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

* MARIO trabajo bec *

CA distance fluctuations for 2502101601583366884

--- normal mode 8 ---

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
PRO 61 0.04 SER 7 -0.14 GLU 219

SER 305 0.03 VAL 8 -0.14 GLU 219

SER 305 0.03 TYR 9 -0.13 SER 223

PRO 61 0.04 ILE 10 -0.14 SER 223

VAL 57 0.04 THR 11 -0.16 GLU 219

SER 305 0.04 VAL 12 -0.16 SER 223

VAL 57 0.03 GLU 13 -0.16 SER 223

VAL 57 0.04 LEU 14 -0.18 SER 223

SER 305 0.04 ALA 15 -0.19 SER 223

SER 305 0.03 ILE 16 -0.19 SER 223

ILE 53 0.03 ALA 17 -0.19 SER 223

ALA 122 0.03 VAL 18 -0.22 SER 223

THR 279 0.05 LEU 19 -0.23 SER 223

THR 279 0.05 ALA 20 -0.22 SER 223

ALA 122 0.04 ILE 21 -0.23 SER 223

THR 279 0.04 LEU 22 -0.27 SER 223

VAL 282 0.06 GLY 23 -0.28 SER 223

VAL 282 0.03 ASN 24 -0.27 SER 223

THR 119 0.04 VAL 25 -0.27 SER 223

VAL 282 0.05 LEU 26 -0.32 SER 223

VAL 283 0.04 VAL 27 -0.33 SER 223

THR 119 0.04 CYS 28 -0.31 SER 223

VAL 283 0.03 TRP 29 -0.33 SER 223

PHE 286 0.04 ALA 30 -0.39 SER 223

THR 119 0.03 VAL 31 -0.39 SER 223

PHE 286 0.02 TRP 32 -0.35 SER 223

PHE 286 0.03 LEU 33 -0.39 SER 223

PHE 286 0.03 ASN 34 -0.46 SER 223

THR 119 0.03 SER 35 -0.46 ARG 220

ARG 293 0.05 ASN 36 -0.55 SER 223

ARG 293 0.06 LEU 37 -0.48 SER 223

THR 119 0.05 GLN 38 -0.38 SER 223

ARG 293 0.08 ASN 39 -0.36 THR 224

ARG 293 0.07 VAL 40 -0.24 THR 224

ILE 292 0.08 THR 41 -0.26 LYS 227

ILE 292 0.06 ASN 42 -0.32 LYS 227

ARG 293 0.04 TYR 43 -0.25 LYS 227

VAL 45 0.04 PHE 44 -0.22 LYS 227

PHE 44 0.04 VAL 45 -0.28 LYS 227

ALA 122 0.04 VAL 46 -0.26 LYS 227

ALA 122 0.04 SER 47 -0.21 LYS 227

VAL 196 0.03 LEU 48 -0.21 LYS 227

ALA 122 0.04 ALA 49 -0.24 LYS 227

ALA 122 0.04 ALA 50 -0.21 LYS 227

VAL 196 0.05 ALA 51 -0.18 LYS 227

GLY 195 0.04 ASP 52 -0.19 LYS 227

ALA 17 0.03 ILE 53 -0.21 SER 223

GLY 195 0.04 LEU 54 -0.18 SER 223

GLY 195 0.04 VAL 55 -0.17 SER 223

LEU 14 0.04 GLY 56 -0.19 SER 223

LEU 14 0.04 VAL 57 -0.19 SER 223

GLY 195 0.05 LEU 58 -0.16 SER 223

GLY 195 0.06 ALA 59 -0.14 SER 223

GLY 195 0.04 ILE 60 -0.15 SER 223

GLY 195 0.04 PRO 61 -0.15 SER 223

GLY 195 0.06 PHE 62 -0.13 SER 223

