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

* EXSA_mono2 *

CA distance fluctuations for 2401041300393831953

--- 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
GLY 195 0.26 MET 1 -0.35 HIS 16

GLN 83 0.25 GLN 2 -0.31 HIS 16

GLN 83 0.35 GLY 3 -0.23 VAL 130

GLN 83 0.31 ALA 4 -0.24 VAL 130

GLN 83 0.21 LYS 5 -0.24 HIS 16

GLN 83 0.31 SER 6 -0.11 VAL 130

GLN 83 0.28 LEU 7 -0.12 GLY 8

GLN 83 0.09 GLY 8 -0.16 LYS 5

LEU 7 0.05 ARG 9 -0.11 LYS 5

GLY 195 0.03 LYS 10 -0.20 LYS 5

LEU 7 0.13 GLN 11 -0.09 ASN 231

LEU 7 0.05 ILE 12 -0.15 MET 1

ARG 168 0.02 THR 13 -0.23 MET 1

ARG 168 0.02 SER 14 -0.30 MET 1

ARG 168 0.01 CYS 15 -0.31 MET 1

ARG 168 0.01 HIS 16 -0.35 MET 1

ARG 168 0.01 TRP 17 -0.31 MET 1

ARG 168 0.01 ASN 18 -0.31 MET 1

ARG 168 0.01 ILE 19 -0.27 MET 1

ARG 168 0.00 PRO 20 -0.26 MET 1

ARG 168 0.00 THR 21 -0.23 MET 1

ARG 168 0.00 PHE 22 -0.21 MET 1

ARG 168 0.01 GLU 23 -0.21 MET 1

LEU 7 0.01 TYR 24 -0.18 ASN 231

LEU 7 0.02 ARG 25 -0.16 ASN 231

LEU 7 0.04 VAL 26 -0.16 ASN 231

LEU 7 0.07 ASN 27 -0.14 ASN 231

LEU 7 0.09 LYS 28 -0.13 ASN 231

LEU 7 0.14 GLU 29 -0.11 ASN 231

LEU 7 0.14 GLU 30 -0.10 ASN 231

LEU 7 0.12 GLY 31 -0.10 ASN 231

LEU 7 0.09 VAL 32 -0.09 ASN 231

LEU 7 0.06 TYR 33 -0.13 MET 1

LEU 7 0.04 VAL 34 -0.15 MET 1

LEU 7 0.02 LEU 35 -0.19 MET 1

ARG 168 0.01 LEU 36 -0.22 MET 1

ARG 168 0.01 GLU 37 -0.25 MET 1

ARG 168 0.01 GLY 38 -0.25 MET 1

ARG 168 0.01 GLU 39 -0.22 MET 1

LEU 7 0.02 LEU 40 -0.20 MET 1

LEU 7 0.02 THR 41 -0.17 MET 1

LEU 7 0.04 VAL 42 -0.14 ASP 271

LEU 7 0.04 GLN 43 -0.16 ARG 274

LEU 7 0.05 ASP 44 -0.16 ARG 274

LEU 7 0.05 ILE 45 -0.20 GLN 227

LEU 7 0.05 ASP 46 -0.19 ARG 274

LEU 7 0.05 SER 47 -0.17 ARG 274

LEU 7 0.04 THR 48 -0.17 ARG 274

LEU 7 0.04 PHE 49 -0.14 ARG 274

LEU 7 0.03 CYS 50 -0.14 MET 1

LEU 7 0.03 LEU 51 -0.15 MET 1

LEU 7 0.02 ALA 52 -0.17 MET 1

LEU 7 0.02 PRO 53 -0.19 MET 1

LEU 7 0.03 GLY 54 -0.16 MET 1

LEU 7 0.04 GLU 55 -0.13 MET 1

LEU 7 0.06 LEU 56 -0.10 MET 1

LEU 7 0.07 LEU 57 -0.10 ARG 274

LEU 7 0.09 PHE 58 -0.09 ARG 274

LEU 7 0.09 VAL 59 -0.10 GLN 227

LEU 7 0.11 ARG 60 -0.11 GLN 227

LEU 7 0.10 ARG 61 -0.12 ASN 231

LEU 7 0.08 GLY 62 -0.15 ASN 231

LEU 7 0.05 SER 63 -0.18 ASN 231

LEU 7 0.04 TYR 64 -0.17 ASN 231

LEU 7 0.03 VAL 65 -0.17 LYS 270

LEU 7 0.02 VAL 66 -0.18 MET 1

ARG 168 0.01 SER 67 -0.21 MET 1

ARG 168 0.01 THR 68 -0.24 MET 1

ARG 168 0.00 LYS 69 -0.24 MET 1

