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

* *

CA distance fluctuations for 2403061220191900826

--- normal mode 9 ---

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
SER 183 1.02 MET 1 -0.46 GLY 20

THR 210 1.11 ALA 2 -0.52 GLY 20

TYR 211 1.19 ASP 3 -0.38 PRO 19

THR 162 1.28 LYS 4 -0.36 THR 67

TYR 211 1.20 ALA 5 -0.29 THR 67

TYR 211 1.32 LYS 6 -0.32 PRO 19

TYR 211 1.41 PRO 7 -0.35 PRO 19

TYR 211 1.49 ALA 8 -0.45 PRO 19

TYR 211 1.42 LYS 9 -0.41 PRO 19

TYR 211 1.35 ALA 10 -0.41 PRO 19

TYR 211 1.59 ALA 11 -0.30 PRO 19

THR 210 1.28 ASN 12 -0.27 PRO 19

THR 210 1.29 ARG 13 -0.34 PRO 19

LYS 24 1.01 THR 14 -0.31 LYS 17

SER 23 0.89 PRO 15 -0.18 ALA 28

SER 23 0.82 PRO 16 -0.21 ALA 27

THR 210 0.55 LYS 17 -0.59 LEU 33

THR 210 0.54 SER 18 -0.69 LEU 33

THR 210 0.44 PRO 19 -0.91 LEU 33

THR 210 0.46 GLY 20 -0.72 LEU 33

GLU 36 0.91 ASP 21 -0.68 ARG 56

THR 210 0.80 PRO 22 -0.96 THR 67

THR 14 0.97 SER 23 -0.81 GLY 68

THR 210 1.07 LYS 24 -0.67 GLY 68

TYR 211 0.88 ASP 25 -0.79 PRO 19

TYR 211 0.89 ARG 26 -0.71 PRO 19

TYR 211 0.78 ALA 27 -0.71 ALA 44

TYR 211 0.66 ALA 28 -0.71 ALA 44

TYR 211 0.71 LYS 29 -0.59 ALA 44

TYR 211 0.85 ARG 30 -0.49 ALA 44

TYR 211 0.99 LEU 31 -0.56 PRO 19

TYR 211 1.12 SER 32 -0.63 PRO 19

TYR 211 1.02 LEU 33 -0.91 PRO 19

THR 210 1.26 GLU 34 -0.73 PRO 19

THR 210 1.06 SER 35 -0.58 SER 18

ASP 21 0.91 GLU 36 -0.11 SER 18

ASP 21 0.85 GLY 37 -0.17 LEU 33

THR 210 0.56 ALA 38 -0.30 ALA 27

THR 210 0.60 GLY 39 -0.27 ALA 28

VAL 202 0.47 GLU 40 -0.40 ALA 28

THR 210 0.33 GLY 41 -0.57 ALA 27

LYS 147 0.28 ALA 42 -0.66 ALA 27

LYS 147 0.34 ALA 43 -0.58 ALA 27

LYS 147 0.27 ALA 44 -0.71 ALA 27

THR 167 0.30 SER 45 -0.68 ALA 27

THR 167 0.36 PRO 46 -0.52 ALA 27

THR 167 0.43 GLU 47 -0.40 ALA 27

THR 167 0.49 LEU 48 -0.37 ALA 27

THR 167 0.43 SER 49 -0.38 ALA 27

THR 167 0.51 ALA 50 -0.46 SER 23

THR 167 0.64 LEU 51 -0.49 SER 23

THR 167 0.61 GLU 52 -0.66 PRO 22

THR 167 0.59 GLU 53 -0.59 PRO 22

THR 167 0.74 ALA 54 -0.44 PRO 22

THR 167 0.77 PHE 55 -0.58 PRO 22

THR 167 0.70 ARG 56 -0.72 PRO 22

THR 167 0.77 ARG 57 -0.36 GLY 146

THR 167 0.94 PHE 58 -0.41 GLY 146

THR 167 0.92 ALA 59 -0.38 PRO 22

THR 167 0.82 VAL 60 -0.48 PRO 22

THR 167 0.81 HIS 61 -0.39 GLY 146

THR 167 0.87 GLY 62 -0.53 GLY 146

THR 167 0.88 ASP 63 -0.41 GLY 146

THR 167 0.78 ALA 64 -0.33 GLY 146

THR 167 0.71 ARG 65 -0.32 MET 1

THR 167 0.72 ALA 66 -0.50 PRO 22

THR 167 0.66 THR 67 -0.96 PRO 22

THR 167 0.65 GLY 68 -0.87 PRO 22

THR 167 0.67 ARG 69 -0.72 PRO 22

THR 167 0.76 GLU 70 -0.55 PRO 22

THR 167 0.87 MET 71 -0.43 PRO 22

THR 167 0.89 HIS 72 -0.29 PRO 22

