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

* *

CA distance fluctuations for 2503091527343953881

--- normal mode 29 ---

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
THR 284 0.79 HIS 88 -0.80 ARG 181

THR 284 0.87 HIS 89 -0.81 LEU 289

THR 284 0.95 HIS 90 -0.85 LEU 289

ASN 288 1.03 HIS 91 -0.87 LEU 289

THR 284 1.13 HIS 92 -0.97 LEU 289

ASN 288 1.23 HIS 93 -0.93 LEU 289

ASN 288 1.28 SER 94 -0.88 ARG 290

ASN 288 1.37 SER 95 -0.91 ARG 290

ASN 288 1.37 SER 96 -1.00 ARG 290

ASN 288 1.47 VAL 97 -1.05 ARG 290

GLU 285 1.43 PRO 98 -1.11 ARG 290

ASN 288 1.55 SER 99 -1.39 GLY 262

GLU 285 1.40 GLN 100 -1.41 GLY 262

GLU 285 1.58 LYS 101 -1.28 ARG 290

GLU 285 1.79 THR 102 -1.12 ARG 290

GLU 285 1.39 TYR 103 -1.26 PRO 222

GLU 285 1.46 GLN 104 -1.40 PRO 222

GLU 285 1.28 GLY 105 -1.43 PRO 222

GLU 285 1.19 SER 106 -1.29 ARG 290

GLU 285 1.25 TYR 107 -1.35 PRO 222

GLU 285 1.43 GLY 108 -1.36 PRO 222

GLU 285 1.48 PHE 109 -1.53 PRO 222

GLU 285 1.45 ARG 110 -1.06 PRO 222

ALA 159 1.24 LEU 111 -0.90 GLU 287

GLU 285 0.96 GLY 112 -1.03 GLU 287

THR 150 0.97 PHE 113 -0.94 GLU 287

THR 150 0.97 LEU 114 -1.20 ARG 283

GLU 224 0.85 HIS 115 -1.30 ARG 283

THR 150 0.82 SER 116 -1.10 ARG 283

SER 127 0.91 GLY 117 -1.00 ARG 283

LEU 130 1.40 THR 118 -0.64 GLY 199

LEU 130 1.08 ALA 119 -0.63 GLY 199

LEU 130 0.87 LYS 120 -0.53 GLY 199

LEU 130 0.73 SER 121 -0.59 GLY 199

LEU 130 0.65 VAL 122 -0.63 GLY 199

ASP 184 0.76 THR 123 -0.42 PRO 153

ASP 184 0.82 CYS 124 -0.64 GLU 286

THR 150 0.76 THR 125 -0.63 PRO 142

THR 150 0.80 TYR 126 -0.90 PRO 142

THR 118 0.98 SER 127 -0.96 PRO 142

THR 118 0.72 PRO 128 -0.99 PRO 142

THR 118 0.94 ALA 129 -0.78 PRO 142

THR 118 1.40 LEU 130 -0.66 ASN 268

GLU 285 0.96 ASN 131 -1.00 PRO 142

GLU 285 0.82 LYS 132 -1.22 GLU 286

GLY 112 0.91 MET 133 -1.08 GLU 286

GLY 112 0.91 PHE 134 -0.96 GLU 286

ASP 184 0.93 CYS 135 -0.81 GLU 286

ASP 184 1.05 GLN 136 -0.65 GLU 286

ASP 184 1.28 LEU 137 -0.66 GLU 286

ASP 184 1.74 ALA 138 -0.68 GLU 286

ASP 184 1.20 LYS 139 -0.64 GLU 286

ASP 184 1.03 THR 140 -0.75 GLU 286

ASP 184 0.96 CYS 141 -0.95 GLU 286

THR 150 0.79 PRO 142 -1.00 ASN 131

ASP 184 0.88 VAL 143 -0.95 PRO 128

THR 150 1.11 GLN 144 -0.87 GLU 287

VAL 157 1.17 LEU 145 -0.85 GLU 287

GLU 285 1.17 TRP 146 -0.92 GLU 287

GLU 285 1.37 VAL 147 -1.73 PRO 223

GLU 285 1.29 ASP 148 -1.15 VAL 225

ASP 228 1.36 SER 149 -1.09 VAL 225

CYS 229 1.85 THR 150 -0.98 ARG 290

ASP 228 1.30 PRO 151 -1.20 GLU 224

ASP 228 1.17 PRO 152 -1.32 GLU 224

SER 261 0.81 PRO 153 -1.10 ASN 200

ASP 228 0.84 GLY 154 -1.07 ARG 290

GLU 285 0.89 THR 155 -1.12 ARG 290

GLU 285 0.88 ARG 156 -1.07 ARG 290

