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

* LIVA_SerB *

CA distance fluctuations for 2401170857471422894

--- normal mode 11 ---

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 241 0.54 VAL 9 -0.18 ALA 276

LEU 241 0.42 SER 10 -0.19 LEU 11

GLU 244 0.44 LEU 11 -0.19 SER 10

GLU 244 0.32 VAL 12 -0.19 GLY 211

GLU 244 0.29 ALA 13 -0.18 GLY 211

GLU 244 0.20 THR 14 -0.20 GLY 211

GLU 244 0.17 LEU 15 -0.18 GLY 211

GLU 244 0.10 ILE 16 -0.20 GLY 211

LYS 279 0.08 ALA 17 -0.19 GLY 211

PRO 19 0.11 ASN 18 -0.28 THR 162

ASN 18 0.11 PRO 19 -0.35 PRO 163

LYS 298 0.07 ALA 20 -0.48 PRO 163

LYS 279 0.06 LYS 21 -0.37 THR 162

ILE 48 0.08 ALA 22 -0.31 PRO 163

LYS 279 0.09 ALA 23 -0.26 PRO 163

GLU 244 0.10 LEU 24 -0.21 PRO 163

GLU 244 0.10 ALA 25 -0.22 PRO 163

GLU 244 0.12 PRO 26 -0.19 GLN 303

GLU 244 0.14 SER 27 -0.18 PRO 163

GLU 244 0.16 LEU 28 -0.17 PRO 163

GLU 244 0.17 GLY 29 -0.18 GLY 211

GLU 244 0.18 ILE 30 -0.16 GLY 211

GLU 244 0.20 LYS 31 -0.16 GLY 211

GLU 244 0.24 ALA 32 -0.16 GLY 211

GLU 244 0.25 SER 33 -0.16 GLY 211

GLU 244 0.25 ALA 34 -0.15 GLY 211

GLU 244 0.28 ALA 35 -0.14 GLY 211

GLU 244 0.33 VAL 36 -0.13 GLY 211

GLU 244 0.31 ASN 37 -0.14 GLY 211

GLU 244 0.31 ASN 37 -0.14 GLY 211

GLU 244 0.28 ALA 38 -0.15 GLY 211

GLU 244 0.26 THR 39 -0.16 GLY 211

GLU 244 0.20 GLY 40 -0.17 GLY 211

GLU 244 0.18 LEU 41 -0.18 GLY 211

GLN 83 0.14 TYR 42 -0.19 GLY 211

GLU 84 0.11 TRP 43 -0.20 GLY 211

GLU 84 0.08 LEU 44 -0.21 GLY 211

GLU 84 0.06 ALA 45 -0.21 GLY 211

ALA 22 0.08 ASP 46 -0.22 GLN 303

GLY 295 0.08 ASP 47 -0.23 PRO 163

ALA 22 0.08 ILE 48 -0.23 GLY 164

GLY 295 0.11 ALA 49 -0.21 GLY 211

GLY 295 0.14 CYS 50 -0.20 GLY 211

GLU 244 0.16 ASP 51 -0.20 GLY 211

GLU 244 0.24 ILE 52 -0.18 GLY 211

GLU 244 0.28 PRO 53 -0.17 GLY 211

GLU 244 0.36 LEU 54 -0.15 GLY 211

GLU 244 0.36 PRO 55 -0.14 GLY 211

LEU 241 0.41 LEU 56 -0.14 GLY 211

GLU 244 0.51 GLY 57 -0.10 GLY 211

GLU 244 0.52 MET 58 -0.13 GLU 59

GLU 244 0.65 GLU 59 -0.13 MET 58

GLY 263 0.64 ALA 60 -0.11 LEU 56

GLY 263 0.62 SER 61 -0.08 PRO 272

GLU 244 0.51 GLU 62 -0.09 SER 66

GLU 244 0.43 ALA 63 -0.12 GLY 211

LYS 279 0.42 ASP 64 -0.14 LYS 271

LYS 279 0.43 ALA 65 -0.15 LYS 271

