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

* cadenabwt *

CA distance fluctuations for 260812233919701448

--- 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
ARG 58 0.20 PRO 1 -0.04 GLY 5

GLU 197 0.18 GLY 2 -0.04 GLU 157

GLU 197 0.18 SER 3 -0.05 GLY 188

GLU 197 0.16 SER 4 -0.06 ASP 187

GLU 197 0.14 GLY 5 -0.06 ASP 187

GLU 197 0.13 LEU 6 -0.07 ASP 187

GLU 197 0.12 PRO 7 -0.07 ASP 187

GLU 197 0.12 PRO 8 -0.07 ASP 187

GLU 197 0.13 GLU 9 -0.09 ASP 187

SER 149 0.12 LYS 10 -0.09 ASP 187

GLU 197 0.12 PRO 11 -0.09 ASP 187

SER 149 0.14 LYS 12 -0.12 ASP 187

ASP 194 0.16 ASN 13 -0.14 LYS 189

ASP 194 0.13 LEU 14 -0.12 LYS 189

ASP 194 0.12 SER 15 -0.14 LYS 189

ASP 194 0.08 CYS 16 -0.09 LYS 189

PRO 1 0.07 ILE 17 -0.08 GLY 190

PRO 1 0.09 VAL 18 -0.04 PHE 214

PRO 1 0.12 ASN 19 -0.07 TRP 192

ILE 131 0.13 GLU 20 -0.10 VAL 71

ILE 131 0.18 GLY 21 -0.11 SER 69

PRO 1 0.14 LYS 22 -0.11 ASP 194

SER 133 0.12 LYS 23 -0.08 ASP 194

PRO 1 0.09 MET 24 -0.05 PHE 214

PRO 1 0.10 ARG 25 -0.05 LYS 189

PRO 1 0.08 CYS 26 -0.08 LYS 189

GLU 197 0.12 GLU 27 -0.11 LYS 189

GLU 197 0.13 TRP 28 -0.12 LYS 189

GLU 197 0.17 ASP 29 -0.11 GLY 188

GLU 197 0.15 GLY 30 -0.09 GLY 188

GLU 197 0.17 GLY 31 -0.10 ASP 187

GLU 197 0.18 ARG 32 -0.09 ASP 187

GLU 197 0.18 GLU 33 -0.07 GLY 188

GLU 197 0.15 THR 34 -0.06 GLY 188

GLU 197 0.16 HIS 35 -0.05 GLY 188

GLU 197 0.13 LEU 36 -0.05 GLY 188

ASN 109 0.13 GLU 37 -0.05 GLY 188

ASN 109 0.11 THR 38 -0.06 GLY 188

ASN 109 0.09 ASN 39 -0.05 GLY 188

ASN 109 0.09 PHE 40 -0.05 GLY 188

PRO 1 0.07 THR 41 -0.04 LYS 189

PRO 1 0.06 LEU 42 -0.04 LYS 189

PRO 208 0.05 LYS 43 -0.02 PHE 214

PRO 208 0.06 SER 44 -0.03 GLY 21

PRO 212 0.06 GLU 45 -0.05 SER 130

PRO 212 0.07 TRP 46 -0.07 SER 130

PRO 212 0.08 ALA 47 -0.08 SER 130

PRO 212 0.07 THR 48 -0.09 SER 130

PRO 212 0.06 HIS 49 -0.07 SER 130

PRO 212 0.05 LYS 50 -0.05 GLY 21

PRO 1 0.07 PHE 51 -0.05 GLY 21

PRO 1 0.08 ALA 52 -0.05 PHE 214

PRO 1 0.08 ASP 53 -0.04 PHE 214

PRO 1 0.10 CYS 54 -0.05 PHE 214

PRO 1 0.11 LYS 55 -0.06 PHE 214

PRO 1 0.12 ALA 56 -0.06 PHE 214

PRO 1 0.16 LYS 57 -0.07 PHE 214

PRO 1 0.20 ARG 58 -0.07 PHE 214

PRO 1 0.18 ASP 59 -0.08 PHE 214

ASN 109 0.16 THR 60 -0.07 GLY 188

PRO 1 0.13 PRO 61 -0.07 GLY 188

GLU 197 0.13 THR 62 -0.09 GLY 188

HIS 108 0.12 SER 63 -0.08 GLY 188

PRO 1 0.11 CYS 64 -0.06 PHE 214

PRO 1 0.12 THR 65 -0.06 PHE 214

PRO 1 0.11 VAL 66 -0.06 PHE 214

PRO 1 0.12 ASP 67 -0.07 PHE 214

PRO 1 0.10 TYR 68 -0.07 GLY 21

PRO 1 0.10 SER 69 -0.11 GLY 21

PRO 1 0.09 THR 70 -0.10 GLY 21

TYR 68 0.08 VAL 71 -0.12 SER 130

