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

* *

CA distance fluctuations for 2403041038051524752

--- 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
THR 167 0.26 MET 1 -1.76 ARG 56

THR 167 0.22 ALA 2 -1.76 HIS 61

THR 162 0.26 ASP 3 -1.82 VAL 60

THR 162 0.28 LYS 4 -1.77 HIS 72

THR 162 0.30 ALA 5 -1.67 HIS 72

THR 162 0.36 LYS 6 -1.64 LYS 74

THR 162 0.37 PRO 7 -1.46 LYS 74

THR 162 0.33 ALA 8 -1.36 LYS 74

THR 162 0.26 LYS 9 -1.19 ASP 63

SER 159 0.24 ALA 10 -1.05 ASP 63

SER 159 0.28 ALA 11 -0.98 LYS 78

GLU 40 0.28 ASN 12 -0.83 ASP 63

ASP 21 0.32 ARG 13 -0.84 ASP 63

SER 23 0.33 THR 14 -0.63 ASP 63

GLY 41 0.41 PRO 15 -0.54 THR 210

SER 23 0.50 PRO 16 -0.57 THR 210

SER 23 0.32 LYS 17 -0.51 THR 210

SER 23 0.36 SER 18 -0.56 ALA 27

THR 67 0.24 PRO 19 -0.77 ASP 25

THR 167 0.30 GLY 20 -1.16 ASP 25

GLU 36 0.75 ASP 21 -0.92 GLY 68

GLU 36 0.67 PRO 22 -0.75 GLY 68

GLU 36 0.75 SER 23 -0.47 GLY 68

GLU 36 0.49 LYS 24 -0.78 GLY 20

THR 167 0.18 ASP 25 -1.16 GLY 20

THR 167 0.16 ARG 26 -1.24 ARG 65

THR 167 0.14 ALA 27 -0.92 ALA 64

THR 167 0.12 ALA 28 -0.83 ALA 64

THR 167 0.13 LYS 29 -1.01 ALA 64

THR 162 0.16 ARG 30 -1.31 ALA 64

THR 162 0.19 LEU 31 -1.32 ALA 64

THR 162 0.21 SER 32 -1.48 ALA 64

SER 23 0.27 LEU 33 -1.18 GLY 62

ASP 21 0.37 GLU 34 -1.33 ASP 63

ASP 21 0.55 SER 35 -0.90 LYS 147

SER 23 0.75 GLU 36 -0.95 LYS 147

SER 23 0.61 GLY 37 -0.55 LYS 147

ASP 21 0.40 ALA 38 -0.47 THR 210

ASP 21 0.41 GLY 39 -0.57 THR 210

PRO 15 0.33 GLU 40 -0.60 THR 210

PRO 15 0.41 GLY 41 -0.49 VAL 202

PRO 15 0.27 ALA 42 -0.43 ASP 25

ALA 148 0.21 ALA 43 -0.52 MET 1

SER 49 0.26 ALA 44 -0.60 MET 1

ALA 148 0.28 SER 45 -0.75 MET 1

ALA 148 0.40 PRO 46 -0.79 MET 1

ALA 148 0.57 GLU 47 -0.79 MET 1

GLU 145 0.49 LEU 48 -1.02 MET 1

SER 45 0.28 SER 49 -1.00 MET 1

SER 45 0.26 ALA 50 -1.13 MET 1

GLU 145 0.26 LEU 51 -1.23 MET 1

GLY 146 0.33 GLU 52 -1.41 MET 1

GLY 146 0.41 GLU 53 -1.49 MET 1

GLU 145 0.50 ALA 54 -1.36 MET 1

GLY 146 0.46 PHE 55 -1.47 MET 1

GLY 146 0.54 ARG 56 -1.76 MET 1

GLY 146 0.77 ARG 57 -1.58 ALA 2

GLY 146 0.84 PHE 58 -1.49 ALA 2

GLY 146 0.57 ALA 59 -1.61 ASP 3

GLY 146 0.57 VAL 60 -1.82 ASP 3

GLY 146 0.73 HIS 61 -1.76 ALA 2

GLY 146 0.88 GLY 62 -1.47 ALA 2

GLY 146 0.62 ASP 63 -1.48 SER 32

GLY 146 0.54 ALA 64 -1.48 SER 32

GLY 146 0.52 ARG 65 -1.38 ASP 3

GLY 146 0.48 ALA 66 -1.47 ASP 3

GLY 146 0.41 THR 67 -1.42 LYS 4

GLY 146 0.36 GLY 68 -1.46 LYS 4

GLY 146 0.33 ARG 69 -1.48 LYS 4

GLY 146 0.33 GLU 70 -1.68 LYS 4

GLY 146 0.40 MET 71 -1.75 LYS 4

GLY 146 0.43 HIS 72 -1.77 LYS 4

GLY 146 0.36 GLY 73 -1.64 ALA 5

GLY 146 0.40 LYS 74 -1.64 LYS 6

GLY 146 0.56 ASN 75 -1.55 ASP 3

GLY 146 0.45 TRP 76 -1.39 ASP 3

THR 169 0.43 SER 77 -1.42 LYS 6

THR 169 0.50 LYS 78 -1.25 ALA 8

THR 169 0.41 LEU 79 -1.15 ASP 3

THR 170 0.35 CYS 80 -1.21 LYS 6

THR 170 0.43 LYS 81 -1.13 PRO 7

