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

* *

CA distance fluctuations for 2404140341484168739

--- normal mode 12 ---

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 263 0.66 SER 96 -0.78 PHE 212

ASN 263 0.66 VAL 97 -0.80 PHE 212

ASN 263 0.56 PRO 98 -0.84 ARG 209

ASN 263 0.39 SER 99 -0.90 SER 166

GLY 262 0.38 GLN 100 -1.05 SER 166

LEU 206 0.26 LYS 101 -1.19 SER 166

LEU 206 0.28 THR 102 -1.01 SER 166

LEU 206 0.44 TYR 103 -0.96 ASN 210

LEU 206 0.43 GLN 104 -1.02 ASN 210

LEU 206 0.65 GLY 105 -1.16 ASN 210

LEU 206 0.69 SER 106 -1.28 ASN 210

LEU 206 0.59 TYR 107 -1.19 ASN 210

LEU 206 0.49 GLY 108 -1.06 ASN 210

LEU 257 0.42 PHE 109 -1.00 ASN 210

ARG 156 0.59 ARG 110 -0.88 ASN 210

ARG 156 0.68 LEU 111 -0.78 ASN 210

ARG 156 0.66 GLY 112 -0.74 ASN 210

ARG 158 0.71 PHE 113 -0.62 ASN 210

ARG 156 0.59 LEU 114 -0.75 SER 227

ARG 158 0.52 HIS 115 -0.71 SER 227

GLY 262 0.57 SER 116 -0.67 SER 227

GLY 262 0.57 SER 116 -0.67 SER 227

GLY 262 0.62 GLY 117 -0.56 SER 227

GLY 262 0.74 THR 118 -0.47 SER 227

GLY 262 0.76 ALA 119 -0.49 ASP 186

GLY 262 0.87 LYS 120 -0.58 ASP 186

GLY 262 0.85 SER 121 -0.60 ASP 186

GLY 262 0.82 VAL 122 -0.56 ASP 186

GLY 262 0.82 VAL 122 -0.56 ASP 186

GLY 262 0.91 THR 123 -0.63 ASP 186

GLY 262 0.83 CYS 124 -0.49 ASP 186

GLY 262 0.83 CYS 124 -0.49 ASP 186

GLY 262 0.74 THR 125 -0.45 SER 227

ARG 158 0.70 TYR 126 -0.41 ASP 228

GLY 262 0.61 SER 127 -0.41 ASN 210

ARG 158 0.57 PRO 128 -0.52 ASN 210

GLY 262 0.47 ALA 129 -0.54 ARG 248

GLY 262 0.56 LEU 130 -0.62 ARG 248

GLY 262 0.54 ASN 131 -0.65 GLY 112

GLY 262 0.69 LYS 132 -0.57 GLY 112

GLY 262 0.79 MET 133 -0.34 ASP 186

GLY 262 0.79 MET 133 -0.34 ASP 186

GLY 262 0.92 PHE 134 -0.47 GLU 285

GLY 262 1.00 CYS 135 -0.53 ASP 186

GLY 262 1.11 GLN 136 -0.69 ASP 186

GLY 262 1.22 LEU 137 -0.75 ASP 186

GLY 262 1.13 ALA 138 -0.87 ASP 186

GLY 226 1.09 LYS 139 -0.79 ASP 186

GLY 226 1.12 THR 140 -0.58 LEU 188

GLY 226 0.88 CYS 141 -0.41 ASP 186

GLY 226 0.88 CYS 141 -0.41 ASP 186

ARG 156 0.89 PRO 142 -0.50 ASN 210

ARG 156 0.96 VAL 143 -0.73 THR 253

ARG 156 0.83 GLN 144 -0.75 ASN 210

ARG 156 0.74 LEU 145 -0.88 ASN 210

ARG 156 0.66 TRP 146 -0.91 ASN 210

ARG 156 0.58 VAL 147 -1.02 ASN 210

PRO 222 0.50 ASP 148 -1.05 ASN 210

LEU 206 0.53 SER 149 -1.14 ASN 210

GLU 204 0.53 THR 150 -1.10 ASN 210

LEU 206 0.67 PRO 151 -1.14 ASN 210

LEU 206 0.93 PRO 152 -1.07 ASN 210

GLU 204 0.95 PRO 153 -1.00 ASN 210

GLU 204 1.36 GLY 154 -1.02 ASN 210

GLU 204 1.28 THR 155 -1.08 ASN 210

TYR 234 1.02 ARG 156 -0.94 ASN 210

ARG 156 0.83 VAL 157 -0.95 ARG 209