GLU 244 0.34 SER 66 -0.14 LYS 271

GLU 244 0.29 LEU 67 -0.17 LYS 271

LYS 279 0.29 ARG 68 -0.21 LYS 271

LYS 279 0.28 ALA 69 -0.18 LYS 271

GLU 244 0.23 THR 70 -0.17 LYS 271

LYS 279 0.22 LEU 71 -0.19 LYS 271

LYS 279 0.23 ASP 72 -0.21 LYS 271

LYS 279 0.21 GLY 73 -0.21 ALA 123

LYS 279 0.17 ALA 74 -0.21 ALA 123

LYS 279 0.12 PRO 75 -0.23 ALA 123

LYS 279 0.14 ILE 76 -0.20 LYS 271

LYS 279 0.15 ASP 77 -0.20 LYS 271

THR 264 0.24 VAL 78 -0.17 LYS 271

THR 264 0.32 VAL 79 -0.18 GLY 211

GLY 263 0.43 VAL 80 -0.17 GLY 211

GLU 244 0.45 GLN 81 -0.24 MET 280

GLU 244 0.44 GLU 82 -0.21 GLY 211

LEU 241 0.28 GLN 83 -0.23 GLY 211

GLY 240 0.33 GLU 84 -0.26 LYS 279

VAL 9 0.37 ARG 85 -0.27 GLY 211

ALA 60 0.36 ARG 86 -0.27 GLY 211

ALA 60 0.33 ARG 87 -0.29 GLY 211

ALA 60 0.36 LYS 88 -0.33 GLY 211

GLU 59 0.36 LYS 89 -0.39 GLY 211

GLU 59 0.36 ILE 90 -0.42 GLY 211

SER 61 0.30 LEU 91 -0.40 GLY 211

SER 61 0.29 ILE 92 -0.42 GLY 211

SER 61 0.23 ALA 93 -0.36 GLY 211

SER 61 0.18 ASP 94 -0.32 GLY 211

SER 61 0.14 MET 95 -0.29 GLY 211

GLU 103 0.13 ASP 96 -0.28 ALA 20

GLN 102 0.20 SER 97 -0.29 ALA 20

GLY 101 0.20 THR 98 -0.28 ALA 20

SER 61 0.15 MET 99 -0.33 ALA 20

ARG 158 0.16 ILE 100 -0.35 ALA 20

ALA 270 0.23 GLY 101 -0.33 ALA 20

SER 97 0.20 GLN 102 -0.26 ALA 20

LYS 271 0.18 GLU 103 -0.24 ALA 20

LYS 271 0.13 CYS 104 -0.22 ALA 20

LYS 271 0.14 ILE 105 -0.18 ALA 20

LYS 271 0.26 ASP 106 -0.15 ALA 20

LYS 271 0.25 GLU 107 -0.12 ALA 20

LYS 271 0.19 LEU 108 -0.18 SER 188

LYS 271 0.25 ALA 109 -0.16 SER 188

LYS 271 0.32 GLU 110 -0.15 SER 188

LYS 271 0.25 GLU 111 -0.20 SER 188

LYS 271 0.24 ALA 112 -0.19 SER 188

LYS 271 0.30 GLY 113 -0.15 SER 188

LYS 271 0.30 LEU 114 -0.12 SER 188

LYS 271 0.37 ARG 115 -0.11 SER 188

LYS 271 0.46 ASP 116 -0.16 HIS 117

LYS 271 0.31 HIS 117 -0.16 ASP 116

LYS 271 0.25 VAL 118 -0.13 ALA 20

LYS 271 0.36 ALA 119 -0.15 ALA 20

ALA 123 0.36 ALA 120 -0.16 LYS 21

ARG 225 0.22 ILE 121 -0.19 LYS 21

ARG 225 0.25 THR 122 -0.22 LYS 21

ALA 120 0.36 ALA 123 -0.26 LYS 21

ARG 225 0.30 ARG 124 -0.23 LYS 21

ARG 225 0.34 ALA 125 -0.20 LYS 21

ALA 253 0.29 MET 126 -0.23 HIS 284

ALA 253 0.30 MET 126 -0.23 HIS 284

