Should you encounter any unexpected behaviour,
please let us know.

* cd1d *

CA distance fluctuations for 2402011637291200144

--- 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
TRP 217 0.11 GLN 5 -0.03 GLU 34

TRP 217 0.10 ARG 6 -0.04 GLU 34

PRO 215 0.18 LEU 7 -0.03 GLN 36

PRO 215 0.18 PHE 8 -0.04 GLN 36

PRO 232 0.24 PRO 9 -0.03 GLN 36

ASP 234 0.24 LEU 10 -0.02 ALA 30

ASP 234 0.32 ARG 11 -0.03 ALA 30

ASP 234 0.30 CYS 12 -0.02 SER 39

ASP 234 0.38 LEU 13 -0.02 GLY 28

ASP 234 0.37 GLN 14 -0.01 ASN 111

ASP 234 0.40 ILE 15 -0.01 ASN 111

ASP 234 0.36 SER 16 -0.01 ASN 111

ASP 234 0.36 SER 17 -0.01 ARG 74

PRO 197 0.37 PHE 18 -0.01 VAL 72

PRO 197 0.39 ALA 19 -0.01 VAL 72

PRO 197 0.38 ASN 20 -0.02 VAL 72

PRO 197 0.35 SER 21 -0.02 VAL 72

GLY 198 0.31 SER 22 -0.02 HIS 68

PRO 197 0.31 TRP 23 -0.02 HIS 68

PRO 197 0.31 THR 24 -0.01 HIS 68

ASP 234 0.28 ARG 25 -0.01 ASP 45

ASP 234 0.30 THR 26 -0.01 ASN 111

ASP 234 0.29 ASP 27 -0.01 ASN 111

ASP 234 0.29 GLY 28 -0.02 LEU 13

ASP 234 0.26 LEU 29 -0.02 SER 39

ASP 234 0.25 ALA 30 -0.03 ARG 11

ASP 234 0.23 TRP 31 -0.03 GLN 36

ASP 234 0.18 LEU 32 -0.04 PHE 8

PRO 215 0.17 GLY 33 -0.05 LEU 35

LYS 214 0.16 GLU 34 -0.04 ARG 6

ASP 234 0.12 LEU 35 -0.05 GLY 33

ASP 234 0.16 GLN 36 -0.04 PHE 8

ASP 234 0.14 THR 37 -0.04 LYS 183

ASP 234 0.17 HIS 38 -0.03 LYS 183

ASP 234 0.19 SER 39 -0.02 LEU 29

ASP 234 0.21 TRP 40 -0.02 SER 54

ASP 234 0.21 SER 41 -0.01 LEU 13

ASP 234 0.22 ASN 42 -0.01 SER 54

ASP 234 0.18 ASP 43 -0.01 PRO 52

ASP 234 0.16 SER 44 -0.02 PRO 52

ASP 234 0.16 ASP 45 -0.03 PRO 52

ASP 234 0.16 THR 46 -0.04 LYS 183

ASP 234 0.17 VAL 47 -0.03 LYS 183

ASP 234 0.13 ARG 48 -0.04 LYS 183

ASP 234 0.11 SER 49 -0.06 ASP 240

ASP 234 0.08 LEU 50 -0.08 ASP 240

ASP 234 0.06 LYS 51 -0.10 ASP 240

ASP 234 0.04 PRO 52 -0.13 VAL 185

ASP 234 0.06 TRP 53 -0.12 VAL 185

ASP 234 0.10 SER 54 -0.08 LYS 183

ASP 234 0.11 GLN 55 -0.09 LYS 183

ASP 234 0.10 GLY 56 -0.10 LYS 183

ASP 234 0.09 THR 57 -0.11 LYS 183

ASP 234 0.11 PHE 58 -0.09 LYS 183

ASP 234 0.10 SER 59 -0.09 LYS 183

ASP 234 0.10 ASP 60 -0.08 LYS 183

ASP 234 0.11 GLN 61 -0.07 LYS 183

ASP 234 0.13 GLN 62 -0.07 LYS 183

ASP 234 0.14 TRP 63 -0.07 LYS 183

ASP 234 0.14 GLU 64 -0.06 LYS 183

ASP 234 0.15 THR 65 -0.05 LYS 183

ASP 234 0.18 LEU 66 -0.05 LYS 183

ASP 234 0.17 GLN 67 -0.04 LYS 183

ASP 234 0.18 HIS 68 -0.04 LYS 183

ASP 234 0.20 ILE 69 -0.03 SER 179

ASP 234 0.22 PHE 70 -0.03 SER 54

ASP 234 0.20 ARG 71 -0.03 PRO 52

ASP 234 0.21 VAL 72 -0.04 SER 76