LEU 145 1.17 VAL 157 -1.00 ARG 290

LEU 145 1.09 ARG 158 -1.01 ARG 290

LEU 111 1.24 ALA 159 -0.91 ARG 290

LEU 111 1.05 MET 160 -0.90 ARG 290

ASP 281 1.05 ALA 161 -0.78 ARG 290

ASN 288 1.23 ILE 162 -0.86 GLU 286

ASN 288 1.29 TYR 163 -0.92 GLU 286

ASN 288 1.34 LYS 164 -1.08 GLU 286

ASN 288 1.40 GLN 165 -0.93 LEU 289

ASN 288 1.56 SER 166 -0.81 GLU 286

THR 284 1.64 GLN 167 -0.93 LEU 289

THR 284 1.47 HIS 168 -1.01 LEU 289

ASN 288 1.52 MET 169 -0.83 LEU 289

ASN 288 1.46 THR 170 -0.85 LEU 289

ASN 288 1.27 GLU 171 -0.98 LEU 289

ASN 288 1.17 VAL 172 -0.88 LEU 289

ASN 288 1.06 VAL 173 -0.87 LEU 289

THR 284 0.98 ARG 174 -0.85 LEU 289

THR 284 0.96 ARG 175 -0.82 LEU 289

THR 284 1.08 CYS 176 -0.90 LEU 289

THR 284 1.02 PRO 177 -0.87 LEU 289

THR 284 0.95 HIS 178 -0.76 LEU 289

THR 284 0.89 HIS 179 -0.67 SER 185

THR 284 0.85 GLU 180 -0.72 LEU 289

THR 284 0.80 ARG 181 -0.80 HIS 88

LEU 137 0.96 CYS 182 -0.64 HIS 88

ALA 138 1.05 SER 183 -0.71 HIS 88

ALA 138 1.74 ASP 184 -0.33 LEU 289

GLY 199 0.58 SER 185 -0.67 HIS 179

GLY 199 0.61 ASP 186 -0.73 PRO 153

GLY 199 0.46 GLY 187 -0.75 PRO 153

GLY 199 0.72 LEU 188 -0.67 PRO 153

ASN 288 0.53 ALA 189 -0.69 ARG 290

ASN 288 0.64 PRO 190 -0.66 ARG 290

THR 284 0.71 PRO 191 -0.63 LEU 289

THR 284 0.81 GLN 192 -0.72 LEU 289

ASN 288 0.73 HIS 193 -0.67 LEU 289

ASP 281 0.75 LEU 194 -0.76 GLU 286

ASP 184 0.79 ILE 195 -0.78 GLU 286

ASP 184 0.79 ARG 196 -0.75 GLU 286

ASP 184 0.75 VAL 197 -0.78 ARG 290

ASP 184 0.71 GLU 198 -0.88 PRO 153

LEU 188 0.72 GLY 199 -0.98 SER 227

LEU 188 0.42 ASN 200 -1.10 PRO 153

PRO 222 0.40 LEU 201 -0.79 PRO 153

GLU 285 0.51 ARG 202 -0.85 PRO 153

GLU 285 0.54 VAL 203 -0.81 ARG 290

ASN 288 0.65 GLU 204 -0.86 ARG 290

ASN 288 0.73 TYR 205 -0.84 ARG 290

ASN 288 0.82 LEU 206 -0.92 ARG 290

ASN 288 0.89 ASP 207 -0.89 ARG 290

ASN 288 0.95 ASP 208 -0.99 ARG 290

ASN 288 0.94 ARG 209 -0.98 ARG 290

ASN 288 1.01 ASN 210 -1.04 ARG 290

ASN 288 1.10 THR 211 -1.01 ARG 290

ASN 288 1.06 PHE 212 -0.89 ARG 290

ASN 288 1.07 ARG 213 -0.89 ARG 290

ASN 288 0.95 HIS 214 -0.84 ARG 290

ASN 288 0.87 SER 215 -0.89 ARG 290

LEU 111 0.84 VAL 216 -0.86 ARG 290

LEU 145 0.90 VAL 217 -0.93 ARG 290

THR 231 0.89 VAL 218 -0.90 ARG 290

GLU 285 0.77 PRO 219 -0.93 ARG 290

THR 150 1.03 TYR 220 -0.95 ARG 290

THR 231 0.97 GLU 221 -0.96 ARG 290

GLU 285 0.46 PRO 222 -1.53 PHE 109

GLU 285 0.60 PRO 223 -1.73 VAL 147

HIS 115 0.85 GLU 224 -1.32 PRO 152

HIS 115 0.56 VAL 225 -1.16 VAL 147

SER 149 0.75 GLY 226 -0.83 GLY 199

SER 149 0.95 SER 227 -0.98 GLY 199

SER 149 1.36 ASP 228 -0.82 GLU 287

THR 150 1.85 CYS 229 -0.85 GLU 287

THR 150 1.33 THR 230 -0.97 GLY 199