GLY 195 0.06 ALA 63 -0.12 SER 223

GLY 195 0.05 ILE 64 -0.13 SER 223

GLY 195 0.05 THR 65 -0.12 SER 223

GLY 195 0.06 ILE 66 -0.10 SER 223

GLY 195 0.06 SER 67 -0.09 SER 223

GLY 195 0.05 THR 68 -0.09 SER 223

GLY 195 0.06 GLY 69 -0.09 SER 223

GLY 195 0.06 PHE 70 -0.11 GLY 160

GLY 195 0.06 CYS 71 -0.12 GLY 160

GLY 195 0.06 ALA 72 -0.12 LEU 58

ARG 199 0.08 ALA 73 -0.09 LYS 227

GLU 161 0.12 CYS 74 -0.08 GLY 147

ARG 199 0.09 HIS 75 -0.09 LYS 227

ARG 199 0.07 GLY 76 -0.11 LYS 227

ARG 199 0.08 CYS 77 -0.09 LYS 227

ARG 199 0.09 LEU 78 -0.08 LYS 227

ARG 199 0.08 PHE 79 -0.10 LYS 227

GLY 195 0.07 ILE 80 -0.11 SER 223

GLY 195 0.08 ALA 81 -0.09 LYS 227

ARG 199 0.10 CYS 82 -0.09 LYS 227

ARG 199 0.08 PHE 83 -0.11 LYS 227

GLY 195 0.08 VAL 84 -0.11 LYS 227

ARG 199 0.10 LEU 85 -0.09 LYS 227

ARG 199 0.10 VAL 86 -0.11 LYS 227

ARG 199 0.07 LEU 87 -0.13 LYS 227

ARG 199 0.09 ALA 88 -0.11 LYS 227

ARG 199 0.12 GLN 89 -0.09 LYS 227

ARG 199 0.09 SER 90 -0.12 LYS 227

ARG 199 0.07 SER 91 -0.13 LYS 227

ARG 199 0.12 ILE 92 -0.09 LYS 227

ARG 199 0.13 PHE 93 -0.09 LYS 227

ARG 199 0.07 SER 94 -0.15 LYS 227

ARG 199 0.07 LEU 95 -0.12 LYS 227

ARG 199 0.12 LEU 96 -0.07 LYS 227

ILE 100 0.08 ALA 97 -0.10 LYS 227

ILE 292 0.06 ILE 98 -0.14 LYS 227

PHE 93 0.06 ALA 99 -0.07 LYS 227

GLN 214 0.09 ILE 100 -0.06 GLY 195

ILE 292 0.06 ASP 101 -0.09 LYS 227

ALA 231 0.07 ARG 102 -0.07 LYS 227

ALA 221 0.10 TYR 103 -0.07 ASN 36

PRO 215 0.10 ILE 104 -0.06 ASN 36

ALA 221 0.08 ALA 105 -0.12 ASN 36

ALA 221 0.15 ILE 106 -0.15 ASN 36

ALA 221 0.19 ALA 107 -0.10 ASN 36

ALA 221 0.19 ILE 108 -0.09 ASN 36

ALA 221 0.15 PRO 109 -0.12 ASN 36

GLY 218 0.15 LEU 110 -0.08 ASN 36

LEU 216 0.14 ARG 111 -0.05 ALA 202

LEU 216 0.08 TYR 112 -0.05 ALA 203

ALA 231 0.07 ASN 113 -0.07 GLY 118

PRO 215 0.08 GLY 114 -0.05 GLY 195

PRO 215 0.09 LEU 115 -0.05 GLY 195

ARG 293 0.06 VAL 116 -0.09 LYS 227

ARG 293 0.06 THR 117 -0.13 THR 224

ARG 293 0.06 GLY 118 -0.18 THR 224

ARG 293 0.05 THR 119 -0.14 THR 224

ARG 293 0.04 ARG 120 -0.11 LYS 227

ARG 293 0.04 ALA 121 -0.15 LYS 227

SER 47 0.04 ALA 122 -0.16 LYS 227

ARG 199 0.06 GLY 123 -0.12 LYS 227

