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

* vp2-c4 *

CA distance fluctuations for 2408010529592259715

--- normal mode 25 ---

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
ALA 15 0.25 THR 1 -0.22 LYS 28

ALA 15 0.30 ASN 2 -0.22 LYS 28

ALA 15 0.35 TYR 3 -0.23 LYS 28

ALA 15 0.42 GLU 4 -0.22 LYS 28

ALA 15 0.36 ASP 5 -0.23 LYS 28

ALA 15 0.35 VAL 6 -0.27 LYS 28

ALA 15 0.45 ILE 7 -0.28 LYS 28

ALA 15 0.51 ASP 8 -0.26 LYS 28

LYS 13 0.38 LYS 9 -0.32 LYS 28

ALA 15 0.40 TYR 10 -0.36 LYS 28

ALA 15 0.53 LYS 11 -0.29 LYS 28

ALA 15 0.40 PRO 12 -0.26 LYS 28

LYS 9 0.38 LYS 13 -0.33 LYS 28

ASP 8 0.32 ASP 14 -0.29 LYS 28

LYS 11 0.53 ALA 15 -0.19 ALA 20

LYS 11 0.43 THR 16 -0.17 HSP 19

SER 21 0.55 PHE 17 -0.16 ALA 15

PRO 12 0.36 ASP 18 -0.08 LYS 28

PRO 12 0.35 HSP 19 -0.17 THR 16

THR 31 0.34 ALA 20 -0.19 ALA 15

PHE 17 0.55 SER 21 -0.11 ALA 20

VAL 30 0.47 TYR 22 -0.17 LYS 28

VAL 30 0.61 ASP 23 -0.07 GLN 121

VAL 30 0.42 TRP 24 -0.23 ASN 60

PHE 17 0.39 ARG 25 -0.35 GLN 61

PHE 17 0.25 LEU 26 -0.47 ALA 56

PHE 17 0.15 HSP 27 -0.55 ILE 57

GLY 29 0.50 LYS 28 -0.52 ILE 57

LYS 28 0.50 GLY 29 -0.36 ILE 57

ASP 23 0.61 VAL 30 -0.30 LEU 26

ASP 23 0.48 THR 31 -0.33 LEU 26

ASP 23 0.41 PRO 32 -0.31 ASP 109

ASP 23 0.31 VAL 33 -0.34 ASP 109

PHE 17 0.26 LYS 34 -0.39 ASP 109

TYR 106 0.37 ASP 35 -0.38 ASP 109

TYR 106 0.43 GLN 36 -0.46 ASP 109

TYR 106 0.43 ALA 37 -0.59 ASP 109

TYR 106 0.36 ASN 38 -0.78 ASP 109

TYR 106 0.22 CYS 39 -1.02 ASP 109

ASP 154 0.22 GLY 40 -0.84 ASP 109

ARG 226 0.19 SER 41 -0.77 ASP 109

ARG 226 0.21 CYM 42 -0.62 ASP 109

ARG 226 0.25 TRP 43 -0.55 ASP 109

ARG 226 0.21 ALA 44 -0.54 ASP 109

TYR 106 0.21 PHE 45 -0.51 ASP 109

ARG 226 0.21 SER 46 -0.44 ASP 109

ARG 226 0.22 THR 47 -0.40 ASP 109

ARG 226 0.19 VAL 48 -0.37 ASP 109

TYR 106 0.20 GLY 49 -0.35 ASP 109

ALA 15 0.22 VAL 50 -0.36 HSP 27

ALA 15 0.21 VAL 51 -0.34 HSP 27

PHE 17 0.21 GLU 52 -0.37 HSP 27

PHE 17 0.22 SER 53 -0.45 HSP 27

PHE 17 0.23 GLN 54 -0.40 HSP 27

PHE 17 0.23 TYR 55 -0.38 HSP 27

PRO 32 0.28 ALA 56 -0.52 HSP 27

THR 31 0.39 ILE 57 -0.55 HSP 27

THR 31 0.30 ARG 58 -0.45 LYS 28

THR 31 0.26 LYS 59 -0.31 LYS 28

THR 31 0.31 ASN 60 -0.41 LEU 26