ALA 120 0.29 ASN 127 -0.26 ALA 270

GLY 257 0.34 GLY 128 -0.41 ALA 131

ARG 225 0.36 GLU 129 -0.21 PRO 75

ARG 225 0.40 ILE 130 -0.18 LYS 21

GLU 226 0.34 ALA 131 -0.41 GLY 128

GLU 226 0.25 PHE 132 -0.29 GLY 252

GLU 133 0.14 GLU 133 -0.27 ALA 253

GLU 133 0.14 GLU 133 -0.27 ALA 253

ALA 227 0.08 PRO 134 -0.22 GLY 128

ARG 225 0.14 ALA 135 -0.19 LYS 21

GLU 59 0.07 LEU 136 -0.19 ALA 20

ARG 206 0.08 ARG 137 -0.16 LYS 21

GLY 216 0.13 GLU 138 -0.15 LYS 21

ILE 121 0.12 ARG 139 -0.15 ALA 20

GLY 216 0.13 VAL 140 -0.15 ALA 20

GLY 216 0.14 ALA 141 -0.15 LEU 223

GLY 145 0.18 LEU 142 -0.14 SER 188

VAL 118 0.16 LEU 143 -0.21 SER 188

ASP 210 0.16 LYS 144 -0.23 GLU 234

LEU 114 0.20 GLY 145 -0.28 SER 188

ALA 112 0.23 LEU 146 -0.34 SER 188

GLU 111 0.18 PRO 147 -0.40 SER 188

SER 149 0.18 LEU 148 -0.58 SER 188

LEU 148 0.18 SER 149 -0.35 SER 188

ILE 208 0.15 VAL 150 -0.28 SER 188

LEU 207 0.26 ILE 151 -0.25 SER 188

LEU 207 0.22 ASP 152 -0.20 ARG 191

ILE 208 0.18 LYS 153 -0.16 ARG 191

LYS 271 0.17 VAL 154 -0.14 ALA 20

ARG 206 0.16 ILE 155 -0.21 ALA 20

LEU 207 0.15 SER 156 -0.19 ALA 20

LYS 271 0.15 THR 157 -0.14 ALA 20

ALA 270 0.19 ARG 158 -0.14 ALA 20

ALA 270 0.13 ILE 159 -0.26 ALA 20

ARG 158 0.17 THR 160 -0.32 ALA 20

THR 160 0.16 LEU 161 -0.40 ALA 20

ARG 158 0.17 THR 162 -0.44 ALA 20

ARG 158 0.15 PRO 163 -0.48 ALA 20

ARG 158 0.13 GLY 164 -0.32 ALA 20

SER 61 0.13 GLY 165 -0.31 ALA 20

ALA 60 0.13 PRO 166 -0.30 ALA 20

ALA 60 0.12 GLN 167 -0.24 GLY 211

ALA 60 0.16 LEU 168 -0.27 GLY 211

ALA 60 0.19 VAL 169 -0.32 GLY 211

ALA 60 0.17 ARG 170 -0.30 GLY 211

GLU 84 0.17 THR 171 -0.28 GLY 211

ALA 60 0.22 MET 172 -0.32 GLY 211

GLU 84 0.23 ARG 173 -0.36 GLY 211

GLU 84 0.24 LYS 174 -0.32 GLY 211

GLU 84 0.30 HIS 175 -0.33 GLY 211

GLU 84 0.32 GLY 176 -0.38 GLY 211

VAL 9 0.29 ALA 177 -0.40 GLY 211

GLU 59 0.30 TYR 178 -0.47 GLY 211

GLU 59 0.26 THR 179 -0.45 GLY 211

GLU 59 0.25 ALA 180 -0.50 GLY 211

SER 61 0.19 LEU 181 -0.44 GLY 211

SER 61 0.19 VAL 182 -0.46 GLY 211

GLU 59 0.13 SER 183 -0.36 GLY 211

ILE 130 0.11 GLY 184 -0.29 GLY 211

PRO 221 0.12 GLY 185 -0.27 GLY 211

PRO 221 0.20 PHE 186 -0.36 GLY 211

PRO 221 0.26 THR 187 -0.54 GLY 211