ASP 234 0.24 TYR 73 -0.03 LEU 66

ASP 234 0.25 ARG 74 -0.02 SER 54

PRO 197 0.24 SER 75 -0.03 HIS 68

PRO 197 0.26 SER 76 -0.04 VAL 72

PRO 197 0.29 PHE 77 -0.03 TYR 73

PRO 197 0.30 THR 78 -0.02 VAL 72

PRO 197 0.30 ARG 79 -0.03 VAL 72

PRO 197 0.32 ASP 80 -0.03 VAL 72

PRO 197 0.35 VAL 81 -0.02 VAL 72

PRO 197 0.35 LYS 82 -0.03 VAL 72

PRO 197 0.35 GLU 83 -0.03 VAL 72

PRO 197 0.38 PHE 84 -0.02 VAL 72

PRO 197 0.40 ALA 85 -0.02 VAL 72

PRO 197 0.39 LYS 86 -0.02 VAL 72

PRO 197 0.39 MET 87 -0.02 THR 65

PRO 197 0.43 LEU 88 -0.02 THR 65

PRO 197 0.44 ARG 89 -0.02 VAL 72

PRO 197 0.46 LEU 90 -0.02 VAL 72

PRO 197 0.47 SER 91 -0.02 VAL 72

PRO 197 0.45 TYR 92 -0.01 VAL 72

PRO 197 0.45 PRO 93 -0.01 VAL 72

PRO 197 0.44 LEU 94 -0.01 VAL 72

PRO 197 0.43 GLU 95 -0.01 ARG 74

ASP 234 0.43 LEU 96 -0.01 ARG 74

ASP 234 0.45 GLN 97 -0.01 ASN 111

ASP 234 0.41 VAL 98 -0.01 ASN 111

ASP 234 0.42 SER 99 -0.02 ASN 111

ASP 234 0.34 ALA 100 -0.02 ASN 111

ASP 234 0.28 GLY 101 -0.01 SER 39

PRO 232 0.25 CYS 102 -0.01 SER 39

PRO 232 0.22 GLU 103 -0.02 GLN 36

PRO 232 0.17 VAL 104 -0.04 LYS 183

GLN 228 0.17 HIS 105 -0.03 LYS 183

GLN 228 0.13 PRO 106 -0.05 LYS 182

GLN 228 0.12 GLY 107 -0.06 GLU 269

GLN 228 0.15 ASN 108 -0.06 LYS 183

GLN 228 0.18 ALA 109 -0.04 LYS 183

GLY 229 0.21 SER 110 -0.02 LYS 183

GLY 229 0.26 ASN 111 -0.02 ALA 100

GLN 231 0.28 ASN 112 -0.02 PHE 113

GLN 231 0.33 PHE 113 -0.02 ASN 112

ASP 234 0.35 PHE 114 -0.02 PHE 169

ASP 234 0.42 HIS 115 -0.01 SER 16

ASP 234 0.43 VAL 116 -0.01 ARG 74

ASP 234 0.49 ALA 117 -0.01 ARG 74

GLN 231 0.47 PHE 118 -0.01 TYR 73

PRO 197 0.52 GLN 119 -0.01 ARG 74

ASP 234 0.59 GLY 120 -0.01 SER 125

GLN 231 0.58 LYS 121 -0.01 SER 125

GLN 231 0.53 ASP 122 -0.01 SER 125

GLN 231 0.48 ILE 123 -0.01 TYR 73

GLN 231 0.44 LEU 124 -0.01 ILE 69

GLN 231 0.40 SER 125 -0.01 THR 165

GLN 231 0.35 PHE 126 -0.02 THR 165

GLY 229 0.35 GLN 127 -0.02 GLY 164

GLY 229 0.31 GLY 128 -0.02 GLY 172

GLY 229 0.29 THR 129 -0.03 GLY 172

GLY 229 0.32 SER 130 -0.02 PHE 58

GLY 229 0.36 TRP 131 -0.02 PHE 58

GLY 229 0.40 GLU 132 -0.02 PRO 133

GLY 229 0.44 PRO 133 -0.02 GLU 132

GLY 229 0.49 THR 134 -0.01 GLU 132

GLY 229 0.54 GLN 135 -0.01 GLU 132

GLY 229 0.58 GLU 136 -0.01 GLU 132

GLY 229 0.52 ALA 137 -0.01 VAL 72

PRO 197 0.51 PRO 138 -0.01 VAL 72

PRO 197 0.48 LEU 139 -0.01 THR 65

PRO 197 0.46 TRP 140 -0.02 THR 65

PRO 197 0.44 VAL 141 -0.02 THR 65

PRO 197 0.41 ASN 142 -0.02 THR 65

PRO 197 0.40 LEU 143 -0.02 THR 65

PRO 197 0.38 ALA 144 -0.02 THR 65

GLY 229 0.37 ILE 145 -0.02 THR 65