PHE 17 0.25 GLN 61 -0.39 LEU 26

PHE 17 0.25 LEU 62 -0.37 LEU 26

ASP 35 0.27 VAL 63 -0.36 LEU 26

ASP 35 0.29 SER 64 -0.35 LEU 26

GLN 36 0.24 ILE 65 -0.32 LEU 26

GLN 36 0.25 SER 66 -0.28 LEU 26

TYR 106 0.23 GLU 67 -0.42 ASP 109

ARG 226 0.16 GLN 68 -0.45 ASP 109

ARG 226 0.17 GLN 69 -0.26 ASP 109

ARG 226 0.19 MET 70 -0.38 ASP 109

ARG 226 0.18 VAL 71 -0.54 ASP 109

ARG 226 0.17 ASP 72 -0.40 PRO 111

ARG 226 0.18 CYS 73 -0.31 PRO 111

ARG 226 0.20 SER 74 -0.40 ILE 110

ARG 226 0.22 THR 75 -0.42 ILE 110

ARG 226 0.25 GLN 76 -0.48 ILE 110

ARG 226 0.25 ASN 77 -0.58 ILE 110

ARG 226 0.22 THR 78 -0.73 ILE 110

ARG 226 0.18 GLY 79 -0.94 ILE 110

ASP 154 0.19 CYS 80 -1.00 ASP 109

ARG 226 0.22 TYR 81 -0.82 ILE 110

ARG 226 0.25 GLY 82 -0.66 ASP 109

ARG 226 0.29 GLY 83 -0.58 ILE 110

ARG 226 0.32 PHE 84 -0.48 ASP 109

ARG 226 0.30 ILE 85 -0.44 ASP 109

ARG 226 0.30 PRO 86 -0.38 ASP 109

ARG 226 0.28 LEU 87 -0.40 ASP 109

ARG 226 0.25 ALA 88 -0.42 ASP 109

ARG 226 0.24 PHE 89 -0.34 ASP 109

ARG 226 0.24 GLU 90 -0.31 ASP 109

ARG 226 0.23 ASP 91 -0.32 ASP 109

ARG 226 0.21 MET 92 -0.28 ASP 109

ARG 226 0.20 ILE 93 -0.22 ASP 109

ARG 226 0.20 GLU 94 -0.21 ASP 109

ARG 226 0.18 MET 95 -0.19 LEU 26

ARG 226 0.18 GLY 96 -0.19 LEU 26

ARG 226 0.17 GLY 97 -0.23 LEU 26

ARG 226 0.17 LEU 98 -0.24 LEU 26

GLN 36 0.20 CYS 99 -0.24 ARG 25

ASP 35 0.25 SER 100 -0.27 ARG 25

GLN 36 0.32 SER 101 -0.26 LEU 26

ASP 35 0.35 GLU 102 -0.25 ARG 25

ASP 35 0.27 ASP 103 -0.24 ARG 25

GLN 36 0.26 TYR 104 -0.22 ARG 25

GLN 36 0.31 PRO 105 -0.16 ARG 25

ALA 37 0.43 TYR 106 -0.13 ARG 25

ASN 38 0.33 VAL 107 -0.19 LEU 26

PRO 105 0.27 ALA 108 -0.24 GLY 79

PRO 105 0.24 ASP 109 -1.02 CYS 39

PRO 105 0.21 ILE 110 -0.95 CYS 80

ALA 108 0.07 PRO 111 -0.49 THR 78

ILE 110 0.15 GLU 112 -0.21 THR 78

ARG 226 0.15 MET 113 -0.20 THR 75

ARG 226 0.16 CYS 114 -0.18 ARG 25

ILE 110 0.18 LYS 115 -0.17 ARG 25

ARG 226 0.15 PHE 116 -0.17 ARG 25

ILE 110 0.19 ASP 117 -0.18 ARG 25

ILE 110 0.21 ILE 118 -0.19 ARG 25

GLN 36 0.20 CYS 119 -0.21 ARG 25

ASP 35 0.18 GLU 120 -0.21 ARG 25

ASP 35 0.17 GLN 121 -0.25 ARG 25

PHE 17 0.15 LYS 122 -0.24 ARG 25

PHE 17 0.17 TYR 123 -0.25 LEU 26