ARG 199 0.08 ILE 124 -0.11 LYS 227

ARG 199 0.07 ILE 125 -0.14 LYS 227

ARG 199 0.08 ALA 126 -0.13 LYS 227

ARG 199 0.10 ILE 127 -0.09 LYS 227

ARG 199 0.11 CYS 128 -0.10 LYS 227

ARG 199 0.10 TRP 129 -0.12 LYS 227

ARG 199 0.11 VAL 130 -0.10 LYS 227

ARG 199 0.14 LEU 131 -0.07 LYS 227

ARG 199 0.12 SER 132 -0.09 LYS 227

ARG 199 0.11 PHE 133 -0.10 LYS 227

ARG 199 0.14 ALA 134 -0.07 LYS 227

ARG 199 0.15 ILE 135 -0.05 LYS 227

ARG 199 0.13 GLY 136 -0.08 LYS 227

ARG 199 0.12 LEU 137 -0.08 LYS 227

ARG 199 0.14 THR 138 -0.05 LYS 227

GLU 161 0.16 PRO 139 -0.05 LYS 227

GLU 161 0.13 MET 140 -0.07 LYS 227

GLU 161 0.13 LEU 141 -0.05 TRP 29

GLU 161 0.20 GLY 142 -0.05 TRP 29

GLU 161 0.22 TRP 143 -0.04 PRO 260

GLU 161 0.26 ASN 144 -0.04 PRO 260

GLU 161 0.32 ASN 145 -0.04 LEU 54

GLU 161 0.38 CYS 146 -0.06 GLY 147

GLU 161 0.52 GLY 147 -0.08 CYS 74

GLU 161 0.40 GLN 148 -0.05 CYS 166

GLU 161 0.30 PRO 149 -0.09 ALA 165

ASP 170 0.12 GLY 158 -0.06 SER 223

GLY 147 0.12 CYS 159 -0.10 GLY 160

GLY 147 0.25 GLY 160 -0.12 LEU 58

GLY 147 0.52 GLU 161 -0.09 SER 305

CYS 146 0.20 GLY 162 -0.09 VAL 25

CYS 146 0.14 GLN 163 -0.10 LEU 58

GLU 161 0.21 VAL 164 -0.07 PRO 149

GLU 161 0.16 ALA 165 -0.09 PRO 149

GLU 161 0.11 CYS 166 -0.07 SER 223

GLU 161 0.14 LEU 167 -0.06 LYS 227

GLU 161 0.15 PHE 168 -0.06 LYS 227

GLU 161 0.19 GLU 169 -0.04 PRO 260

GLU 161 0.25 ASP 170 -0.04 LYS 227

GLU 161 0.25 VAL 171 -0.05 LYS 227

GLU 161 0.21 VAL 172 -0.05 PRO 260

GLU 161 0.24 PRO 173 -0.06 PRO 260

GLU 161 0.22 MET 174 -0.05 PRO 260

GLU 161 0.21 ASN 175 -0.05 PRO 260

GLU 161 0.20 TYR 176 -0.05 ASN 175

GLU 161 0.17 MET 177 -0.04 LEU 131

GLU 161 0.17 VAL 178 -0.04 LEU 131

ALA 202 0.20 TYR 179 -0.07 PHE 180

ARG 199 0.19 PHE 180 -0.07 TYR 179

ARG 199 0.16 ASN 181 -0.05 LEU 131

ALA 202 0.17 PHE 182 -0.05 LEU 131

ALA 202 0.21 PHE 183 -0.04 ILE 127

ARG 199 0.21 ALA 184 -0.05 ILE 124

ARG 199 0.18 CYS 185 -0.05 ILE 124

GLY 195 0.17 VAL 186 -0.04 ILE 124

GLY 195 0.21 LEU 187 -0.06 VAL 188

GLY 195 0.24 VAL 188 -0.06 LEU 187

ARG 199 0.20 PRO 189 -0.04 ARG 120

GLY 195 0.19 LEU 190 -0.03 LEU 244

GLY 195 0.30 LEU 191 -0.04 LEU 244