TYR 234 0.91 ARG 158 -1.29 ARG 209

GLY 262 0.61 ALA 159 -0.70 ARG 209

ASN 263 0.76 MET 160 -0.64 ILE 232

GLY 262 0.88 ALA 161 -0.62 ILE 232

GLY 262 0.85 ILE 162 -0.60 ILE 232

GLY 262 0.95 TYR 163 -0.52 GLN 100

GLY 262 0.82 LYS 164 -0.75 GLN 100

GLY 262 0.86 GLN 165 -0.83 LYS 101

GLY 262 0.71 SER 166 -1.19 LYS 101

GLY 262 0.93 GLN 167 -0.83 LYS 101

GLY 262 1.02 HIS 168 -0.59 GLN 100

GLY 262 0.83 MET 169 -0.74 GLN 100

GLY 262 0.83 MET 169 -0.74 GLN 100

ASN 263 0.96 THR 170 -0.44 GLN 100

ASN 263 1.16 GLU 171 -0.36 ILE 232

ASN 263 1.23 VAL 172 -0.35 ILE 232

ASN 263 1.17 VAL 173 -0.32 ILE 232

ASN 263 1.38 ARG 174 -0.21 ILE 232

GLY 262 1.42 ARG 175 -0.35 GLU 285

GLY 262 1.62 CYS 176 -0.44 GLU 285

GLY 262 1.56 PRO 177 -0.42 GLU 285

GLY 262 1.56 HIS 178 -0.50 GLU 285

GLY 262 1.47 HIS 179 -0.50 GLU 285

ASN 263 1.47 GLU 180 -0.39 GLU 285

ASN 263 1.43 ARG 181 -0.43 GLU 285

GLY 262 1.30 CYS 182 -0.54 ALA 276

SER 260 1.35 SER 183 -0.50 ALA 276

SER 260 1.35 ASP 184 -0.49 ALA 276

SER 260 1.46 SER 185 -0.56 ALA 138

SER 260 1.30 ASP 186 -0.87 ALA 138

SER 260 1.36 GLY 187 -0.68 ALA 138

SER 260 1.50 LEU 188 -0.64 LYS 139

SER 260 1.65 ALA 189 -0.46 ALA 138

SER 260 1.96 PRO 190 -0.37 ALA 138

SER 260 1.73 PRO 191 -0.36 ALA 138

SER 260 1.60 GLN 192 -0.24 GLU 285

SER 260 1.60 GLN 192 -0.24 GLU 285

SER 260 1.47 HIS 193 -0.23 LEU 252

SER 260 1.20 LEU 194 -0.39 LEU 252

SER 260 1.07 ILE 195 -0.46 LEU 252

SER 260 1.07 ARG 196 -0.50 LEU 252

GLY 226 0.83 VAL 197 -0.60 THR 253

GLY 226 0.99 GLU 198 -0.50 LEU 188

GLY 226 1.02 GLY 199 -0.44 ASP 208

GLY 226 0.80 ASN 200 -0.57 GLU 221

ASP 186 0.74 LEU 201 -0.48 ASP 208

GLY 154 0.69 ARG 202 -0.63 ASP 208

SER 260 0.89 VAL 203 -0.68 ASP 208

GLY 154 1.36 GLU 204 -0.72 ASP 208

ASP 259 1.60 TYR 205 -0.42 ASP 208

ASP 259 1.57 LEU 206 -0.33 ASP 208

ASP 259 1.55 ASP 207 -0.20 ILE 232

ASN 263 1.12 ASP 208 -0.84 VAL 217

ASN 263 1.49 ARG 209 -1.29 ARG 158

SER 261 0.66 ASN 210 -1.39 ASP 259

ASN 263 1.12 THR 211 -1.55 PHE 212

ASN 263 1.55 PHE 212 -1.55 THR 211

ASN 263 1.14 ARG 213 -0.40 ILE 232

ASP 259 1.18 HIS 214 -0.33 ILE 232

LEU 264 1.12 SER 215 -0.67 ASP 208

SER 260 1.05 VAL 216 -0.76 ASP 208

ARG 156 0.72 VAL 217 -0.86 ARG 209

ARG 156 0.71 VAL 217 -0.86 ARG 209

TYR 234 0.89 VAL 218 -0.80 ARG 209

THR 230 0.69 PRO 219 -0.82 ASN 210

ARG 156 0.54 TYR 220 -0.91 ASN 210

SER 149 0.44 GLU 221 -0.87 ASN 210

ASP 148 0.50 PRO 222 -0.92 ASN 210

ARG 156 0.54 PRO 223 -0.88 ASN 210

PRO 219 0.65 GLU 224 -0.77 ASN 210

ARG 156 0.50 VAL 225 -0.82 ASN 210

THR 140 1.12 GLY 226 -0.79 ASN 210

