Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* HYDROLASE 21-FEB-23 8CMV *

CA distance fluctuations for 2606131810021463505

--- 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 199 0.48 ASP 36 -0.76 SER 83

ASN 266 0.48 ASN 37 -0.46 LEU 84

SER 180 0.10 PRO 38 -0.37 ASN 37

ARG 40 0.18 TYR 39 -0.22 LYS 278

TYR 39 0.18 ARG 40 -0.35 ASN 37

TYR 39 0.05 ARG 41 -0.49 ASP 36

ALA 52 0.08 GLY 42 -0.57 ASP 36

ALA 52 0.10 PRO 43 -0.59 ASP 36

LEU 262 0.07 ASN 44 -0.41 ASP 36

LEU 262 0.08 PRO 45 -0.44 LYS 278

ARG 271 0.12 THR 46 -0.47 LYS 278

PHE 273 0.11 ARG 47 -0.49 LYS 278

ARG 271 0.08 ASP 48 -0.42 LYS 278

ARG 271 0.08 ASP 48 -0.42 LYS 278

LEU 262 0.07 ALA 49 -0.37 LYS 278

SER 258 0.07 LEU 50 -0.35 LYS 278

LEU 262 0.05 THR 51 -0.28 LYS 278

PRO 43 0.10 ALA 52 -0.27 LYS 278

GLY 54 0.10 ASP 53 -0.30 SER 64

ASP 53 0.10 GLY 54 -0.33 LYS 278

GLY 113 0.09 PRO 55 -0.46 ASP 36

TRP 104 0.08 PHE 56 -0.50 ASP 36

ALA 103 0.11 LYS 57 -0.46 ASP 36

ALA 103 0.13 VAL 58 -0.38 ASP 36

SER 100 0.16 ALA 59 -0.36 ASP 36

SER 100 0.17 THR 60 -0.32 SER 64

VAL 75 0.19 TYR 61 -0.36 LEU 66

ASN 120 0.21 THR 62 -0.38 SER 64

ASP 129 0.18 VAL 63 -0.34 SER 64

SER 130 0.20 SER 64 -0.40 VAL 75

ASN 122 0.31 ARG 65 -0.21 ALA 103

GLY 70 0.68 LEU 66 -0.36 TYR 61

GLY 70 0.39 SER 67 -0.33 TYR 61

LEU 66 0.36 VAL 68 -0.16 TYR 61

LEU 66 0.55 SER 69 -0.18 GLY 72

LEU 66 0.68 GLY 70 -0.11 ASN 140

LEU 66 0.48 PHE 71 -0.12 ASN 122

SER 130 0.27 GLY 72 -0.18 SER 69

ASP 129 0.19 GLY 73 -0.16 TRP 104

THR 62 0.19 GLY 74 -0.30 SER 64

TYR 61 0.19 VAL 75 -0.40 SER 64

ALA 99 0.13 ILE 76 -0.33 SER 64

SER 100 0.11 TYR 77 -0.30 SER 64

SER 100 0.11 TYR 78 -0.31 ASP 36

SER 100 0.10 PRO 79 -0.45 ASP 36

SER 100 0.12 THR 80 -0.53 ASP 36

SER 100 0.10 GLY 81 -0.65 ASP 36

SER 100 0.09 THR 82 -0.73 ASP 36

SER 100 0.08 SER 83 -0.76 ASP 36

ALA 103 0.07 LEU 84 -0.67 ASP 36

PHE 86 0.06 THR 85 -0.42 ASP 36

THR 85 0.06 PHE 86 -0.25 ASP 36

PRO 55 0.06 GLY 87 -0.15 LYS 278

VAL 115 0.06 GLY 88 -0.12 LYS 278

ASN 37 0.09 ILE 89 -0.11 SER 64

VAL 212 0.09 ALA 90 -0.08 SER 64

HIS 164 0.11 MET 91 -0.11 SER 64

HIS 164 0.11 MET 91 -0.10 SER 64

VAL 212 0.14 SER 92 -0.06 SER 133

VAL 212 0.17 PRO 93 -0.06 SER 64

VAL 212 0.23 GLY 94 -0.10 PRO 128

VAL 212 0.43 TYR 95 -0.14 PRO 128

VAL 212 0.43 THR 96 -0.12 GLY 127

VAL 212 0.26 ALA 97 -0.09 GLY 127

VAL 212 0.20 ASP 98 -0.14 SER 64

TYR 61 0.16 ALA 99 -0.24 SER 64

