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

* 1DQZ *

CA distance fluctuations for 240228060125923889

--- 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
ASP 43 0.46 ARG 1 -0.75 GLY 280

ILE 49 0.78 PRO 2 -0.56 GLY 28

ILE 49 0.51 GLY 3 -0.54 GLY 27

PRO 52 0.30 LEU 4 -0.38 GLY 27

ILE 49 0.09 PRO 5 -0.36 LEU 4

PRO 2 0.22 VAL 6 -0.07 LYS 109

PRO 2 0.22 GLU 7 -0.04 GLU 55

PRO 2 0.37 TYR 8 -0.04 GLU 55

PRO 2 0.21 LEU 9 -0.03 GLU 55

PRO 2 0.22 GLN 10 -0.02 GLU 55

PRO 2 0.10 VAL 11 -0.05 PRO 5

PRO 2 0.10 PRO 12 -0.05 ARG 1

PRO 2 0.11 SER 13 -0.06 ARG 1

PRO 2 0.07 ALA 14 -0.09 ARG 1

PRO 2 0.10 SER 15 -0.08 ARG 1

PRO 2 0.20 MET 16 -0.02 PRO 5

PRO 2 0.19 GLY 17 -0.02 PRO 221

PRO 2 0.25 ARG 18 -0.02 ASP 42

PRO 2 0.25 ASP 19 -0.02 ASP 43

PRO 2 0.28 ILE 20 -0.02 ASN 45

PRO 2 0.36 LYS 21 -0.02 GLU 55

PRO 2 0.27 VAL 22 -0.03 PRO 5

PRO 2 0.32 GLN 23 -0.03 GLU 55

PRO 2 0.10 PHE 24 -0.13 PRO 5

TYR 58 0.07 GLN 25 -0.27 PRO 5

GLN 59 0.10 GLY 26 -0.37 GLY 3

GLN 59 0.05 GLY 27 -0.54 GLY 3

SER 63 0.04 GLY 28 -0.68 ARG 1

VAL 111 0.02 PRO 29 -0.73 ARG 1

ALA 31 0.03 HIS 30 -0.61 ARG 1

HIS 30 0.03 ALA 31 -0.43 ARG 1

HIS 30 0.02 VAL 32 -0.30 ARG 1

PRO 2 0.04 TYR 33 -0.20 ARG 1

PRO 2 0.18 LEU 34 -0.06 PRO 5

PRO 2 0.25 LEU 35 -0.04 PRO 5

PRO 2 0.39 ASP 36 -0.02 GLY 26

PRO 2 0.43 GLY 37 -0.02 SER 259

PRO 2 0.45 LEU 38 -0.03 ALA 222

PRO 2 0.56 ARG 39 -0.03 ALA 222

PRO 2 0.54 ALA 40 -0.03 SER 259

PRO 2 0.65 GLN 41 -0.03 SER 259

PRO 2 0.63 ASP 42 -0.02 SER 259

PRO 2 0.74 ASP 43 -0.02 ARG 18

PRO 2 0.69 TYR 44 -0.02 LYS 21

PRO 2 0.55 ASN 45 -0.02 LYS 21

PRO 2 0.59 GLY 46 -0.02 ASN 264

PRO 2 0.48 TRP 47 -0.02 LYS 21

PRO 2 0.61 ASP 48 -0.02 PRO 52

PRO 2 0.78 ILE 49 -0.02 ASN 264

PRO 2 0.69 ASN 50 -0.03 ASN 264

PRO 2 0.55 THR 51 -0.03 VAL 268

PRO 2 0.47 PRO 52 -0.04 ALA 53

PRO 2 0.30 ALA 53 -0.04 GLN 25

PRO 2 0.24 PHE 54 -0.11 GLU 55

LEU 4 0.27 GLU 55 -0.11 PHE 54

LEU 4 0.12 GLU 56 -0.06 PRO 5

PHE 54 0.06 TYR 57 -0.18 ARG 1

PHE 54 0.09 TYR 58 -0.20 ARG 1

GLY 26 0.10 GLN 59 -0.42 GLY 3

PHE 54 0.03 SER 60 -0.44 ARG 1

ASP 214 0.02 GLY 61 -0.61 ARG 1

GLY 28 0.03 LEU 62 -0.50 ARG 1

GLN 59 0.05 SER 63 -0.39 ARG 1

GLN 59 0.05 VAL 64 -0.21 ARG 1

PRO 2 0.07 ILE 65 -0.14 ARG 1

PRO 2 0.26 MET 66 -0.05 PRO 5

PRO 2 0.28 PRO 67 -0.04 PRO 5

PRO 2 0.43 VAL 68 -0.02 ASN 45

PRO 2 0.47 GLY 69 -0.02 SER 259

