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 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
GLU 215 0.29 LYS 4 -0.73 ASP 22

GLU 215 0.25 LEU 5 -0.70 LEU 23

ASP 30 0.29 VAL 6 -0.53 LEU 23

ASP 30 0.31 VAL 7 -0.54 LEU 23

ASP 30 0.23 ALA 8 -0.32 LEU 23

VAL 29 0.20 THR 9 -0.26 LEU 23

ARG 75 0.16 ASP 10 -0.22 LYS 226

LYS 19 0.28 THR 11 -0.17 TYR 43

LYS 19 0.46 ALA 12 -0.16 ALA 33

PHE 18 0.37 PHE 13 -0.20 LYS 226

GLN 20 0.43 VAL 14 -0.14 LYS 37

GLN 20 0.28 PRO 15 -0.13 LYS 37

PHE 18 0.22 PHE 16 -0.18 LYS 226

PHE 18 0.19 GLU 17 -0.24 ALA 33

ASP 140 0.39 PHE 18 -0.31 ALA 33

ASP 140 0.76 LYS 19 -0.62 ALA 33

ALA 168 1.08 GLN 20 -0.71 LYS 37

MET 144 1.02 GLY 21 -0.85 LYS 40

MET 144 0.84 ASP 22 -1.08 LYS 40

ALA 168 0.59 LEU 23 -1.22 ALA 33

ALA 168 0.38 TYR 24 -0.82 ALA 33

ALA 168 0.37 VAL 25 -0.67 ALA 33

LYS 46 0.25 GLY 26 -0.22 ALA 34

LEU 45 0.18 PHE 27 -0.29 LEU 23

LYS 46 0.18 ASP 28 -0.44 LEU 23

LEU 45 0.34 VAL 29 -0.64 LEU 23

GLU 44 0.39 ASP 30 -0.64 LEU 23

TRP 32 0.28 LEU 31 -0.64 LEU 23

GLU 215 0.29 TRP 32 -0.91 LEU 23

GLU 215 0.44 ALA 33 -1.22 LEU 23

GLU 215 0.35 ALA 34 -0.97 LEU 23

GLU 215 0.22 ILE 35 -0.95 LEU 23

GLU 215 0.28 ALA 36 -1.20 LEU 23

THR 212 0.28 LYS 37 -1.22 LEU 23

THR 212 0.21 GLU 38 -1.00 LEU 23

LEU 196 0.22 LEU 39 -0.99 LEU 23

SER 193 0.21 LYS 40 -1.15 LEU 23

GLU 215 0.24 LEU 41 -1.12 LEU 23

GLU 215 0.35 ASP 42 -1.08 LEU 23

GLU 215 0.33 TYR 43 -1.00 LEU 23

ASP 30 0.39 GLU 44 -0.78 LEU 23

ASP 30 0.39 LEU 45 -0.59 LEU 23

VAL 29 0.31 LYS 46 -0.24 ASP 22

VAL 29 0.21 PRO 47 -0.16 TYR 43

LYS 19 0.16 MET 48 -0.20 LYS 226

LYS 19 0.25 ASP 49 -0.24 LYS 226

ARG 75 0.25 PHE 50 -0.32 LYS 226

ARG 75 0.32 SER 51 -0.33 LYS 226

LYS 77 0.22 GLY 52 -0.30 LYS 226

ILE 54 0.19 ILE 53 -0.33 LYS 226

ILE 53 0.19 ILE 54 -0.42 LYS 226

LYS 77 0.16 PRO 55 -0.39 ASP 122

ASP 30 0.16 ALA 56 -0.30 LYS 226

LEU 41 0.15 LEU 57 -0.34 LYS 226

LEU 41 0.16 GLN 58 -0.38 LYS 226

LEU 41 0.17 THR 59 -0.31 LYS 226

LEU 41 0.22 LYS 60 -0.27 LYS 226

ASP 30 0.21 ASN 61 -0.25 ASP 122

ASP 30 0.23 VAL 62 -0.30 LEU 23

LEU 41 0.23 ASP 63 -0.45 LEU 23

ASP 30 0.17 LEU 64 -0.49 LEU 23

ASP 30 0.18 ALA 65 -0.43 LEU 23

ASP 30 0.12 LEU 66 -0.43 LEU 23

PHE 18 0.14 ALA 67 -0.32 LYS 226

PHE 18 0.17 GLY 68 -0.41 LYS 226

PHE 18 0.16 ILE 69 -0.50 LYS 226

ASP 83 0.14 THR 70 -0.64 LYS 226

ASP 198 0.16 ILE 71 -0.73 LYS 226

GLY 117 0.27 THR 72 -0.80 LYS 226

GLY 117 0.31 ASP 73 -0.80 LYS 226

GLY 117 0.36 GLU 74 -0.71 LYS 226

GLY 117 0.35 ARG 75 -0.63 LYS 226

GLY 117 0.27 LYS 76 -0.66 LYS 226

SER 51 0.30 LYS 77 -0.60 LYS 226

SER 51 0.26 ALA 78 -0.52 LYS 226

