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

* COMPLEX (BINDING PROTEIN/PEPTIDE) 17-MAY-97 1WDN *

CA distance fluctuations for 2402060933351647297

--- normal mode 11 ---

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 126 0.18 LYS 4 -1.17 ASP 22

ALA 126 0.20 LEU 5 -1.11 LEU 23

ASP 122 0.19 VAL 6 -1.06 LEU 23

LYS 226 0.24 VAL 7 -0.99 LEU 23

LYS 226 0.28 ALA 8 -0.67 LEU 23

LYS 226 0.27 THR 9 -0.49 LEU 23

LYS 226 0.29 ASP 10 -0.17 LEU 23

LYS 226 0.23 THR 11 -0.13 ARG 75

LYS 19 0.49 ALA 12 -0.10 VAL 14

PHE 18 0.44 PHE 13 -0.09 TYR 163

GLN 20 0.57 VAL 14 -0.10 ALA 12

GLN 20 0.41 PRO 15 -0.07 ALA 12

PHE 18 0.30 PHE 16 -0.18 LEU 23

PHE 18 0.30 GLU 17 -0.17 GLY 26

VAL 14 0.45 PHE 18 -0.22 GLU 44

ASP 140 0.71 LYS 19 -0.62 GLU 44

ALA 168 1.20 GLN 20 -0.75 GLU 44

ALA 168 1.15 GLY 21 -0.88 ASP 42

ALA 168 0.91 ASP 22 -1.22 ASP 42

ALA 168 0.61 LEU 23 -1.44 TYR 43

ALA 168 0.31 TYR 24 -0.74 LEU 45

ALA 168 0.27 VAL 25 -0.44 ASP 30

PHE 164 0.12 GLY 26 -0.33 VAL 25

PHE 18 0.14 PHE 27 -0.36 LEU 23

LYS 226 0.19 ASP 28 -0.50 LEU 23

GLU 17 0.14 VAL 29 -0.71 LEU 23

VAL 104 0.12 ASP 30 -0.76 LEU 23

ILE 128 0.13 LEU 31 -0.70 LEU 23

ASP 28 0.16 TRP 32 -0.94 LEU 23

ASP 28 0.13 ALA 33 -1.09 LEU 23

ILE 128 0.14 ALA 34 -0.88 LEU 23

ALA 126 0.15 ILE 35 -0.89 LEU 23

ALA 126 0.15 ALA 36 -1.08 LEU 23

ALA 126 0.14 LYS 37 -0.97 LEU 23

ALA 126 0.15 GLU 38 -0.81 LEU 23

ALA 126 0.15 LEU 39 -0.86 LEU 23

ALA 126 0.15 LYS 40 -0.94 LEU 23

ALA 126 0.16 LEU 41 -1.09 LEU 23

ALA 126 0.16 ASP 42 -1.26 LEU 23

ALA 126 0.17 TYR 43 -1.44 LEU 23

ASP 122 0.15 GLU 44 -1.40 LEU 23

LYS 46 0.17 LEU 45 -1.09 LEU 23

LYS 226 0.19 LYS 46 -0.65 LEU 23

LYS 226 0.21 PRO 47 -0.30 LEU 23

LYS 226 0.25 MET 48 -0.19 TYR 24

LYS 226 0.30 ASP 49 -0.18 ARG 75

LYS 226 0.37 PHE 50 -0.20 ARG 75

LYS 226 0.39 SER 51 -0.24 ARG 75

LYS 226 0.35 GLY 52 -0.24 LEU 23

LYS 226 0.38 ILE 53 -0.39 LEU 23

LYS 226 0.47 ILE 54 -0.42 LEU 23

LYS 226 0.41 PRO 55 -0.40 LEU 23

LYS 226 0.36 ALA 56 -0.52 LEU 23

LYS 226 0.40 LEU 57 -0.60 LEU 23

