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

* *

CA distance fluctuations for 2503091505273813692

--- normal mode 20 ---

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 264 0.68 HIS 88 -0.88 ASN 263

LEU 264 0.54 HIS 89 -0.86 ASN 263

LEU 264 0.50 HIS 90 -0.99 ASN 263

GLN 104 0.41 HIS 91 -1.00 ASN 263

GLN 104 0.38 HIS 92 -1.05 ASN 263

GLN 104 0.41 HIS 93 -1.02 ASN 263

GLN 104 0.48 SER 94 -1.00 ASN 263

THR 155 0.55 SER 95 -0.79 ASN 263

GLN 104 0.54 SER 96 -0.84 ASN 263

GLN 104 0.55 VAL 97 -0.95 THR 256

GLN 104 0.69 PRO 98 -0.95 ASN 263

TYR 103 0.68 SER 99 -0.75 ASN 263

GLY 262 0.58 GLN 100 -0.83 THR 256

GLY 262 0.75 LYS 101 -0.56 ASN 263

GLY 262 0.75 THR 102 -0.62 VAL 157

GLY 262 1.12 TYR 103 -1.10 GLY 105

GLY 262 1.52 GLN 104 -0.42 ASP 148

LEU 265 1.57 GLY 105 -1.10 TYR 103

THR 256 1.00 SER 106 -0.55 GLY 266

THR 256 1.15 TYR 107 -0.63 GLY 154

GLY 262 1.13 GLY 108 -1.32 ASP 148

GLY 262 0.83 PHE 109 -1.05 GLY 105

GLY 262 0.65 ARG 110 -0.76 TYR 103

GLY 262 0.53 LEU 111 -0.80 LEU 257

GLY 262 0.42 GLY 112 -0.96 LEU 257

GLY 266 0.42 PHE 113 -1.12 ILE 255

LEU 264 0.48 LEU 114 -1.05 LEU 257

LEU 264 0.40 HIS 115 -1.24 LEU 257

LEU 264 0.31 SER 116 -1.42 LEU 257

LEU 264 0.36 GLY 117 -1.31 LEU 257

LEU 264 0.36 THR 118 -1.24 LEU 257

LEU 264 0.43 ALA 119 -1.10 LEU 257

LEU 264 0.47 LYS 120 -0.99 LEU 257

LEU 264 0.56 SER 121 -0.91 LEU 257

LEU 264 0.55 VAL 122 -0.98 LEU 257

LEU 264 0.63 THR 123 -0.87 LEU 257

LEU 264 0.58 CYS 124 -1.01 ILE 255

LEU 264 0.45 THR 125 -1.17 LEU 257

LEU 264 0.32 TYR 126 -1.32 LEU 257

GLY 262 0.32 SER 127 -1.53 LEU 257

GLY 262 0.37 PRO 128 -1.63 LEU 257

GLY 262 0.37 ALA 129 -1.69 LEU 257

GLY 262 0.36 LEU 130 -1.45 LEU 257

GLY 262 0.39 ASN 131 -1.32 LEU 257

GLY 262 0.32 LYS 132 -1.23 LEU 257

LEU 264 0.35 MET 133 -1.27 ILE 255

LEU 264 0.41 PHE 134 -1.06 LEU 257

LEU 264 0.55 CYS 135 -0.95 ILE 255

LEU 264 0.63 GLN 136 -0.94 ASN 263

LEU 264 0.71 LEU 137 -1.01 ASN 263

LEU 264 0.85 ALA 138 -1.03 ASN 263

LEU 264 0.83 LYS 139 -0.93 ASN 263

LEU 264 0.87 THR 140 -0.90 ASN 263

LEU 264 0.73 CYS 141 -1.03 ILE 255

GLY 266 0.73 PRO 142 -0.99 ILE 255

GLY 266 0.76 VAL 143 -1.08 ILE 255

GLY 266 0.70 GLN 144 -0.82 THR 155

GLY 266 0.77 LEU 145 -0.64 THR 155

THR 256 0.59 TRP 146 -0.62 THR 155

THR 256 0.88 VAL 147 -0.76 GLY 108

THR 256 0.89 ASP 148 -1.32 GLY 108

THR 256 1.12 SER 149 -0.65 GLY 108

THR 256 1.25 THR 150 -0.58 GLY 154

THR 256 1.65 PRO 151 -0.82 GLY 154

THR 256 1.65 PRO 152 -0.60 GLY 154

ARG 156 1.51 PRO 153 -0.20 GLU 221

LEU 257 0.70 GLY 154 -1.29 LEU 265

ASN 210 0.65 THR 155 -1.23 SER 227

PRO 153 1.51 ARG 156 -1.52 VAL 217

PRO 219 1.40 VAL 157 -1.10 LEU 265

