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

* no_ter *

CA distance fluctuations for 22123015423170986

--- normal mode 10 ---

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
SER 134 0.14 ASP 54 -0.19 GLY 68

SER 134 0.16 PHE 55 -0.18 GLY 68

SER 134 0.16 ASP 56 -0.23 THR 277

SER 134 0.20 PHE 57 -0.33 LYS 190

ARG 138 0.16 ALA 58 -0.42 LYS 190

ASN 114 0.13 PRO 59 -0.32 LYS 190

ASN 114 0.15 GLY 60 -0.36 LYS 190

ASN 114 0.15 SER 61 -0.38 LYS 190

ASN 114 0.19 PHE 62 -0.34 LYS 190

ASN 114 0.22 ASP 63 -0.33 LYS 190

ASN 114 0.31 ASP 64 -0.29 LYS 190

ASN 114 0.38 GLN 65 -0.27 TYR 66

ASN 114 0.53 TYR 66 -0.27 GLN 65

ASN 114 0.61 GLN 67 -0.31 ASN 274

ASN 114 0.82 GLY 68 -0.29 LEU 275

ASN 114 0.73 CYS 69 -0.23 LEU 275

ASN 114 0.74 SER 70 -0.24 ASN 274

THR 116 0.89 LYS 71 -0.21 ASN 274

THR 116 0.64 GLN 72 -0.20 ASN 274

THR 116 0.53 VAL 73 -0.20 LYS 190

THR 116 0.58 MET 74 -0.20 GLN 168

THR 117 0.53 GLU 75 -0.18 ASN 274

THR 117 0.36 LYS 76 -0.17 LYS 190

THR 117 0.30 LEU 77 -0.17 SER 165

LEU 105 0.37 THR 78 -0.23 SER 165

LEU 105 0.32 GLN 79 -0.17 GLN 168

LEU 105 0.23 GLY 80 -0.14 SER 165

ARG 152 0.18 ASP 81 -0.13 LEU 169

LEU 105 0.15 TYR 82 -0.13 GLY 221

HIS 101 0.17 PHE 83 -0.14 LEU 169

LEU 102 0.12 THR 84 -0.14 LEU 169

ALA 139 0.15 LYS 85 -0.23 LYS 289

PHE 136 0.14 ASP 86 -0.20 LYS 289

VAL 132 0.15 ILE 87 -0.15 LYS 289

VAL 132 0.14 GLU 88 -0.17 THR 118

ASP 135 0.18 ALA 89 -0.25 LYS 289

VAL 132 0.20 GLN 90 -0.27 LYS 289

VAL 132 0.20 LYS 91 -0.23 LYS 289

LEU 213 0.24 ASN 92 -0.26 SER 153

VAL 132 0.19 TYR 93 -0.23 SER 153

LEU 213 0.14 PHE 94 -0.17 THR 118

MET 96 0.19 ARG 95 -0.16 SER 153

LYS 71 0.19 MET 96 -0.19 SER 153

LYS 71 0.24 TRP 97 -0.19 GLY 221

LYS 71 0.27 GLN 98 -0.19 GLY 221

LYS 71 0.29 LYS 99 -0.23 GLY 221

LYS 71 0.32 ALA 100 -0.28 GLY 221

LYS 71 0.42 HIS 101 -0.25 GLY 221

LYS 71 0.41 LEU 102 -0.28 GLY 221

LYS 71 0.38 ALA 103 -0.34 GLY 221

LYS 71 0.47 TRP 104 -0.33 GLU 219

LYS 71 0.50 LEU 105 -0.32 GLN 218

LYS 71 0.45 ASN 106 -0.38 GLN 218

LYS 71 0.46 GLN 107 -0.41 GLN 218

LYS 71 0.52 GLY 108 -0.37 GLN 218

LYS 71 0.53 LYS 109 -0.37 GLN 218

LYS 71 0.56 VAL 110 -0.35 GLN 218

LYS 71 0.64 LEU 111 -0.30 GLN 218

