Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
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CA distance fluctuations for 2605111359451716543

--- normal mode 8 ---

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
ASN 212 0.59 ALA 1 -0.11 LYS 107

ASN 212 0.53 SER 2 -0.14 LYS 107

ASN 212 0.54 LYS 3 -0.13 LYS 126

ASN 212 0.56 GLY 4 -0.13 LYS 126

ASN 212 0.61 GLU 5 -0.10 ASP 76

ASN 212 0.68 GLU 6 -0.10 ASP 76

ASN 212 0.69 LEU 7 -0.08 PRO 75

ASN 212 0.72 PHE 8 -0.13 THR 9

ASN 212 0.77 THR 9 -0.13 PHE 8

ASN 212 0.90 GLY 10 -0.16 ASP 117

ASN 212 0.94 VAL 11 -0.09 ASP 117

ASN 212 0.84 VAL 12 -0.10 LEU 119

ASN 212 0.82 PRO 13 -0.08 LYS 41

ASN 212 0.63 ILE 14 -0.11 GLU 34

ASN 212 0.50 LEU 15 -0.10 GLU 34

ASN 212 0.34 VAL 16 -0.06 GLU 34

ASN 212 0.23 GLU 17 -0.09 VAL 29

ASN 212 0.12 LEU 18 -0.16 GLU 111

LYS 126 0.11 ASP 19 -0.22 GLU 111

GLY 127 0.12 GLY 20 -0.29 GLU 124

VAL 29 0.11 ASP 21 -0.32 LYS 158

GLY 33 0.10 VAL 22 -0.32 LYS 158

GLY 33 0.09 ASN 23 -0.35 GLN 157

GLY 33 0.09 GLY 24 -0.34 LYS 158

GLY 33 0.11 HIS 25 -0.29 LYS 158

GLY 33 0.11 LYS 26 -0.27 LYS 158

GLY 33 0.13 PHE 27 -0.23 LYS 214

VAL 29 0.16 SER 28 -0.17 GLU 111

SER 28 0.16 VAL 29 -0.11 LYS 214

ASN 212 0.23 SER 30 -0.06 GLU 142

ASN 212 0.35 GLY 31 -0.08 LEU 220

ASN 212 0.56 GLU 32 -0.13 LEU 44

ASN 212 0.74 GLY 33 -0.14 THR 43

ASN 212 0.83 GLU 34 -0.11 ILE 14

ASN 212 0.73 GLY 35 -0.10 LYS 41

ASN 212 0.76 ASP 36 -0.09 ASP 117

ASN 212 0.65 ALA 37 -0.10 PHE 71

ASN 212 0.68 THR 38 -0.10 ASP 117

ASN 212 0.66 TYR 39 -0.10 SER 202

ASN 212 0.56 GLY 40 -0.11 VAL 224

ASP 210 0.59 LYS 41 -0.10 PHE 223

ASP 210 0.63 LEU 42 -0.10 GLU 34

ASP 210 0.72 THR 43 -0.14 GLY 33

LYS 45 0.66 LEU 44 -0.13 GLU 32

GLY 33 0.68 LYS 45 -0.22 VAL 219

GLY 33 0.34 PHE 46 -0.09 SER 208

GLY 33 0.33 ILE 47 -0.10 GLU 172

GLY 33 0.21 CYS 48 -0.19 LYS 214

GLY 33 0.18 THR 49 -0.13 LYS 214

GLY 33 0.15 THR 50 -0.23 LYS 214

GLY 33 0.19 GLY 51 -0.35 LYS 214

GLY 33 0.21 LYS 52 -0.44 LYS 214

GLY 33 0.17 LEU 53 -0.37 LYS 214

GLY 33 0.14 PRO 54 -0.37 LYS 214

LEU 221 0.12 VAL 55 -0.38 PRO 211

