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

* vp2-c4 *

CA distance fluctuations for 2408010529592259715

--- normal mode 31 ---

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 20 0.35 THR 1 -0.16 ARG 226

ALA 20 0.36 ASN 2 -0.16 GLU 170

ALA 20 0.38 TYR 3 -0.17 GLU 170

ALA 20 0.40 GLU 4 -0.15 GLU 170

ALA 20 0.42 ASP 5 -0.15 GLU 170

ALA 20 0.47 VAL 6 -0.16 ALA 15

ALA 20 0.49 ILE 7 -0.20 ALA 15

ALA 20 0.51 ASP 8 -0.24 ALA 15

ALA 20 0.61 LYS 9 -0.25 ALA 15

ALA 20 0.63 TYR 10 -0.26 ALA 15

ALA 20 0.55 LYS 11 -0.36 ALA 15

ALA 20 0.62 PRO 12 -0.40 ALA 15

ALA 20 0.60 LYS 13 -0.25 LEU 26

HSP 19 0.33 ASP 14 -0.25 TYR 22

ALA 20 0.17 ALA 15 -0.40 PRO 12

TYR 106 0.13 THR 16 -0.28 TYR 22

TYR 106 0.15 PHE 17 -0.39 TYR 22

TYR 106 0.26 ASP 18 -0.03 THR 16

PRO 12 0.52 HSP 19 -0.06 ARG 25

TYR 10 0.63 ALA 20 -0.10 PHE 17

ARG 58 0.44 SER 21 -0.25 PHE 17

ARG 58 0.44 TYR 22 -0.39 PHE 17

TYR 106 0.28 ASP 23 -0.29 PHE 17

TYR 106 0.25 TRP 24 -0.27 ALA 15

TYR 106 0.18 ARG 25 -0.23 LYS 13

TYR 106 0.20 LEU 26 -0.25 LYS 13

TYR 106 0.28 HSP 27 -0.23 ALA 15

TYR 22 0.32 LYS 28 -0.17 ALA 15

TYR 106 0.30 GLY 29 -0.16 LYS 213

TYR 106 0.31 VAL 30 -0.23 LEU 62

TYR 106 0.36 THR 31 -0.25 LEU 62

TYR 106 0.45 PRO 32 -0.13 VAL 208

TYR 106 0.52 VAL 33 -0.18 VAL 30

TYR 106 0.66 LYS 34 -0.25 ASP 35

TYR 106 0.65 ASP 35 -0.25 SER 64

TYR 106 0.62 GLN 36 -0.23 SER 64

TYR 106 0.68 ALA 37 -0.22 SER 64

TYR 106 0.47 ASN 38 -0.26 ILE 110

VAL 107 0.51 CYS 39 -0.25 ILE 110

TYR 106 0.42 GLY 40 -0.21 ILE 110

TYR 106 0.50 SER 41 -0.13 ILE 110

TYR 106 0.52 CYM 42 -0.14 ALA 157

TYR 106 0.47 TRP 43 -0.12 ALA 157

TYR 106 0.56 ALA 44 -0.12 TRP 206

TYR 106 0.69 PHE 45 -0.15 VAL 48

TYR 106 0.58 SER 46 -0.14 ALA 157

TYR 106 0.52 THR 47 -0.12 ALA 157

TYR 106 0.62 VAL 48 -0.15 PHE 45

TYR 106 0.66 GLY 49 -0.18 SER 205

TYR 106 0.55 VAL 50 -0.15 ALA 15

TYR 106 0.50 VAL 51 -0.15 SER 205

TYR 106 0.56 GLU 52 -0.19 SER 205

TYR 106 0.53 SER 53 -0.19 SER 205

ALA 20 0.44 GLN 54 -0.18 ALA 15

ALA 20 0.41 TYR 55 -0.18 ALA 15

TYR 106 0.43 ALA 56 -0.19 GLY 214

ALA 20 0.50 ILE 57 -0.22 ALA 15

ALA 20 0.58 ARG 58 -0.23 ALA 15

ALA 20 0.46 LYS 59 -0.24 ALA 15