GLY 68 0.52 PRO 112 -0.25 PHE 220

GLY 68 0.67 GLN 113 -0.20 PHE 220

GLY 68 0.82 ASN 114 -0.18 PHE 220

LYS 71 0.76 MET 115 -0.22 PHE 220

LYS 71 0.89 THR 116 -0.21 GLY 221

LYS 71 0.70 THR 117 -0.24 GLY 221

LYS 71 0.60 THR 118 -0.21 GLY 221

LYS 71 0.52 HIS 119 -0.23 LYS 190

LYS 71 0.48 ALA 120 -0.26 GLY 221

LYS 71 0.43 VAL 121 -0.25 GLY 221

LYS 71 0.33 ALA 122 -0.24 LYS 190

LYS 71 0.28 ILE 123 -0.28 LYS 190

LYS 71 0.30 LEU 124 -0.30 GLY 221

LYS 71 0.25 PHE 125 -0.26 GLY 221

LYS 71 0.20 TYR 126 -0.29 LYS 190

LEU 246 0.20 THR 127 -0.33 GLY 221

GLU 244 0.23 LEU 128 -0.31 GLY 221

THR 210 0.28 ASN 129 -0.26 ALA 103

THR 210 0.41 SER 130 -0.26 ALA 103

THR 210 0.30 ASN 131 -0.26 SER 153

ASN 92 0.21 VAL 132 -0.23 GLY 221

THR 210 0.23 HIS 133 -0.27 GLY 221

LEU 208 0.25 SER 134 -0.26 GLY 221

GLN 90 0.18 ASP 135 -0.27 SER 153

ALA 89 0.15 PHE 136 -0.28 LYS 190

GLN 206 0.16 THR 137 -0.39 LYS 190

PHE 57 0.20 ARG 138 -0.35 LYS 190

LYS 85 0.15 ALA 139 -0.30 LYS 190

ASN 114 0.10 MET 140 -0.37 LYS 190

ALA 58 0.14 ALA 141 -0.44 LYS 190

ALA 58 0.14 SER 142 -0.37 LYS 190

ASP 81 0.12 VAL 143 -0.32 LYS 190

ASN 114 0.16 ALA 144 -0.32 LYS 190

ASN 114 0.17 ARG 145 -0.34 LYS 190

ASN 114 0.22 THR 146 -0.31 LYS 190

ASN 114 0.26 PRO 147 -0.28 LYS 190

ASN 114 0.22 GLN 148 -0.26 LYS 190

ASN 114 0.17 GLN 149 -0.28 LYS 190

ASN 114 0.18 TYR 150 -0.28 LYS 190

ASN 114 0.20 GLU 151 -0.27 LYS 289

GLY 80 0.21 ARG 152 -0.27 LYS 289

GLY 80 0.17 SER 153 -0.27 ASP 135

GLY 80 0.12 PHE 154 -0.24 LYS 190

ALA 139 0.13 HIS 155 -0.21 LYS 289

TYR 158 0.10 PHE 156 -0.21 LYS 190

TYR 158 0.14 LYS 157 -0.21 LYS 190

HIS 101 0.16 TYR 158 -0.19 LYS 190

LYS 71 0.15 LEU 159 -0.21 LYS 190

ASN 114 0.10 HIS 160 -0.25 LYS 190

TYR 162 0.32 TYR 161 -0.23 LYS 190

TYR 161 0.32 TYR 162 -0.22 LYS 190

LYS 71 0.17 LEU 163 -0.26 LYS 190

ASN 114 0.15 THR 164 -0.24 LYS 190

MET 115 0.28 SER 165 -0.23 THR 78

GLY 68 0.31 ALA 166 -0.22 LYS 190

GLY 68 0.17 ILE 167 -0.23 LYS 190

GLN 65 0.31 GLN 168 -0.22 THR 78

GLY 68 0.41 LEU 169 -0.21 THR 78

GLY 68 0.29 LEU 170 -0.20 LYS 190

SER 276 0.19 ARG 171 -0.17 LYS 190

GLY 68 0.34 LYS 172 -0.20 THR 78

GLY 68 0.37 ASP 173 -0.17 ARG 188