ARG 168 0.01 GLY 70 -0.28 MET 1

ARG 168 0.01 LYS 71 -0.29 MET 1

ARG 168 0.01 ASP 72 -0.32 MET 1

ARG 168 0.01 SER 73 -0.29 MET 1

ARG 168 0.01 ARG 74 -0.29 MET 1

ARG 168 0.01 ILE 75 -0.24 MET 1

LEU 7 0.02 LEU 76 -0.20 MET 1

LEU 7 0.04 TRP 77 -0.16 MET 1

LEU 7 0.09 ILE 78 -0.09 ASN 231

LEU 7 0.14 PRO 79 -0.10 ASN 231

LEU 7 0.19 LEU 80 -0.09 ASN 231

LEU 7 0.24 SER 81 -0.09 ASN 231

GLY 3 0.27 ALA 82 -0.08 ASN 231

GLY 3 0.35 GLN 83 -0.07 ASN 231

GLY 3 0.29 PHE 84 -0.07 ASN 231

GLY 3 0.25 LEU 85 -0.06 ASN 231

GLY 3 0.31 GLN 86 -0.05 ASN 231

GLY 3 0.34 GLY 87 -0.05 ASN 231

GLY 3 0.27 PHE 88 -0.05 ASN 231

GLY 3 0.27 VAL 89 -0.04 ASN 231

GLY 3 0.32 GLN 90 -0.04 ASN 231

GLY 3 0.30 ARG 91 -0.04 ASN 231

GLY 3 0.25 PHE 92 -0.04 ASN 231

GLY 3 0.26 GLY 93 -0.03 ASN 231

GLY 3 0.24 ALA 94 -0.02 ASN 231

GLY 3 0.21 LEU 95 -0.02 ASN 231

GLY 3 0.20 LEU 96 -0.03 ASN 231

GLY 3 0.21 SER 97 -0.02 ASN 231

GLY 3 0.18 GLU 98 -0.01 ASN 231

GLY 3 0.16 VAL 99 -0.02 ASN 231

GLY 3 0.16 GLU 100 -0.01 ARG 274

GLY 3 0.17 ARG 101 -0.01 ARG 274

GLY 3 0.14 CYS 102 -0.03 ASN 277

GLY 3 0.15 ASP 103 -0.05 GLY 210

GLY 3 0.12 GLU 104 -0.08 GLY 210

GLY 3 0.11 PRO 105 -0.09 TYR 209

GLY 3 0.12 VAL 106 -0.08 LEU 223

GLY 3 0.09 PRO 107 -0.10 ASN 277

LEU 7 0.08 GLY 108 -0.12 GLN 227

LEU 7 0.08 ILE 109 -0.11 ARG 274

LEU 7 0.08 ILE 110 -0.10 ARG 274

LEU 7 0.07 ALA 111 -0.10 ARG 274

LEU 7 0.07 PHE 112 -0.08 ARG 274

LEU 7 0.06 ALA 113 -0.08 ASN 278

LEU 7 0.05 ALA 114 -0.10 MET 1

LEU 7 0.05 THR 115 -0.08 MET 1

LEU 7 0.05 PRO 116 -0.08 MET 1

LEU 7 0.06 LEU 117 -0.06 MET 1

LEU 7 0.06 LEU 118 -0.07 MET 1

LEU 7 0.04 ALA 119 -0.12 MET 1

LEU 7 0.04 GLY 120 -0.10 MET 1

LEU 7 0.06 CYS 121 -0.08 MET 1

LEU 7 0.05 VAL 122 -0.13 MET 1

LEU 7 0.02 LYS 123 -0.16 MET 1

LEU 7 0.03 GLY 124 -0.13 MET 1

LEU 7 0.04 LEU 125 -0.14 MET 1

GLY 195 0.01 LYS 126 -0.22 MET 1

GLY 195 0.02 GLU 127 -0.22 MET 1

GLY 195 0.02 LEU 128 -0.19 MET 1

GLY 195 0.02 LEU 129 -0.28 MET 1

GLY 195 0.02 VAL 130 -0.33 MET 1

GLY 195 0.02 HIS 131 -0.28 MET 1

GLY 195 0.02 GLU 132 -0.25 MET 1

THR 200 0.02 HIS 133 -0.12 MET 1

ALA 4 0.04 PRO 134 -0.07 ASN 231

ALA 4 0.09 PRO 135 -0.07 ASN 231

ALA 4 0.20 MET 136 -0.07 ASN 231

LEU 7 0.09 LEU 137 -0.06 ASN 231

LEU 7 0.12 ALA 138 -0.07 ASN 231

LEU 7 0.19 CYS 139 -0.07 ASN 231

GLY 3 0.15 LEU 140 -0.06 ASN 231

LEU 7 0.11 LYS 141 -0.06 ASN 231

LEU 7 0.14 ILE 142 -0.07 ASN 231