ARG 156 0.57 SER 227 -0.79 ASN 210

ARG 156 0.57 SER 227 -0.79 ASN 210

ARG 156 0.49 ASP 228 -0.91 ASN 210

ARG 156 0.66 CYS 229 -0.87 ASN 210

ARG 156 0.85 THR 230 -0.83 ASN 210

ARG 156 0.92 THR 231 -0.71 ASN 210

GLY 226 0.86 ILE 232 -0.97 THR 253

ARG 156 0.99 HIS 233 -0.57 THR 253

ARG 156 1.02 TYR 234 -0.65 THR 253

GLY 262 0.96 ASN 235 -0.54 LEU 188

GLY 262 1.10 TYR 236 -0.52 ASP 186

GLY 262 1.27 MET 237 -0.45 ASP 186

GLY 262 1.43 CYS 238 -0.51 GLU 285

GLY 262 1.45 ASN 239 -0.64 GLU 285

GLY 262 1.41 SER 240 -0.69 GLU 285

GLY 262 1.58 SER 241 -0.78 GLU 285

GLY 262 1.73 CYS 242 -0.63 GLU 285

GLY 262 1.89 MET 243 -0.56 GLU 285

GLY 262 1.77 GLY 244 -0.45 GLU 287

GLY 262 1.62 GLY 245 -0.44 GLU 285

GLY 262 1.47 MET 246 -0.41 LEU 130

GLY 262 1.61 ASN 247 -0.56 GLU 287

GLY 262 1.44 ARG 248 -0.64 GLU 287

GLY 262 1.28 ARG 249 -0.57 LEU 130

GLY 262 1.08 PRO 250 -0.55 LEU 130

GLY 262 0.95 ILE 251 -0.54 ILE 232

GLY 262 0.74 LEU 252 -0.76 ILE 232

GLY 262 0.72 THR 253 -0.97 ILE 232

GLY 262 0.54 ILE 254 -0.82 ILE 232

MET 133 0.55 ILE 255 -0.70 ASN 210

MET 133 0.44 THR 256 -0.83 ASN 210

LEU 206 0.44 THR 256 -0.82 ASN 210

MET 133 0.43 THR 256 -0.83 ASN 210

ARG 110 0.57 LEU 257 -1.00 ASN 210

LEU 206 0.88 GLU 258 -1.05 ASN 210

TYR 205 1.60 ASP 259 -1.39 ASN 210

PRO 190 1.96 SER 260 -1.21 ASN 210

HIS 178 1.19 SER 261 -0.28 SER 149

MET 243 1.89 GLY 262 -0.38 ASN 210

PHE 212 1.55 ASN 263 -0.91 ASN 210

LEU 206 1.35 LEU 264 -1.19 ASN 210

LEU 206 1.05 LEU 265 -1.20 ASN 210

LEU 206 0.67 GLY 266 -1.03 ASN 210

LEU 206 0.41 ARG 267 -0.88 ASN 210

PRO 128 0.38 ASN 268 -0.78 ASN 210

GLY 262 0.44 SER 269 -0.66 ILE 232

GLY 262 0.58 PHE 270 -0.71 LEU 111

GLY 262 0.73 GLU 271 -0.68 VAL 143

GLY 262 0.73 GLU 271 -0.68 VAL 143

GLY 262 0.89 VAL 272 -0.49 VAL 143

GLY 262 0.89 VAL 272 -0.50 VAL 143

GLY 262 1.09 ARG 273 -0.63 GLU 285

GLY 262 1.20 VAL 274 -0.61 GLU 285

GLY 262 1.24 CYS 275 -0.66 GLU 285

GLY 262 1.20 ALA 276 -0.67 ASP 186

GLY 262 1.08 CYS 277 -0.61 ASP 186

GLY 262 1.08 CYS 277 -0.61 ASP 186

GLY 262 0.99 PRO 278 -0.54 ASP 186

GLY 262 0.99 PRO 278 -0.53 ASP 186

GLY 262 0.88 GLY 279 -0.48 ASP 186

GLY 262 0.94 ARG 280 -0.47 ASP 186

GLY 262 0.98 ASP 281 -0.45 ASP 186

GLY 262 0.83 ARG 282 -0.41 ASP 186

GLY 262 0.78 ARG 283 -0.38 ASP 186

GLY 262 0.84 THR 284 -0.42 ASP 186

GLY 262 0.73 GLU 285 -0.78 SER 241

GLY 262 0.64 GLU 286 -0.63 ARG 248

GLY 262 0.62 GLU 287 -0.66 SER 241

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 2404140341484168739

--- normal mode 12 ---

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

* *