG 209

ASN 210 0.63 CYS 229 -0.67 SER 166

ASN 210 0.57 THR 230 -0.69 SER 166

GLY 226 0.53 THR 231 -0.66 SER 166

ASN 210 0.38 ILE 232 -0.74 ALA 159

SER 261 0.45 HIS 233 -0.58 VAL 225

SER 261 0.57 TYR 234 -0.48 VAL 225

SER 261 0.57 ASN 235 -0.48 VAL 225

SER 261 0.54 TYR 236 -0.41 VAL 225

SER 261 0.52 MET 237 -0.41 VAL 225

GLN 167 0.54 CYS 238 -0.36 VAL 225

GLN 167 0.55 ASN 239 -0.31 VAL 225

GLN 167 0.52 SER 240 -0.34 GLU 171

GLN 167 0.71 SER 241 -0.40 THR 211

GLN 167 0.85 CYS 242 -0.48 THR 211

GLN 167 1.13 MET 243 -0.60 THR 211

GLN 167 1.19 GLY 244 -0.72 THR 211

GLN 167 0.87 GLY 245 -0.60 THR 211

GLN 167 0.65 LEU 246 -0.49 THR 211

GLN 167 0.90 ASN 247 -0.54 THR 211

GLN 167 0.65 ARG 248 -0.49 GLU 171

GLN 167 0.48 ARG 249 -0.72 GLU 171

SER 95 0.38 PRO 250 -0.50 GLU 171

PRO 98 0.38 ILE 251 -0.51 ASP 208

PRO 98 0.46 LEU 252 -0.66 ASP 208

GLY 262 0.47 THR 253 -0.61 ILE 232

GLY 262 0.52 ILE 254 -0.83 ASP 208

THR 211 0.59 ILE 255 -0.83 ASP 208

THR 211 0.80 THR 256 -0.93 THR 256

THR 211 0.80 THR 256 -0.93 THR 256

THR 211 0.83 LEU 257 -0.87 ASP 208

THR 211 0.83 LEU 257 -0.87 ASP 208

THR 211 1.01 GLU 258 -0.80 ASP 207

THR 211 1.15 ASP 259 -0.79 ARG 209

THR 211 1.10 SER 260 -0.70 ARG 209

THR 211 1.27 SER 261 -0.82 ARG 209

THR 211 1.34 GLY 262 -0.70 ARG 209

THR 211 1.55 ASN 263 -0.86 ARG 209

THR 211 1.17 LEU 264 -1.05 ASP 208

THR 211 0.99 LEU 265 -1.05 ASP 208

THR 211 0.83 GLY 266 -1.17 ASP 208

THR 211 0.71 ARG 267 -1.23 ASP 208

THR 211 0.52 ASN 268 -1.15 ASP 208

THR 211 0.42 SER 269 -0.97 SER 166

SER 95 0.38 PHE 270 -0.75 ASP 208

SER 95 0.44 GLU 271 -0.64 ASP 208

GLY 262 0.36 VAL 272 -0.45 ASP 208

GLY 262 0.35 VAL 272 -0.46 PRO 142

SER 261 0.35 ARG 273 -0.34 ASP 208

SER 261 0.40 VAL 274 -0.30 VAL 225

GLN 167 0.38 CYS 275 -0.26 VAL 225

GLN 167 0.39 ALA 276 -0.24 VAL 225

GLY 226 0.42 CYS 277 -0.22 GLU 171

GLY 226 0.45 PRO 278 -0.23 GLU 171

GLY 226 0.53 GLY 279 -0.25 ASP 208

GLY 226 0.48 ARG 280 -0.27 GLU 171

GLY 226 0.42 ASP 281 -0.33 GLU 171

GLY 226 0.47 ARG 282 -0.38 ASP 208

GLY 226 0.49 ARG 283 -0.37 ASP 208

GLY 226 0.43 THR 284 -0.38 ASP 208

SER 95 0.44 GLU 285 -0.44 ASP 208

SER 95 0.46 GLU 286 -0.50 ASP 208

SER 95 0.50 GLU 287 -0.44 ASP 208

SER 95 0.60 ASN 288 -0.40 ASP 208

SER 95 0.61 LEU 289 -0.55 ASP 208

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.

*** ***

CA distance fluctuations for 2404260151392809221

--- normal mode 16 ---

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

* *