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

* TPP_E.coli_OtsB *

CA distance fluctuations for 261012193747778604

--- normal mode 7 ---

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 265 0.07 MET 1 -0.03 GLN 249

SER 265 0.07 THR 2 -0.03 GLN 249

SER 265 0.05 GLU 3 -0.04 SER 256

ASP 258 0.02 PRO 4 -0.07 SER 256

ASP 258 0.04 LEU 5 -0.06 SER 256

PRO 9 0.01 THR 6 -0.10 SER 256

PRO 9 0.01 GLU 7 -0.09 SER 256

ASP 258 0.05 THR 8 -0.06 SER 256

SER 261 0.11 PRO 9 -0.02 GLN 249

SER 261 0.15 GLU 10 -0.03 ALA 51

SER 261 0.18 LEU 11 -0.03 ALA 51

SER 261 0.28 SER 12 -0.06 ALA 51

SER 261 0.30 ALA 13 -0.04 ALA 51

SER 261 0.37 LYS 14 -0.02 ALA 51

SER 261 0.30 TYR 15 -0.01 ALA 51

SER 265 0.30 ALA 16 -0.01 GLN 135

SER 265 0.24 TRP 17 -0.01 GLN 135

SER 265 0.23 PHE 18 -0.01 ARG 134

SER 265 0.18 PHE 19 -0.02 THR 245

SER 265 0.16 ASP 20 -0.02 ARG 134

SER 265 0.13 LEU 21 -0.03 ARG 134

SER 265 0.11 ASP 22 -0.04 HIS 132

ASP 258 0.08 GLY 23 -0.05 ARG 134

ASP 258 0.10 THR 24 -0.04 ARG 134

ASP 258 0.10 LEU 25 -0.04 ARG 134

ASP 258 0.08 ALA 26 -0.04 ARG 134

ASP 258 0.06 GLU 27 -0.06 ARG 134

ASP 258 0.07 ILE 28 -0.07 ARG 134

ASP 258 0.06 LYS 29 -0.07 GLN 135

ASP 258 0.06 PRO 30 -0.08 GLU 121

ASP 258 0.07 HIS 31 -0.07 GLU 121

SER 265 0.10 PRO 32 -0.06 GLU 123

ASP 258 0.09 ASP 33 -0.04 GLU 123

ASP 258 0.07 GLN 34 -0.05 GLU 121

ASP 258 0.08 VAL 35 -0.04 GLU 121

ASP 258 0.08 VAL 36 -0.04 GLN 135

ASP 258 0.09 VAL 37 -0.03 GLN 135

ASP 258 0.05 PRO 38 -0.06 SER 256

ASP 258 0.06 ASP 39 -0.06 SER 256

ASP 258 0.04 ASN 40 -0.08 SER 256

ASP 258 0.08 ILE 41 -0.05 SER 256

ASP 258 0.12 LEU 42 -0.03 THR 245

ASP 258 0.12 GLN 43 -0.03 THR 245

ASP 258 0.11 GLY 44 -0.04 THR 245

ASP 258 0.17 LEU 45 -0.02 THR 245

ASP 258 0.22 GLN 46 -0.03 SER 12

ASP 258 0.21 LEU 47 -0.04 SER 12

ASP 258 0.23 LEU 48 -0.03 SER 12

ASP 258 0.30 ALA 49 -0.02 SER 12

ASP 258 0.35 THR 50 -0.04 SER 12

ASP 258 0.37 ALA 51 -0.06 SER 12

ASP 258 0.39 SER 52 -0.03 ALA 13

ASP 258 0.47 ASP 53 -0.02 ALA 13

ASP 258 0.38 GLY 54 -0.01 ALA 13

SER 261 0.35 ALA 55 -0.01 GLN 135

ASP 258 0.28 LEU 56 -0.01 GLN 135

SER 265 0.26 ALA 57 -0.01 GLN 135

SER 265 0.22 LEU 58 -0.01 THR 245

SER 265 0.22 ILE 59 -0.01 THR 245

SER 265 0.19 SER 60 -0.02 THR 245

SER 265 0.18 GLY 61 -0.02 THR 245

SER 265 0.18 ARG 62 -0.03 LYS 125

SER 265 0.20 SER 63 -0.02 GLY 126

SER 265 0.23 MET 64 -0.01 THR 245

SER 265 0.21 VAL 65 -0.01 THR 245