GLY 266 1.38 ARG 158 -1.16 ASN 263

GLY 266 0.94 ALA 159 -1.33 ASN 263

GLY 266 0.63 MET 160 -1.64 ASN 263

GLN 104 0.47 ALA 161 -1.60 ASN 263

GLN 104 0.45 ILE 162 -1.73 THR 256

GLN 104 0.32 TYR 163 -1.41 THR 256

GLN 104 0.26 LYS 164 -1.23 THR 256

GLN 104 0.23 GLN 165 -1.07 THR 256

TYR 103 0.28 SER 166 -1.01 GLU 258

GLN 104 0.26 GLN 167 -1.08 GLU 258

GLN 104 0.31 HIS 168 -1.06 THR 256

GLN 104 0.37 MET 169 -1.17 THR 256

GLN 104 0.41 THR 170 -1.03 THR 256

GLN 104 0.39 GLU 171 -1.13 ASN 263

GLN 104 0.44 VAL 172 -1.31 ASN 263

LEU 264 0.41 VAL 173 -1.44 ASN 263

LEU 264 0.56 ARG 174 -1.38 ASN 263

LEU 264 0.65 ARG 175 -1.26 ASN 263

LEU 264 0.59 CYS 176 -1.11 ASN 263

LEU 264 0.63 PRO 177 -1.02 ASN 263

LEU 264 0.69 HIS 178 -1.06 ASP 259

LEU 264 0.77 HIS 179 -1.05 ASN 263

LEU 264 0.80 GLU 180 -1.08 ASN 263

LEU 264 0.82 ARG 181 -1.00 ASP 259

LEU 264 0.88 CYS 182 -1.04 ASP 259

LEU 264 1.01 SER 183 -0.97 ASP 259

LEU 264 1.05 ASP 184 -0.94 ASN 263

LEU 264 1.16 SER 185 -0.97 ASN 263

LEU 264 1.32 ASP 186 -0.89 ASN 263

LEU 264 1.40 GLY 187 -0.84 ASN 263

LEU 264 1.39 LEU 188 -0.91 ASN 263

LEU 264 1.18 ALA 189 -1.09 ASN 263

LEU 264 1.05 PRO 190 -1.11 ASN 263

LEU 264 0.95 PRO 191 -1.12 ASN 263

LEU 264 0.80 GLN 192 -1.24 ASN 263

LEU 264 0.82 HIS 193 -1.41 ASN 263

LEU 264 0.73 LEU 194 -1.44 ASN 263

LEU 264 0.79 ILE 195 -1.44 ASN 263

LEU 264 0.99 ARG 196 -1.24 ASN 263

LEU 264 1.08 VAL 197 -1.06 ASN 263

LEU 264 1.21 GLU 198 -0.90 ASN 263

LEU 264 1.33 GLY 199 -0.82 THR 155

LEU 264 1.39 ASN 200 -0.71 ASN 263

LEU 264 1.61 LEU 201 -0.65 ASN 263

LEU 264 1.42 ARG 202 -0.62 ASN 263

LEU 264 1.28 VAL 203 -0.84 ASN 263

LEU 264 1.15 GLU 204 -0.92 ARG 156

LEU 264 1.01 TYR 205 -1.15 ASN 263

LEU 264 0.81 LEU 206 -1.17 ASN 263

LEU 264 0.69 ASP 207 -1.20 ASN 263

ILE 255 0.59 ASP 208 -1.06 ASN 263

THR 155 0.54 ARG 209 -0.85 ASN 263

THR 155 0.65 ASN 210 -0.77 ASN 263

ILE 255 0.59 THR 211 -0.97 ASN 263

GLN 104 0.52 PHE 212 -1.13 ASN 263

GLN 104 0.57 ARG 213 -1.40 ASN 263

GLY 266 0.61 HIS 214 -1.59 ASN 263

GLY 266 0.80 SER 215 -1.59 ASN 263

GLY 266 1.05 VAL 216 -1.33 ASN 263

GLY 266 1.38 VAL 217 -1.52 ARG 156

GLY 266 1.46 VAL 218 -0.84 ARG 156

GLY 266 1.43 PRO 219 -0.74 LEU 265

GLY 266 1.02 TYR 220 -1.32 LEU 265

LEU 264 0.82 GLU 221 -1.00 LEU 265

THR 256 0.90 PRO 222 -0.69 THR 155

THR 256 0.70 PRO 223 -0.95 THR 155

LEU 264 0.74 GLU 224 -1.13 THR 155

LEU 264 0.63 VAL 225 -1.11 THR 155

LEU 264 0.55 GLY 226 -1.22 THR 155

LEU 264 0.57 SER 227 -1.23 THR 155

THR 256 0.55 ASP 228 -1.02 THR 155

GLY 266 0.59 CYS 229 -0.95 THR 155

GLY 266 0.85 THR 230 -0.95 THR 155

GLY 266 0.92 THR 231 -0.94 THR 155

GLY 266 1.09 ILE 232 -0.78 ASN 263