GLY 68 0.24 SER 174 -0.18 LEU 212

ASN 274 0.23 ILE 175 -0.16 THR 78

GLY 68 0.31 MET 176 -0.16 THR 78

GLY 68 0.29 GLU 177 -0.20 LEU 212

GLY 68 0.19 ASN 178 -0.21 LEU 213

GLY 273 0.18 GLY 179 -0.14 LEU 213

SER 130 0.15 THR 180 -0.12 THR 78

THR 272 0.16 LEU 181 -0.16 THR 78

SER 130 0.19 CYS 182 -0.14 MET 74

SER 130 0.23 TYR 183 -0.14 GLU 184

SER 130 0.25 GLU 184 -0.17 VAL 110

SER 130 0.30 VAL 185 -0.20 VAL 110

SER 130 0.30 HIS 186 -0.23 VAL 110

SER 130 0.31 TYR 187 -0.26 GLU 244

ASN 131 0.15 ARG 188 -0.39 LYS 242

ASN 92 0.13 THR 189 -0.33 LEU 208

TRP 266 0.07 LYS 190 -0.44 ALA 141

TRP 266 0.09 ASP 191 -0.39 ALA 58

LYS 91 0.11 VAL 192 -0.29 ALA 58

LYS 91 0.10 HIS 193 -0.23 ALA 58

LYS 91 0.12 PHE 194 -0.15 THR 277

LYS 91 0.11 ASN 195 -0.15 LYS 242

ASN 131 0.11 ALA 196 -0.14 GLY 68

ASN 131 0.10 TYR 197 -0.14 GLY 68

TYR 260 0.12 THR 198 -0.13 GLY 68

SER 130 0.13 GLY 199 -0.15 GLY 68

SER 134 0.13 ALA 200 -0.17 GLY 68

SER 134 0.15 THR 201 -0.19 GLY 68

SER 134 0.17 ILE 202 -0.18 GLN 67

SER 134 0.17 ARG 203 -0.25 LYS 190

SER 134 0.22 PHE 204 -0.35 LYS 190

SER 134 0.15 GLY 205 -0.36 LYS 190

SER 134 0.21 GLN 206 -0.41 LYS 190

SER 130 0.21 PHE 207 -0.38 LYS 190

SER 130 0.32 LEU 208 -0.37 LYS 190

SER 130 0.39 SER 209 -0.34 LYS 190

SER 130 0.41 THR 210 -0.36 ARG 188

SER 130 0.37 SER 211 -0.28 PHE 220

SER 130 0.30 LEU 212 -0.28 VAL 110

SER 130 0.31 LEU 213 -0.28 VAL 110

SER 130 0.27 LYS 214 -0.24 VAL 110

SER 130 0.17 GLU 215 -0.31 LYS 243

THR 227 0.11 GLU 216 -0.36 LEU 241

GLN 268 0.22 ALA 217 -0.31 LEU 241

ASN 257 0.17 GLN 218 -0.47 LEU 241

SER 259 0.18 GLU 219 -0.46 LEU 241

TRP 266 0.11 PHE 220 -0.47 LYS 242

SER 259 0.12 GLY 221 -0.44 LEU 241

TRP 266 0.13 ASN 222 -0.39 LEU 241

TRP 266 0.14 GLN 223 -0.40 LYS 242

ASN 92 0.09 THR 224 -0.30 LYS 242

ASN 92 0.13 LEU 225 -0.29 LYS 242

SER 130 0.21 PHE 226 -0.19 LYS 242

SER 130 0.23 THR 227 -0.18 VAL 110

SER 130 0.25 ILE 228 -0.14 VAL 110

SER 130 0.24 PHE 229 -0.12 GLN 67

SER 130 0.24 THR 230 -0.13 GLN 67

SER 130 0.20 CYS 231 -0.16 SER 70

SER 130 0.18 LEU 232 -0.17 MET 74

SER 130 0.22 GLY 233 -0.20 LYS 190

SER 130 0.18 ALA 234 -0.22 ARG 188

SER 130 0.17 PRO 235 -0.26 ARG 188

