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

* LAO_open_cutoff8 *

CA distance fluctuations for 260611150511729176

--- normal mode 15 ---

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
ASP 202 0.80 ALA 1 -0.65 GLN 42

ASP 203 0.66 LEU 2 -0.68 GLN 42

ASP 65 0.48 PRO 3 -0.17 GLU 205

ARG 200 0.24 GLN 4 -0.29 THR 5

GLU 80 0.18 THR 5 -0.29 GLN 4

PRO 3 0.32 VAL 6 -0.28 LEU 206

GLU 80 0.26 ARG 7 -0.23 LEU 206

GLU 80 0.27 ILE 8 -0.21 LEU 206

GLU 80 0.34 GLY 9 -0.13 LEU 206

ARG 77 0.34 THR 10 -0.10 LEU 206

ARG 77 0.41 ASP 11 -0.11 TRP 47

ARG 77 0.32 THR 12 -0.14 TRP 47

LYS 76 0.37 THR 13 -0.10 TRP 47

LYS 76 0.30 TYR 14 -0.07 ASP 21

GLU 167 0.25 ALA 15 -0.16 ASP 21

GLU 167 0.21 PRO 16 -0.18 ASP 21

GLU 167 0.20 PHE 17 -0.13 ASP 21

ARG 77 0.25 SER 18 -0.10 ASP 21

ARG 77 0.26 SER 19 -0.13 ASN 35

GLU 80 0.26 LYS 20 -0.17 ASN 35

ALA 49 0.24 ASP 21 -0.35 LYS 229

ALA 49 0.32 ALA 22 -0.42 LYS 229

ALA 49 0.35 LYS 23 -0.41 LYS 229

ALA 49 0.55 GLY 24 -0.22 LYS 229

ALA 49 0.28 GLU 25 -0.26 ASN 35

ALA 49 0.29 PHE 26 -0.25 ASN 35

GLU 80 0.18 ILE 27 -0.23 ASP 21

ARG 77 0.14 GLY 28 -0.21 ASP 21

GLU 167 0.12 PHE 29 -0.25 LEU 87

GLU 167 0.14 ASP 30 -0.21 LEU 87

ARG 77 0.16 ILE 31 -0.18 PHE 210

TRP 47 0.13 ASP 32 -0.26 LYS 23

GLU 167 0.12 LEU 33 -0.23 LEU 214

ARG 77 0.15 GLY 34 -0.24 PHE 210

ARG 77 0.13 ASN 35 -0.29 LYS 23

ARG 77 0.12 GLU 36 -0.33 LYS 23

TYR 236 0.15 MET 37 -0.33 LEU 2

ARG 77 0.16 CYS 38 -0.41 LEU 2

ARG 77 0.13 LYS 39 -0.43 ALA 1

TYR 236 0.14 ARG 40 -0.55 ALA 1

LEU 199 0.14 MET 41 -0.64 LEU 2

LEU 199 0.12 GLN 42 -0.68 LEU 2

GLU 80 0.14 VAL 43 -0.67 LEU 2

GLU 80 0.17 LYS 44 -0.39 LEU 2

GLU 80 0.18 CYS 45 -0.28 LEU 2

GLU 80 0.22 THR 46 -0.17 LEU 206

GLU 80 0.25 TRP 47 -0.14 LEU 206

GLY 24 0.42 VAL 48 -0.14 LEU 206

GLY 24 0.55 ALA 49 -0.10 LEU 206

GLY 24 0.48 SER 50 -0.08 LEU 206

GLU 80 0.44 ASP 51 -0.05 LEU 206

ARG 77 0.50 PHE 52 -0.07 PHE 17

LYS 76 0.59 ASP 53 -0.06 SER 69

GLU 80 0.60 ALA 54 -0.05 VAL 48

GLU 80 0.62 LEU 55 -0.05 LYS 207

GLU 80 0.89 ILE 56 -0.06 SER 69

GLU 80 0.78 PRO 57 -0.05 VAL 48

GLU 80 0.58 SER 58 -0.08 LYS 207