PRO 221 0.26 THR 187 -0.54 GLY 211

ARG 206 0.24 SER 188 -0.58 LEU 148

PRO 221 0.19 PHE 189 -0.36 LEU 148

PRO 221 0.18 THR 190 -0.41 GLY 211

PRO 221 0.21 ARG 191 -0.51 GLY 211

PRO 221 0.19 ARG 192 -0.35 GLY 211

PRO 221 0.14 ILE 193 -0.31 GLY 211

GLU 59 0.15 ALA 194 -0.40 GLY 211

PRO 221 0.17 GLU 195 -0.37 GLY 211

PRO 221 0.13 MET 196 -0.30 ALA 20

ALA 60 0.14 ILE 197 -0.31 ALA 20

ALA 60 0.16 GLY 198 -0.36 GLY 211

GLU 59 0.19 PHE 199 -0.43 GLY 211

GLU 59 0.23 ASN 200 -0.52 GLY 211

GLU 59 0.22 GLU 201 -0.60 GLY 211

GLU 59 0.19 GLU 202 -0.58 GLY 211

GLU 59 0.18 ARG 203 -0.62 GLY 211

PRO 221 0.21 ALA 204 -0.50 GLY 211

PRO 221 0.28 ASN 205 -0.40 ALA 227

SER 188 0.24 ARG 206 -0.50 ASP 209

ILE 151 0.26 LEU 207 -0.40 ALA 227

ILE 151 0.25 ILE 208 -0.43 GLU 230

THR 215 0.20 ASP 209 -0.52 ARG 203

THR 215 0.16 ASP 210 -0.54 GLU 234

ALA 112 0.11 GLY 211 -0.65 GLU 234

ALA 112 0.16 THR 212 -0.53 ARG 238

ALA 112 0.18 ARG 213 -0.41 GLU 234

LEU 142 0.10 LEU 214 -0.37 ARG 203

ASP 209 0.20 THR 215 -0.32 GLU 234

ALA 141 0.14 GLY 216 -0.22 GLU 234

ILE 151 0.15 THR 217 -0.27 ALA 227

ILE 151 0.16 VAL 218 -0.41 LEU 223

SER 188 0.20 ALA 219 -0.50 ALA 227

SER 188 0.20 GLU 220 -0.49 GLU 226

ASN 205 0.28 PRO 221 -0.58 GLU 226

ASN 205 0.20 ILE 222 -0.45 ARG 225

ILE 130 0.16 LEU 223 -0.44 ALA 219

PHE 132 0.25 GLY 224 -0.38 ARG 225

ILE 130 0.40 ARG 225 -0.47 PRO 221

ILE 130 0.38 GLU 226 -0.58 PRO 221

ILE 130 0.29 ALA 227 -0.50 ALA 219

ILE 130 0.27 LYS 228 -0.46 GLY 211

SER 61 0.33 VAL 229 -0.47 GLY 211

GLU 59 0.33 GLU 230 -0.56 GLY 211

GLU 59 0.33 LYS 231 -0.60 GLY 211

GLU 59 0.38 LEU 232 -0.52 GLY 211

GLU 59 0.45 VAL 233 -0.56 GLY 211

GLU 59 0.40 GLU 234 -0.65 GLY 211

GLU 59 0.39 ILE 235 -0.61 GLY 211

GLU 59 0.47 ALA 236 -0.54 GLY 211

GLU 59 0.48 GLU 237 -0.59 GLY 211

GLU 59 0.42 ARG 238 -0.64 GLY 211

VAL 9 0.44 VAL 239 -0.57 GLY 211

VAL 9 0.52 GLY 240 -0.54 GLY 211

VAL 9 0.54 LEU 241 -0.50 GLY 211

GLU 59 0.59 THR 242 -0.47 GLY 211

GLU 59 0.55 PRO 243 -0.45 GLY 211

GLU 59 0.65 GLU 244 -0.39 GLY 211

GLU 59 0.52 ASP 245 -0.39 GLY 211

ALA 60 0.45 ALA 246 -0.39 GLY 211

SER 61 0.39 ILE 247 -0.34 GLY 211

SER 61 0.36 ALA 248 -0.35 GLY 211