SER 265 0.17 GLU 66 -0.02 THR 124

SER 265 0.18 LEU 67 -0.02 THR 245

SER 265 0.20 ASP 68 -0.01 THR 245

SER 265 0.16 ALA 69 -0.02 GLU 121

ASP 258 0.13 LEU 70 -0.02 GLU 121

ASP 258 0.16 ALA 71 -0.02 THR 245

ASP 258 0.15 LYS 72 -0.02 GLN 135

ASP 258 0.16 PRO 73 -0.02 GLN 135

ASP 258 0.21 TYR 74 -0.02 SER 12

PHE 262 0.25 ARG 75 -0.01 GLN 135

PHE 262 0.27 PHE 76 -0.01 GLN 135

SER 265 0.30 PRO 77 -0.01 GLN 135

SER 265 0.27 LEU 78 -0.01 GLN 135

SER 265 0.26 ALA 79 -0.01 THR 245

SER 265 0.23 GLY 80 -0.01 THR 245

SER 265 0.22 VAL 81 -0.01 THR 245

SER 265 0.22 HIS 82 -0.01 THR 245

SER 265 0.26 GLY 83 -0.01 GLU 177

SER 265 0.27 ALA 84 -0.01 ILE 28

SER 265 0.28 GLU 85 -0.01 GLU 177

SER 265 0.30 ARG 86 -0.01 GLU 177

SER 265 0.33 ARG 87 -0.01 GLY 91

SER 265 0.37 ASP 88 -0.01 ALA 181

SER 265 0.39 ILE 89 -0.01 GLN 135

SER 265 0.42 ASN 90 -0.01 GLU 185

SER 265 0.37 GLY 91 -0.01 VAL 65

SER 265 0.38 LYS 92 -0.01 GLU 177

SER 265 0.34 THR 93 -0.01 GLU 177

SER 265 0.34 HIS 94 -0.01 GLU 177

SER 265 0.31 ILE 95 -0.01 GLU 177

SER 265 0.30 VAL 96 -0.01 PRO 30

SER 265 0.30 HIS 97 -0.02 PRO 30

SER 265 0.29 LEU 98 -0.02 PRO 30

SER 265 0.28 PRO 99 -0.02 PRO 30

SER 265 0.26 ASP 100 -0.03 PRO 30

SER 265 0.25 ALA 101 -0.03 PRO 30

SER 265 0.24 ILE 102 -0.03 PRO 30

SER 265 0.23 ALA 103 -0.03 PRO 30

SER 265 0.22 ARG 104 -0.03 PRO 30

SER 265 0.21 ASP 105 -0.03 PRO 30

SER 265 0.20 ILE 106 -0.04 PRO 30

SER 265 0.19 SER 107 -0.04 PRO 30

SER 265 0.18 VAL 108 -0.04 PRO 30

SER 265 0.18 GLN 109 -0.04 PRO 30

SER 265 0.17 LEU 110 -0.05 PRO 30

SER 265 0.15 HIS 111 -0.05 PRO 30

SER 265 0.15 THR 112 -0.05 PRO 30

SER 265 0.15 VAL 113 -0.05 PRO 30

SER 265 0.13 ILE 114 -0.06 PRO 30

SER 265 0.12 ALA 115 -0.06 PRO 30

SER 265 0.12 GLN 116 -0.05 PRO 30

SER 265 0.11 TYR 117 -0.06 PRO 30

SER 265 0.09 PRO 118 -0.06 PRO 30

SER 265 0.08 GLY 119 -0.08 PRO 30

SER 265 0.10 ALA 120 -0.07 PRO 30

SER 265 0.11 GLU 121 -0.08 PRO 30

SER 265 0.14 LEU 122 -0.07 PRO 30

SER 265 0.14 GLU 123 -0.06 PRO 30

SER 265 0.17 THR 124 -0.05 HIS 31

SER 265 0.19 LYS 125 -0.04 PRO 32

SER 265 0.22 GLY 126 -0.03 PRO 32

SER 265 0.23 MET 127 -0.03 PRO 30

SER 265 0.21 ALA 128 -0.03 PRO 30

SER 265 0.18 PHE 129 -0.04 PRO 30

SER 265 0.16 ALA 130 -0.05 PRO 30

SER 265 0.14 LEU 131 -0.06 PRO 30

SER 265 0.11 HIS 132 -0.07 PRO 30

SER 265 0.10 TYR 133 -0.07 PRO 30

SER 265 0.08 ARG 134 -0.07 PRO 30

SER 265 0.07 GLN 135 -0.08 PRO 30