PRO 197 0.35 GLN 146 -0.02 THR 65

PRO 197 0.34 VAL 147 -0.03 THR 65

PRO 197 0.32 LEU 148 -0.03 THR 65

GLY 229 0.32 ASN 149 -0.02 PHE 58

PRO 197 0.30 GLN 150 -0.03 PHE 58

PRO 197 0.28 ASP 151 -0.03 PHE 58

GLY 229 0.26 LYS 152 -0.03 PHE 58

GLY 229 0.24 TRP 153 -0.04 PHE 58

GLN 231 0.26 THR 154 -0.03 PHE 58

GLY 229 0.28 ARG 155 -0.03 PHE 58

GLY 229 0.24 GLU 156 -0.04 PHE 58

GLN 231 0.23 THR 157 -0.04 PHE 58

GLN 231 0.26 VAL 158 -0.03 GLY 172

GLY 229 0.25 GLN 159 -0.03 GLY 172

GLN 231 0.22 TRP 160 -0.04 GLY 172

GLN 231 0.22 LEU 161 -0.04 GLY 172

GLN 231 0.25 LEU 162 -0.03 GLY 172

GLY 229 0.22 ASN 163 -0.03 SER 179

GLN 231 0.19 GLY 164 -0.05 SER 179

GLN 231 0.18 THR 165 -0.05 LYS 183

ASP 234 0.20 CYS 166 -0.04 LYS 183

GLN 231 0.17 PRO 167 -0.05 LYS 183

GLN 231 0.14 GLN 168 -0.07 LYS 183

ASP 234 0.15 PHE 169 -0.07 LYS 183

ASP 234 0.15 VAL 170 -0.07 LYS 183

PRO 232 0.12 SER 171 -0.09 LYS 183

ASP 234 0.10 GLY 172 -0.10 LYS 183

ASP 234 0.10 LEU 173 -0.10 LYS 183

PRO 232 0.09 LEU 174 -0.11 LYS 183

ASP 234 0.06 GLU 175 -0.12 LYS 183

ASP 234 0.06 SER 176 -0.14 LYS 183

ASP 234 0.06 GLY 177 -0.14 LYS 183

GLU 34 0.06 LYS 178 -0.15 LYS 183

GLY 120 0.05 SER 179 -0.18 LYS 183

GLY 120 0.06 GLU 180 -0.19 LYS 183

GLY 120 0.07 LEU 181 -0.10 LYS 183

GLY 120 0.08 LYS 182 -0.12 SER 267

GLY 120 0.09 LYS 183 -0.19 GLU 180

GLY 120 0.13 GLN 184 -0.13 SER 179

GLY 120 0.16 VAL 185 -0.15 SER 179

GLY 120 0.19 LYS 186 -0.13 SER 179

GLY 120 0.23 PRO 187 -0.12 SER 179

GLY 120 0.25 LYS 188 -0.12 SER 179

GLY 120 0.29 ALA 189 -0.10 SER 179

GLY 120 0.31 TRP 190 -0.09 SER 179

GLY 120 0.35 LEU 191 -0.07 SER 179

GLY 120 0.37 SER 192 -0.06 SER 179

GLY 120 0.41 ARG 193 -0.05 SER 179

GLY 120 0.46 GLY 194 -0.03 SER 179

GLY 120 0.47 PRO 195 -0.02 SER 179

LYS 121 0.49 SER 196 -0.02 LYS 186

LYS 121 0.53 PRO 197 -0.01 ARG 201

GLU 136 0.51 GLY 198 -0.01 TRP 190

GLU 136 0.49 PRO 199 -0.02 TRP 190

GLU 136 0.48 GLY 200 -0.02 LYS 186

GLU 136 0.48 ARG 201 -0.02 LYS 186

GLU 136 0.46 LEU 202 -0.03 LYS 186

LYS 121 0.46 LEU 203 -0.03 SER 179

LYS 121 0.44 LEU 204 -0.03 SER 179

GLY 120 0.44 VAL 205 -0.04 SER 179

GLY 120 0.39 CYS 206 -0.05 SER 179

GLY 120 0.37 HIS 207 -0.06 SER 179

GLY 120 0.33 VAL 208 -0.07 SER 179

GLY 120 0.29 SER 209 -0.08 PRO 52

GLY 120 0.23 GLY 210 -0.11 PRO 52

GLY 120 0.23 PHE 211 -0.08 SER 179

GLY 120 0.18 TYR 212 -0.08 GLU 180

GLY 120 0.16 PRO 213 -0.03 GLU 180

GLY 120 0.23 LYS 214 -0.02 PRO 237

ASP 122 0.24 PRO 215 -0.02 TYR 244

LYS 121 0.29 VAL 216 -0.03 GLN 184