ARG 199 0.25 LEU 192 -0.06 LEU 194

ARG 199 0.18 MET 193 -0.05 LEU 194

ALA 202 0.19 LEU 194 -0.06 LEU 192

LEU 191 0.30 GLY 195 -0.10 VAL 196

LEU 192 0.19 VAL 196 -0.10 GLY 195

LEU 191 0.15 TYR 197 -0.11 LEU 198

LEU 191 0.24 LEU 198 -0.11 TYR 197

LEU 192 0.25 ARG 199 -0.08 HIS 230

LEU 191 0.17 ILE 200 -0.09 ASN 36

LEU 191 0.18 PHE 201 -0.12 HIS 230

LEU 191 0.25 ALA 202 -0.14 HIS 230

LEU 191 0.22 ALA 203 -0.16 GLU 294

LEU 191 0.17 ALA 204 -0.22 HIS 230

LEU 191 0.19 ARG 205 -0.23 GLU 294

LEU 191 0.22 ARG 206 -0.22 GLU 294

LEU 191 0.18 GLN 207 -0.26 GLU 294

LEU 191 0.16 LEU 208 -0.33 GLU 294

LEU 191 0.19 LYS 209 -0.28 GLU 294

VAL 188 0.20 GLN 210 -0.27 GLU 294

LEU 191 0.16 MET 211 -0.33 GLU 294

VAL 188 0.15 GLU 212 -0.35 GLU 294

VAL 188 0.17 SER 213 -0.30 GLU 294

VAL 188 0.17 GLN 214 -0.31 GLU 294

ILE 108 0.16 PRO 215 -0.31 GLN 297

ILE 108 0.17 LEU 216 -0.35 GLN 297

ILE 108 0.14 PRO 217 -0.42 GLU 294

ILE 108 0.18 GLY 218 -0.41 GLU 294

ILE 108 0.13 GLU 219 -0.51 GLU 294

ILE 108 0.14 ARG 220 -0.53 ASN 36

ILE 108 0.19 ALA 221 -0.43 ASN 36

ALA 107 0.13 ARG 222 -0.47 GLU 294

PHE 201 0.10 SER 223 -0.62 GLU 294

PHE 201 0.09 THR 224 -0.53 ASN 36

PHE 201 0.13 LEU 225 -0.38 ASN 36

PHE 201 0.15 GLN 226 -0.47 GLU 294

VAL 229 0.07 LYS 227 -0.53 GLU 294

CYS 259 0.04 GLU 228 -0.28 LEU 37

LEU 191 0.08 VAL 229 -0.25 HIS 230

CYS 259 0.05 HIS 230 -0.25 LEU 208

ALA 105 0.08 ALA 231 -0.21 LYS 227

PHE 183 0.05 ALA 232 -0.10 VAL 45

PHE 183 0.06 LYS 233 -0.11 LEU 208

ARG 291 0.05 SER 234 -0.14 LEU 208

ARG 291 0.05 ALA 235 -0.13 LYS 227

PHE 183 0.06 ALA 236 -0.06 LEU 198

TYR 290 0.07 ILE 237 -0.08 GLU 212

TYR 290 0.07 ILE 238 -0.12 LYS 227

LEU 194 0.06 ALA 239 -0.07 LYS 227

TYR 290 0.07 GLY 240 -0.04 VAL 12

ILE 287 0.07 LEU 241 -0.07 SER 223

ASN 284 0.06 PHE 242 -0.07 LYS 227

ALA 202 0.09 ALA 243 -0.04 LEU 244

GLU 161 0.07 LEU 244 -0.04 LEU 191

ILE 303 0.06 CYS 245 -0.06 SER 223

ALA 202 0.08 TRP 246 -0.05 LYS 227

ALA 202 0.12 LEU 247 -0.03 VAL 188

GLU 161 0.10 PRO 248 -0.02 VAL 188

GLU 161 0.11 LEU 249 -0.03 LYS 227

ALA 202 0.13 HIS 250 -0.03 LEU 131

ALA 202 0.14 ILE 251 -0.02 LEU 131