ALA 206 0.15 PRO 56 -0.44 PRO 211

LEU 221 0.17 TRP 57 -0.30 PRO 211

LEU 221 0.14 PRO 58 -0.27 PRO 211

SER 205 0.09 THR 59 -0.26 PRO 211

VAL 61 0.10 LEU 60 -0.16 GLN 183

LEU 60 0.10 VAL 61 -0.09 GLN 183

ASP 210 0.11 THR 62 -0.10 GLN 183

ASP 210 0.10 THR 63 -0.12 GLN 94

ASN 212 0.19 PHE 64 -0.05 GLN 157

ASN 212 0.26 SER 65 -0.05 GLU 34

ASN 212 0.20 TYR 66 -0.07 GLY 40

ASN 212 0.25 GLY 67 -0.09 THR 63

ASN 212 0.38 VAL 68 -0.08 GLY 40

ASN 212 0.38 GLN 69 -0.09 GLY 40

ASN 212 0.47 CYS 70 -0.10 THR 108

ASN 212 0.54 PHE 71 -0.10 ALA 37

ASN 212 0.47 SER 72 -0.07 GLN 183

ASN 212 0.53 ARG 73 -0.10 THR 9

ASN 212 0.47 TYR 74 -0.09 THR 97

ASN 212 0.48 PRO 75 -0.09 THR 9

ASN 212 0.51 ASP 76 -0.10 GLU 5

ASN 212 0.44 HIS 77 -0.11 THR 97

ASN 212 0.41 MET 78 -0.13 THR 97

ASN 212 0.47 LYS 79 -0.13 THR 97

ASN 212 0.42 ARG 80 -0.16 THR 97

ASN 212 0.37 HIS 81 -0.17 THR 97

ASN 212 0.41 ASP 82 -0.16 LYS 107

ASN 212 0.37 PHE 83 -0.19 LYS 107

ASN 212 0.41 PHE 84 -0.16 LYS 107

ASN 212 0.50 LYS 85 -0.14 LYS 107

ASN 212 0.45 SER 86 -0.17 LYS 126

ASN 212 0.41 ALA 87 -0.19 LYS 126

ASN 212 0.49 MET 88 -0.15 LYS 126

ASN 212 0.52 PRO 89 -0.13 LYS 126

ASN 212 0.42 GLU 90 -0.19 LYS 126

ASN 212 0.39 GLY 91 -0.18 LYS 126

ASN 212 0.31 TYR 92 -0.24 LYS 126

ASN 212 0.22 VAL 93 -0.28 LYS 126

ASN 212 0.18 GLN 94 -0.27 THR 108

ASN 212 0.10 GLU 95 -0.37 LYS 107

TYR 182 0.10 ARG 96 -0.32 TYR 106

THR 108 0.12 THR 97 -0.38 GLN 184

GLU 124 0.09 ILE 98 -0.28 GLN 183

ALA 179 0.09 PHE 99 -0.31 GLN 157

ARG 168 0.07 PHE 100 -0.29 PRO 211

ILE 128 0.06 LYS 101 -0.30 PRO 211

ARG 168 0.06 ASP 102 -0.33 PRO 211

ARG 168 0.08 ASP 103 -0.32 PRO 211

GLY 20 0.08 GLY 104 -0.35 GLN 157

GLY 20 0.07 ASN 105 -0.36 GLN 157

LEU 18 0.09 TYR 106 -0.34 LYS 158

GLU 124 0.12 LYS 107 -0.40 LYS 158

THR 97 0.12 THR 108 -0.35 GLU 95

ASN 212 0.10 ARG 109 -0.36 LEU 125

ASN 212 0.18 ALA 110 -0.23 LEU 125

ASN 212 0.26 GLU 111 -0.23 ILE 123

ASN 212 0.35 VAL 112 -0.14 ILE 123

ASN 212 0.43 LYS 113 -0.13 GLU 124

ASN 212 0.54 PHE 114 -0.09 GLY 10

ASN 212 0.52 GLU 115 -0.10 GLY 10

ASN 212 0.61 GLY 116 -0.13 GLY 10