ALA 20 0.38 ASN 60 -0.26 ALA 15

TYR 106 0.34 GLN 61 -0.20 ALA 15

TYR 106 0.38 LEU 62 -0.25 THR 31

TYR 106 0.41 VAL 63 -0.22 ASP 35

TYR 106 0.59 SER 64 -0.25 ASP 35

TYR 106 0.63 ILE 65 -0.21 ALA 37

TYR 106 0.77 SER 66 -0.18 ALA 37

TYR 106 0.79 GLU 67 -0.18 ALA 37

TYR 106 0.61 GLN 68 -0.24 SER 101

TYR 106 0.42 GLN 69 -0.11 ASN 38

TYR 106 0.43 MET 70 -0.12 ALA 37

TYR 106 0.39 VAL 71 -0.13 GLU 67

ALA 20 0.21 ASP 72 -0.10 SER 101

ALA 20 0.22 CYS 73 -0.08 SER 209

ALA 20 0.23 SER 74 -0.08 GLY 207

ALA 20 0.22 THR 75 -0.13 MET 113

ALA 20 0.23 GLN 76 -0.09 MET 113

TYR 106 0.25 ASN 77 -0.09 ARG 226

TYR 106 0.22 THR 78 -0.11 ILE 110

ASP 109 0.30 GLY 79 -0.20 ILE 110

VAL 107 0.38 CYS 80 -0.23 ILE 110

VAL 107 0.30 TYR 81 -0.18 ILE 110

TYR 106 0.34 GLY 82 -0.13 ILE 110

TYR 106 0.32 GLY 83 -0.12 ARG 226

TYR 106 0.32 PHE 84 -0.12 ARG 226

TYR 106 0.39 ILE 85 -0.15 ARG 226

TYR 106 0.33 PRO 86 -0.13 ARG 226

TYR 106 0.27 LEU 87 -0.10 ARG 226

TYR 106 0.34 ALA 88 -0.11 ARG 226

TYR 106 0.35 PHE 89 -0.12 ARG 226

ALA 20 0.27 GLU 90 -0.10 ARG 226

ALA 20 0.25 ASP 91 -0.09 ARG 226

TYR 106 0.29 MET 92 -0.09 GLY 207

ALA 20 0.27 ILE 93 -0.09 LEU 26

ALA 20 0.23 GLU 94 -0.10 ASP 117

ALA 20 0.23 MET 95 -0.11 ASP 117

ALA 20 0.24 GLY 96 -0.11 LEU 26

ALA 20 0.27 GLY 97 -0.11 LEU 26

TYR 106 0.32 LEU 98 -0.13 ALA 37

TYR 106 0.27 CYS 99 -0.14 ALA 37

TYR 106 0.36 SER 100 -0.19 ASP 35

TYR 106 0.62 SER 101 -0.24 GLN 68

PRO 105 0.30 GLU 102 -0.28 VAL 107

ALA 20 0.22 ASP 103 -0.28 VAL 107

ALA 20 0.23 TYR 104 -0.30 VAL 107

SER 66 0.48 PRO 105 -0.26 CYS 119

GLU 67 0.79 TYR 106 -0.31 ASP 109

CYS 39 0.51 VAL 107 -0.30 TYR 104

CYS 39 0.24 ALA 108 -0.30 ASP 109

CYS 80 0.34 ASP 109 -0.31 TYR 106

LYS 115 0.20 ILE 110 -0.26 ASN 38

ALA 20 0.16 PRO 111 -0.16 ALA 108

ALA 20 0.20 GLU 112 -0.10 TYR 106

ALA 20 0.19 MET 113 -0.13 THR 75

ALA 20 0.22 CYS 114 -0.12 THR 75

ILE 110 0.20 LYS 115 -0.14 PRO 105

ALA 20 0.19 PHE 116 -0.16 PRO 105

ALA 20 0.17 ASP 117 -0.16 PRO 105

ALA 20 0.19 ILE 118 -0.23 PRO 105

ALA 20 0.20 CYS 119 -0.26 PRO 105

ALA 20 0.18 GLU 120 -0.23 PRO 105

ALA 20 0.22 GLN 121 -0.18 LEU 26

ALA 20 0.24 LYS 122 -0.16 LEU 26

