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

* EXSA_mono2 *

CA distance fluctuations for 2401041300393831953

--- normal mode 10 ---

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
PRO 134 0.45 MET 1 -0.27 TYR 24

PRO 134 0.38 GLN 2 -0.27 VAL 26

PRO 134 0.33 GLY 3 -0.15 TYR 24

PRO 134 0.43 ALA 4 -0.12 GLU 23

PRO 134 0.33 LYS 5 -0.19 VAL 26

PRO 134 0.10 SER 6 -0.09 LYS 28

GLN 83 0.14 LEU 7 -0.07 GLY 8

SER 6 0.08 GLY 8 -0.07 LEU 7

ASN 231 0.08 ARG 9 -0.17 LYS 5

ASN 231 0.06 LYS 10 -0.09 LYS 5

ALA 4 0.10 GLN 11 -0.02 SER 6

ALA 4 0.06 ILE 12 -0.02 SER 6

ASN 278 0.05 THR 13 -0.10 GLN 2

ASN 278 0.05 SER 14 -0.11 GLN 2

ASN 278 0.06 CYS 15 -0.17 GLN 2

ASN 278 0.07 HIS 16 -0.18 MET 1

ASN 278 0.08 TRP 17 -0.21 MET 1

ASN 278 0.09 ASN 18 -0.22 MET 1

ASN 278 0.11 ILE 19 -0.23 MET 1

ASN 278 0.12 PRO 20 -0.22 MET 1

ASN 278 0.14 THR 21 -0.23 MET 1

ASN 278 0.15 PHE 22 -0.24 MET 1

ASN 278 0.14 GLU 23 -0.27 MET 1

ASN 278 0.15 TYR 24 -0.27 MET 1

ARG 274 0.13 ARG 25 -0.27 GLN 2

ARG 274 0.13 VAL 26 -0.27 GLN 2

ARG 274 0.10 ASN 27 -0.23 GLN 2

ASN 231 0.12 LYS 28 -0.25 GLN 2

LEU 7 0.08 GLU 29 -0.17 GLN 2

LEU 7 0.08 GLU 30 -0.12 GLN 2

LEU 7 0.07 GLY 31 -0.10 GLN 2

LEU 7 0.05 VAL 32 -0.07 GLN 2

ASN 278 0.04 TYR 33 -0.10 GLN 2

LEU 7 0.03 VAL 34 -0.06 GLN 2

ASN 278 0.03 LEU 35 -0.07 GLN 2

ASN 278 0.02 LEU 36 -0.05 GLN 2

ASN 278 0.03 GLU 37 -0.07 GLN 2

ASN 278 0.05 GLY 38 -0.10 GLN 2

ASN 278 0.06 GLU 39 -0.11 GLN 2

ASN 278 0.07 LEU 40 -0.13 GLN 2

ASN 278 0.08 THR 41 -0.14 GLN 2

ASN 278 0.09 VAL 42 -0.15 GLN 2

ASN 278 0.12 GLN 43 -0.16 GLN 2

ASN 278 0.13 ASP 44 -0.17 GLN 2

ASN 278 0.18 ILE 45 -0.17 GLN 2

ASN 278 0.15 ASP 46 -0.23 ASN 231

ASN 278 0.11 SER 47 -0.20 ASN 231

ASN 278 0.10 THR 48 -0.17 ASN 231

ASN 278 0.06 PHE 49 -0.14 ASN 231

ASN 278 0.06 CYS 50 -0.13 ASN 231

ASN 278 0.03 LEU 51 -0.10 ASN 231

SER 207 0.02 ALA 52 -0.10 ASN 231

SER 207 0.02 PRO 53 -0.08 ASN 231

ALA 4 0.04 GLY 54 -0.07 ASN 231

ALA 4 0.04 GLU 55 -0.08 ASN 231

ALA 4 0.05 LEU 56 -0.07 ASN 231

LEU 7 0.04 LEU 57 -0.07 GLN 2

LEU 7 0.05 PHE 58 -0.07 GLN 2

LEU 7 0.05 VAL 59 -0.11 GLN 2

LEU 7 0.07 ARG 60 -0.13 GLN 2

ARG 274 0.09 ARG 61 -0.17 GLN 2

ARG 274 0.12 GLY 62 -0.21 GLN 2

ARG 274 0.14 SER 63 -0.23 GLN 2

ASN 278 0.13 TYR 64 -0.21 GLN 2

ASN 278 0.14 VAL 65 -0.21 GLN 2

ASN 278 0.11 VAL 66 -0.20 GLN 2

ASN 278 0.11 SER 67 -0.19 MET 1