THR 150 1.07 THR 231 -0.87 GLY 199

THR 150 0.73 ILE 232 -0.89 ARG 267

ASP 184 0.76 HIS 233 -0.95 PHE 270

ASP 184 0.98 TYR 234 -1.12 PHE 270

ASP 184 1.24 ASN 235 -0.90 GLU 286

ASP 184 1.22 TYR 236 -0.88 GLU 286

ASP 184 1.20 MET 237 -0.69 GLU 286

ASP 281 0.88 CYS 238 -0.75 LEU 289

ASP 281 0.98 ASN 239 -0.79 LEU 289

ASP 281 0.98 ASN 239 -0.79 LEU 289

ASP 281 1.30 SER 240 -0.92 LEU 289

ASP 281 1.42 SER 240 -0.89 LEU 289

ARG 280 1.02 SER 241 -0.94 LEU 289

ASP 281 1.22 SER 241 -1.00 LEU 289

THR 284 1.04 CYS 242 -0.94 LEU 289

THR 284 1.08 CYS 242 -0.97 LEU 289

THR 284 1.24 MET 243 -1.00 LEU 289

THR 284 1.29 MET 243 -1.06 LEU 289

THR 284 1.32 GLY 244 -1.07 LEU 289

THR 284 1.30 GLY 244 -1.06 LEU 289

THR 284 1.22 GLY 245 -1.01 LEU 289

THR 284 1.21 GLY 245 -1.00 LEU 289

THR 284 1.24 MET 246 -1.04 LEU 289

THR 284 1.23 MET 246 -1.03 LEU 289

THR 284 1.38 ASN 247 -1.17 LEU 289

ASP 281 1.38 ARG 248 -1.16 LEU 289

ASP 281 1.43 ARG 249 -1.14 LEU 289

ASP 281 1.56 PRO 250 -1.07 GLU 286

ASP 281 1.32 ILE 251 -1.05 GLU 286

PRO 98 1.13 LEU 252 -1.05 GLU 286

LEU 111 1.13 THR 253 -0.87 GLU 286

GLU 285 1.23 ILE 254 -0.93 ARG 290

GLU 285 1.17 ILE 255 -0.95 ARG 290

GLU 285 1.12 THR 256 -1.10 ARG 290

GLU 285 1.10 LEU 257 -1.12 ARG 290

GLU 285 0.97 GLU 258 -1.24 ARG 290

GLU 285 0.92 ASP 259 -1.27 ARG 290

GLU 285 0.78 SER 260 -1.23 ARG 290

PRO 153 0.81 SER 261 -1.34 ARG 290

GLU 285 0.74 GLY 262 -1.41 GLN 100

GLU 285 0.86 ASN 263 -1.44 ARG 290

GLU 285 1.00 LEU 264 -1.39 ARG 290

GLU 285 1.13 LEU 265 -1.39 PRO 222

GLU 285 1.27 GLY 266 -1.51 PRO 222

GLU 285 1.30 ARG 267 -1.25 PRO 222

GLU 285 1.48 ASN 268 -0.96 ARG 290

GLU 285 1.36 SER 269 -0.89 ARG 290

GLU 285 1.33 PHE 270 -1.12 TYR 234

GLU 285 1.06 GLU 271 -1.23 GLU 286

ASP 281 1.05 VAL 272 -1.17 GLU 286

ASP 281 1.12 ARG 273 -1.15 GLU 286

ASP 281 0.88 VAL 274 -0.89 GLU 286

ASP 184 0.81 CYS 275 -0.64 GLU 286

CYS 182 0.86 ALA 276 -0.51 LEU 289

CYS 182 0.78 CYS 277 -0.34 LEU 289

ASP 184 0.78 PRO 278 -0.44 GLU 286

LEU 130 1.06 GLY 279 -0.47 GLY 199

ARG 248 1.07 ARG 280 -0.47 GLY 117

PRO 250 1.56 ASP 281 -0.47 ARG 280

LEU 130 1.06 ARG 282 -0.69 SER 116

ARG 248 0.79 ARG 283 -1.30 HIS 115

GLN 167 1.64 THR 284 -0.41 HIS 115

THR 102 1.79 GLU 285 -0.30 CYS 277

ALA 119 0.63 GLU 286 -1.23 GLU 271

MET 243 0.74 GLU 287 -1.03 GLY 112

SER 166 1.56 ASN 288 -0.15 ARG 280

GLY 226 0.56 LEU 289 -1.17 ASN 247

LYS 120 0.23 ARG 290 -1.44 ASN 263

MET 243 0.62 LYS 291 -0.88 GLY 112

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 2503091527343953881

--- normal mode 29 ---

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

* *