LYS 13 0.17 LYS 124 -0.23 LEU 26

LYS 13 0.19 ILE 125 -0.25 HSP 27

LYS 13 0.21 ASN 126 -0.23 LYS 28

ALA 15 0.22 ASN 127 -0.24 LYS 28

ALA 15 0.23 PHE 128 -0.27 ASP 109

ALA 15 0.27 LEU 129 -0.27 ASP 109

ARG 226 0.31 GLU 130 -0.29 ASP 109

ARG 226 0.30 ILE 131 -0.28 ASP 109

ARG 226 0.36 PRO 132 -0.28 ASP 109

ARG 226 0.40 GLU 133 -0.28 ASP 109

GLY 224 0.33 ASP 134 -0.25 ASP 109

ALA 15 0.32 LYS 135 -0.25 ASP 109

ALA 15 0.30 PHE 136 -0.26 ASP 109

ALA 15 0.30 LYS 137 -0.24 ASP 109

ALA 15 0.37 GLU 138 -0.25 LYS 28

ALA 15 0.38 ALA 139 -0.28 LYS 28

ALA 15 0.33 ILE 140 -0.31 LYS 28

ALA 15 0.36 ARG 141 -0.32 LYS 28

ALA 15 0.40 PHE 142 -0.34 LYS 28

ALA 15 0.34 LEU 143 -0.36 LYS 28

THR 31 0.30 GLY 144 -0.39 LYS 28

ALA 15 0.26 PRO 145 -0.36 HSP 27

ALA 15 0.26 LEU 146 -0.32 ASP 109

ARG 226 0.26 SER 147 -0.37 ASP 109

ARG 226 0.32 VAL 148 -0.38 ASP 109

ARG 226 0.33 SER 149 -0.41 ASP 109

ARG 226 0.28 ILE 150 -0.38 ASP 109

ARG 226 0.23 ALA 151 -0.35 ASP 109

TYR 81 0.20 VAL 152 -0.35 ASP 109

TYR 106 0.21 SER 153 -0.31 ASP 109

TYR 106 0.24 ASP 154 -0.29 ASP 109

TYR 106 0.23 ASP 155 -0.29 ASP 109

TYR 106 0.23 PHE 156 -0.34 ASP 109

TYR 106 0.26 ALA 157 -0.37 ASP 109

TYR 106 0.27 PHE 158 -0.31 ASP 109

TYR 106 0.25 TYR 159 -0.30 ASP 109

TYR 106 0.26 ARG 160 -0.27 ASP 109

TYR 106 0.22 GLY 161 -0.25 ASP 109

TYR 106 0.20 GLY 162 -0.23 ASP 109

TYR 106 0.18 ILE 163 -0.24 ASP 109

TYR 106 0.19 PHE 164 -0.26 ASP 109

TYR 106 0.18 ASP 165 -0.29 ARG 226

TYR 106 0.19 GLY 166 -0.26 ASP 109

TYR 106 0.19 GLU 167 -0.25 ASP 109

TYR 106 0.18 CYS 168 -0.28 ASP 109

TYR 81 0.17 GLY 169 -0.28 ASP 109

ARG 226 0.26 GLU 170 -0.29 ASP 109

ARG 226 0.33 ALA 171 -0.33 ASP 109

ARG 226 0.36 PRO 172 -0.38 ASP 109

ARG 226 0.26 ASN 173 -0.43 ASP 109

ARG 226 0.23 HSP 174 -0.48 ASP 109

ARG 226 0.26 ALA 175 -0.48 ASP 109

ARG 226 0.20 VAL 176 -0.43 ASP 109

ALA 15 0.21 ILE 177 -0.37 ASP 109

ALA 15 0.23 LEU 178 -0.32 ASP 109

THR 16 0.24 VAL 179 -0.34 HSP 27

PRO 32 0.26 GLY 180 -0.32 HSP 27

THR 16 0.25 PHE 181 -0.26 HSP 27

PRO 32 0.25 GLY 182 -0.24 HSP 27

PRO 32 0.24 ALA 183 -0.19 HSP 27

ASP 23 0.22 GLU 184 -0.17 ARG 226

ASP 23 0.22 ASP 185 -0.20 ARG 226