GLU 80 0.55 LEU 59 -0.09 LYS 207

ALA 1 0.68 LYS 60 -0.05 LYS 207

ALA 1 0.65 ALA 61 -0.10 ASP 203

ALA 1 0.66 LYS 62 -0.18 ASP 203

ALA 1 0.45 LYS 63 -0.16 ASP 203

ALA 1 0.37 ILE 64 -0.19 LEU 206

PRO 3 0.48 ASP 65 -0.26 LEU 206

PRO 3 0.37 ALA 66 -0.22 LYS 207

GLU 80 0.33 ILE 67 -0.13 LYS 207

ARG 77 0.26 ILE 68 -0.10 SER 84

ARG 77 0.31 SER 69 -0.07 PHE 52

ARG 77 0.26 SER 70 -0.08 ALA 89

ARG 77 0.37 LEU 71 -0.05 PHE 29

ARG 77 0.20 SER 72 -0.07 PHE 29

ALA 1 0.22 ILE 73 -0.10 PHE 29

ALA 1 0.25 THR 74 -0.13 GLY 237

ASP 53 0.36 ASP 75 -0.21 ASP 193

ASP 53 0.59 LYS 76 -0.13 LYS 188

ILE 56 0.58 ARG 77 -0.09 LYS 189

ILE 56 0.43 GLN 78 -0.18 ASP 85

ILE 56 0.59 GLN 79 -0.15 THR 215

ILE 56 0.89 GLU 80 -0.08 LYS 201

ALA 1 0.51 ILE 81 -0.07 THR 215

ALA 1 0.39 ALA 82 -0.10 ASP 211

ALA 1 0.23 PHE 83 -0.11 THR 215

PRO 3 0.14 SER 84 -0.19 ASP 30

LYS 207 0.18 ASP 85 -0.18 GLN 78

PRO 3 0.14 LYS 86 -0.17 PHE 29

PRO 3 0.15 LEU 87 -0.25 PHE 29

PRO 3 0.13 TYR 88 -0.21 PHE 29

PRO 3 0.12 ALA 89 -0.19 PHE 29

PRO 3 0.14 ALA 90 -0.12 GLY 237

PRO 3 0.13 ASP 91 -0.24 GLY 237

LYS 76 0.13 SER 92 -0.19 GLY 237

PRO 3 0.12 ARG 93 -0.13 PHE 233

THR 13 0.11 LEU 94 -0.10 PHE 233

LYS 76 0.12 ILE 95 -0.09 PHE 233

THR 13 0.11 ALA 96 -0.06 PHE 233

THR 13 0.11 ALA 97 -0.04 SER 108

TYR 14 0.11 LYS 98 -0.05 ALA 22

TYR 14 0.10 GLY 99 -0.06 LYS 23

THR 13 0.10 SER 100 -0.06 SER 108

PRO 3 0.09 PRO 101 -0.06 SER 108

PRO 3 0.10 ILE 102 -0.05 SER 108

PRO 3 0.10 GLN 103 -0.06 ALA 126

PRO 3 0.11 PRO 104 -0.10 ALA 126

PRO 3 0.11 THR 105 -0.06 ASN 129

ALA 1 0.12 LEU 106 -0.05 ASN 129

PRO 3 0.10 GLU 107 -0.05 PRO 101

PRO 3 0.10 SER 108 -0.06 SER 100

PRO 3 0.11 LEU 109 -0.04 ASN 234

ALA 1 0.11 LYS 110 -0.03 SER 100

ALA 1 0.11 GLY 111 -0.03 ASN 234

ALA 1 0.10 LYS 112 -0.04 ASN 234

ALA 1 0.11 HIS 113 -0.05 GLY 237

LYS 76 0.13 VAL 114 -0.07 GLY 237

LYS 76 0.16 GLY 115 -0.08 GLY 237

LYS 76 0.20 VAL 116 -0.10 GLY 237

LYS 76 0.25 LEU 117 -0.11 GLY 237

LYS 76 0.27 GLN 118 -0.10 GLY 237

LYS 76 0.33 GLY 119 -0.12 GLY 237

LYS 76 0.35 SER 120 -0.14 GLY 237

LYS 76 0.32 THR 121 -0.16 GLY 237