PRO 2 0.40 GLY 70 -0.02 PRO 221

PRO 2 0.47 GLN 71 -0.03 PRO 221

PRO 2 0.41 SER 72 -0.03 PRO 221

PRO 2 0.33 SER 73 -0.02 PRO 221

PRO 2 0.27 PHE 74 -0.03 GLY 26

PRO 2 0.21 TYR 75 -0.04 PRO 5

PRO 2 0.17 THR 76 -0.06 ARG 1

PRO 2 0.15 ASP 77 -0.06 ARG 1

PRO 2 0.20 TRP 78 -0.03 GLY 26

PRO 2 0.18 TYR 79 -0.03 GLY 26

PRO 2 0.23 GLN 80 -0.02 PRO 221

PRO 2 0.30 PRO 81 -0.02 PRO 221

PRO 2 0.35 SER 82 -0.03 PRO 221

PRO 2 0.35 GLN 83 -0.03 PRO 221

PRO 2 0.41 SER 84 -0.03 PRO 221

PRO 2 0.46 ASN 85 -0.03 PRO 221

PRO 2 0.43 GLY 86 -0.03 PRO 221

PRO 2 0.41 GLN 87 -0.03 PRO 221

PRO 2 0.36 ASN 88 -0.02 PRO 221

PRO 2 0.29 TYR 89 -0.02 PRO 221

PRO 2 0.25 THR 90 -0.02 PRO 221

PRO 2 0.25 TYR 91 -0.02 PRO 221

PRO 2 0.16 LYS 92 -0.04 ARG 1

PRO 2 0.17 TRP 93 -0.05 ARG 1

PRO 2 0.08 GLU 94 -0.15 ARG 1

PRO 2 0.03 THR 95 -0.18 ARG 1

PRO 2 0.06 PHE 96 -0.15 ARG 1

PRO 2 0.03 LEU 97 -0.20 ARG 1

GLY 280 0.01 THR 98 -0.30 ARG 1

GLY 280 0.01 ARG 99 -0.32 ARG 1

GLN 59 0.01 GLU 100 -0.25 ARG 1

GLN 59 0.02 MET 101 -0.24 ARG 1

GLY 280 0.02 PRO 102 -0.39 ARG 1

GLY 280 0.02 ALA 103 -0.43 ARG 1

GLN 59 0.02 TRP 104 -0.35 ARG 1

GLN 59 0.03 LEU 105 -0.40 ARG 1

GLY 280 0.02 GLN 106 -0.56 ARG 1

GLN 59 0.02 ALA 107 -0.54 ARG 1

GLN 59 0.03 ASN 108 -0.44 ARG 1

GLN 59 0.04 LYS 109 -0.48 ARG 1

GLN 59 0.02 GLY 110 -0.68 ARG 1

ASN 279 0.02 VAL 111 -0.60 ARG 1

GLY 280 0.03 SER 112 -0.66 ARG 1

GLY 280 0.02 PRO 113 -0.55 ARG 1

GLY 115 0.03 THR 114 -0.60 ARG 1

THR 114 0.03 GLY 115 -0.61 ARG 1

LEU 267 0.02 ASN 116 -0.48 ARG 1

LEU 267 0.02 ALA 117 -0.37 ARG 1

ALA 53 0.01 ALA 118 -0.25 ARG 1

PRO 2 0.10 VAL 119 -0.15 ARG 1

PRO 2 0.20 GLY 120 -0.05 ARG 1

PRO 2 0.29 LEU 121 -0.03 GLY 26

PRO 2 0.33 SER 122 -0.02 GLY 26

PRO 2 0.32 MET 123 -0.02 GLY 26

PRO 2 0.25 SER 124 -0.03 GLY 26

PRO 2 0.20 GLY 125 -0.05 ARG 1

PRO 2 0.16 GLY 126 -0.08 ARG 1

PRO 2 0.15 SER 127 -0.10 ARG 1

PRO 2 0.08 ALA 128 -0.17 ARG 1

PRO 2 0.04 LEU 129 -0.21 ARG 1

PRO 2 0.04 ILE 130 -0.21 ARG 1

ALA 53 0.01 LEU 131 -0.25 ARG 1

ILE 203 0.01 ALA 132 -0.33 ARG 1

LEU 196 0.01 ALA 133 -0.32 ARG 1

THR 95 0.01 TYR 134 -0.33 ARG 1

THR 201 0.01 TYR 135 -0.39 ARG 1

THR 201 0.02 PRO 136 -0.45 ARG 1

ARG 202 0.01 GLN 137 -0.54 ARG 1

ARG 99 0.01 GLN 138 -0.48 ARG 1

TYR 141 0.01 PHE 139 -0.43 ARG 1

GLN 137 0.01 PRO 140 -0.49 ARG 1

GLN 137 0.01 TYR 141 -0.40 ARG 1

ALA 53 0.01 ALA 142 -0.29 ARG 1