THR 60 0.17 SER 100 -0.30 SER 64

ALA 59 0.13 SER 101 -0.20 SER 64

ALA 59 0.11 LEU 102 -0.24 SER 64

ALA 59 0.14 ALA 103 -0.35 SER 64

LYS 57 0.10 TRP 104 -0.33 SER 64

LYS 57 0.07 LEU 105 -0.27 SER 64

LEU 102 0.08 GLY 106 -0.30 SER 64

LYS 57 0.10 ARG 107 -0.33 SER 64

ASN 246 0.06 ARG 108 -0.30 SER 64

VAL 264 0.06 LEU 109 -0.25 SER 64

ARG 107 0.08 ALA 110 -0.26 SER 64

TRP 104 0.08 SER 111 -0.32 ASP 36

ASP 53 0.08 HIS 112 -0.29 LYS 278

PRO 55 0.09 GLY 113 -0.32 ASP 36

SER 101 0.06 PHE 114 -0.20 LYS 278

HIS 164 0.07 VAL 115 -0.20 SER 64

TYR 78 0.09 VAL 116 -0.20 SER 64

VAL 212 0.11 LEU 117 -0.21 SER 64

ILE 76 0.13 VAL 118 -0.22 SER 64

VAL 212 0.17 ILE 119 -0.11 SER 64

THR 62 0.21 ASN 120 -0.10 TRP 104

LEU 66 0.26 THR 121 -0.10 ALA 137

LEU 66 0.42 ASN 122 -0.12 ALA 137

VAL 212 0.33 SER 123 -0.11 ALA 137

VAL 212 0.34 ARG 124 -0.13 SER 133

VAL 212 0.44 PHE 125 -0.21 ASP 126

LEU 66 0.38 ASP 126 -0.21 PHE 125

LEU 66 0.37 GLY 127 -0.15 ASP 129

LEU 66 0.40 PRO 128 -0.14 TYR 95

LEU 66 0.49 ASP 129 -0.15 GLY 127

LEU 66 0.53 SER 130 -0.15 PHE 125

LEU 66 0.41 ARG 131 -0.14 ALA 132

LEU 66 0.40 ALA 132 -0.14 ARG 131

LEU 66 0.53 SER 133 -0.16 PHE 125

LEU 66 0.53 SER 133 -0.16 PHE 125

LEU 66 0.47 GLN 134 -0.11 SER 136

LEU 66 0.32 LEU 135 -0.08 PHE 125

LEU 66 0.36 SER 136 -0.11 GLN 134

LEU 66 0.36 SER 136 -0.11 GLN 134

LEU 66 0.44 ALA 137 -0.12 ASN 122

LEU 66 0.25 ALA 138 -0.10 ASN 122

LEU 66 0.20 LEU 139 -0.07 ASN 122

LEU 66 0.23 ASN 140 -0.11 GLY 70

LEU 66 0.23 ASN 140 -0.11 GLY 70

LEU 66 0.19 TYR 141 -0.09 GLY 70

GLN 177 0.13 LEU 142 -0.08 ARG 41

GLN 177 0.13 LEU 142 -0.08 ARG 41

GLN 177 0.13 ARG 143 -0.07 LYS 278

GLN 177 0.16 THR 144 -0.08 GLY 70

GLN 177 0.17 ARG 145 -0.19 SER 146

ASP 129 0.14 SER 146 -0.19 ARG 145

ASP 129 0.13 PRO 147 -0.27 ASP 36

ASP 129 0.12 SER 148 -0.33 ASP 36

ASP 129 0.12 SER 148 -0.34 ASP 36

ALA 99 0.10 ALA 149 -0.41 ASP 36

ALA 99 0.09 VAL 150 -0.32 ASP 36

GLN 177 0.09 ARG 151 -0.27 ASP 36

SER 100 0.08 ALA 152 -0.39 ASP 36

LEU 154 0.10 ARG 153 -0.40 ASP 36

ARG 153 0.10 LEU 154 -0.22 ASP 36

SER 83 0.07 ASP 155 -0.14 LYS 278

GLN 177 0.07 ALA 156 -0.10 LYS 278

ASN 37 0.21 ASN 157 -0.10 LYS 293

ASN 37 0.23 ARG 158 -0.10 LYS 293

ASN 37 0.19 LEU 159 -0.07 LYS 293

ASN 37 0.21 ALA 160 -0.05 SER 64

ASN 37 0.17 VAL 161 -0.05 ASP 126

ASN 37 0.14 ALA 162 -0.07 SER 64

LEU 66 0.12 GLY 163 -0.05 ARG 173