SER 51 0.19 ILE 79 -0.49 LYS 226

SER 51 0.15 ASP 80 -0.49 LYS 226

ASP 198 0.13 PHE 81 -0.54 LYS 226

ILE 71 0.13 SER 82 -0.49 LEU 23

GLN 184 0.23 ASP 83 -0.55 LYS 226

ASN 201 0.20 GLY 84 -0.63 LYS 226

LYS 205 0.21 TYR 85 -0.57 LYS 226

LYS 205 0.23 TYR 86 -0.70 PRO 225

LYS 205 0.22 LYS 87 -0.95 LYS 226

GLN 20 0.18 SER 88 -0.76 LYS 226

GLY 21 0.24 GLY 89 -0.70 LYS 226

GLY 21 0.33 LEU 90 -0.58 LYS 226

GLY 21 0.41 LEU 91 -0.48 LYS 226

GLY 21 0.50 VAL 92 -0.41 LYS 226

GLY 21 0.62 MET 93 -0.31 LYS 226

GLY 21 0.70 VAL 94 -0.26 LYS 226

GLY 21 0.79 LYS 95 -0.19 LYS 226

GLY 21 0.77 ALA 96 -0.15 THR 223

GLY 21 0.73 ASN 97 -0.16 LYS 226

GLY 21 0.69 ASN 98 -0.22 LYS 226

GLY 21 0.61 ASN 99 -0.25 LYS 226

GLY 21 0.57 ASP 100 -0.29 LYS 226

GLY 21 0.54 VAL 101 -0.34 LYS 226

GLY 21 0.49 LYS 102 -0.37 LYS 226

GLY 21 0.44 SER 103 -0.45 LYS 226

GLY 21 0.42 VAL 104 -0.49 LYS 226

GLY 21 0.43 LYS 105 -0.44 LYS 226

GLY 21 0.48 ASP 106 -0.40 LYS 226

GLY 21 0.41 LEU 107 -0.44 LYS 226

GLY 21 0.44 ASP 108 -0.39 LYS 226

GLY 21 0.48 GLY 109 -0.35 LYS 226

GLY 21 0.53 LYS 110 -0.34 LYS 226

GLY 21 0.57 VAL 111 -0.32 LYS 226

GLY 21 0.56 VAL 112 -0.34 LYS 226

GLY 21 0.60 ALA 113 -0.31 LYS 226

GLY 21 0.51 VAL 114 -0.35 LYS 226

GLY 21 0.46 LYS 115 -0.33 LYS 226

GLY 21 0.36 SER 116 -0.34 LYS 226

GLU 74 0.36 GLY 117 -0.39 LYS 226

GLY 21 0.26 THR 118 -0.44 LYS 226

GLY 21 0.24 GLY 119 -0.53 LYS 226

GLY 21 0.34 SER 120 -0.49 LYS 226

GLY 21 0.34 VAL 121 -0.45 LYS 226

GLY 21 0.26 ASP 122 -0.52 LYS 226

GLY 21 0.29 TYR 123 -0.56 LYS 226

GLY 21 0.36 ALA 124 -0.48 LYS 226

GLY 21 0.31 LYS 125 -0.47 LYS 226

GLY 21 0.27 ALA 126 -0.53 LYS 226

GLY 21 0.31 ASN 127 -0.53 LYS 226

GLY 21 0.36 ILE 128 -0.47 LYS 226

GLY 21 0.38 LYS 129 -0.42 LYS 226

GLY 21 0.44 THR 130 -0.39 LYS 226

GLY 21 0.47 LYS 131 -0.34 LYS 226

GLY 21 0.50 ASP 132 -0.33 LYS 226

GLY 21 0.49 LEU 133 -0.34 LYS 226

GLY 21 0.55 ARG 134 -0.30 LYS 226

GLY 21 0.49 GLN 135 -0.31 LYS 226

GLY 21 0.54 PHE 136 -0.27 LYS 226

GLY 21 0.45 PRO 137 -0.25 LYS 226

GLY 21 0.53 ASN 138 -0.23 LYS 226

GLY 21 0.63 ILE 139 -0.24 LYS 226

GLY 21 0.86 ASP 140 -0.16 LYS 226

GLY 21 0.83 ASN 141 -0.18 LYS 226

GLY 21 0.76 ALA 142 -0.23 LYS 226

GLY 21 0.89 TYR 143 -0.19 LYS 226

GLY 21 1.02 MET 144 -0.15 LYS 226

GLY 21 0.86 GLU 145 -0.20 LYS 226

GLY 21 0.85 LEU 146 -0.21 LYS 226

GLY 21 1.00 GLY 147 -0.15 LYS 226

GLY 21 0.97 THR 148 -0.15 LYS 226

GLY 21 0.84 ASN 149 -0.19 LYS 226

GLY 21 0.77 ARG 150 -0.21 LYS 226

GLY 21 0.71 ALA 151 -0.26 LYS 226

GLY 21 0.67 ASP 152 -0.28 LYS 226

GLY 21 0.64 ALA 153 -0.31 LYS 226

GLY 21 0.62 VAL 154 -0.32 LYS 226

GLY 21 0.50 LEU 155 -0.41 LYS 226