PRO 2 0.05 ALA 143 -0.20 ARG 1

PRO 2 0.14 SER 144 -0.11 ARG 1

PRO 2 0.22 LEU 145 -0.03 PRO 5

PRO 2 0.27 SER 146 -0.02 GLY 26

PRO 2 0.24 GLY 147 -0.03 GLY 26

PRO 2 0.24 PHE 148 -0.03 GLY 26

PRO 2 0.17 LEU 149 -0.06 ARG 1

PRO 2 0.17 ASN 150 -0.06 ARG 1

PRO 2 0.21 PRO 151 -0.03 GLY 26

PRO 2 0.18 SER 152 -0.03 ARG 1

PRO 2 0.19 GLU 153 -0.02 GLY 26

PRO 2 0.22 SER 154 -0.02 GLY 26

PRO 2 0.27 TRP 155 -0.02 GLY 26

PRO 2 0.27 TRP 156 -0.02 GLY 26

PRO 2 0.27 PRO 157 -0.02 GLY 26

PRO 2 0.31 THR 158 -0.01 GLY 26

PRO 2 0.35 LEU 159 -0.02 PHE 224

PRO 2 0.34 ILE 160 -0.02 PHE 224

PRO 2 0.35 GLY 161 -0.03 PRO 221

PRO 2 0.41 LEU 162 -0.03 PRO 221

PRO 2 0.43 ALA 163 -0.05 PRO 221

PRO 2 0.42 MET 164 -0.04 PRO 221

PRO 2 0.45 ASN 165 -0.04 PRO 221

PRO 2 0.51 ASP 166 -0.06 PRO 221

PRO 2 0.53 SER 167 -0.05 PRO 221

PRO 2 0.54 GLY 168 -0.04 PRO 221

PRO 2 0.49 GLY 169 -0.04 PRO 221

PRO 2 0.42 TYR 170 -0.03 PRO 221

PRO 2 0.36 ASN 171 -0.03 PRO 221

PRO 2 0.31 ALA 172 -0.02 PRO 221

PRO 2 0.28 ASN 173 -0.02 PRO 221

PRO 2 0.27 SER 174 -0.02 PRO 221

PRO 2 0.25 MET 175 -0.02 GLY 26

PRO 2 0.20 TRP 176 -0.03 GLY 26

PRO 2 0.21 GLY 177 -0.02 GLY 26

PRO 2 0.22 PRO 178 -0.02 GLY 26

PRO 2 0.21 SER 179 -0.02 GLY 26

PRO 2 0.17 SER 180 -0.03 ARG 1

PRO 2 0.15 ASP 181 -0.05 ARG 1

PRO 2 0.10 PRO 182 -0.11 ARG 1

PRO 2 0.12 ALA 183 -0.09 ARG 1

PRO 2 0.15 TRP 184 -0.06 ARG 1

PRO 2 0.11 LYS 185 -0.12 ARG 1

PRO 2 0.07 ARG 186 -0.16 ARG 1

PRO 2 0.11 ASN 187 -0.12 ARG 1

PRO 2 0.12 ASP 188 -0.11 ARG 1

PRO 2 0.08 PRO 189 -0.16 ARG 1

PRO 2 0.08 MET 190 -0.15 ARG 1

PRO 2 0.06 VAL 191 -0.18 ARG 1

PRO 2 0.01 GLN 192 -0.23 ARG 1

ALA 53 0.01 ILE 193 -0.26 ARG 1

SER 15 0.01 PRO 194 -0.31 ARG 1

SER 15 0.01 ARG 195 -0.34 ARG 1

ALA 133 0.01 LEU 196 -0.35 ARG 1

THR 95 0.01 VAL 197 -0.38 ARG 1

SER 15 0.01 ALA 198 -0.43 ARG 1

THR 95 0.01 ASN 199 -0.46 ARG 1

VAL 249 0.01 ASN 200 -0.46 ARG 1

PRO 136 0.02 THR 201 -0.43 ARG 1

PRO 136 0.02 ARG 202 -0.41 ARG 1

PRO 136 0.01 ILE 203 -0.31 ARG 1

ALA 53 0.02 TRP 204 -0.24 ARG 1

PRO 2 0.09 VAL 205 -0.15 ARG 1

PRO 2 0.16 TYR 206 -0.07 ARG 1

PRO 2 0.22 CYS 207 -0.02 GLY 26

PRO 2 0.27 GLY 208 -0.02 ASP 166

PRO 2 0.29 ASN 209 -0.03 ASP 166

PRO 2 0.36 GLY 210 -0.03 ASP 166

PRO 2 0.37 THR 211 -0.03 ASP 166

PRO 2 0.42 PRO 212 -0.03 ASP 166

PRO 2 0.39 SER 213 -0.02 ASP 166

PRO 2 0.44 ASP 214 -0.02 ASP 166

