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

* *

CA distance fluctuations for 2604241152241960399

--- normal mode 9 ---

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
GLN 42 0.32 ALA 1 -0.25 ASP 202

ALA 1 0.08 LEU 2 -0.08 GLY 24

THR 132 0.08 PRO 3 -0.12 GLY 24

THR 132 0.08 GLN 4 -0.11 GLY 24

THR 132 0.08 THR 5 -0.14 GLY 24

THR 132 0.08 VAL 6 -0.13 GLY 24

THR 132 0.10 ARG 7 -0.15 GLY 24

ASN 127 0.08 ILE 8 -0.14 GLY 24

ASN 127 0.10 GLY 9 -0.14 GLY 24

ASN 127 0.09 THR 10 -0.10 GLY 24

TYR 140 0.11 ASP 11 -0.09 PRO 173

TYR 140 0.11 THR 12 -0.12 GLN 172

SER 19 0.11 THR 13 -0.12 PRO 173

LEU 117 0.06 TYR 14 -0.08 GLN 172

PRO 16 0.11 ALA 15 -0.11 GLN 172

VAL 235 0.13 PRO 16 -0.10 LYS 171

TYR 236 0.10 PHE 17 -0.11 GLU 162

THR 13 0.08 SER 18 -0.10 THR 46

THR 13 0.11 SER 19 -0.12 GLN 172

ASP 144 0.12 LYS 20 -0.12 GLN 172

LYS 229 0.17 ASP 21 -0.11 THR 46

LYS 229 0.26 ALA 22 -0.15 VAL 48

LYS 229 0.20 LYS 23 -0.15 VAL 48

LYS 229 0.12 GLY 24 -0.22 VAL 48

TYR 140 0.11 GLU 25 -0.13 THR 46

TYR 140 0.10 PHE 26 -0.14 THR 46

MET 226 0.14 ILE 27 -0.14 THR 46

MET 226 0.12 GLY 28 -0.11 LYS 171

ALA 22 0.12 PHE 29 -0.15 PRO 183

ASP 224 0.06 ASP 30 -0.11 GLU 162

THR 222 0.08 ILE 31 -0.11 THR 46

ALA 22 0.13 ASP 32 -0.14 PRO 183

ALA 22 0.10 LEU 33 -0.14 PRO 183

ALA 49 0.07 GLY 34 -0.11 PRO 183

ALA 49 0.10 ASN 35 -0.11 PRO 183

ALA 1 0.14 GLU 36 -0.14 PRO 183

ALA 1 0.16 MET 37 -0.12 PRO 183

ALA 1 0.16 CYS 38 -0.10 PRO 183

ALA 1 0.20 LYS 39 -0.11 PRO 183

ALA 1 0.26 ARG 40 -0.12 PRO 183

ALA 1 0.31 MET 41 -0.09 PRO 183

ALA 1 0.32 GLN 42 -0.09 PRO 183

ALA 1 0.24 VAL 43 -0.08 PRO 183

ALA 1 0.12 LYS 44 -0.10 GLY 24

TYR 140 0.06 CYS 45 -0.12 GLY 24

THR 132 0.08 THR 46 -0.19 GLY 24

ASN 35 0.09 TRP 47 -0.18 GLY 24

THR 132 0.11 VAL 48 -0.22 GLY 24

TYR 140 0.12 ALA 49 -0.14 GLY 24

THR 132 0.13 SER 50 -0.14 ALA 22

THR 132 0.13 ASP 51 -0.10 ALA 22

ASN 127 0.13 PHE 52 -0.07 ARG 77

ASN 127 0.18 ASP 53 -0.14 ARG 77

THR 132 0.17 ALA 54 -0.10 ALA 22

ASN 127 0.16 LEU 55 -0.09 ALA 1

ASN 127 0.17 ILE 56 -0.11 ALA 1

ASP 128 0.23 PRO 57 -0.13 ALA 1

THR 132 0.18 SER 58 -0.13 ALA 1