SER 265 0.08 ALA 136 -0.06 PRO 30

SER 265 0.08 PRO 137 -0.05 PRO 30

SER 265 0.09 GLN 138 -0.04 PRO 30

SER 265 0.10 HIS 139 -0.05 PRO 30

SER 265 0.11 GLU 140 -0.04 PRO 30

SER 265 0.13 ASP 141 -0.04 PRO 30

SER 265 0.13 ALA 142 -0.04 PRO 30

SER 265 0.14 LEU 143 -0.04 PRO 30

SER 265 0.15 MET 144 -0.04 PRO 30

SER 265 0.16 THR 145 -0.03 PRO 30

SER 265 0.17 LEU 146 -0.04 PRO 30

SER 265 0.18 ALA 147 -0.03 PRO 30

SER 265 0.19 GLN 148 -0.03 PRO 30

SER 265 0.19 ARG 149 -0.03 PRO 30

SER 265 0.20 ILE 150 -0.03 PRO 30

SER 265 0.22 THR 151 -0.03 PRO 30

SER 265 0.22 GLN 152 -0.02 PRO 30

SER 265 0.23 ILE 153 -0.03 PRO 30

SER 265 0.24 TRP 154 -0.02 PRO 30

SER 265 0.25 PRO 155 -0.02 PRO 30

SER 265 0.27 GLN 156 -0.02 PRO 30

SER 265 0.24 MET 157 -0.02 PRO 30

SER 265 0.23 ALA 158 -0.02 PRO 30

SER 265 0.20 LEU 159 -0.02 ILE 28

SER 265 0.18 GLN 160 -0.02 GLY 222

SER 265 0.16 GLN 161 -0.03 GLY 222

SER 265 0.13 GLY 162 -0.04 GLY 222

SER 265 0.10 LYS 163 -0.05 THR 221

SER 265 0.10 CYS 164 -0.05 ILE 28

SER 265 0.12 VAL 165 -0.05 ILE 28

SER 265 0.15 VAL 166 -0.04 ILE 28

SER 265 0.17 GLU 167 -0.04 ILE 28

SER 265 0.20 ILE 168 -0.03 PRO 30

SER 265 0.22 LYS 169 -0.03 ILE 28

SER 265 0.25 PRO 170 -0.02 PRO 30

SER 265 0.26 ARG 171 -0.02 ILE 28

SER 265 0.28 GLY 172 -0.01 THR 201

SER 265 0.26 THR 173 -0.01 ILE 28

SER 265 0.24 SER 174 -0.01 THR 245

SER 265 0.23 LYS 175 -0.01 THR 245

SER 265 0.25 GLY 176 -0.01 HIS 94

SER 265 0.29 GLU 177 -0.01 HIS 94

SER 265 0.29 ALA 178 -0.01 THR 93

SER 265 0.29 ILE 179 -0.01 ASP 88

SER 265 0.32 ALA 180 -0.01 ALA 181

SER 265 0.35 ALA 181 -0.01 ALA 180

SER 265 0.36 PHE 182 -0.01 ALA 208

SER 265 0.37 MET 183 -0.01 LEU 212

SER 265 0.42 GLN 184 -0.01 LEU 212

SER 265 0.44 GLU 185 -0.01 LEU 212

SER 265 0.47 ALA 186 -0.01 PHE 76

SER 265 0.45 PRO 187 -0.01 PHE 76

SER 265 0.40 PHE 188 -0.01 PHE 76

SER 265 0.44 ILE 189 -0.01 LEU 212

SER 265 0.44 GLY 190 -0.01 GLY 213

SER 265 0.38 ARG 191 -0.01 GLN 135

SER 265 0.31 THR 192 -0.01 ALA 51

SER 265 0.27 PRO 193 -0.01 GLN 135

SER 265 0.21 VAL 194 -0.01 ARG 134

SER 265 0.19 PHE 195 -0.02 LYS 163

SER 265 0.14 LEU 196 -0.02 LYS 163

SER 265 0.14 GLY 197 -0.03 LYS 163

SER 265 0.10 ASP 198 -0.04 LYS 163

SER 265 0.12 ASP 199 -0.04 LYS 163

SER 265 0.14 LEU 200 -0.03 GLY 162

SER 265 0.17 THR 201 -0.02 THR 245

SER 265 0.17 ASP 202 -0.02 THR 245

SER 265 0.17 GLU 203 -0.01 THR 245

SER 265 0.21 SER 204 -0.01 THR 245