GLY 206 0.12 HIS 164 -0.07 GLY 168

LEU 66 0.19 SER 165 -0.10 THR 192

LEU 66 0.27 MET 166 -0.09 PRO 128

LEU 66 0.24 GLY 167 -0.06 ARG 173

LEU 66 0.21 GLY 168 -0.07 HIS 164

LEU 66 0.30 GLY 169 -0.07 ARG 173

LEU 66 0.33 GLY 170 -0.08 TYR 95

LEU 66 0.25 THR 171 -0.06 ALA 175

LEU 66 0.28 LEU 172 -0.06 PRO 186

LEU 66 0.36 ARG 173 -0.08 TYR 95

LEU 66 0.33 ILE 174 -0.10 PHE 125

ASP 36 0.32 ALA 175 -0.07 PHE 125

ASP 36 0.34 GLU 176 -0.07 PHE 125

LEU 66 0.36 GLN 177 -0.11 PHE 125

ASP 36 0.35 ASN 178 -0.11 SER 130

ASP 36 0.45 PRO 179 -0.08 ASP 126

ASP 36 0.44 SER 180 -0.07 ASP 126

ASP 36 0.35 LEU 181 -0.07 ASP 126

ASP 36 0.37 LYS 182 -0.06 LYS 293

ASP 36 0.30 ALA 183 -0.05 SER 64

ASP 36 0.24 ALA 184 -0.03 SER 64

ASP 36 0.17 VAL 185 -0.06 SER 64

SER 69 0.16 PRO 186 -0.06 LEU 172

SER 69 0.12 LEU 187 -0.07 THR 192

TYR 95 0.19 THR 188 -0.08 THR 192

LEU 66 0.22 PRO 189 -0.09 THR 192

GLY 127 0.32 TRP 190 -0.10 SER 165

LEU 66 0.34 HIS 191 -0.10 SER 165

LEU 66 0.38 THR 192 -0.10 SER 165

LEU 66 0.38 ASP 193 -0.08 PRO 189

LEU 66 0.33 LYS 194 -0.09 ALA 213

LEU 66 0.32 THR 195 -0.06 ALA 213

LEU 66 0.31 PHE 196 -0.06 ASP 193

ASP 36 0.37 ASN 197 -0.04 ASP 193

ASP 36 0.40 THR 198 -0.05 ASP 193

ASP 36 0.48 SER 199 -0.04 ASP 193

ASP 36 0.43 VAL 200 -0.03 ASP 126

ASP 36 0.40 PRO 201 -0.05 LYS 182

ASP 36 0.29 VAL 202 -0.04 PHE 86

ASP 36 0.21 LEU 203 -0.05 GLY 113

ASP 36 0.17 ILE 204 -0.06 THR 256

LYS 278 0.15 VAL 205 -0.07 GLY 206

THR 96 0.19 GLY 206 -0.09 ILE 252

THR 96 0.23 ALA 207 -0.10 ILE 252

THR 96 0.25 GLU 208 -0.11 ALA 250

THR 96 0.29 ARG 209 -0.13 ALA 250

THR 96 0.33 ASP 210 -0.10 ASN 249

PHE 125 0.41 THR 211 -0.08 ALA 250

PHE 125 0.44 VAL 212 -0.07 THR 192

PHE 125 0.36 ALA 213 -0.09 HIS 218

PHE 125 0.33 PRO 214 -0.07 ASN 249

GLY 127 0.27 VAL 215 -0.08 ILE 252

GLY 127 0.27 SER 216 -0.07 ILE 252

GLY 127 0.27 SER 216 -0.07 ILE 252

GLY 127 0.33 GLN 217 -0.06 ILE 252

GLY 127 0.29 HIS 218 -0.09 ALA 213

GLY 127 0.22 ALA 219 -0.07 ILE 252

GLY 127 0.21 ILE 220 -0.06 ILE 252

LEU 66 0.25 PRO 221 -0.06 GLN 217

LEU 66 0.26 PHE 222 -0.05 ALA 213

ASP 36 0.24 TYR 223 -0.05 GLN 217

ASP 36 0.25 GLN 224 -0.05 SER 228

ASP 36 0.29 ASN 225 -0.05 ALA 213

ASP 36 0.33 LEU 226 -0.05 ALA 213

ASP 36 0.39 PRO 227 -0.04 ALA 213

ASP 36 0.39 SER 228 -0.05 SER 216

ASP 36 0.39 SER 228 -0.05 SER 216

ASP 36 0.47 THR 229 -0.05 PHE 86

ASP 36 0.45 THR 230 -0.04 PHE 86

ASP 36 0.42 PRO 231 -0.07 PHE 86