ASP 187 0.09 TYR 72 -0.13 SER 130

ASP 187 0.11 PHE 73 -0.13 SER 130

ASP 187 0.09 VAL 74 -0.11 ASN 75

PRO 212 0.09 ASN 75 -0.11 VAL 74

PRO 212 0.08 ILE 76 -0.07 GLU 77

PRO 212 0.08 GLU 77 -0.08 VAL 74

PRO 212 0.07 VAL 78 -0.05 VAL 74

SER 149 0.07 TRP 79 -0.05 VAL 74

GLU 197 0.07 VAL 80 -0.05 ASP 187

GLU 197 0.07 GLU 81 -0.05 ASP 187

GLU 197 0.09 ALA 82 -0.06 ASP 187

GLU 197 0.08 GLU 83 -0.05 ASP 187

GLU 197 0.09 ASN 84 -0.05 GLY 188

GLU 197 0.09 ALA 85 -0.04 ASP 187

GLU 197 0.10 LEU 86 -0.06 GLY 87

GLU 197 0.09 GLY 87 -0.06 LEU 86

GLU 197 0.08 LYS 88 -0.05 ASP 187

SER 149 0.09 VAL 89 -0.07 PRO 7

SER 149 0.09 THR 90 -0.06 ASP 187

SER 149 0.11 SER 91 -0.08 ASP 187

SER 149 0.12 ASP 92 -0.10 ASN 95

THR 150 0.11 HIS 93 -0.09 ASP 92

THR 150 0.11 ILE 94 -0.12 ASN 95

THR 150 0.10 ASN 95 -0.12 ILE 94

PRO 212 0.09 PHE 96 -0.12 ASP 97

PRO 212 0.09 ASP 97 -0.12 PHE 96

PRO 212 0.08 PRO 98 -0.07 SER 130

PRO 212 0.09 VAL 99 -0.11 VAL 134

GLY 190 0.11 TYR 100 -0.10 SER 15

TYR 191 0.09 LYS 101 -0.08 TYR 100

PRO 208 0.08 VAL 102 -0.04 GLY 190

PRO 1 0.09 LYS 103 -0.06 TRP 192

PRO 1 0.10 PRO 104 -0.06 VAL 71

PRO 1 0.15 ASN 105 -0.08 VAL 71

PRO 1 0.14 PRO 106 -0.08 PHE 214

PRO 1 0.14 PRO 107 -0.09 PRO 129

PRO 1 0.17 HIS 108 -0.10 PHE 214

PRO 1 0.18 ASN 109 -0.11 PHE 214

PRO 1 0.16 LEU 110 -0.11 PHE 214

PRO 1 0.16 SER 111 -0.12 PHE 214

PRO 1 0.14 VAL 112 -0.11 PHE 214

PRO 1 0.14 ILE 113 -0.09 PHE 214

PRO 208 0.13 ASN 114 -0.06 PHE 214

PRO 208 0.19 SER 115 -0.03 GLU 205

PRO 208 0.27 GLU 116 -0.02 GLN 169

PRO 208 0.25 GLU 117 -0.02 SER 120

PRO 208 0.34 LEU 118 -0.04 SER 120

PRO 208 0.18 SER 119 -0.02 LYS 210

PRO 208 0.21 SER 120 -0.04 LEU 118

PRO 208 0.21 ILE 121 -0.02 GLN 169

PRO 208 0.15 LEU 122 -0.04 LYS 210

PRO 208 0.16 LYS 123 -0.03 GLU 205

PRO 208 0.12 LEU 124 -0.04 PHE 214

PRO 1 0.13 THR 125 -0.06 SER 133

PRO 1 0.14 TRP 126 -0.07 SER 133

PRO 1 0.15 THR 127 -0.09 SER 133

PRO 1 0.12 ASN 128 -0.08 LYS 132

PRO 1 0.13 PRO 129 -0.09 GLU 197

GLY 21 0.15 SER 130 -0.13 TYR 72

GLY 21 0.18 ILE 131 -0.11 PHE 73

GLY 21 0.12 LYS 132 -0.09 PHE 73

GLY 21 0.17 SER 133 -0.12 PHE 73

GLY 21 0.13 VAL 134 -0.12 PHE 73

PRO 212 0.11 ILE 135 -0.08 PHE 96

PRO 212 0.13 ILE 136 -0.07 ASN 13

PRO 212 0.12 LEU 137 -0.04 ASN 13

PRO 212 0.13 LYS 138 -0.05 ASN 13

PRO 212 0.11 TYR 139 -0.02 ARG 182

PRO 208 0.10 ASN 140 -0.04 PRO 156

PRO 208 0.10 ILE 141 -0.03 PHE 214

PRO 208 0.08 GLN 142 -0.06 PHE 214

ASN 13 0.08 TYR 143 -0.09 PHE 214

ASN 13 0.10 ARG 144 -0.14 PHE 214

ARG 32 0.11 THR 145 -0.21 PHE 214

ARG 32 0.14 LYS 146 -0.26 PHE 214