ASN 278 0.09 THR 68 -0.17 MET 1

ASN 278 0.10 LYS 69 -0.17 MET 1

ASN 278 0.10 GLY 70 -0.19 MET 1

ASN 278 0.08 LYS 71 -0.16 MET 1

ASN 278 0.07 ASP 72 -0.16 MET 1

ASN 278 0.06 SER 73 -0.13 GLN 2

ASN 278 0.05 ARG 74 -0.11 GLN 2

ASN 278 0.05 ILE 75 -0.11 GLN 2

ASN 278 0.04 LEU 76 -0.08 GLN 2

ASN 278 0.05 TRP 77 -0.12 GLN 2

LEU 7 0.06 ILE 78 -0.07 GLN 2

LEU 7 0.08 PRO 79 -0.11 GLN 2

LEU 7 0.10 LEU 80 -0.06 GLN 2

LEU 7 0.13 SER 81 -0.07 GLN 2

LEU 7 0.12 ALA 82 -0.06 GLN 2

ALA 4 0.18 GLN 83 -0.04 ARG 168

ALA 4 0.20 PHE 84 -0.02 ARG 168

ALA 4 0.16 LEU 85 -0.02 SER 6

ALA 4 0.18 GLN 86 -0.03 ARG 168

ALA 4 0.23 GLY 87 -0.03 SER 207

ALA 4 0.21 PHE 88 -0.03 SER 207

ALA 4 0.18 VAL 89 -0.04 SER 207

ALA 4 0.21 GLN 90 -0.04 SER 207

ALA 4 0.24 ARG 91 -0.04 SER 207

ALA 4 0.20 PHE 92 -0.05 ASN 278

ALA 4 0.18 GLY 93 -0.06 ASN 278

ALA 4 0.18 ALA 94 -0.08 ASN 278

ALA 4 0.17 LEU 95 -0.08 ASN 278

ALA 4 0.15 LEU 96 -0.07 ASN 278

ALA 4 0.14 SER 97 -0.09 ASN 278

ALA 4 0.14 GLU 98 -0.11 ASN 278

ALA 4 0.12 VAL 99 -0.10 ASN 277

ALA 4 0.10 GLU 100 -0.11 ASN 277

ALA 4 0.09 ARG 101 -0.10 ASN 277

ALA 4 0.08 CYS 102 -0.11 LEU 223

SER 207 0.10 ASP 103 -0.13 LEU 223

SER 207 0.10 GLU 104 -0.16 LEU 223

GLY 210 0.12 PRO 105 -0.16 GLU 178

GLY 210 0.08 VAL 106 -0.12 GLU 178

GLY 210 0.08 PRO 107 -0.11 LYS 179

ASN 278 0.07 GLY 108 -0.12 GLN 2

GLY 210 0.06 ILE 109 -0.11 GLN 2

LEU 7 0.05 ILE 110 -0.10 ASN 231

ALA 4 0.04 ALA 111 -0.11 ASN 231

ALA 4 0.06 PHE 112 -0.10 ASN 231

ALA 4 0.06 ALA 113 -0.11 ASN 231

ALA 4 0.06 ALA 114 -0.09 ASN 231

ALA 4 0.09 THR 115 -0.09 ASN 231

MET 1 0.10 PRO 116 -0.08 LYS 270

MET 1 0.12 LEU 117 -0.07 LYS 270

ALA 4 0.11 LEU 118 -0.06 ASN 231

ALA 4 0.09 ALA 119 -0.06 ASN 231

MET 1 0.13 GLY 120 -0.05 LYS 270

MET 1 0.13 CYS 121 -0.04 LYS 270

ALA 4 0.09 VAL 122 -0.03 ASN 231

MET 1 0.11 LYS 123 -0.03 ASN 231

MET 1 0.17 GLY 124 -0.02 LYS 270

MET 1 0.12 LEU 125 -0.01 ASN 231

MET 1 0.09 LYS 126 -0.01 SER 232

MET 1 0.17 GLU 127 -0.00 GLN 268

MET 1 0.19 LEU 128 -0.00 GLU 98

MET 1 0.10 LEU 129 -0.02 LEU 7

MET 1 0.14 VAL 130 -0.03 LEU 7

MET 1 0.25 HIS 131 -0.03 LEU 7

MET 1 0.34 GLU 132 -0.03 LEU 7

MET 1 0.38 HIS 133 -0.01 LEU 7

MET 1 0.45 PRO 134 -0.01 SER 207

ALA 4 0.39 PRO 135 -0.01 HIS 16

ALA 4 0.40 MET 136 -0.01 SER 207

ALA 4 0.31 LEU 137 -0.01 SER 207

ALA 4 0.24 ALA 138 -0.01 SER 207

ALA 4 0.27 CYS 139 -0.01 SER 207

ALA 4 0.27 LEU 140 -0.02 ASN 278