PRO 2 0.46 LEU 215 -0.02 GLN 41

PRO 2 0.54 GLY 216 -0.02 SER 167

PRO 2 0.55 GLY 217 -0.03 SER 167

PRO 2 0.54 ASP 218 -0.03 ASP 166

PRO 2 0.56 ASN 219 -0.04 ASP 166

PRO 2 0.51 ILE 220 -0.05 ASP 166

PRO 2 0.51 PRO 221 -0.06 ASP 166

PRO 2 0.49 ALA 222 -0.04 ASP 166

PRO 2 0.44 LYS 223 -0.04 ASP 166

PRO 2 0.41 PHE 224 -0.04 ASP 166

PRO 2 0.39 LEU 225 -0.04 ALA 163

PRO 2 0.35 GLU 226 -0.03 ALA 163

PRO 2 0.32 GLY 227 -0.03 ALA 163

PRO 2 0.32 LEU 228 -0.03 ALA 163

PRO 2 0.28 THR 229 -0.03 ALA 163

PRO 2 0.24 LEU 230 -0.02 ALA 163

PRO 2 0.21 ARG 231 -0.02 GLY 26

PRO 2 0.19 THR 232 -0.03 ARG 1

PRO 2 0.16 ASN 233 -0.06 ARG 1

PRO 2 0.13 GLN 234 -0.09 ARG 1

PRO 2 0.11 THR 235 -0.10 ARG 1

PRO 2 0.09 PHE 236 -0.14 ARG 1

PRO 2 0.05 ARG 237 -0.18 ARG 1

PRO 2 0.04 ASP 238 -0.18 ARG 1

PRO 2 0.03 THR 239 -0.20 ARG 1

ALA 53 0.01 TYR 240 -0.25 ARG 1

ALA 53 0.01 ALA 241 -0.28 ARG 1

ALA 53 0.01 ALA 242 -0.26 ARG 1

ALA 53 0.01 ASP 243 -0.30 ARG 1

PRO 253 0.01 GLY 244 -0.35 ARG 1

PRO 253 0.01 GLY 245 -0.35 ARG 1

PRO 253 0.01 ARG 246 -0.39 ARG 1

PRO 136 0.01 ASN 247 -0.40 ARG 1

VAL 249 0.02 GLY 248 -0.32 ARG 1

GLY 248 0.02 VAL 249 -0.27 ARG 1

PRO 2 0.05 PHE 250 -0.18 ARG 1

PRO 2 0.10 ASN 251 -0.12 ARG 1

PRO 2 0.16 PHE 252 -0.05 ARG 1

PRO 2 0.19 PRO 253 -0.02 ASP 166

PRO 2 0.23 PRO 254 -0.02 ASP 166

PRO 2 0.30 ASN 255 -0.02 ASP 166

PRO 2 0.34 GLY 256 -0.02 ASP 166

PRO 2 0.41 THR 257 -0.03 ASP 166

PRO 2 0.42 HIS 258 -0.03 SER 167

PRO 2 0.49 SER 259 -0.03 ARG 39

PRO 2 0.50 TRP 260 -0.02 GLN 41

PRO 2 0.47 PRO 261 -0.02 GLN 41

PRO 2 0.36 TYR 262 -0.02 GLN 41

PRO 2 0.33 TRP 263 -0.02 GLN 41

PRO 2 0.33 ASN 264 -0.03 ASN 50

PRO 2 0.26 GLU 265 -0.03 ASN 50

PRO 2 0.18 GLN 266 -0.05 ARG 1

PRO 2 0.15 LEU 267 -0.08 ARG 1

PRO 2 0.10 VAL 268 -0.10 ARG 1

PRO 2 0.05 ALA 269 -0.16 ARG 1

ASP 273 0.02 MET 270 -0.24 ARG 1

VAL 268 0.02 LYS 271 -0.30 ARG 1

ASP 214 0.02 ALA 272 -0.40 ARG 1

MET 270 0.02 ASP 273 -0.42 ARG 1

LEU 267 0.02 ILE 274 -0.44 ARG 1

ASN 279 0.03 GLN 275 -0.54 ARG 1

SER 112 0.02 HIS 276 -0.59 ARG 1

THR 114 0.02 VAL 277 -0.58 ARG 1

THR 114 0.02 LEU 278 -0.63 ARG 1

GLN 275 0.03 ASN 279 -0.74 ARG 1

SER 112 0.03 GLY 280 -0.75 ARG 1

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.

*** 1DQZ ***

CA distance fluctuations for 240228060125923889

--- normal mode 7 ---

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

* 1DQZ *