SER 61 0.26 VAL 249 -0.30 GLY 211

ASP 116 0.21 GLY 250 -0.27 ASN 205

ASP 116 0.25 ASP 251 -0.24 ASN 205

ASP 116 0.26 GLY 252 -0.29 PHE 132

MET 126 0.30 ALA 253 -0.28 ILE 222

ALA 125 0.26 ASN 254 -0.34 ILE 222

ALA 253 0.25 ASP 255 -0.32 ASN 205

GLY 128 0.30 LEU 256 -0.35 PRO 221

GLY 128 0.34 GLY 257 -0.41 PRO 221

SER 61 0.37 MET 258 -0.38 GLY 211

SER 61 0.41 ILE 259 -0.32 GLY 211

SER 61 0.52 GLN 260 -0.33 PRO 221

SER 61 0.56 LEU 261 -0.38 GLY 211

SER 61 0.54 ALA 262 -0.38 GLY 211

ALA 60 0.64 GLY 263 -0.35 GLY 211

SER 61 0.53 THR 264 -0.31 GLY 211

SER 61 0.45 GLY 265 -0.29 GLY 211

SER 61 0.30 VAL 266 -0.25 GLY 211

ASP 116 0.25 ALA 267 -0.23 PRO 221

ASP 116 0.23 LEU 268 -0.22 ASN 205

ASP 116 0.25 HIS 269 -0.24 PHE 132

ASP 116 0.34 ALA 270 -0.27 ALA 131

ASP 116 0.46 LYS 271 -0.26 ASP 283

ASP 116 0.40 PRO 272 -0.26 ALA 131

ASP 116 0.37 ALA 273 -0.30 ALA 131

ASP 116 0.32 VAL 274 -0.28 ALA 131

ASP 116 0.31 ALA 275 -0.25 PRO 221

ASP 116 0.30 ALA 276 -0.27 PRO 221

SER 61 0.29 GLN 277 -0.31 PRO 221

SER 61 0.37 ALA 278 -0.28 PRO 221

SER 61 0.57 LYS 279 -0.26 GLU 84

SER 61 0.32 MET 280 -0.24 GLN 81

ASP 116 0.23 ARG 281 -0.21 GLN 81

ASP 116 0.23 ARG 281 -0.21 GLN 81

ASP 116 0.19 ILE 282 -0.19 ASN 205

ASP 116 0.18 ASP 283 -0.26 LYS 271

ASP 116 0.10 HIS 284 -0.23 ASN 127

ASP 116 0.10 GLY 285 -0.20 ASN 205

ASP 116 0.11 ASP 286 -0.24 THR 98

SER 61 0.12 LEU 287 -0.24 GLY 211

ARG 158 0.11 THR 288 -0.23 GLY 211

ASP 116 0.12 ALA 289 -0.22 GLY 211

SER 61 0.19 LEU 290 -0.26 GLY 211

ALA 60 0.16 LEU 291 -0.26 GLY 211

ALA 60 0.12 TYR 292 -0.23 GLY 211

ALA 60 0.19 ILE 293 -0.24 GLY 211

ALA 60 0.23 GLN 294 -0.26 GLY 211

ALA 60 0.16 GLY 295 -0.24 GLY 211

ALA 60 0.12 TYR 296 -0.24 GLY 211

GLU 84 0.10 ARG 297 -0.22 GLY 211

PRO 19 0.09 LYS 298 -0.21 GLY 211

GLU 84 0.10 ALA 299 -0.19 GLY 211

GLU 84 0.14 ASP 300 -0.23 GLY 211

GLU 84 0.13 PHE 301 -0.23 GLY 211

GLU 84 0.14 VAL 302 -0.23 GLY 211

ARG 158 0.12 GLN 303 -0.22 ASP 46

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.

*** LIVA_SerB ***

CA distance fluctuations for 2401170857471422894

--- normal mode 11 ---

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

* LIVA_SerB *