LYS 226 0.43 GLN 58 -0.52 LEU 23

LYS 226 0.36 THR 59 -0.53 LEU 23

LYS 226 0.34 LYS 60 -0.65 LEU 23

LYS 226 0.28 ASN 61 -0.66 LEU 23

LYS 226 0.28 VAL 62 -0.76 LEU 23

LYS 226 0.29 ASP 63 -0.86 LEU 23

LYS 226 0.34 LEU 64 -0.82 LEU 23

LYS 226 0.36 ALA 65 -0.72 LEU 23

LYS 226 0.37 LEU 66 -0.59 LEU 23

LYS 226 0.39 ALA 67 -0.36 LEU 23

LYS 226 0.51 GLY 68 -0.29 LEU 23

LYS 226 0.59 ILE 69 -0.33 LEU 23

LYS 226 0.74 THR 70 -0.27 LEU 23

LYS 226 0.82 ILE 71 -0.34 LEU 23

LYS 226 0.88 THR 72 -0.28 LEU 23

LYS 226 0.85 ASP 73 -0.33 LEU 23

LYS 226 0.77 GLU 74 -0.29 LEU 23

LYS 226 0.68 ARG 75 -0.37 LEU 23

LYS 226 0.71 LYS 76 -0.42 LEU 23

LYS 226 0.64 LYS 77 -0.41 LEU 23

LYS 226 0.57 ALA 78 -0.44 LEU 23

LYS 226 0.55 ILE 79 -0.52 LEU 23

LYS 226 0.55 ASP 80 -0.56 LEU 23

LYS 226 0.61 PHE 81 -0.54 LEU 23

LYS 226 0.55 SER 82 -0.58 LEU 23

LYS 226 0.66 ASP 83 -0.50 LEU 23

LYS 226 0.72 GLY 84 -0.43 LEU 23

LYS 226 0.62 TYR 85 -0.43 LEU 23

PRO 225 0.78 TYR 86 -0.32 LEU 23

LYS 226 1.09 LYS 87 -0.24 LEU 23

LYS 226 0.94 SER 88 -0.13 LEU 23

LYS 226 0.89 GLY 89 -0.13 ALA 182

LYS 226 0.76 LEU 90 -0.07 HIS 156

LYS 226 0.64 LEU 91 -0.06 ASP 178

GLY 21 0.58 VAL 92 -0.10 ALA 124

GLY 21 0.69 MET 93 -0.07 ASN 127

GLY 21 0.74 VAL 94 -0.08 ASN 127

GLY 21 0.82 LYS 95 -0.07 ASN 127

GLY 21 0.81 ALA 96 -0.07 LYS 102

GLY 21 0.74 ASN 97 -0.06 LYS 102

GLY 21 0.70 ASN 98 -0.05 ASN 127

GLY 21 0.62 ASN 99 -0.06 ASP 108

GLY 21 0.58 ASP 100 -0.07 ASP 108

GLY 21 0.58 VAL 101 -0.05 ASN 127

GLY 21 0.53 LYS 102 -0.07 ALA 96

LYS 226 0.62 SER 103 -0.08 ASN 127

LYS 226 0.66 VAL 104 -0.10 ASN 127

LYS 226 0.60 LYS 105 -0.08 ASN 127

LYS 226 0.56 ASP 106 -0.05 LYS 95

LYS 226 0.61 LEU 107 -0.06 LYS 129

LYS 226 0.54 ASP 108 -0.07 ASP 100

GLY 21 0.49 GLY 109 -0.06 ASN 149

GLY 21 0.55 LYS 110 -0.05 ASN 149

GLY 21 0.59 VAL 111 -0.05 ALA 151

GLY 21 0.59 VAL 112 -0.07 ASN 127

GLY 21 0.63 ALA 113 -0.06 ALA 124

GLY 21 0.55 VAL 114 -0.06 ASP 178

GLY 21 0.50 LYS 115 -0.07 GLU 181

LYS 226 0.42 SER 116 -0.11 GLU 74

LYS 226 0.47 GLY 117 -0.18 GLU 74

