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

* *

CA distance fluctuations for 2404260310462850495

--- normal mode 15 ---

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
ASN 288 1.42 SER 96 -0.37 LYS 164

ASN 288 1.71 VAL 97 -0.94 ARG 213

ASN 288 1.51 PRO 98 -0.41 PHE 113

LEU 289 1.64 SER 99 -0.54 LYS 164

ASN 288 1.70 GLN 100 -0.64 PHE 270

ASN 288 1.69 LYS 101 -0.66 PHE 113

ASN 288 1.45 THR 102 -0.71 PHE 113

LEU 289 1.44 TYR 103 -0.59 PRO 152

LEU 289 1.31 GLN 104 -0.73 PRO 152

LEU 289 1.36 GLY 105 -0.55 PRO 152

LEU 289 1.27 SER 106 -0.52 PRO 152

LEU 289 1.24 TYR 107 -0.84 PRO 152

LEU 130 1.40 GLY 108 -0.78 PRO 152

LEU 130 1.31 PHE 109 -1.08 PRO 152

GLU 286 1.29 ARG 110 -1.04 PRO 152

GLU 285 1.46 LEU 111 -1.15 PRO 152

LYS 132 1.34 GLY 112 -1.08 PRO 152

SER 127 1.80 PHE 113 -0.81 SER 269

SER 127 1.12 LEU 114 -0.85 PRO 151

ASP 186 1.03 HIS 115 -0.74 PRO 151

ASP 186 1.11 SER 116 -0.83 PRO 151

ASP 186 1.13 GLY 117 -0.76 PRO 151

ASP 186 1.15 THR 118 -0.73 PRO 151

ASP 186 0.98 ALA 119 -0.90 PRO 151

ASP 186 0.93 LYS 120 -0.90 PRO 151

ASP 186 0.89 SER 121 -1.06 PRO 151

ASP 186 1.10 VAL 122 -1.03 PRO 151

ASP 186 1.25 THR 123 -1.03 PRO 151

ASP 186 1.42 CYS 124 -0.88 PRO 151

ASP 186 1.41 THR 125 -0.66 PRO 151

ASP 186 1.38 TYR 126 -0.62 LYS 101

PHE 113 1.80 SER 127 -0.24 PRO 151

THR 230 1.58 PRO 128 -0.29 ARG 248

PRO 223 1.71 ALA 129 -0.39 ARG 248

CYS 229 1.50 LEU 130 -0.57 ARG 248

THR 230 1.78 ASN 131 -0.42 ARG 248

GLY 112 1.34 LYS 132 -0.39 SER 99

ASP 186 1.51 MET 133 -0.46 PRO 151

ASP 186 1.71 PHE 134 -0.53 PRO 151

ASP 186 1.75 CYS 135 -0.77 PRO 151

ASP 186 1.42 GLN 136 -0.88 PRO 151

SER 185 1.38 LEU 137 -0.85 PRO 151

SER 185 1.42 ALA 138 -0.94 PRO 151

GLY 187 1.60 LYS 139 -1.05 PRO 151

GLY 187 1.73 THR 140 -1.12 PRO 151

ASP 186 1.47 CYS 141 -0.97 PRO 151

MET 133 1.31 PRO 142 -1.15 PRO 151

MET 133 1.34 VAL 143 -1.14 PRO 152

PHE 270 1.42 GLN 144 -1.26 PRO 152

ASN 131 1.29 LEU 145 -1.51 PRO 152

LEU 130 1.41 TRP 146 -1.39 PRO 152

LEU 130 1.27 VAL 147 -0.94 PRO 152

GLU 221 1.47 ASP 148 -0.51 PRO 152

TYR 220 1.55 SER 149 -0.40 ASP 228

ASP 259 1.68 THR 150 -0.92 ASP 228

LEU 289 0.73 PRO 151 -1.19 THR 231

LEU 289 0.87 PRO 152 -1.52 THR 230

LEU 289 1.09 PRO 153 -0.89 PRO 222

THR 150 1.24 GLY 154 -0.98 PRO 222

THR 150 1.43 THR 155 -0.65 PRO 222

LEU 289 1.28 ARG 156 -0.42 VAL 197

LEU 289 1.30 VAL 157 -0.62 VAL 197

LEU 289 1.34 ARG 158 -0.52 VAL 97

GLU 285 1.35 ALA 159 -0.64 VAL 97

GLU 285 1.38 MET 160 -0.81 VAL 97