ARG 32 0.14 ASP 147 -0.29 PHE 214

ASN 13 0.13 ALA 148 -0.22 PHE 214

ASN 13 0.15 SER 149 -0.20 PHE 214

ASN 13 0.14 THR 150 -0.15 PHE 214

ASN 13 0.11 TRP 151 -0.11 PHE 214

GLY 188 0.09 SER 152 -0.06 PHE 214

PRO 212 0.09 GLN 153 -0.04 ASP 59

PRO 212 0.14 ILE 154 -0.03 ASP 59

PRO 212 0.17 PRO 155 -0.05 ASP 59

PRO 212 0.15 PRO 156 -0.05 THR 60

PRO 212 0.19 GLU 157 -0.08 ASN 13

PRO 212 0.20 ASP 158 -0.05 ASN 13

PRO 212 0.17 THR 159 -0.04 ASN 13

PRO 212 0.16 ALA 160 -0.07 ASN 13

PRO 212 0.16 SER 161 -0.07 ASN 13

PRO 212 0.14 THR 162 -0.07 ARG 163

PRO 212 0.15 ARG 163 -0.07 THR 162

PRO 208 0.13 SER 164 -0.05 ILE 136

PRO 208 0.15 SER 165 -0.04 GLY 201

PRO 208 0.17 PHE 166 -0.03 GLY 201

PRO 208 0.19 THR 167 -0.02 ILE 154

PRO 208 0.18 VAL 168 -0.02 SER 152

PRO 212 0.22 GLN 169 -0.02 GLU 116

PRO 212 0.23 ASP 170 -0.03 LEU 118

PRO 208 0.12 LEU 171 -0.03 LYS 210

PRO 1 0.06 LYS 172 -0.10 LYS 210

PRO 1 0.08 PRO 173 -0.18 LYS 210

GLY 2 0.10 PHE 174 -0.30 LYS 210

GLY 2 0.10 THR 175 -0.27 PHE 214

GLY 2 0.12 GLU 176 -0.26 PHE 214

GLY 2 0.11 TYR 177 -0.19 PHE 214

ARG 32 0.13 VAL 178 -0.17 PHE 214

PRO 1 0.11 PHE 179 -0.12 PHE 214

PRO 1 0.12 ARG 180 -0.10 PHE 214

PRO 1 0.10 ILE 181 -0.06 PHE 214

PRO 1 0.09 ARG 182 -0.05 PHE 214

PRO 208 0.09 CYS 183 -0.02 PHE 214

PRO 208 0.09 MET 184 -0.03 TYR 191

PRO 212 0.11 LYS 185 -0.07 ASN 13

PRO 212 0.14 GLU 186 -0.09 ASN 13

PRO 212 0.14 ASP 187 -0.14 ASN 13

PRO 212 0.13 GLY 188 -0.13 ASN 13

PRO 212 0.11 LYS 189 -0.14 ASN 13

TYR 100 0.11 GLY 190 -0.08 ILE 17

LYS 101 0.09 TYR 191 -0.06 GLY 188

TRP 195 0.09 TRP 192 -0.07 ASN 19

ASN 13 0.10 SER 193 -0.08 LYS 22

ASN 13 0.16 ASP 194 -0.11 LYS 22

ASN 13 0.15 TRP 195 -0.10 PHE 214

PRO 1 0.15 SER 196 -0.10 PHE 214

GLU 33 0.18 GLU 197 -0.14 PHE 214

ARG 32 0.16 GLU 198 -0.16 PHE 214

PRO 1 0.16 ALA 199 -0.16 PHE 214

GLY 2 0.15 SER 200 -0.19 PHE 214

PRO 1 0.14 GLY 201 -0.18 PHE 214

GLY 2 0.12 ILE 202 -0.22 PHE 214

PRO 1 0.10 THR 203 -0.15 PHE 214

PRO 1 0.10 TYR 204 -0.16 LYS 210

GLY 2 0.09 GLU 205 -0.22 LYS 210

LEU 118 0.10 ASP 206 -0.10 LYS 210

LEU 118 0.20 ARG 207 -0.08 PHE 174

LEU 118 0.34 PRO 208 -0.06 PHE 174

LEU 118 0.20 SER 209 -0.15 PHE 174

LEU 118 0.09 LYS 210 -0.30 PHE 174

LEU 118 0.20 GLU 211 -0.18 PHE 174

LEU 118 0.23 PRO 212 -0.15 ASP 147

ASP 170 0.12 SER 213 -0.27 ASP 147

GLU 116 0.10 PHE 214 -0.29 ASP 147

GLU 116 0.19 TRP 215 -0.21 ASP 147

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.

*** cadenabwt ***

CA distance fluctuations for 260812233919701448

--- 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.

* cadenabwt *