THR 167 0.96 GLY 73 -0.18 GLY 146

THR 167 0.98 LYS 74 -0.21 GLY 146

THR 167 1.01 ASN 75 -0.30 GLY 146

THR 167 1.14 TRP 76 -0.22 GLY 146

THR 167 1.19 SER 77 -0.13 GLY 146

THR 167 1.35 LYS 78 -0.07 GLY 146

THR 167 1.41 LEU 79 -0.11 GLY 146

THR 167 1.36 CYS 80 -0.06 GLU 145

THR 167 1.52 LYS 81 -0.03 ASP 63

THR 167 1.77 ASP 82 -0.07 ASP 63

THR 167 1.52 CYS 83 -0.08 ASP 63

THR 167 1.30 GLN 84 -0.09 PRO 22

ASP 168 1.24 VAL 85 -0.13 PRO 22

ASP 168 1.52 ILE 86 -0.06 PRO 22

ASP 168 1.50 ASP 87 -0.05 ASP 63

ASP 168 1.59 GLY 88 -0.04 ASP 63

ASP 168 1.30 ARG 89 -0.04 ASP 63

ASP 168 1.16 ASN 90 -0.07 PRO 22

ASP 168 1.29 VAL 91 -0.08 PRO 22

ASP 168 1.40 THR 92 -0.03 ASP 63

ASP 168 1.45 VAL 93 -0.03 ASP 63

ASP 168 1.24 THR 94 -0.03 LEU 51

ASP 168 1.19 ASP 95 -0.07 PRO 22

ASP 168 1.19 VAL 96 -0.11 PRO 22

THR 167 1.15 ASP 97 -0.09 PRO 22

ASP 168 1.01 ILE 98 -0.12 PRO 22

THR 167 0.97 VAL 99 -0.19 PRO 22

THR 167 1.04 PHE 100 -0.20 PRO 22

THR 167 0.96 SER 101 -0.18 PRO 22

THR 167 0.86 LYS 102 -0.22 SER 23

THR 167 0.80 ILE 103 -0.26 SER 23

THR 167 0.74 LYS 104 -0.23 SER 23

THR 167 0.72 GLY 105 -0.22 SER 23

THR 167 0.79 LYS 106 -0.17 SER 23

THR 167 0.87 SER 107 -0.13 SER 23

THR 167 0.93 CYS 108 -0.12 PRO 22

THR 167 1.01 ARG 109 -0.15 PRO 22

THR 167 0.91 THR 110 -0.28 PRO 22

THR 167 0.85 ILE 111 -0.35 PRO 22

THR 167 0.75 THR 112 -0.48 SER 23

THR 167 0.72 PHE 113 -0.55 SER 23

THR 167 0.66 GLU 114 -0.51 SER 23

THR 167 0.74 GLN 115 -0.41 SER 23

THR 167 0.82 PHE 116 -0.40 PRO 22

THR 167 0.72 GLN 117 -0.42 SER 23

THR 167 0.73 GLU 118 -0.36 SER 23

THR 167 0.88 ALA 119 -0.29 SER 23

THR 167 0.90 LEU 120 -0.28 PRO 22

ASP 168 0.75 GLU 121 -0.29 SER 23

ASP 168 0.84 GLU 122 -0.24 SER 23

ASP 168 1.01 LEU 123 -0.19 PRO 22

ASP 168 0.92 ALA 124 -0.20 PRO 22

ASP 168 0.78 LYS 125 -0.21 SER 23

ASP 168 0.91 LYS 126 -0.16 PRO 22

ASP 168 1.01 ARG 127 -0.13 PRO 22

ASP 168 0.79 PHE 128 -0.15 PRO 22

THR 170 0.67 LYS 129 -0.16 GLN 216

THR 170 0.55 ASP 130 -0.21 GLN 216

THR 170 0.32 LYS 131 -0.33 GLN 216

THR 170 0.33 SER 132 -0.29 GLN 216

THR 170 0.51 SER 133 -0.22 GLN 216

ASP 168 0.42 GLU 134 -0.31 GLN 216

ASP 168 0.37 GLU 135 -0.35 GLN 216

ASP 168 0.58 ALA 136 -0.21 SER 23

ASP 168 0.64 VAL 137 -0.24 SER 23

ASP 168 0.50 ARG 138 -0.30 SER 23

THR 167 0.53 GLU 139 -0.28 SER 23

THR 167 0.74 VAL 140 -0.29 SER 23

THR 167 0.74 HIS 141 -0.32 PRO 22

THR 167 0.73 ARG 142 -0.24 PRO 22

THR 167 0.98 LEU 143 -0.17 PRO 22

THR 167 1.14 ILE 144 -0.14 PRO 22

THR 167 1.10 GLU 145 -0.29 PHE 58

THR 167 1.20 GLY 146 -0.53 GLY 62

ASP 181 1.20 LYS 147 -0.40 GLY 62

THR 167 0.80 ALA 148 -0.17 GLY 20