GLY 3 0.16 GLU 143 -0.06 ASN 231

LEU 7 0.12 GLU 144 -0.05 ASN 231

LEU 7 0.11 LEU 145 -0.06 ASN 231

LEU 7 0.13 LEU 146 -0.06 ASN 231

GLY 3 0.14 MET 147 -0.05 ASN 231

LEU 7 0.10 LEU 148 -0.05 ASP 271

LEU 7 0.10 PHE 149 -0.06 ARG 274

GLY 3 0.14 ALA 150 -0.04 ARG 274

GLY 3 0.12 PHE 151 -0.04 ARG 274

GLY 3 0.09 SER 152 -0.05 ASN 278

GLY 3 0.09 PRO 153 -0.05 ASN 278

GLY 3 0.09 GLN 154 -0.06 ASN 278

GLY 3 0.12 GLY 155 -0.05 ARG 274

GLY 3 0.14 PRO 156 -0.04 ASN 277

GLY 3 0.12 LEU 157 -0.06 ASN 277

GLY 3 0.14 LEU 158 -0.06 ARG 274

GLY 3 0.17 MET 159 -0.04 GLN 227

GLY 3 0.17 SER 160 -0.04 ARG 274

GLY 3 0.16 VAL 161 -0.06 GLN 227

GLY 3 0.20 LEU 162 -0.05 GLN 227

GLY 3 0.22 ARG 163 -0.04 GLN 227

GLY 3 0.21 GLN 164 -0.05 GLN 227

GLY 3 0.23 LEU 165 -0.06 GLN 227

GLY 3 0.28 SER 166 -0.05 ASN 231

GLY 3 0.26 ASN 167 -0.03 ASN 231

GLY 3 0.29 ARG 168 -0.03 ASN 231

GLY 3 0.27 HIS 169 -0.02 VAL 170

GLY 3 0.22 VAL 170 -0.02 HIS 169

GLY 3 0.23 GLU 171 -0.03 GLN 227

GLY 3 0.25 ARG 172 -0.03 GLN 227

GLY 3 0.22 LEU 173 -0.02 GLN 174

GLY 3 0.19 GLN 174 -0.03 LEU 223

GLY 3 0.20 LEU 175 -0.04 GLU 178

GLY 3 0.21 PHE 176 -0.02 GLN 227

GLY 3 0.18 MET 177 -0.04 ILE 45

GLY 3 0.15 GLU 178 -0.06 GLY 62

GLY 3 0.17 LYS 179 -0.04 GLY 62

GLY 3 0.17 HIS 180 -0.04 GLY 62

GLY 3 0.15 TYR 181 -0.06 ILE 45

GLY 3 0.13 LEU 182 -0.07 ILE 45

GLY 3 0.16 ASN 183 -0.05 ILE 45

GLY 3 0.16 GLU 184 -0.05 ILE 45

GLY 3 0.19 TRP 185 -0.04 ILE 45

GLY 3 0.19 LYS 186 -0.05 ILE 45

GLY 3 0.20 LEU 187 -0.05 ASP 46

GLY 3 0.22 SER 188 -0.04 ASP 46

GLY 3 0.23 ASP 189 -0.03 ILE 45

GLY 3 0.22 PHE 190 -0.03 ILE 45

GLY 3 0.24 SER 191 -0.03 ASP 46

GLY 3 0.27 ARG 192 -0.02 ASP 46

GLY 3 0.27 GLU 193 -0.02 ASP 46

GLY 3 0.27 PHE 194 -0.02 ASP 46

GLY 3 0.30 GLY 195 -0.01 ASP 46

GLY 3 0.28 MET 196 -0.02 ASP 46

GLY 3 0.27 GLY 197 -0.03 ASP 46

GLY 3 0.24 LEU 198 -0.03 ASP 46

GLY 3 0.23 THR 199 -0.03 ASP 46

GLY 3 0.25 THR 200 -0.03 ASP 46

GLY 3 0.24 PHE 201 -0.03 ASP 46

GLY 3 0.21 LYS 202 -0.04 ASP 46

GLY 3 0.21 GLU 203 -0.04 ASP 46

GLY 3 0.22 LEU 204 -0.03 PRO 105

GLY 3 0.19 PHE 205 -0.05 PRO 105

GLY 3 0.18 GLY 206 -0.06 PRO 105

GLY 3 0.19 SER 207 -0.05 GLU 104

GLY 3 0.18 VAL 208 -0.05 PRO 105

GLY 3 0.15 TYR 209 -0.09 PRO 105

GLY 3 0.15 GLY 210 -0.08 PRO 105

GLY 3 0.15 VAL 211 -0.08 PRO 105

GLY 3 0.16 SER 212 -0.07 ASP 46

GLY 3 0.17 PRO 213 -0.06 ASP 46