GLU 285 1.44 ALA 161 -0.69 VAL 97

GLU 285 1.42 ILE 162 -0.85 VAL 97

GLU 285 1.28 TYR 163 -0.47 VAL 97

THR 284 1.53 LYS 164 -0.54 SER 99

GLU 287 1.48 GLN 165 -0.48 SER 99

GLU 287 1.68 SER 166 -0.47 THR 211

GLU 287 1.68 SER 166 -0.47 THR 211

GLU 287 1.46 GLN 167 -0.53 THR 211

GLU 287 1.33 HIS 168 -0.55 THR 211

ASN 288 1.45 MET 169 -0.62 THR 211

ASN 288 1.46 THR 170 -1.05 THR 211

ASN 288 1.30 GLU 171 -0.68 PHE 212

ASN 288 1.32 VAL 172 -0.32 GLU 171

ASN 288 1.13 VAL 173 -0.36 VAL 97

ASN 288 1.00 ARG 174 -0.35 LEU 201

GLU 285 0.85 ARG 175 -0.44 PRO 151

ASN 288 0.75 CYS 176 -0.41 PRO 151

ASN 288 0.71 PRO 177 -0.43 LEU 201

ASN 288 0.55 HIS 178 -0.52 PRO 151

ASP 184 0.74 HIS 179 -0.60 PRO 151

LEU 289 0.72 GLU 180 -0.58 LEU 201

LEU 289 0.62 ARG 181 -0.57 LEU 201

LEU 289 0.51 CYS 182 -0.72 LEU 201

LEU 289 0.51 CYS 182 -0.71 LEU 201

GLU 285 0.69 SER 183 -0.58 LEU 201

CYS 238 1.33 ASP 184 -0.96 LEU 201

TYR 236 1.70 SER 185 -0.71 LEU 201

CYS 135 1.75 ASP 186 -0.48 LEU 201

THR 140 1.73 GLY 187 -0.32 PRO 151

GLU 198 1.59 LEU 188 -0.35 ARG 202

GLU 285 0.95 ALA 189 -1.04 LEU 201

LEU 289 0.90 PRO 190 -0.55 LEU 201

LEU 289 0.82 PRO 191 -0.73 LEU 201

LEU 289 0.91 GLN 192 -0.52 LEU 201

GLU 285 0.99 HIS 193 -0.52 LEU 201

GLU 285 1.04 LEU 194 -0.52 PRO 151

GLU 285 1.14 ILE 195 -0.59 PRO 151

GLU 285 1.01 ARG 196 -0.71 PRO 151

LEU 188 1.39 VAL 197 -0.86 PRO 151

LEU 188 1.59 GLU 198 -1.06 PRO 151

LEU 188 1.03 GLY 199 -1.11 PRO 151

PRO 128 0.97 ASN 200 -0.76 PRO 151

PRO 128 0.84 LEU 201 -1.04 ALA 189

LEU 289 0.97 ARG 202 -0.74 ALA 189

LEU 289 1.01 VAL 203 -0.74 ALA 189

LEU 289 1.06 GLU 204 -0.52 VAL 97

LEU 289 1.06 GLU 204 -0.52 VAL 97

LEU 289 1.09 TYR 205 -0.57 VAL 97

LEU 289 1.17 LEU 206 -0.68 VAL 97

LEU 289 1.15 ASP 207 -0.68 VAL 97

LEU 289 1.25 ASP 208 -0.78 VAL 97

LEU 289 1.19 ARG 209 -0.62 THR 170

LEU 289 1.27 ASN 210 -0.76 THR 170

LEU 289 1.33 THR 211 -1.05 THR 170

LEU 289 1.21 PHE 212 -0.81 THR 170

LEU 289 1.25 ARG 213 -0.94 VAL 97

LEU 289 1.20 HIS 214 -0.77 VAL 97

LEU 289 1.22 SER 215 -0.80 VAL 97

LEU 289 1.15 VAL 216 -0.62 VAL 97

LEU 289 1.21 VAL 217 -0.52 VAL 97

LEU 289 1.13 VAL 218 -0.47 VAL 197

SER 149 1.21 PRO 219 -0.39 GLU 224

SER 149 1.55 TYR 220 -0.67 VAL 197

ASP 148 1.47 GLU 221 -0.58 GLY 199

ASN 131 1.46 PRO 222 -0.98 GLY 154

ALA 129 1.71 PRO 223 -0.95 PRO 152

ALA 129 1.55 GLU 224 -0.88 PRO 151

ALA 129 1.45 VAL 225 -0.69 PRO 151

ALA 129 1.50 GLY 226 -0.79 PRO 152

ALA 129 1.66 SER 227 -1.01 PRO 152