LYS 71 0.19 VAL 236 -0.29 PHE 220

LYS 71 0.20 GLN 237 -0.33 PHE 220

LYS 71 0.30 TYR 238 -0.32 VAL 110

LYS 71 0.34 PHE 239 -0.33 PHE 220

LYS 71 0.27 SER 240 -0.38 PHE 220

LYS 71 0.25 LEU 241 -0.47 GLN 218

ARG 95 0.17 LYS 242 -0.47 PHE 220

LEU 128 0.16 LYS 243 -0.38 GLN 218

SER 130 0.25 GLU 244 -0.37 ARG 188

SER 130 0.27 VAL 245 -0.28 ARG 188

SER 130 0.28 LEU 246 -0.28 LYS 190

SER 130 0.25 ILE 247 -0.26 LYS 190

SER 130 0.19 PRO 248 -0.28 LYS 190

SER 134 0.16 PRO 249 -0.33 LYS 190

LYS 172 0.15 TYR 250 -0.27 LYS 190

SER 130 0.17 GLU 251 -0.22 LYS 190

SER 130 0.17 LEU 252 -0.23 GLN 67

SER 130 0.18 PHE 253 -0.18 GLN 67

SER 130 0.16 LYS 254 -0.17 GLY 68

SER 130 0.16 VAL 255 -0.15 GLY 68

ALA 217 0.18 ILE 256 -0.12 GLY 68

ALA 217 0.20 ASN 257 -0.13 LYS 214

ASN 257 0.14 MET 258 -0.16 LYS 242

GLU 219 0.18 SER 259 -0.20 LYS 242

ASN 257 0.13 TYR 260 -0.24 LYS 242

SER 259 0.13 HIS 261 -0.30 LYS 242

SER 259 0.08 PRO 262 -0.32 LEU 241

SER 259 0.17 ARG 263 -0.37 LEU 241

SER 259 0.12 GLY 264 -0.35 LYS 242

ASN 222 0.11 ASN 265 -0.28 LYS 242

GLN 218 0.15 TRP 266 -0.24 LYS 242

ALA 217 0.16 LEU 267 -0.17 LYS 242

ALA 217 0.22 GLN 268 -0.13 VAL 110

SER 130 0.20 LEU 269 -0.14 GLN 67

SER 130 0.20 ARG 270 -0.15 GLN 67

SER 130 0.19 SER 271 -0.18 GLN 67

ILE 175 0.19 THR 272 -0.22 GLY 68

ILE 175 0.22 GLY 273 -0.27 GLY 68

LYS 172 0.24 ASN 274 -0.31 GLN 67

LYS 172 0.21 LEU 275 -0.29 GLN 67

ASN 114 0.27 SER 276 -0.28 LYS 190

ASN 114 0.26 THR 277 -0.29 LYS 190

ASN 114 0.32 TYR 278 -0.30 LYS 190

ASN 114 0.41 ASN 279 -0.26 LYS 190

ASN 114 0.48 CYS 280 -0.25 LYS 190

ASN 114 0.36 GLN 281 -0.26 LYS 190

ASN 114 0.33 LEU 282 -0.23 LYS 190

ASN 114 0.42 LEU 283 -0.21 LYS 190

ASN 114 0.39 LYS 284 -0.23 LYS 190

ASN 114 0.30 ALA 285 -0.25 LYS 190

ASN 114 0.31 SER 286 -0.22 LYS 190

ASN 114 0.40 SER 287 -0.21 LYS 190

ASN 114 0.33 LYS 288 -0.23 LYS 190

ASN 114 0.28 LYS 289 -0.27 GLN 90

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: October 18th, 2018.

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

*** no_ter ***

CA distance fluctuations for 22123015423170986

--- normal mode 10 ---

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

* no_ter *