LYS 76 0.23 GLN 122 -0.15 GLY 237

LYS 76 0.22 GLU 123 -0.12 GLY 237

ASP 75 0.21 ALA 124 -0.13 GLY 237

ALA 1 0.19 TYR 125 -0.12 GLY 237

ALA 1 0.16 ALA 126 -0.11 GLY 237

ALA 1 0.18 ASN 127 -0.09 GLY 237

ALA 1 0.20 ASP 128 -0.08 GLY 237

ALA 1 0.18 ASN 129 -0.07 GLY 237

ALA 1 0.16 TRP 130 -0.06 GLY 237

ALA 1 0.16 ARG 131 -0.06 GLY 237

ALA 1 0.18 THR 132 -0.05 GLY 237

ALA 1 0.16 LYS 133 -0.04 GLY 237

ALA 1 0.15 GLY 134 -0.04 GLY 237

ALA 1 0.14 VAL 135 -0.04 GLY 237

ALA 1 0.14 ASP 136 -0.05 GLY 237

ALA 1 0.14 VAL 137 -0.07 GLY 237

LYS 76 0.16 VAL 138 -0.07 GLY 237

LYS 76 0.20 ALA 139 -0.09 GLY 237

LYS 76 0.21 TYR 140 -0.09 GLY 237

LYS 76 0.24 ALA 141 -0.09 GLY 237

LYS 76 0.24 ASN 142 -0.09 GLY 237

LYS 76 0.23 GLN 143 -0.09 GLY 237

LYS 76 0.20 ASP 144 -0.08 ALA 164

LYS 76 0.19 LEU 145 -0.07 GLY 237

LYS 76 0.18 ILE 146 -0.08 GLY 237

LYS 76 0.17 TYR 147 -0.08 ALA 164

LYS 76 0.16 SER 148 -0.07 GLY 168

LYS 76 0.15 ASP 149 -0.06 PHE 233

LYS 76 0.14 LEU 150 -0.06 PHE 233

LYS 76 0.13 THR 151 -0.09 PHE 169

LYS 76 0.13 ALA 152 -0.07 GLY 168

LYS 76 0.11 GLY 153 -0.05 GLY 168

LYS 76 0.13 ARG 154 -0.05 PHE 233

LYS 76 0.13 LEU 155 -0.05 PHE 233

LYS 76 0.11 ASP 156 -0.05 ASN 234

LYS 76 0.12 ALA 157 -0.06 PHE 233

LYS 76 0.15 ALA 158 -0.08 GLY 237

LYS 76 0.16 LEU 159 -0.11 GLY 237

LYS 76 0.20 GLN 160 -0.12 GLY 237

LYS 76 0.22 ASP 161 -0.12 PHE 233

LYS 76 0.14 GLU 162 -0.17 PHE 233

ARG 77 0.18 VAL 163 -0.15 PHE 233

TYR 14 0.25 ALA 164 -0.12 PHE 233

LYS 76 0.20 ALA 165 -0.13 PHE 233

TYR 14 0.19 SER 166 -0.17 PHE 233

ALA 15 0.25 GLU 167 -0.13 PHE 233

TYR 14 0.26 GLY 168 -0.11 PHE 233

LYS 76 0.20 PHE 169 -0.10 PHE 233

TYR 14 0.17 LEU 170 -0.10 PHE 233

ALA 15 0.18 LYS 171 -0.11 PHE 233

LYS 76 0.18 GLN 172 -0.09 PHE 233

LYS 76 0.17 PRO 173 -0.06 PHE 233

LYS 76 0.18 ALA 174 -0.06 PHE 233

LYS 76 0.16 GLY 175 -0.07 PHE 233

LYS 76 0.13 LYS 176 -0.06 ALA 22

LYS 76 0.12 GLU 177 -0.04 ALA 22

THR 13 0.13 TYR 178 -0.05 PHE 233

TYR 14 0.13 ALA 179 -0.06 ALA 22

TYR 14 0.13 PHE 180 -0.07 PHE 233

THR 13 0.10 ALA 181 -0.06 ASN 234