ALA 4 0.20 LYS 141 -0.01 ASN 278

ALA 4 0.18 ILE 142 -0.01 CYS 102

ALA 4 0.21 GLU 143 -0.02 ASN 278

ALA 4 0.19 GLU 144 -0.03 ASN 278

ALA 4 0.14 LEU 145 -0.03 LYS 270

ALA 4 0.14 LEU 146 -0.03 LYS 270

ALA 4 0.16 MET 147 -0.05 ARG 274

ALA 4 0.13 LEU 148 -0.06 LYS 270

ALA 4 0.11 PHE 149 -0.06 ASN 231

ALA 4 0.13 ALA 150 -0.06 LYS 270

ALA 4 0.13 PHE 151 -0.08 ARG 274

ALA 4 0.10 SER 152 -0.10 LYS 270

ALA 4 0.09 PRO 153 -0.12 LYS 270

ALA 4 0.08 GLN 154 -0.11 ASN 231

ALA 4 0.10 GLY 155 -0.08 LYS 270

ALA 4 0.09 PRO 156 -0.09 GLN 227

ALA 4 0.08 LEU 157 -0.09 GLN 227

ALA 4 0.09 LEU 158 -0.06 ASN 231

ALA 4 0.11 MET 159 -0.05 LYS 270

ALA 4 0.09 SER 160 -0.05 GLN 227

ALA 4 0.08 VAL 161 -0.05 GLN 2

ALA 4 0.11 LEU 162 -0.03 GLN 2

ALA 4 0.11 ARG 163 -0.03 SER 6

ALA 4 0.08 GLN 164 -0.06 GLN 2

ALA 4 0.09 LEU 165 -0.06 GLN 2

ALA 4 0.11 SER 166 -0.06 ARG 168

ALA 4 0.12 ASN 167 -0.05 ARG 168

ALA 4 0.11 ARG 168 -0.06 SER 166

ALA 4 0.10 HIS 169 -0.03 SER 6

ALA 4 0.09 VAL 170 -0.04 ASN 277

ALA 4 0.09 GLU 171 -0.05 GLN 2

ALA 4 0.09 ARG 172 -0.05 GLN 2

ALA 4 0.08 LEU 173 -0.05 GLN 2

LEU 7 0.08 GLN 174 -0.08 PRO 105

LEU 7 0.09 LEU 175 -0.09 PRO 105

LEU 7 0.08 PHE 176 -0.09 PRO 105

LEU 7 0.08 MET 177 -0.10 PRO 105

LEU 7 0.09 GLU 178 -0.16 PRO 105

LEU 7 0.10 LYS 179 -0.14 ASP 46

LEU 7 0.08 HIS 180 -0.11 ASP 46

LEU 7 0.08 TYR 181 -0.11 PRO 105

LEU 7 0.08 LEU 182 -0.12 ASP 46

LEU 7 0.08 ASN 183 -0.11 ASP 46

LEU 7 0.07 GLU 184 -0.09 ASP 46

LEU 7 0.06 TRP 185 -0.07 GLN 2

LEU 7 0.05 LYS 186 -0.06 GLN 2

ALA 4 0.05 LEU 187 -0.06 GLN 2

ALA 4 0.05 SER 188 -0.06 GLN 2

ALA 4 0.05 ASP 189 -0.06 GLN 2

ALA 4 0.06 PHE 190 -0.06 GLN 2

ALA 4 0.06 SER 191 -0.05 GLN 2

ALA 4 0.06 ARG 192 -0.06 GLN 2

ALA 4 0.06 GLU 193 -0.07 ILE 45

ALA 4 0.07 PHE 194 -0.06 GLN 2

ALA 94 0.07 GLY 195 -0.06 GLY 62

ALA 4 0.07 MET 196 -0.04 LYS 28

ALA 4 0.06 GLY 197 -0.04 NMA 278

ALA 4 0.06 LEU 198 -0.04 NMA 278

ALA 4 0.06 THR 199 -0.05 NMA 278

ALA 4 0.07 THR 200 -0.05 NMA 278

ALA 4 0.07 PHE 201 -0.04 NMA 278

ALA 4 0.07 LYS 202 -0.05 ASN 277

ALA 4 0.07 GLU 203 -0.06 ASN 277

ALA 4 0.08 LEU 204 -0.05 ASN 277

ALA 4 0.07 PHE 205 -0.05 ASN 277

PRO 105 0.07 GLY 206 -0.07 ASN 277

GLU 104 0.10 SER 207 -0.07 ASN 277

PRO 105 0.09 VAL 208 -0.07 ARG 101

PRO 105 0.10 TYR 209 -0.08 ARG 101

PRO 105 0.12 GLY 210 -0.08 GLU 98

ILE 45 0.08 VAL 211 -0.08 ASN 277

ALA 4 0.06 SER 212 -0.06 ASN 277