GLU 161 0.14 ILE 252 -0.02 LEU 131

GLU 161 0.16 ASN 253 -0.03 LEU 131

ALA 202 0.17 CYS 254 -0.03 LEU 131

GLU 161 0.15 PHE 255 -0.03 LEU 131

GLU 161 0.17 THR 256 -0.03 LEU 131

GLU 161 0.19 PHE 257 -0.04 TYR 176

ALA 202 0.18 PHE 258 -0.04 TYR 176

GLU 161 0.17 CYS 259 -0.03 TYR 176

GLU 161 0.18 PRO 260 -0.06 PRO 173

GLU 161 0.16 ASP 261 -0.05 PRO 173

GLU 161 0.15 CYS 262 -0.03 PRO 173

GLU 161 0.14 SER 263 -0.03 PRO 173

GLU 161 0.15 HIS 264 -0.03 PRO 173

GLU 161 0.14 ALA 265 -0.02 LEU 131

GLU 161 0.12 PRO 266 -0.03 SER 223

GLU 161 0.11 LEU 267 -0.05 SER 223

GLU 161 0.09 TRP 268 -0.06 SER 223

GLU 161 0.09 LEU 269 -0.05 SER 223

GLU 161 0.10 MET 270 -0.05 SER 223

GLU 161 0.07 TYR 271 -0.08 SER 223

GLU 161 0.07 LEU 272 -0.08 SER 223

GLU 161 0.08 ALA 273 -0.06 SER 223

GLU 161 0.07 ILE 274 -0.08 SER 223

ARG 304 0.04 VAL 275 -0.11 SER 223

ILE 303 0.06 LEU 276 -0.10 SER 223

GLY 195 0.05 ALA 277 -0.10 SER 223

GLY 195 0.04 HIS 278 -0.13 SER 223

ILE 303 0.06 THR 279 -0.15 SER 223

ILE 303 0.05 ASN 280 -0.14 SER 223

ILE 303 0.04 SER 281 -0.18 SER 223

ILE 303 0.06 VAL 282 -0.20 SER 223

ILE 303 0.07 VAL 283 -0.20 SER 223

PHE 242 0.06 ASN 284 -0.23 LYS 227

ILE 303 0.06 PRO 285 -0.28 SER 223

ARG 300 0.07 PHE 286 -0.26 SER 223

LEU 241 0.07 ILE 287 -0.25 SER 223

ILE 238 0.07 TYR 288 -0.33 SER 223

LEU 244 0.06 ALA 289 -0.35 SER 223

ILE 238 0.07 TYR 290 -0.29 SER 223

THR 41 0.06 ARG 291 -0.30 SER 223

THR 41 0.08 ILE 292 -0.44 SER 223

ASN 39 0.08 ARG 293 -0.52 SER 223

ARG 293 0.07 GLU 294 -0.62 SER 223

LEU 244 0.05 PHE 295 -0.48 SER 223

LEU 244 0.06 ARG 296 -0.43 SER 223

LEU 244 0.05 GLN 297 -0.49 SER 223

PHE 286 0.05 THR 298 -0.47 SER 223

PHE 286 0.07 PHE 299 -0.40 SER 223

PHE 286 0.07 ARG 300 -0.40 GLU 219

PHE 286 0.06 LYS 301 -0.43 GLU 219

PHE 286 0.06 ILE 302 -0.38 GLU 219

VAL 283 0.07 ILE 303 -0.35 GLU 219

LEU 244 0.07 ARG 304 -0.37 GLU 219

LEU 244 0.05 SER 305 -0.37 GLU 219

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.

*** MARIO trabajo bec ***

CA distance fluctuations for 2502101601583366884

--- normal mode 8 ---

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

* MARIO trabajo bec *