GLY 62 0.62 PRO 149 -0.14 LEU 33

THR 210 0.53 ILE 150 -0.19 ALA 27

THR 210 0.46 ILE 151 -0.47 LEU 33

THR 210 0.43 SER 152 -0.55 ALA 27

THR 210 0.32 GLY 153 -0.68 ALA 27

THR 167 0.32 VAL 154 -0.54 ALA 27

LYS 147 0.43 THR 155 -0.38 ALA 27

VAL 202 0.51 LYS 156 -0.34 ALA 28

VAL 202 0.66 ALA 157 -0.16 ALA 28

VAL 202 0.98 ILE 158 -0.22 GLY 41

TYR 201 1.14 SER 159 -0.18 GLY 41

ASP 3 1.02 SER 160 -0.12 GLY 41

LYS 4 1.11 PRO 161 -0.40 VAL 202

LYS 4 1.28 THR 162 -0.42 VAL 202

LYS 4 1.17 VAL 163 -0.39 TYR 201

LYS 4 1.19 SER 164 -0.14 VAL 202

GLY 146 1.16 ARG 165 -0.30 GLU 198

ASP 82 1.36 LEU 166 -0.46 SER 199

ASP 82 1.77 THR 167 -0.33 SER 199

GLY 88 1.59 ASP 168 -0.51 SER 199

ASP 87 1.39 THR 169 -0.58 SER 199

GLY 88 1.36 THR 170 -0.80 SER 199

GLY 88 1.13 LYS 171 -1.16 SER 199

GLY 88 0.98 PHE 172 -1.11 GLU 198

GLY 146 0.84 THR 173 -0.78 GLU 198

GLY 146 0.69 GLY 174 -0.47 GLU 198

GLY 146 0.58 SER 175 -0.32 GLU 135

LYS 147 0.68 HIS 176 -0.25 GLU 135

GLY 146 0.90 LYS 177 -0.17 GLU 135

GLY 146 0.84 GLU 178 -0.16 GLU 135

LYS 147 0.72 ARG 179 -0.25 ALA 28

LYS 147 0.92 PHE 180 -0.17 PRO 161

LYS 147 1.20 ASP 181 -0.11 GLU 135

LYS 147 1.08 PRO 182 -0.09 SER 132

LYS 147 1.17 SER 183 -0.10 SER 132

LYS 147 0.99 GLY 184 -0.10 GLY 41

LYS 147 1.03 LYS 185 -0.12 GLU 178

LYS 147 0.81 GLY 186 -0.22 ALA 28

LYS 147 0.64 LYS 187 -0.34 ALA 28

LYS 147 0.49 GLY 188 -0.44 ALA 28

LYS 147 0.40 LYS 189 -0.56 ALA 28

LYS 147 0.49 ALA 190 -0.47 ALA 28

LYS 147 0.48 GLY 191 -0.44 ALA 28

LYS 147 0.53 ARG 192 -0.31 LYS 171

LYS 147 0.46 VAL 193 -0.35 ALA 28

LYS 147 0.49 ASP 194 -0.37 ALA 28

LYS 147 0.65 LEU 195 -0.26 ALA 28

LYS 147 0.64 VAL 196 -0.36 PHE 172

LYS 4 0.75 ASP 197 -0.57 PHE 172

LYS 4 0.86 GLU 198 -1.11 PHE 172

PRO 7 0.99 SER 199 -1.16 LYS 171

ALA 11 0.90 GLY 200 -0.88 LYS 171

SER 159 1.14 TYR 201 -0.68 LYS 171

ILE 158 0.98 VAL 202 -0.50 LYS 171

ALA 11 0.67 SER 203 -0.55 LYS 171

ALA 11 0.81 GLY 204 -0.72 LYS 171

ALA 11 0.89 TYR 205 -0.67 LYS 171

ALA 11 0.94 LYS 206 -0.71 LYS 171

ALA 11 1.14 HIS 207 -0.76 LYS 171

ALA 11 1.26 ALA 208 -0.65 LYS 171

ALA 11 1.48 GLY 209 -0.64 LYS 171

ALA 11 1.54 THR 210 -0.63 LYS 171

ALA 11 1.59 TYR 211 -0.63 LYS 171

ALA 11 1.35 ASP 212 -0.79 LYS 171

ALA 11 1.21 GLN 213 -0.91 LYS 171

ALA 11 1.00 LYS 214 -1.00 LYS 171

PRO 7 0.82 VAL 215 -0.91 LYS 171

ALA 11 0.77 GLN 216 -0.75 LYS 171

ALA 11 0.72 GLY 217 -0.63 LYS 171

ALA 11 0.73 GLY 218 -0.57 LYS 171

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.

*** ***

CA distance fluctuations for 2403061220191900826

--- normal mode 9 ---

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

* *