ASP 128 0.15 LEU 59 -0.15 ALA 1

ASP 128 0.18 LYS 60 -0.18 ALA 1

THR 132 0.19 ALA 61 -0.19 ALA 1

THR 132 0.15 LYS 62 -0.22 ALA 1

THR 132 0.16 LYS 63 -0.17 ALA 1

THR 132 0.13 ILE 64 -0.15 ALA 1

ASN 127 0.10 ASP 65 -0.16 ALA 1

ASN 127 0.08 ALA 66 -0.10 GLY 24

ASN 127 0.08 ILE 67 -0.09 GLY 24

ASN 127 0.05 ILE 68 -0.06 GLY 24

SER 120 0.06 SER 69 -0.06 GLU 162

PRO 16 0.06 SER 70 -0.07 ASP 91

PRO 16 0.05 LEU 71 -0.10 ASP 53

PRO 16 0.06 SER 72 -0.11 GLY 119

SER 166 0.05 ILE 73 -0.10 GLY 119

SER 166 0.06 THR 74 -0.10 GLY 119

LYS 188 0.07 ASP 75 -0.12 GLY 119

LYS 189 0.11 LYS 76 -0.14 GLY 119

THR 105 0.09 ARG 77 -0.14 ASP 53

THR 105 0.07 GLN 78 -0.11 ASP 53

THR 105 0.09 GLN 79 -0.12 ASP 53

ASP 128 0.11 GLU 80 -0.11 ASP 53

THR 105 0.08 ILE 81 -0.11 ALA 1

THR 105 0.05 ALA 82 -0.09 ALA 1

PRO 16 0.03 PHE 83 -0.07 ASP 53

PHE 29 0.04 SER 84 -0.06 ASP 193

PHE 29 0.06 ASP 85 -0.11 ASP 193

PRO 16 0.06 LYS 86 -0.15 GLN 219

PRO 16 0.07 LEU 87 -0.12 PRO 183

PRO 16 0.10 TYR 88 -0.17 ARG 218

GLU 167 0.10 ALA 89 -0.18 ASN 129

VAL 163 0.10 ALA 90 -0.18 ASP 91

LYS 171 0.10 ASP 91 -0.26 PHE 233

TYR 190 0.09 SER 92 -0.26 PHE 233

TYR 190 0.09 ARG 93 -0.31 PHE 233

TYR 190 0.09 LEU 94 -0.28 PHE 233

TYR 190 0.07 ILE 95 -0.24 PHE 233

TYR 190 0.05 ALA 96 -0.21 PHE 233

PRO 183 0.05 ALA 97 -0.17 PHE 233

PRO 183 0.07 LYS 98 -0.20 PHE 233

PRO 183 0.07 GLY 99 -0.22 PHE 233

TYR 190 0.05 SER 100 -0.23 PHE 233

PRO 57 0.07 PRO 101 -0.26 PHE 233

PRO 57 0.09 ILE 102 -0.26 PHE 233

TYR 125 0.11 GLN 103 -0.31 PHE 233

TYR 125 0.15 PRO 104 -0.30 PHE 233

TYR 125 0.17 THR 105 -0.28 PHE 233

PRO 57 0.14 LEU 106 -0.25 PHE 233

PRO 57 0.13 GLU 107 -0.24 PHE 233

PRO 57 0.11 SER 108 -0.25 PHE 233

PRO 57 0.11 LEU 109 -0.24 PHE 233

PRO 57 0.12 LYS 110 -0.22 PHE 233

PRO 57 0.11 GLY 111 -0.18 PHE 233

PRO 57 0.09 LYS 112 -0.19 PHE 233

PRO 57 0.09 HIS 113 -0.16 PHE 233

THR 105 0.09 VAL 114 -0.17 PHE 233

THR 105 0.09 GLY 115 -0.14 PHE 233

THR 105 0.11 VAL 116 -0.13 PHE 233

THR 105 0.09 LEU 117 -0.10 PHE 233

ASN 127 0.17 GLN 118 -0.10 LYS 76

ASN 127 0.20 GLY 119 -0.14 LYS 76

ILE 56 0.12 SER 120 -0.10 PHE 233