LYS 226 0.54 THR 118 -0.09 ASP 73

LYS 226 0.65 GLY 119 -0.09 GLU 181

LYS 226 0.61 SER 120 -0.10 GLU 181

LYS 226 0.56 VAL 121 -0.07 GLU 181

LYS 226 0.63 ASP 122 -0.07 LEU 180

LYS 226 0.70 TYR 123 -0.08 ASP 178

LYS 226 0.62 ALA 124 -0.10 VAL 92

LYS 226 0.60 LYS 125 -0.08 GLY 177

LYS 226 0.67 ALA 126 -0.10 GLY 177

LYS 226 0.70 ASN 127 -0.12 GLY 177

LYS 226 0.64 ILE 128 -0.06 LYS 105

LYS 226 0.57 LYS 129 -0.06 LEU 107

LYS 226 0.53 THR 130 -0.04 ASN 149

GLY 21 0.49 LYS 131 -0.05 ARG 150

GLY 21 0.51 ASP 132 -0.04 THR 130

GLY 21 0.52 LEU 133 -0.05 ASN 127

GLY 21 0.56 ARG 134 -0.05 ASN 127

GLY 21 0.52 GLN 135 -0.06 ASP 178

GLY 21 0.56 PHE 136 -0.07 ARG 75

GLY 21 0.46 PRO 137 -0.14 ARG 75

GLY 21 0.56 ASN 138 -0.10 ARG 75

GLY 21 0.68 ILE 139 -0.06 ALA 182

GLY 21 0.90 ASP 140 -0.06 ARG 75

GLY 21 0.83 ASN 141 -0.06 ARG 75

GLY 21 0.78 ALA 142 -0.05 ASP 178

GLY 21 0.92 TYR 143 -0.05 ASN 127

GLY 21 1.00 MET 144 -0.04 ASN 127

GLY 21 0.84 GLU 145 -0.05 ASN 127

GLY 21 0.85 LEU 146 -0.06 ASP 152

GLY 21 0.97 GLY 147 -0.05 ASN 127

GLY 21 0.91 THR 148 -0.04 GLY 109

GLY 21 0.81 ASN 149 -0.06 GLY 109

GLY 21 0.74 ARG 150 -0.05 GLY 109

GLY 21 0.70 ALA 151 -0.06 ASN 127

GLY 21 0.67 ASP 152 -0.06 ASN 127

GLY 21 0.68 ALA 153 -0.08 ASN 127

GLY 21 0.67 VAL 154 -0.08 ALA 124

GLY 21 0.56 LEU 155 -0.08 ASP 178

LYS 226 0.55 HIS 156 -0.08 GLU 181

LYS 226 0.61 ASP 157 -0.08 ALA 182

LYS 226 0.62 THR 158 -0.05 ALA 182

PRO 225 0.48 PRO 159 -0.05 LYS 166

GLN 20 0.59 ASN 160 -0.09 LEU 162

GLN 20 0.67 ILE 161 -0.05 ILE 139

GLN 20 0.60 LEU 162 -0.09 PHE 164

GLN 20 0.69 TYR 163 -0.09 PHE 13

GLN 20 0.94 PHE 164 -0.09 LEU 162

GLY 21 0.83 ILE 165 -0.05 LEU 162

GLN 20 0.76 LYS 166 -0.09 LEU 162

GLN 20 0.97 THR 167 -0.06 LEU 162

GLN 20 1.20 ALA 168 -0.05 LEU 162

GLY 21 1.09 GLY 169 -0.04 ASN 127

GLY 21 0.99 ASN 170 -0.05 LYS 174

GLY 21 0.94 GLY 171 -0.06 ASN 127

GLY 21 0.99 GLN 172 -0.06 ASN 127

GLY 21 0.88 PHE 173 -0.07 ASN 127

GLY 21 0.74 LYS 174 -0.07 ASN 127

GLY 21 0.64 ALA 175 -0.07 ASN 127

GLY 21 0.58 VAL 176 -0.10 ASN 127