GLY 266 0.92 HIS 233 -0.88 ASN 263

GLY 266 0.88 TYR 234 -1.08 ASN 263

LEU 264 0.87 ASN 235 -1.12 ASN 263

LEU 264 0.74 TYR 236 -1.22 ASN 263

LEU 264 0.80 MET 237 -1.18 ASN 263

LEU 264 0.66 CYS 238 -1.16 ASN 263

LEU 264 0.55 ASN 239 -1.07 ASN 263

LEU 264 0.55 ASN 239 -1.07 ASN 263

LEU 264 0.42 SER 240 -1.02 ASN 263

LEU 264 0.42 SER 240 -1.08 ASN 263

LEU 264 0.45 SER 241 -1.00 ASP 259

LEU 264 0.41 SER 241 -1.00 ASN 263

LEU 264 0.51 CYS 242 -1.00 ASP 259

LEU 264 0.49 CYS 242 -1.02 ASN 263

LEU 264 0.47 MET 243 -1.04 ASP 259

LEU 264 0.44 MET 243 -1.01 ASP 259

LEU 264 0.44 GLY 244 -1.02 ASN 263

LEU 264 0.45 GLY 244 -1.02 ASN 263

LEU 264 0.47 GLY 245 -1.15 ASN 263

LEU 264 0.47 GLY 245 -1.14 ASN 263

LEU 264 0.39 MET 246 -1.16 ASN 263

LEU 264 0.39 MET 246 -1.16 ASN 263

LEU 264 0.35 ASN 247 -1.03 ASN 263

LEU 264 0.30 ARG 248 -0.99 ASN 263

LEU 264 0.22 ARG 249 -1.03 ASN 263

GLN 104 0.21 PRO 250 -1.09 THR 256

GLN 104 0.28 ILE 251 -1.34 THR 256

GLN 104 0.33 LEU 252 -1.36 THR 256

GLY 266 0.49 THR 253 -1.28 ASN 263

GLN 104 0.71 ILE 254 -1.16 ASN 263

SER 261 1.25 ILE 255 -1.27 MET 133

PRO 151 1.65 THR 256 -1.73 ILE 162

SER 261 0.80 LEU 257 -1.69 ALA 129

PRO 153 0.40 GLU 258 -1.08 GLN 167

SER 106 0.16 ASP 259 -1.06 HIS 178

THR 256 1.35 SER 260 -0.72 GLU 204

ILE 255 1.25 SER 261 -0.29 GLU 221

GLN 104 1.52 GLY 262 -0.64 LEU 206

THR 155 0.61 ASN 263 -1.64 MET 160

LEU 201 1.61 LEU 264 -0.29 LYS 101

GLY 105 1.57 LEU 265 -1.32 TYR 220

VAL 218 1.46 GLY 266 -0.60 TYR 103

GLN 104 0.85 ARG 267 -0.78 VAL 157

GLY 262 0.62 ASN 268 -0.87 VAL 157

GLY 262 0.53 SER 269 -0.90 ASN 263

GLY 262 0.41 PHE 270 -0.95 ASN 263

GLY 262 0.36 GLU 271 -0.96 ASN 263

GLY 266 0.34 VAL 272 -1.07 ASN 263

LEU 264 0.37 ARG 273 -1.00 ASN 263

LEU 264 0.49 VAL 274 -1.04 ASN 263

LEU 264 0.48 CYS 275 -0.93 ASN 263

LEU 264 0.52 ALA 276 -0.95 ASP 259

LEU 264 0.45 CYS 277 -0.94 LEU 257

LEU 264 0.43 PRO 278 -1.04 LEU 257

LEU 264 0.38 GLY 279 -1.15 LEU 257

LEU 264 0.32 ARG 280 -1.13 LEU 257

LEU 264 0.28 ASP 281 -1.14 LEU 257

LEU 264 0.24 ARG 282 -1.30 LEU 257

GLY 262 0.21 ARG 283 -1.35 LEU 257

GLY 262 0.20 THR 284 -1.25 LEU 257

GLY 262 0.23 GLU 285 -1.29 LEU 257

GLY 262 0.27 GLU 286 -1.47 LEU 257

GLY 262 0.25 GLU 287 -1.37 LEU 257

GLY 262 0.25 ASN 288 -1.26 LEU 257

GLY 262 0.29 LEU 289 -1.37 LEU 257

GLY 262 0.30 ARG 290 -1.39 LEU 257

GLY 262 0.28 LYS 291 -1.24 LEU 257

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 8th, 2025.

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

*** ***

CA distance fluctuations for 2503091505273813692

--- normal mode 20 ---

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

* *