ALA 20 0.29 TYR 123 -0.14 GLN 36

ALA 20 0.31 LYS 124 -0.13 SER 205

ALA 20 0.35 ILE 125 -0.13 ALA 15

ALA 20 0.36 ASN 126 -0.11 ARG 226

ALA 20 0.36 ASN 127 -0.14 ARG 226

ALA 20 0.37 PHE 128 -0.15 ARG 226

ALA 20 0.37 LEU 129 -0.18 ARG 226

TYR 106 0.35 GLU 130 -0.21 ARG 226

TYR 106 0.37 ILE 131 -0.23 ARG 226

TYR 106 0.34 PRO 132 -0.27 ARG 226

TYR 106 0.35 GLU 133 -0.33 ARG 226

ASN 223 0.41 ASP 134 -0.28 GLU 170

TYR 106 0.35 LYS 135 -0.23 GLU 170

TYR 106 0.38 PHE 136 -0.24 GLU 170

TYR 106 0.38 LYS 137 -0.22 GLU 170

ALA 20 0.41 GLU 138 -0.20 GLU 170

ALA 20 0.42 ALA 139 -0.19 GLU 170

TYR 106 0.42 ILE 140 -0.18 GLU 170

ALA 20 0.45 ARG 141 -0.19 ALA 15

ALA 20 0.53 PHE 142 -0.23 ALA 15

ALA 20 0.49 LEU 143 -0.21 ALA 15

TYR 106 0.45 GLY 144 -0.20 ALA 15

TYR 106 0.50 PRO 145 -0.18 ALA 15

TYR 106 0.48 LEU 146 -0.18 ARG 226

TYR 106 0.48 SER 147 -0.17 ARG 226

TYR 106 0.44 VAL 148 -0.22 ARG 226

TYR 106 0.41 SER 149 -0.24 ARG 226

TYR 106 0.39 ILE 150 -0.27 ARG 226

TYR 106 0.35 ALA 151 -0.37 ARG 226

TYR 106 0.36 VAL 152 -0.34 ARG 226

TYR 106 0.32 SER 153 -0.26 ARG 226

TYR 106 0.28 ASP 154 -0.18 ARG 226

TYR 106 0.29 ASP 155 -0.15 PRO 228

TYR 106 0.35 PHE 156 -0.15 ARG 226

TYR 106 0.34 ALA 157 -0.16 ARG 226

TYR 106 0.29 PHE 158 -0.18 ILE 110

TYR 106 0.31 TYR 159 -0.15 ILE 110

TYR 106 0.29 ARG 160 -0.17 ILE 110

TYR 106 0.29 GLY 161 -0.14 ILE 110

TYR 106 0.28 GLY 162 -0.13 ALA 56

TYR 106 0.29 ILE 163 -0.11 TRP 24

TYR 106 0.31 PHE 164 -0.12 ASP 221

TYR 106 0.27 ASP 165 -0.16 ASP 221

TYR 106 0.27 GLY 166 -0.16 ASP 221

TYR 106 0.27 GLU 167 -0.24 PRO 228

TYR 106 0.30 CYS 168 -0.31 ARG 226

TYR 106 0.33 GLY 169 -0.58 ARG 226

TYR 106 0.30 GLU 170 -0.77 ARG 226

TYR 106 0.34 ALA 171 -0.52 ARG 226

TYR 106 0.36 PRO 172 -0.38 ARG 226

TYR 106 0.38 ASN 173 -0.27 ARG 226

TYR 106 0.44 HSP 174 -0.21 ARG 226

TYR 106 0.47 ALA 175 -0.18 ARG 226

TYR 106 0.50 VAL 176 -0.16 ARG 226

TYR 106 0.55 ILE 177 -0.16 ARG 226

TYR 106 0.48 LEU 178 -0.17 SER 230

TYR 106 0.50 VAL 179 -0.19 ALA 15

TYR 106 0.44 GLY 180 -0.18 ALA 15

TYR 106 0.41 PHE 181 -0.15 GLU 170

TYR 106 0.38 GLY 182 -0.15 THR 16

TYR 106 0.35 ALA 183 -0.14 ASP 190