PRO 57 0.13 THR 121 -0.13 PHE 233

PRO 104 0.12 GLN 122 -0.17 PHE 233

PRO 57 0.15 GLU 123 -0.13 PHE 233

PRO 57 0.19 ALA 124 -0.13 PHE 233

THR 105 0.17 TYR 125 -0.19 PHE 233

THR 105 0.16 ALA 126 -0.20 PHE 233

PRO 57 0.22 ASN 127 -0.16 PHE 233

PRO 57 0.23 ASP 128 -0.22 LYS 188

PRO 57 0.17 ASN 129 -0.30 LYS 186

PRO 57 0.17 TRP 130 -0.23 PHE 233

PRO 57 0.19 ARG 131 -0.18 PHE 233

PRO 57 0.21 THR 132 -0.19 LYS 186

PRO 57 0.17 LYS 133 -0.21 PHE 233

PRO 57 0.16 GLY 134 -0.19 PHE 233

PRO 57 0.14 VAL 135 -0.20 PHE 233

PRO 57 0.13 ASP 136 -0.16 PHE 233

PRO 57 0.14 VAL 137 -0.15 PHE 233

ALA 141 0.13 VAL 138 -0.12 PHE 233

ASP 53 0.14 ALA 139 -0.11 PHE 233

ALA 141 0.15 TYR 140 -0.08 LYS 76

TYR 140 0.15 ALA 141 -0.10 LYS 76

TYR 140 0.14 ASN 142 -0.08 LYS 76

SER 19 0.09 GLN 143 -0.08 PHE 233

LYS 20 0.12 ASP 144 -0.10 PRO 173

GLY 24 0.12 LEU 145 -0.08 PRO 173

GLY 24 0.09 ILE 146 -0.08 PHE 233

GLY 24 0.08 TYR 147 -0.07 PHE 233

GLY 24 0.12 SER 148 -0.06 LEU 145

GLY 24 0.11 ASP 149 -0.07 PHE 233

GLY 24 0.08 LEU 150 -0.10 PHE 233

GLY 24 0.07 THR 151 -0.07 PHE 233

GLY 24 0.10 ALA 152 -0.06 PHE 233

GLY 24 0.08 GLY 153 -0.10 PHE 233

GLY 24 0.10 ARG 154 -0.10 PHE 233

GLY 24 0.08 LEU 155 -0.13 PHE 233

PRO 101 0.07 ASP 156 -0.17 PHE 233

PRO 57 0.06 ALA 157 -0.20 PHE 233

PRO 57 0.06 ALA 158 -0.18 PHE 233

PRO 57 0.08 LEU 159 -0.21 PHE 233

TYR 190 0.07 GLN 160 -0.18 PHE 233

TYR 190 0.08 ASP 161 -0.20 PHE 233

LYS 171 0.10 GLU 162 -0.31 PHE 233

ALA 90 0.10 VAL 163 -0.23 PHE 233

ASP 193 0.06 ALA 164 -0.14 PHE 233

TYR 190 0.07 ALA 165 -0.17 PHE 233

GLU 162 0.10 SER 166 -0.21 ASP 232

GLY 237 0.11 GLU 167 -0.16 SER 166

VAL 235 0.08 GLY 168 -0.08 LEU 170

GLY 237 0.06 PHE 169 -0.07 THR 46

GLU 162 0.10 LEU 170 -0.11 ASP 232

GLY 237 0.12 LYS 171 -0.11 GLY 28

GLY 237 0.10 GLN 172 -0.12 SER 19

GLY 237 0.09 PRO 173 -0.12 THR 13

GLY 237 0.06 ALA 174 -0.09 THR 13

GLU 162 0.06 GLY 175 -0.07 THR 46

SER 184 0.08 LYS 176 -0.08 THR 46

PRO 183 0.07 GLU 177 -0.10 ASP 232

SER 184 0.06 TYR 178 -0.15 PHE 233

PHE 180 0.10 ALA 179 -0.23 PHE 233

ALA 179 0.10 PHE 180 -0.33 PHE 233

TYR 190 0.09 ALA 181 -0.33 PHE 233