ALA 129 1.55 ASP 228 -1.06 PRO 152

ASN 131 1.70 CYS 229 -1.47 PRO 152

ASN 131 1.78 THR 230 -1.52 PRO 152

ASN 131 1.78 THR 230 -1.52 PRO 152

ASN 131 1.40 THR 231 -1.31 PRO 152

ASN 131 1.05 ILE 232 -1.07 PRO 152

LEU 188 1.17 HIS 233 -1.09 PRO 151

LEU 188 1.27 TYR 234 -0.91 PRO 151

SER 185 1.33 ASN 235 -0.89 PRO 151

SER 185 1.70 TYR 236 -0.74 PRO 151

SER 185 1.54 MET 237 -0.71 PRO 151

ASP 184 1.33 CYS 238 -0.63 PRO 151

SER 185 1.19 ASN 239 -0.61 PRO 151

ASP 186 1.09 SER 240 -0.49 PRO 151

ASP 186 0.91 SER 241 -0.56 LEU 130

ASP 184 0.91 CYS 242 -0.48 PRO 151

ASP 184 0.68 MET 243 -0.44 LEU 130

ASN 288 0.77 GLY 244 -0.31 LEU 130

ASN 288 0.84 GLY 245 -0.34 PRO 151

GLU 285 0.89 MET 246 -0.34 PRO 151

THR 284 0.72 ASN 247 -0.44 LEU 130

ASP 186 0.87 ARG 248 -0.57 LEU 130

THR 284 1.15 ARG 249 -0.38 LEU 130

THR 284 1.36 PRO 250 -0.37 SER 99

GLU 285 1.37 ILE 251 -0.47 VAL 97

GLU 285 1.68 LEU 252 -0.57 VAL 97

GLU 285 1.68 THR 253 -0.52 VAL 97

GLU 285 1.55 ILE 254 -0.59 CYS 141

GLU 285 1.42 ILE 255 -0.68 TYR 234

LEU 289 1.54 THR 256 -0.55 TYR 234

LEU 289 1.47 LEU 257 -0.57 ILE 232

LEU 289 1.52 GLU 258 -0.37 TYR 234

THR 150 1.68 ASP 259 -0.52 PRO 222

THR 150 1.52 SER 260 -0.59 PRO 222

LEU 289 1.45 SER 261 -0.46 PRO 222

LEU 289 1.58 GLY 262 -0.36 PRO 222

LEU 289 1.65 ASN 263 -0.32 PRO 222

LEU 289 1.70 LEU 264 -0.38 TYR 234

LEU 289 1.54 LEU 265 -0.43 ILE 232

LEU 289 1.54 GLY 266 -0.62 PRO 152

LEU 289 1.57 ARG 267 -0.63 PRO 152

LEU 289 1.38 ASN 268 -0.76 CYS 141

GLU 285 1.55 SER 269 -0.85 CYS 141

GLN 144 1.42 PHE 270 -0.64 GLN 100

GLU 285 1.36 GLU 271 -0.53 SER 99

ASP 186 1.39 VAL 272 -0.45 PRO 151

ASP 186 1.44 ARG 273 -0.48 PRO 151

ASP 186 1.48 VAL 274 -0.64 PRO 151

ASP 186 1.33 CYS 275 -0.66 PRO 151

ASP 186 1.15 ALA 276 -0.75 PRO 151

ASP 186 1.16 CYS 277 -0.76 PRO 151

ASP 186 1.16 CYS 277 -0.76 PRO 151

ASP 186 1.42 PRO 278 -0.69 PRO 151

ASP 186 1.23 GLY 279 -0.72 PRO 151

ASP 186 1.10 ARG 280 -0.59 PRO 151

ASP 186 1.31 ASP 281 -0.57 LEU 130

ASP 186 1.37 ARG 282 -0.42 LEU 130

ASP 186 1.10 ARG 283 -0.38 PRO 151

LYS 164 1.53 THR 284 -0.24 ALA 119

LEU 252 1.68 GLU 285 -0.19 GLU 286

LEU 111 1.43 GLU 286 -0.19 GLU 285

SER 166 1.68 GLU 287 -0.33 ALA 119

VAL 97 1.71 ASN 288 -0.17 ALA 119

LEU 264 1.70 LEU 289 -0.10 ALA 119

LYS 101 1.59 ARG 290 -0.24 ALA 119

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 2404260310462850495

--- normal mode 15 ---

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

* *