GLY 21 0.43 HIS 156 -0.41 LYS 226

GLY 21 0.34 ASP 157 -0.47 LYS 226

GLN 20 0.34 THR 158 -0.45 LYS 226

GLN 20 0.31 PRO 159 -0.38 PHE 221

GLN 20 0.44 ASN 160 -0.25 LYS 226

GLN 20 0.54 ILE 161 -0.25 LYS 226

GLN 20 0.44 LEU 162 -0.32 GLY 222

GLN 20 0.49 TYR 163 -0.14 LYS 219

GLN 20 0.76 PHE 164 -0.07 ILE 139

GLY 21 0.70 ILE 165 -0.12 GLY 222

GLY 21 0.58 LYS 166 -0.10 LYS 219

GLN 20 0.74 THR 167 -0.09 ASP 140

GLN 20 1.08 ALA 168 -0.07 ASP 140

GLY 21 0.97 GLY 169 -0.05 MET 144

GLY 21 0.86 ASN 170 -0.04 LYS 37

GLY 21 0.85 GLY 171 -0.07 LYS 218

GLY 21 0.95 GLN 172 -0.08 LYS 226

GLY 21 0.82 PHE 173 -0.15 LYS 226

GLY 21 0.67 LYS 174 -0.23 THR 223

GLY 21 0.55 ALA 175 -0.34 THR 223

GLY 21 0.50 VAL 176 -0.36 THR 223

GLY 21 0.41 GLY 177 -0.46 LYS 226

GLY 21 0.34 ASP 178 -0.56 LYS 226

GLY 21 0.29 SER 179 -0.67 LYS 226

GLY 21 0.28 LEU 180 -0.71 LYS 226

GLY 21 0.22 GLU 181 -0.79 LYS 226

GLN 20 0.18 ALA 182 -0.94 LYS 226

ASP 83 0.21 GLN 183 -0.89 LYS 226

ASP 83 0.23 GLN 184 -0.85 LYS 226

ASP 83 0.17 TYR 185 -0.63 LYS 226

ASN 201 0.12 GLY 186 -0.55 LYS 226

ASP 140 0.09 ILE 187 -0.48 LEU 23

LEU 39 0.11 ALA 188 -0.43 LYS 226

LEU 39 0.16 PHE 189 -0.41 LEU 23

LEU 41 0.18 PRO 190 -0.36 LYS 226

LYS 40 0.17 LYS 191 -0.40 LYS 226

LYS 40 0.18 GLY 192 -0.38 LEU 23

LYS 40 0.21 SER 193 -0.48 LEU 23

ASP 73 0.16 ASP 194 -0.53 LEU 23

ASP 73 0.12 GLU 195 -0.65 LEU 23

LEU 39 0.22 LEU 196 -0.68 LEU 23

LEU 39 0.14 ARG 197 -0.60 LEU 23

ILE 71 0.16 ASP 198 -0.58 LEU 23

GLN 184 0.14 LYS 199 -0.70 LEU 23

GLY 84 0.12 VAL 200 -0.73 LEU 23

GLY 84 0.20 ASN 201 -0.61 LEU 23

GLY 84 0.19 GLY 202 -0.66 LEU 23

TYR 85 0.16 ALA 203 -0.76 LEU 23

TYR 85 0.19 LEU 204 -0.64 LEU 23

TYR 86 0.23 LYS 205 -0.56 LEU 23

TYR 86 0.14 THR 206 -0.64 LEU 23

ASP 42 0.13 LEU 207 -0.62 LEU 23

PRO 225 0.16 ARG 208 -0.47 LEU 23

PRO 225 0.24 GLU 209 -0.47 LEU 23

LYS 226 0.26 ASN 210 -0.50 LEU 23

PRO 225 0.27 GLY 211 -0.37 LEU 23

ALA 34 0.32 THR 212 -0.46 LEU 23

ALA 33 0.24 TYR 213 -0.42 LEU 23

ALA 33 0.28 ASN 214 -0.33 LYS 87

ALA 33 0.44 GLU 215 -0.27 SER 179

ALA 33 0.31 ILE 216 -0.28 LEU 23

GLU 44 0.19 TYR 217 -0.30 SER 88

GLU 44 0.26 LYS 218 -0.39 SER 179

GLU 44 0.31 LYS 219 -0.28 SER 179

GLY 222 0.25 TRP 220 -0.27 PRO 159

GLN 20 0.22 PHE 221 -0.38 PRO 159

GLN 20 0.31 GLY 222 -0.47 ASP 178

GLN 20 0.21 THR 223 -0.57 SER 179

ALA 33 0.19 GLU 224 -0.58 LYS 87

GLY 211 0.27 PRO 225 -0.91 LYS 87

GLY 211 0.26 LYS 226 -0.95 LYS 87

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 10 ---

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

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