ASN 212 0.72 ASP 117 -0.16 GLY 10

ASN 212 0.69 THR 118 -0.10 VAL 12

ASN 212 0.58 LEU 119 -0.10 VAL 12

ASN 212 0.46 VAL 120 -0.07 VAL 12

ASN 212 0.33 ASN 121 -0.08 VAL 12

ASN 212 0.24 ARG 122 -0.16 LEU 18

ASN 212 0.15 ILE 123 -0.23 GLU 111

LYS 107 0.12 GLU 124 -0.29 GLY 20

LEU 18 0.11 LEU 125 -0.36 ARG 109

ASP 19 0.11 LYS 126 -0.38 LYS 158

GLY 20 0.12 GLY 127 -0.36 LYS 158

GLY 20 0.09 ILE 128 -0.39 GLN 157

TYR 145 0.07 ASP 129 -0.39 GLN 157

TYR 145 0.10 PHE 130 -0.32 GLN 157

TYR 145 0.10 LYS 131 -0.37 PRO 211

TYR 145 0.10 GLU 132 -0.43 PRO 211

TYR 145 0.11 ASP 133 -0.48 PRO 211

TYR 145 0.11 GLY 134 -0.45 PRO 211

TYR 145 0.13 ASN 135 -0.48 PRO 211

TYR 145 0.14 ILE 136 -0.44 PRO 211

TYR 145 0.12 LEU 137 -0.45 PRO 211

TYR 145 0.13 GLY 138 -0.55 PRO 211

ALA 206 0.15 HIS 139 -0.60 PRO 211

TYR 145 0.15 LYS 140 -0.62 PRO 211

TYR 145 0.17 LEU 141 -0.56 PRO 211

GLN 204 0.19 GLU 142 -0.60 PRO 211

ALA 206 0.17 TYR 143 -0.47 PRO 211

ALA 206 0.24 ASN 144 -0.30 PRO 211

GLN 204 0.18 TYR 145 -0.19 PRO 211

SER 147 0.19 ASN 146 -0.13 PRO 211

ASN 146 0.19 SER 147 -0.05 GLU 32

GLY 174 0.13 HIS 148 -0.05 PHE 165

GLY 174 0.13 ASN 149 -0.09 GLY 40

ASP 210 0.14 VAL 150 -0.09 PHE 165

ASN 212 0.14 TYR 151 -0.13 ASN 164

ASN 212 0.19 ILE 152 -0.20 TYR 182

ASN 212 0.19 MET 153 -0.24 THR 97

ASN 212 0.22 ALA 154 -0.27 THR 97

ASN 212 0.17 ASP 155 -0.36 THR 97

ASN 212 0.20 LYS 156 -0.31 ASP 129

ASN 212 0.15 GLN 157 -0.39 ASP 129

ASN 212 0.17 LYS 158 -0.40 LYS 107

ASN 212 0.24 ASN 159 -0.32 LYS 107

ASN 212 0.23 GLY 160 -0.33 LYS 107

ASN 212 0.21 ILE 161 -0.30 THR 97

ASN 212 0.14 LYS 162 -0.37 TYR 182

ASN 212 0.13 VAL 163 -0.20 TYR 182

GLU 95 0.07 ASN 164 -0.16 ASP 180

ALA 110 0.05 PHE 165 -0.12 TYR 151

ALA 110 0.05 LYS 166 -0.16 PRO 211

ASN 149 0.07 ILE 167 -0.18 PRO 211

GLN 177 0.11 ARG 168 -0.26 PRO 211

SER 147 0.15 HIS 169 -0.34 PRO 211

SER 147 0.18 ASN 170 -0.43 PRO 211

SER 147 0.17 ILE 171 -0.54 PRO 211

GLN 204 0.17 GLU 172 -0.67 PRO 211

SER 147 0.16 ASP 173 -0.62 PRO 211

SER 147 0.19 GLY 174 -0.53 PRO 211

SER 147 0.15 SER 175 -0.46 PRO 211

SER 147 0.14 VAL 176 -0.40 PRO 211