TYR 190 0.10 GLY 182 -0.41 PHE 233

LYS 189 0.09 PRO 183 -0.47 PHE 233

ALA 179 0.09 SER 184 -0.41 PHE 233

TYR 190 0.11 VAL 185 -0.32 PHE 233

PRO 183 0.09 LYS 186 -0.30 ASN 129

LYS 189 0.14 ASP 187 -0.27 ASN 129

LYS 76 0.08 LYS 188 -0.23 ASN 129

ASP 187 0.14 LYS 189 -0.20 ASP 128

PRO 104 0.12 TYR 190 -0.19 ASP 128

PRO 57 0.09 PHE 191 -0.18 ASN 129

SER 166 0.08 GLY 192 -0.14 GLN 219

LYS 171 0.09 ASP 193 -0.18 GLN 219

GLU 167 0.08 GLY 194 -0.16 ASN 129

PRO 16 0.06 THR 195 -0.11 GLN 219

PRO 16 0.05 GLY 196 -0.08 GLN 219

ALA 124 0.03 VAL 197 -0.05 GLY 24

ALA 124 0.06 GLY 198 -0.07 ALA 1

ASN 127 0.07 LEU 199 -0.12 ALA 1

ASP 128 0.09 ARG 200 -0.18 ALA 1

ASP 128 0.06 LYS 201 -0.16 ALA 1

ASP 128 0.07 ASP 202 -0.25 ALA 1

ASN 127 0.06 ASP 203 -0.25 ALA 1

ASN 127 0.04 THR 204 -0.12 ALA 1

ASN 127 0.04 GLU 205 -0.06 GLY 24

ASN 127 0.04 LEU 206 -0.07 GLY 24

ALA 124 0.03 LYS 207 -0.05 GLY 24

ALA 1 0.12 ALA 208 -0.05 PRO 183

ALA 1 0.23 ALA 209 -0.07 PRO 183

ALA 1 0.13 PHE 210 -0.08 PRO 183

ALA 1 0.11 ASP 211 -0.08 PRO 183

ALA 1 0.20 LYS 212 -0.10 PRO 183

ALA 1 0.21 ALA 213 -0.12 PRO 183

ALA 1 0.13 LEU 214 -0.13 PRO 183

ALA 1 0.16 THR 215 -0.15 PRO 183

ALA 1 0.20 GLU 216 -0.15 PRO 183

ALA 1 0.17 LEU 217 -0.17 PRO 183

ALA 1 0.14 ARG 218 -0.21 PRO 183

ALA 1 0.16 GLN 219 -0.22 PRO 183

ALA 1 0.18 ASP 220 -0.21 PRO 183

ALA 22 0.17 GLY 221 -0.24 PRO 183

ALA 22 0.18 THR 222 -0.19 PRO 183

ALA 22 0.14 TYR 223 -0.20 PRO 183

ALA 22 0.17 ASP 224 -0.24 PRO 183

ALA 22 0.22 LYS 225 -0.22 PRO 183

ALA 22 0.22 MET 226 -0.20 PRO 183

ALA 22 0.18 ALA 227 -0.23 PRO 183

ALA 22 0.22 LYS 228 -0.26 PRO 183

ALA 22 0.26 LYS 229 -0.21 PRO 183

ALA 22 0.22 TYR 230 -0.22 PRO 183

ALA 22 0.17 PHE 231 -0.28 PRO 183

ALA 22 0.16 ASP 232 -0.37 PRO 183

ALA 22 0.12 PHE 233 -0.47 PRO 183

ALA 22 0.13 ASN 234 -0.37 PRO 183

PRO 16 0.13 VAL 235 -0.28 PRO 183

PRO 16 0.12 TYR 236 -0.23 PRO 183

LYS 171 0.12 GLY 237 -0.25 PRO 183

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.

*** ***

CA distance fluctuations for 2604241152241960399

--- normal mode 9 ---

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

* *