GLY 3 0.16 ARG 214 -0.07 ASP 46

GLY 3 0.13 ALA 215 -0.09 ASP 46

GLY 3 0.13 TRP 216 -0.09 ASP 46

GLY 3 0.14 ILE 217 -0.08 ILE 45

GLY 3 0.12 SER 218 -0.10 ILE 45

GLY 3 0.10 GLU 219 -0.13 ASP 46

GLY 3 0.10 ARG 220 -0.13 ILE 45

GLY 3 0.10 ARG 221 -0.11 ILE 45

GLY 3 0.07 ILE 222 -0.14 ILE 45

GLY 3 0.06 LEU 223 -0.18 ILE 45

GLY 3 0.06 TYR 224 -0.15 ILE 45

GLY 3 0.05 ALA 225 -0.14 ILE 45

GLY 3 0.03 HIS 226 -0.18 ILE 45

GLY 3 0.01 GLN 227 -0.20 ILE 45

GLY 3 0.02 LEU 228 -0.15 ILE 45

GLY 3 0.01 LEU 229 -0.15 ILE 45

ALA 215 0.01 LEU 230 -0.18 ILE 45

ALA 215 0.01 ASN 231 -0.18 TYR 24

ALA 215 0.01 SER 232 -0.15 TYR 24

ALA 215 0.01 ASP 233 -0.14 TYR 24

GLY 3 0.02 MET 234 -0.12 TYR 24

GLY 3 0.03 SER 235 -0.11 TYR 24

GLY 3 0.04 ILE 236 -0.11 ILE 45

GLY 3 0.06 VAL 237 -0.09 ILE 45

GLY 3 0.06 ASP 238 -0.09 TYR 24

GLY 3 0.06 ILE 239 -0.10 ILE 45

GLY 3 0.08 ALA 240 -0.10 ILE 45

GLY 3 0.10 MET 241 -0.08 ILE 45

GLY 3 0.08 GLU 242 -0.08 SER 63

GLY 3 0.09 ALA 243 -0.10 ILE 45

GLY 3 0.12 GLY 244 -0.08 ILE 45

GLY 3 0.11 PHE 245 -0.09 ILE 45

GLY 3 0.13 SER 246 -0.07 ILE 45

GLY 3 0.10 SER 247 -0.08 ILE 45

GLY 3 0.08 GLN 248 -0.09 ILE 45

GLY 3 0.09 SER 249 -0.09 ILE 45

GLY 3 0.10 TYR 250 -0.09 ILE 45

GLY 3 0.08 PHE 251 -0.11 ILE 45

GLY 3 0.07 THR 252 -0.11 ILE 45

GLY 3 0.08 GLN 253 -0.11 ILE 45

GLY 3 0.09 SER 254 -0.12 ILE 45

GLY 3 0.06 TYR 255 -0.14 ILE 45

GLY 3 0.06 ARG 256 -0.14 ILE 45

GLY 3 0.07 ARG 257 -0.13 ASP 46

GLY 3 0.06 ARG 258 -0.15 ASP 46

GLY 3 0.04 PHE 259 -0.17 ASP 46

GLY 3 0.04 GLY 260 -0.15 ASP 46

GLY 3 0.03 CYS 261 -0.15 ILE 45

GLY 3 0.04 THR 262 -0.13 ILE 45

GLY 3 0.03 PRO 263 -0.14 ILE 45

GLY 3 0.02 SER 264 -0.13 ILE 45

LYS 186 0.01 ARG 265 -0.14 ILE 45

ALA 215 0.01 SER 266 -0.16 ILE 45

ALA 215 0.01 ARG 267 -0.15 ILE 45

ALA 215 0.01 GLN 268 -0.15 THR 21

ALA 215 0.01 GLY 269 -0.16 THR 21

ALA 215 0.01 LYS 270 -0.18 ILE 45

ALA 215 0.01 ASP 271 -0.18 THR 21

SER 212 0.01 GLU 272 -0.16 ILE 45

ALA 215 0.02 CYS 273 -0.17 ILE 45

SER 212 0.02 ARG 274 -0.19 ASP 46

SER 212 0.02 ALA 275 -0.17 ASP 46

GLY 3 0.03 LYS 276 -0.16 ASP 46

GLY 3 0.03 ASN 277 -0.18 ASP 46

SER 212 0.02 ASN 278 -0.17 ASP 46

GLY 3 0.03 NMA 278 -0.15 ASP 46

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.

*** EXSA_mono2 ***

CA distance fluctuations for 2401041300393831953

--- normal mode 8 ---

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

* EXSA_mono2 *