ARG 168 0.11 GLN 177 -0.38 PRO 211

ARG 168 0.08 LEU 178 -0.29 PRO 211

PHE 99 0.09 ALA 179 -0.25 PRO 211

GLU 124 0.07 ASP 180 -0.20 GLN 157

ALA 110 0.08 HIS 181 -0.22 LYS 162

ARG 96 0.10 TYR 182 -0.37 LYS 162

GLU 95 0.08 GLN 183 -0.35 THR 97

ASN 212 0.13 GLN 184 -0.38 THR 97

ASN 212 0.20 ASN 185 -0.31 LYS 107

ASN 212 0.23 THR 186 -0.31 LYS 126

ASN 212 0.30 PRO 187 -0.28 LYS 126

ASN 212 0.29 ILE 188 -0.29 LYS 126

ASN 212 0.34 GLY 189 -0.26 LYS 126

ASN 212 0.33 ASP 190 -0.27 LYS 126

ASN 212 0.38 GLY 191 -0.24 LYS 126

ASN 212 0.36 PRO 192 -0.25 LYS 126

ASN 212 0.37 VAL 193 -0.23 LYS 126

ASN 212 0.37 LEU 194 -0.21 LYS 107

ASN 212 0.30 LEU 195 -0.23 LYS 107

ASN 212 0.30 PRO 196 -0.21 THR 97

ASN 212 0.26 ASP 197 -0.20 THR 97

ASN 212 0.21 ASN 198 -0.20 TYR 182

ASN 212 0.23 HIS 199 -0.14 TYR 182

ASN 212 0.22 TYR 200 -0.11 TYR 182

ASN 212 0.26 LEU 201 -0.09 GLY 40

ASP 210 0.24 SER 202 -0.10 GLY 40

ASP 210 0.23 THR 203 -0.07 LYS 41

ASP 210 0.23 GLN 204 -0.06 GLY 33

THR 225 0.22 SER 205 -0.08 GLU 32

ASN 144 0.24 ALA 206 -0.09 GLU 32

LEU 221 0.27 LEU 207 -0.15 LYS 45

LEU 221 0.30 SER 208 -0.18 LYS 45

THR 43 0.45 LYS 209 -0.37 GLU 142

GLU 34 0.73 ASP 210 -0.30 GLU 172

VAL 11 0.80 PRO 211 -0.67 GLU 172

VAL 11 0.94 ASN 212 -0.49 GLU 172

VAL 11 0.66 GLU 213 -0.35 GLU 172

VAL 11 0.48 LYS 214 -0.46 HIS 139

GLY 33 0.35 ARG 215 -0.30 LYS 214

GLY 33 0.31 ASP 216 -0.33 LYS 214

GLY 33 0.31 HIS 217 -0.17 GLU 142

VAL 219 0.32 MET 218 -0.15 GLU 142

ASP 210 0.37 VAL 219 -0.22 LYS 45

LEU 42 0.32 LEU 220 -0.10 GLU 32

ASP 210 0.52 LEU 221 -0.09 GLU 32

ASP 210 0.40 GLU 222 -0.09 GLY 33

ASP 210 0.44 PHE 223 -0.10 LYS 41

ASP 210 0.37 VAL 224 -0.11 GLY 40

ASN 212 0.39 THR 225 -0.10 TYR 39

ASN 212 0.35 ALA 226 -0.09 TYR 182

ASN 212 0.30 ALA 227 -0.08 THR 9

ASN 212 0.25 GLY 228 -0.09 TYR 182

ASN 212 0.29 ILE 229 -0.12 TYR 182

ASN 212 0.32 THR 230 -0.10 THR 97

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.

*** prova ***

CA distance fluctuations for 2605111359451716543

--- normal mode 8 ---

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

* prova *