LYS 226 0.62 GLY 177 -0.12 ASN 127

LYS 226 0.74 ASP 178 -0.09 ALA 124

LYS 226 0.87 SER 179 -0.06 LEU 91

LYS 226 0.90 LEU 180 -0.09 SER 120

LYS 226 0.99 GLU 181 -0.10 SER 120

LYS 226 1.17 ALA 182 -0.14 LEU 23

LYS 226 1.08 GLN 183 -0.20 LEU 23

LYS 226 0.98 GLN 184 -0.28 LEU 23

LYS 226 0.73 TYR 185 -0.34 LEU 23

LYS 226 0.63 GLY 186 -0.47 LEU 23

LYS 226 0.47 ILE 187 -0.62 LEU 23

LYS 226 0.50 ALA 188 -0.61 LEU 23

LYS 226 0.43 PHE 189 -0.69 LEU 23

LYS 226 0.43 PRO 190 -0.64 LEU 23

LYS 226 0.46 LYS 191 -0.58 LEU 23

LYS 226 0.40 GLY 192 -0.62 LEU 23

LYS 226 0.36 SER 193 -0.71 LEU 23

LYS 226 0.38 ASP 194 -0.66 LEU 23

LYS 226 0.28 GLU 195 -0.72 LEU 23

LYS 226 0.28 LEU 196 -0.79 LEU 23

LYS 226 0.38 ARG 197 -0.71 LEU 23

LYS 226 0.39 ASP 198 -0.63 LEU 23

LYS 226 0.27 LYS 199 -0.69 LEU 23

LYS 226 0.28 VAL 200 -0.75 LEU 23

LYS 226 0.37 ASN 201 -0.63 LEU 23

LYS 226 0.23 GLY 202 -0.62 LEU 23

LYS 226 0.16 ALA 203 -0.69 LEU 23

LYS 226 0.25 LEU 204 -0.63 LEU 23

LYS 226 0.20 LYS 205 -0.55 LEU 23

ASN 127 0.15 THR 206 -0.58 LEU 23

ASN 127 0.16 LEU 207 -0.61 LEU 23

ASP 83 0.20 ARG 208 -0.52 LEU 23

ASP 73 0.17 GLU 209 -0.49 LEU 23

ASP 178 0.18 ASN 210 -0.52 LEU 23

SER 179 0.24 GLY 211 -0.51 LEU 23

ASP 178 0.20 THR 212 -0.59 LEU 23

SER 179 0.21 TYR 213 -0.53 LEU 23

LYS 87 0.41 ASN 214 -0.46 LEU 23

ASP 178 0.32 GLU 215 -0.55 LEU 23

SER 179 0.22 ILE 216 -0.51 LEU 23

SER 88 0.32 TYR 217 -0.34 LEU 23

SER 179 0.42 LYS 218 -0.32 LEU 23

ASP 178 0.31 LYS 219 -0.35 LEU 23

PRO 159 0.26 TRP 220 -0.24 GLY 222

PRO 159 0.40 PHE 221 -0.10 LEU 23

ASP 178 0.49 GLY 222 -0.24 TRP 220

ASP 178 0.61 THR 223 -0.24 LEU 23

LYS 87 0.65 GLU 224 -0.30 LEU 23

LYS 87 1.06 PRO 225 -0.21 LEU 23

ALA 182 1.17 LYS 226 -0.22 GLY 211

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.

*** COMPLEX (BINDING PROTEIN/PEPTIDE) 17-MAY-97 1WDN ***

CA distance fluctuations for 2402060933351647297

--- normal mode 11 ---

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

* COMPLEX (BINDING PROTEIN/PEPTIDE) 17-MAY-97 1WDN *