LYS 121 0.34 TRP 217 -0.03 ASP 234

LYS 121 0.38 VAL 218 -0.03 GLN 184

GLU 136 0.41 LYS 219 -0.02 LYS 186

GLU 136 0.42 TRP 220 -0.03 LYS 186

GLU 136 0.40 MET 221 -0.03 SER 179

GLU 136 0.39 ARG 222 -0.03 SER 179

GLU 136 0.35 GLY 223 -0.04 SER 179

GLU 136 0.35 GLU 224 -0.03 SER 179

GLU 136 0.40 GLN 225 -0.02 LYS 186

GLU 136 0.44 GLU 226 -0.02 LYS 186

GLU 136 0.47 GLN 227 -0.02 LYS 186

GLU 136 0.54 GLN 228 -0.01 LYS 186

GLU 136 0.58 GLY 229 -0.01 LYS 186

GLU 136 0.53 THR 230 -0.01 LYS 186

LYS 121 0.58 GLN 231 -0.02 ALA 247

LYS 121 0.55 PRO 232 -0.03 ARG 246

GLY 120 0.58 GLY 233 -0.02 TRP 217

GLY 120 0.59 ASP 234 -0.03 TRP 217

GLY 120 0.44 ILE 235 -0.02 PRO 215

GLY 120 0.42 LEU 236 -0.01 PRO 215

GLY 120 0.30 PRO 237 -0.02 LYS 214

GLY 120 0.25 ASN 238 -0.04 PRO 52

GLY 120 0.18 ALA 239 -0.05 PRO 52

GLY 120 0.14 ASP 240 -0.11 PRO 52

GLY 120 0.15 GLU 241 -0.05 PRO 52

GLY 120 0.20 THR 242 -0.07 PRO 52

GLY 120 0.28 TRP 243 -0.04 GLU 180

GLY 120 0.34 TYR 244 -0.05 SER 179

GLY 120 0.42 LEU 245 -0.03 GLN 184

GLY 120 0.45 ARG 246 -0.03 GLN 184

LYS 121 0.47 ALA 247 -0.02 GLN 231

LYS 121 0.51 THR 248 -0.02 LYS 186

LYS 121 0.50 LEU 249 -0.02 LYS 186

GLU 136 0.52 ASP 250 -0.02 LYS 186

GLU 136 0.52 VAL 251 -0.02 LYS 186

GLU 136 0.49 VAL 252 -0.02 LYS 186

GLU 136 0.45 ALA 253 -0.03 SER 179

GLU 136 0.42 GLY 254 -0.03 SER 179

GLU 136 0.43 GLU 255 -0.03 SER 179

GLU 136 0.39 ALA 256 -0.05 SER 179

GLU 136 0.37 ALA 257 -0.05 SER 179

GLU 136 0.37 GLY 258 -0.05 SER 179

GLU 136 0.39 LEU 259 -0.04 SER 179

GLU 136 0.36 SER 260 -0.05 SER 179

LYS 121 0.36 CYS 261 -0.05 SER 179

GLU 136 0.33 ARG 262 -0.05 SER 179

LYS 121 0.30 VAL 263 -0.06 SER 179

LYS 121 0.26 LYS 264 -0.05 SER 179

LYS 121 0.23 HIS 265 -0.06 SER 179

LYS 121 0.17 SER 266 -0.08 LYS 182

GLY 120 0.16 SER 267 -0.14 SER 179

LYS 121 0.17 LEU 268 -0.13 SER 179

LYS 121 0.15 GLU 269 -0.12 SER 179

GLU 136 0.19 GLY 270 -0.08 SER 179

LYS 121 0.20 GLN 271 -0.10 SER 179

LYS 121 0.24 ASP 272 -0.08 SER 179

LYS 121 0.26 ILE 273 -0.10 SER 179

GLU 136 0.29 VAL 274 -0.08 SER 179

LYS 121 0.31 LEU 275 -0.08 SER 179

GLU 136 0.33 TYR 276 -0.07 SER 179

GLU 136 0.35 TRP 277 -0.07 SER 179

LYS 121 0.32 HIS 278 -0.08 SER 179

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).
Last modification: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** cd1d ***

CA distance fluctuations for 2402011637291200144

--- normal mode 7 ---

Should you encounter any unexpected behaviour,
please let us know.

* cd1d *