SER 265 0.22 GLY 205 -0.01 THR 245

SER 265 0.20 PHE 206 -0.01 THR 245

SER 265 0.22 ALA 207 -0.01 MET 242

SER 265 0.26 ALA 208 -0.01 ALA 181

SER 265 0.24 VAL 209 -0.01 MET 242

SER 265 0.22 ASN 210 -0.01 MET 242

SER 265 0.26 ARG 211 -0.01 GLN 184

SER 265 0.29 LEU 212 -0.01 GLN 184

SER 265 0.26 GLY 213 -0.01 ILE 189

SER 265 0.24 GLY 214 -0.01 ARG 134

SER 265 0.18 MET 215 -0.01 ARG 134

SER 265 0.17 SER 216 -0.02 LYS 163

SER 265 0.12 VAL 217 -0.02 LYS 163

SER 265 0.10 LYS 218 -0.03 LYS 163

ASP 258 0.07 ILE 219 -0.04 LYS 163

ASP 258 0.05 GLY 220 -0.05 LYS 163

ASP 258 0.05 THR 221 -0.05 LYS 163

SER 265 0.07 GLY 222 -0.05 LYS 163

SER 265 0.09 ALA 223 -0.03 LYS 163

SER 265 0.12 THR 224 -0.02 LYS 163

SER 265 0.15 GLN 225 -0.01 GLN 249

SER 265 0.14 ALA 226 -0.02 LYS 163

SER 265 0.13 SER 227 -0.02 GLN 249

SER 265 0.09 TRP 228 -0.03 GLN 249

SER 265 0.06 ARG 229 -0.04 SER 256

ASP 258 0.04 LEU 230 -0.06 SER 256

ASP 258 0.02 ALA 231 -0.07 SER 256

ASP 258 0.04 GLY 232 -0.07 SER 256

ASP 258 0.05 VAL 233 -0.06 SER 256

ASP 258 0.01 PRO 234 -0.09 SER 256

ASP 258 0.02 ASP 235 -0.09 SER 256

ASP 258 0.06 VAL 236 -0.06 SER 256

ASP 258 0.04 TRP 237 -0.08 SER 256

GLY 44 0.01 SER 238 -0.12 SER 256

ASP 258 0.03 TRP 239 -0.08 SER 256

ASP 258 0.07 LEU 240 -0.06 SER 256

ASP 258 0.02 GLU 241 -0.11 SER 256

ALA 51 0.01 MET 242 -0.13 SER 256

ASP 258 0.07 ILE 243 -0.06 SER 256

ASP 258 0.08 THR 244 -0.05 SER 256

ALA 51 0.03 THR 245 -0.14 SER 256

ALA 51 0.05 ALA 246 -0.10 SER 256

ASP 258 0.12 LEU 247 -0.03 LEU 11

GLN 249 0.09 GLN 248 -0.08 SER 256

ALA 51 0.12 GLN 249 -0.16 SER 256

ALA 51 0.17 LYS 250 -0.11 ARG 251

ALA 51 0.28 ARG 251 -0.11 LYS 250

ALA 51 0.17 GLU 252 -0.13 SER 256

ASP 53 0.21 ASN 253 -0.13 GLN 249

ASP 53 0.34 ASN 254 -0.04 ARG 255

ASP 53 0.33 ARG 255 -0.07 GLU 252

ASP 53 0.25 SER 256 -0.16 GLN 249

ASP 53 0.35 ASP 257 -0.09 GLN 249

ASP 53 0.47 ASP 258 -0.03 SER 256

ASP 53 0.35 TYR 259 -0.10 GLN 249

ASP 53 0.33 GLU 260 -0.13 GLN 249

ALA 186 0.44 SER 261 -0.05 GLN 249

ALA 186 0.45 PHE 262 -0.05 GLN 249

ALA 186 0.36 SER 263 -0.10 GLN 249

ALA 186 0.40 ARG 264 -0.08 GLN 249

ALA 186 0.47 SER 265 -0.04 GLN 249

ALA 186 0.42 ILE 266 -0.06 GLN 249

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.

*** TPP_E.coli_OtsB ***

CA distance fluctuations for 261012193747778604

--- normal mode 7 ---

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

* TPP_E.coli_OtsB *