ALA 4 0.06 PRO 213 -0.05 GLN 2

LEU 7 0.06 ARG 214 -0.05 GLN 2

LEU 7 0.06 ALA 215 -0.06 ARG 258

LEU 7 0.07 TRP 216 -0.08 ASP 103

LEU 7 0.07 ILE 217 -0.08 GLU 104

LEU 7 0.07 SER 218 -0.08 GLU 104

LEU 7 0.07 GLU 219 -0.11 GLU 104

LEU 7 0.08 ARG 220 -0.15 GLU 104

LEU 7 0.08 ARG 221 -0.12 GLU 104

LEU 7 0.08 ILE 222 -0.12 GLU 104

GLY 62 0.09 LEU 223 -0.16 GLU 104

LEU 7 0.10 TYR 224 -0.16 GLU 104

LEU 7 0.09 ALA 225 -0.13 GLU 104

LYS 28 0.09 HIS 226 -0.14 GLU 104

LYS 28 0.11 GLN 227 -0.17 ASP 46

LEU 7 0.10 LEU 228 -0.19 ASP 46

LEU 7 0.10 LEU 229 -0.14 ASP 46

LYS 28 0.11 LEU 230 -0.15 ASP 46

LYS 28 0.12 ASN 231 -0.23 ASP 46

LEU 7 0.11 SER 232 -0.21 ASP 46

LEU 7 0.10 ASP 233 -0.18 ASP 46

LEU 7 0.10 MET 234 -0.17 ASP 46

LEU 7 0.09 SER 235 -0.13 ASP 46

LEU 7 0.08 ILE 236 -0.11 ASP 46

LEU 7 0.08 VAL 237 -0.11 ASP 46

LEU 7 0.09 ASP 238 -0.14 ASP 46

LEU 7 0.09 ILE 239 -0.14 ASP 46

LEU 7 0.08 ALA 240 -0.11 ASP 46

LEU 7 0.08 MET 241 -0.12 ASP 46

LEU 7 0.09 GLU 242 -0.15 ASP 46

LEU 7 0.09 ALA 243 -0.13 ASP 46

LEU 7 0.08 GLY 244 -0.10 ASP 46

LEU 7 0.07 PHE 245 -0.08 ASP 46

LEU 7 0.06 SER 246 -0.07 GLN 2

LEU 7 0.07 SER 247 -0.07 MET 1

LEU 7 0.07 GLN 248 -0.07 ASP 46

LEU 7 0.06 SER 249 -0.06 MET 1

LEU 7 0.06 TYR 250 -0.06 GLN 2

LEU 7 0.07 PHE 251 -0.08 GLU 104

LEU 7 0.07 THR 252 -0.07 GLU 104

LEU 7 0.06 GLN 253 -0.06 GLU 104

LEU 7 0.07 SER 254 -0.07 GLU 104

LEU 7 0.07 TYR 255 -0.09 GLU 104

VAL 26 0.07 ARG 256 -0.07 GLU 100

SER 63 0.08 ARG 257 -0.08 GLU 100

SER 63 0.09 ARG 258 -0.09 GLU 100

SER 63 0.10 PHE 259 -0.10 GLU 104

SER 63 0.10 GLY 260 -0.09 GLU 100

VAL 26 0.08 CYS 261 -0.08 PRO 153

LEU 7 0.07 THR 262 -0.08 GLU 104

LEU 7 0.08 PRO 263 -0.10 GLU 104

LEU 7 0.08 SER 264 -0.09 GLU 104

LEU 7 0.08 ARG 265 -0.09 GLU 104

VAL 26 0.09 SER 266 -0.11 GLU 104

LEU 7 0.09 ARG 267 -0.11 GLU 104

LEU 7 0.09 GLN 268 -0.10 GLU 104

VAL 26 0.10 GLY 269 -0.11 PRO 153

TYR 24 0.12 LYS 270 -0.12 PRO 153

TYR 24 0.13 ASP 271 -0.12 PRO 153

TYR 24 0.12 GLU 272 -0.10 PRO 153

TYR 24 0.12 CYS 273 -0.10 PRO 153

ILE 45 0.15 ARG 274 -0.11 PRO 153

ILE 45 0.14 ALA 275 -0.10 GLU 100

ILE 45 0.14 LYS 276 -0.10 GLU 100

ILE 45 0.17 ASN 277 -0.11 GLU 100

ILE 45 0.18 ASN 278 -0.11 GLU 100

ILE 45 0.15 NMA 278 -0.10 GLU 98

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 10 ---

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

* EXSA_mono2 *