TYR 106 0.32 GLU 184 -0.11 THR 16

ARG 226 0.34 ASP 185 -0.11 THR 16

ARG 226 0.39 ALA 186 -0.15 PHE 189

ARG 226 0.39 TYR 187 -0.14 THR 193

ARG 226 0.36 ASP 188 -0.23 ASN 223

TYR 106 0.20 PHE 189 -0.32 ASN 223

TYR 106 0.18 ASP 190 -0.42 ASN 223

ARG 226 0.24 THR 191 -0.24 ASN 223

THR 193 0.29 LYS 192 -0.16 ASN 223

ARG 226 0.33 THR 193 -0.14 TYR 187

ARG 226 0.39 MET 194 -0.06 TYR 187

ARG 226 0.43 LYS 195 -0.11 THR 16

ARG 226 0.39 LYS 196 -0.14 PHE 189

ARG 226 0.35 ARG 197 -0.24 PHE 189

TYR 106 0.35 TYR 198 -0.23 ASP 190

TYR 106 0.37 TYR 199 -0.16 ASP 190

TYR 106 0.41 TYR 200 -0.15 ASP 190

TYR 106 0.43 ILE 201 -0.15 THR 16

TYR 106 0.47 VAL 202 -0.16 ALA 15

TYR 106 0.52 LYS 203 -0.19 SER 53

TYR 106 0.54 ASN 204 -0.19 SER 53

TYR 106 0.63 SER 205 -0.19 SER 53

TYR 106 0.56 TRP 206 -0.17 SER 64

TYR 106 0.44 GLY 207 -0.20 ILE 110

TYR 106 0.41 VAL 208 -0.19 ILE 110

TYR 106 0.33 SER 209 -0.20 ILE 110

TYR 106 0.37 TRP 210 -0.17 ILE 110

TYR 106 0.36 GLY 211 -0.16 ALA 56

TYR 106 0.35 GLU 212 -0.17 ALA 56

TYR 106 0.43 LYS 213 -0.18 ALA 56

TYR 106 0.47 GLY 214 -0.19 ALA 56

TYR 106 0.44 PHE 215 -0.18 ALA 56

TYR 106 0.39 ILE 216 -0.15 ILE 57

TYR 106 0.37 ARG 217 -0.14 THR 16

TYR 106 0.36 LEU 218 -0.13 ASP 190

TYR 106 0.34 GLU 219 -0.21 ASP 190

TYR 106 0.34 THR 220 -0.26 ASP 190

TYR 106 0.31 ASP 221 -0.35 ASP 190

TYR 106 0.32 ILE 222 -0.38 ASP 190

ASP 134 0.41 ASN 223 -0.42 ASP 190

TYR 106 0.31 GLY 224 -0.29 GLU 170

TYR 106 0.26 TYR 225 -0.41 GLU 170

LYS 195 0.43 ARG 226 -0.77 GLU 170

TYR 106 0.26 LYS 227 -0.43 GLU 170

TYR 106 0.26 PRO 228 -0.31 GLY 169

TYR 106 0.30 CYS 229 -0.26 PRO 228

TYR 106 0.31 SER 230 -0.43 ARG 226

TYR 106 0.36 LEU 231 -0.37 ARG 226

TYR 106 0.37 GLY 232 -0.37 ARG 226

TYR 106 0.36 THR 233 -0.41 ARG 226

TYR 106 0.37 GLU 234 -0.29 ARG 226

TYR 106 0.40 ALA 235 -0.23 ARG 226

TYR 106 0.41 LEU 236 -0.19 ARG 226

TYR 106 0.43 VAL 237 -0.17 ARG 226

TYR 106 0.41 ALA 238 -0.15 ARG 226

ALA 20 0.43 LEU 239 -0.15 ALA 15

ALA 20 0.43 VAL 240 -0.17 ALA 15

ALA 20 0.46 ASP 241 -0.17 ALA 15

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 31 ---

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

* vp2-c4 *