ASP 36 0.32 LYS 232 -0.06 PHE 86

ASP 36 0.23 VAL 233 -0.07 ARG 41

LYS 278 0.23 TYR 234 -0.07 ARG 41

LYS 278 0.23 VAL 235 -0.09 ARG 41

LYS 278 0.23 GLU 236 -0.09 PHE 273

THR 96 0.18 LEU 237 -0.14 ALA 251

THR 96 0.19 CYS 238 -0.18 ALA 251

THR 96 0.20 ASN 239 -0.24 ALA 250

THR 96 0.21 ASN 239 -0.23 ALA 250

THR 96 0.21 ALA 240 -0.18 ASN 249

THR 96 0.29 SER 241 -0.11 ASN 249

THR 96 0.30 HIS 242 -0.09 THR 192

THR 96 0.25 ILE 243 -0.09 THR 192

THR 96 0.16 ALA 244 -0.11 SER 64

THR 96 0.11 PRO 245 -0.14 SER 64

ALA 59 0.08 ASN 246 -0.17 SER 64

LYS 57 0.06 SER 247 -0.23 SER 64

PRO 43 0.06 ASN 248 -0.26 SER 64

THR 96 0.07 ASN 249 -0.22 ASN 239

LEU 274 0.06 ALA 250 -0.24 ASN 239

THR 96 0.08 ALA 251 -0.21 ASN 239

THR 96 0.08 ILE 252 -0.16 SER 64

THR 96 0.05 SER 253 -0.21 SER 64

ASP 48 0.06 VAL 254 -0.22 LYS 278

THR 96 0.07 TYR 255 -0.14 SER 64

ASN 37 0.09 THR 256 -0.15 SER 64

PRO 43 0.07 ILE 257 -0.21 LYS 278

THR 46 0.09 SER 258 -0.22 LYS 278

ASN 37 0.16 TRP 259 -0.12 MET 260

ASN 37 0.16 MET 260 -0.13 LYS 278

ASN 37 0.14 LYS 261 -0.21 LYS 278

ASN 37 0.24 LEU 262 -0.16 ASP 265

ASN 37 0.35 TRP 263 -0.22 VAL 264

ASN 37 0.27 VAL 264 -0.22 TRP 263

ASN 37 0.25 ASP 265 -0.18 LYS 278

ASN 37 0.48 ASN 266 -0.18 LYS 293

ASN 37 0.21 ASP 267 -0.24 LYS 278

ASP 36 0.26 THR 268 -0.26 LYS 278

PRO 179 0.07 ARG 269 -0.38 LYS 278

THR 46 0.11 TYR 270 -0.33 LYS 278

ASP 36 0.19 ARG 271 -0.26 LYS 278

CYS 292 0.08 GLN 272 -0.41 LYS 278

ARG 47 0.11 PHE 273 -0.40 LYS 278

ASP 36 0.13 LEU 274 -0.14 THR 82

ASP 36 0.16 CYS 275 -0.16 ARG 271

ASN 289 0.27 ASP 276 -0.34 GLN 272

ARG 286 0.16 VAL 277 -0.26 PHE 273

PHE 285 0.40 LYS 278 -0.49 ARG 47

ASP 284 0.15 ASP 279 -0.31 ARG 47

THR 96 0.13 PRO 280 -0.25 ASP 48

THR 96 0.15 ALA 281 -0.18 ASP 48

LYS 278 0.23 LEU 282 -0.14 ASP 48

LYS 278 0.31 CYS 283 -0.12 ASP 48

LYS 278 0.39 ASP 284 -0.10 ARG 269

LYS 278 0.40 PHE 285 -0.12 PHE 273

LYS 278 0.35 ARG 286 -0.09 ARG 41

LYS 278 0.25 THR 287 -0.09 ARG 40

ASP 36 0.32 ASN 288 -0.08 THR 82

ASP 36 0.33 ASN 289 -0.11 ASP 265

ASP 36 0.45 ARG 290 -0.11 ASP 265

ASP 36 0.42 HIS 291 -0.15 ASP 265

ASP 36 0.33 CYS 292 -0.15 ASN 266

ASP 36 0.38 LYS 293 -0.18 ASN 266

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** HYDROLASE 21-FEB-23 8CMV ***

CA distance fluctuations for 2606131810021463505

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* HYDROLASE 21-FEB-23 8CMV *