ASP 23 0.19 ALA 186 -0.27 ARG 226

ASP 23 0.19 TYR 187 -0.29 ARG 226

ASP 23 0.19 ASP 188 -0.30 ARG 226

ASP 23 0.17 PHE 189 -0.32 ARG 226

ASP 23 0.18 ASP 190 -0.26 ARG 226

ASP 23 0.19 THR 191 -0.21 ARG 226

ASP 23 0.19 LYS 192 -0.23 ARG 226

ASP 23 0.21 THR 193 -0.21 ARG 226

ASP 23 0.22 MET 194 -0.22 ARG 226

ASP 23 0.22 LYS 195 -0.23 ARG 226

ASP 23 0.24 LYS 196 -0.22 ARG 226

ASP 23 0.18 ARG 197 -0.22 ARG 226

ASP 23 0.19 TYR 198 -0.20 ASP 109

THR 16 0.19 TYR 199 -0.23 ASP 109

THR 16 0.21 TYR 200 -0.26 ASP 109

THR 16 0.21 ILE 201 -0.27 ASP 109

TYR 106 0.20 VAL 202 -0.32 ASP 109

TYR 106 0.22 LYS 203 -0.36 ASP 109

TYR 106 0.26 ASN 204 -0.41 ASP 109

TYR 106 0.32 SER 205 -0.46 ASP 109

TYR 106 0.34 TRP 206 -0.54 ASP 109

TYR 106 0.36 GLY 207 -0.48 ASP 109

TYR 106 0.39 VAL 208 -0.38 ASP 109

TYR 106 0.33 SER 209 -0.30 ASP 109

TYR 106 0.30 TRP 210 -0.34 ASP 109

TYR 106 0.26 GLY 211 -0.30 ASP 109

TYR 106 0.23 GLU 212 -0.27 ASP 109

TYR 106 0.24 LYS 213 -0.31 ASP 109

TYR 106 0.28 GLY 214 -0.35 ASP 109

TYR 106 0.23 PHE 215 -0.31 ASP 109

TYR 106 0.21 ILE 216 -0.30 ASP 109

TYR 106 0.19 ARG 217 -0.26 ASP 109

TYR 106 0.18 LEU 218 -0.27 ASP 109

TYR 106 0.16 GLU 219 -0.24 ASP 109

THR 16 0.17 THR 220 -0.23 ASP 109

THR 233 0.16 ASP 221 -0.20 ASP 109

THR 16 0.17 ILE 222 -0.20 ASP 109

THR 16 0.20 ASN 223 -0.19 ASP 109

GLU 133 0.39 GLY 224 -0.19 ASP 109

THR 233 0.41 TYR 225 -0.20 PHE 189

THR 233 0.57 ARG 226 -0.32 PHE 189

LEU 231 0.25 LYS 227 -0.22 ASP 109

SER 230 0.18 PRO 228 -0.25 ASP 109

TYR 106 0.17 CYS 229 -0.28 ASP 109

ARG 226 0.31 SER 230 -0.29 ASP 109

ARG 226 0.42 LEU 231 -0.33 ASP 109

ARG 226 0.47 GLY 232 -0.35 ASP 109

ARG 226 0.57 THR 233 -0.32 ASP 109

ARG 226 0.44 GLU 234 -0.32 ASP 109

ARG 226 0.34 ALA 235 -0.33 ASP 109

ARG 226 0.29 LEU 236 -0.33 ASP 109

ALA 15 0.26 VAL 237 -0.30 ASP 109

ALA 15 0.24 ALA 238 -0.29 HSP 27

ALA 15 0.24 LEU 239 -0.29 LYS 28

LYS 13 0.23 VAL 240 -0.29 LYS 28

LYS 13 0.28 ASP 241 -0.27 LYS 28

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.

*** vp2-c4 ***

CA distance fluctuations for 2408010529592259715

--- normal mode 25 ---

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

* vp2-c4 *