PRO 3 0.10 GLY 182 -0.07 LYS 23

PRO 3 0.11 PRO 183 -0.09 ASN 234

PRO 3 0.12 SER 184 -0.17 GLY 237

PRO 3 0.12 VAL 185 -0.17 GLY 237

PRO 3 0.13 LYS 186 -0.26 GLY 237

ALA 1 0.15 ASP 187 -0.21 GLY 237

ALA 1 0.18 LYS 188 -0.21 GLY 237

ALA 1 0.22 LYS 189 -0.16 GLY 237

ALA 1 0.20 TYR 190 -0.17 GLY 237

ALA 1 0.16 PHE 191 -0.19 GLY 237

ALA 1 0.19 GLY 192 -0.16 GLY 237

PRO 3 0.16 ASP 193 -0.21 ASP 75

PRO 3 0.15 GLY 194 -0.16 PHE 29

PRO 3 0.17 THR 195 -0.14 PHE 29

PRO 3 0.20 GLY 196 -0.13 ASP 30

PRO 3 0.25 VAL 197 -0.14 SER 84

PRO 3 0.31 GLY 198 -0.05 ASP 30

ALA 1 0.44 LEU 199 -0.06 LYS 207

ALA 1 0.71 ARG 200 -0.03 ASP 30

ALA 1 0.61 LYS 201 -0.09 ALA 208

ALA 1 0.80 ASP 202 -0.12 ASP 65

LEU 2 0.66 ASP 203 -0.24 ASP 65

LEU 2 0.26 THR 204 -0.18 ASP 65

ASP 85 0.10 GLU 205 -0.22 VAL 6

LEU 2 0.13 LEU 206 -0.28 VAL 6

ASP 85 0.18 LYS 207 -0.24 ASP 65

ASP 85 0.12 ALA 208 -0.28 ALA 1

GLY 237 0.11 ALA 209 -0.43 ALA 1

ASP 85 0.13 PHE 210 -0.24 GLY 34

GLY 237 0.15 ASP 211 -0.25 ALA 1

GLY 237 0.15 LYS 212 -0.45 ALA 1

GLY 237 0.14 ALA 213 -0.42 ALA 1

GLY 237 0.17 LEU 214 -0.28 ALA 1

GLY 237 0.19 THR 215 -0.33 ALA 1

GLY 237 0.16 GLU 216 -0.41 ALA 1

GLY 237 0.15 LEU 217 -0.34 ALA 1

GLY 237 0.20 ARG 218 -0.28 ALA 1

GLY 237 0.18 GLN 219 -0.33 ALA 1

ASN 234 0.14 ASP 220 -0.35 ALA 1

ASN 234 0.15 GLY 221 -0.30 LYS 23

ASN 234 0.12 THR 222 -0.34 LYS 23

ASN 234 0.16 TYR 223 -0.29 LYS 23

ASN 234 0.18 ASP 224 -0.29 LYS 23

ASN 234 0.09 LYS 225 -0.36 LYS 23

ARG 77 0.08 MET 226 -0.36 LYS 23

ARG 77 0.08 ALA 227 -0.30 LYS 23

ARG 77 0.07 LYS 228 -0.34 ALA 22

ARG 77 0.10 LYS 229 -0.42 ALA 22

ARG 77 0.11 TYR 230 -0.36 ALA 22

ARG 77 0.08 PHE 231 -0.29 ALA 22

ASP 224 0.08 ASP 232 -0.29 ALA 22

ASP 224 0.14 PHE 233 -0.23 ALA 22

ARG 218 0.19 ASN 234 -0.20 ALA 22

ARG 218 0.11 VAL 235 -0.19 LYS 23

ARG 218 0.18 TYR 236 -0.16 LYS 23

ARG 218 0.20 GLY 237 -0.26 LYS 186

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.

*** LAO_open_cutoff8 ***

CA distance fluctuations for 260611150511729176

--- normal mode 15 ---

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

* LAO_open_cutoff8 *