THR 169 0.46 ASP 82 -1.00 ALA 8

GLY 174 0.38 CYS 83 -0.96 ASP 3

SER 175 0.38 GLN 84 -0.84 ASP 3

SER 175 0.26 VAL 85 -0.89 LYS 4

GLY 174 0.32 ILE 86 -0.87 LYS 6

GLY 174 0.34 ASP 87 -0.78 PRO 7

GLY 174 0.36 GLY 88 -0.84 PRO 7

GLY 174 0.30 ARG 89 -0.81 PRO 7

GLY 174 0.23 ASN 90 -0.80 LYS 6

GLY 174 0.25 VAL 91 -0.88 LYS 6

THR 170 0.31 THR 92 -0.93 PRO 7

THR 170 0.37 VAL 93 -1.03 PRO 7

THR 170 0.33 THR 94 -1.10 LYS 6

GLY 174 0.24 ASP 95 -1.04 LYS 6

GLY 174 0.24 VAL 96 -1.07 LYS 6

THR 170 0.27 ASP 97 -1.20 LYS 6

THR 170 0.21 ILE 98 -1.16 LYS 6

GLY 174 0.17 VAL 99 -1.15 LYS 4

THR 170 0.20 PHE 100 -1.28 LYS 4

THR 170 0.21 SER 101 -1.30 LYS 4

GLY 146 0.15 LYS 102 -1.23 LYS 4

GLY 146 0.18 ILE 103 -1.30 LYS 4

GLY 146 0.15 LYS 104 -1.19 LYS 4

THR 170 0.17 GLY 105 -1.23 ALA 5

THR 170 0.21 LYS 106 -1.33 LYS 6

THR 170 0.24 SER 107 -1.38 LYS 6

THR 170 0.27 CYS 108 -1.51 LYS 6

GLY 146 0.27 ARG 109 -1.44 LYS 6

GLY 146 0.31 THR 110 -1.63 LYS 4

GLY 146 0.27 ILE 111 -1.52 LYS 4

GLY 146 0.27 THR 112 -1.49 LYS 4

GLY 146 0.28 PHE 113 -1.40 LYS 4

GLY 146 0.21 GLU 114 -1.26 LYS 4

GLY 146 0.19 GLN 115 -1.27 LYS 4

GLY 146 0.23 PHE 116 -1.30 LYS 4

GLY 146 0.16 GLN 117 -1.15 LYS 4

GLY 218 0.13 GLU 118 -1.13 LYS 4

GLY 146 0.13 ALA 119 -1.16 LYS 4

VAL 193 0.14 LEU 120 -1.09 LYS 4

GLY 218 0.15 GLU 121 -1.01 LYS 4

GLY 218 0.15 GLU 122 -1.00 LYS 4

SER 175 0.15 LEU 123 -0.98 LYS 4

GLY 218 0.17 ALA 124 -0.90 LYS 4

GLY 218 0.18 LYS 125 -0.86 LYS 4

GLY 218 0.17 LYS 126 -0.85 LYS 4

GLY 218 0.18 ARG 127 -0.79 LYS 4

GLY 218 0.21 PHE 128 -0.75 LYS 4

GLY 218 0.21 LYS 129 -0.72 LYS 4

GLY 218 0.24 ASP 130 -0.85 THR 167

GLY 218 0.26 LYS 131 -1.00 THR 167

GLY 218 0.27 SER 132 -1.11 THR 167

GLY 218 0.24 SER 133 -0.88 THR 167

GLY 218 0.24 GLU 134 -0.83 THR 167

GLY 218 0.24 GLU 135 -0.78 THR 167

GLY 218 0.22 ALA 136 -0.78 LYS 4

GLY 218 0.19 VAL 137 -0.85 LYS 4

GLY 218 0.20 ARG 138 -0.86 LYS 4

GLY 218 0.19 GLU 139 -0.86 MET 1

VAL 193 0.16 VAL 140 -0.97 LYS 4

GLU 145 0.16 HIS 141 -1.06 MET 1

SER 175 0.20 ARG 142 -0.91 MET 1

SER 175 0.25 LEU 143 -0.92 ASP 3

SER 175 0.29 ILE 144 -1.02 ASP 3

PHE 58 0.62 GLU 145 -0.75 ASP 3

GLY 62 0.88 GLY 146 -0.79 GLU 34

GLY 62 0.70 LYS 147 -0.95 GLU 36

GLU 178 0.58 ALA 148 -0.99 ALA 2

PRO 22 0.43 PRO 149 -0.94 ALA 2

LYS 185 0.41 ILE 150 -0.64 ASP 25

GLU 178 0.24 ILE 151 -0.77 ASP 25

PRO 22 0.16 SER 152 -0.55 ASP 25

LYS 17 0.18 GLY 153 -0.62 ASP 25

ALA 148 0.33 VAL 154 -0.68 MET 1

ALA 148 0.19 THR 155 -0.50 ASP 25

PRO 22 0.25 LYS 156 -0.42 THR 210

ASP 21 0.44 ALA 157 -0.53 THR 210

ASP 21 0.42 ILE 158 -0.64 TYR 201

ASP 21 0.51 SER 159 -0.70 THR 210

ASP 21 0.59 SER 160 -0.52 GLY 146

ASP 21 0.51 PRO 161 -0.44 SER 132

ASP 21 0.54 THR 162 -0.53 SER 132

ASP 21 0.54 VAL 163 -0.57 SER 132

ASP 21 0.60 SER 164 -0.75 SER 132

ASP 21 0.62 ARG 165 -0.84 SER 132

ASP 21 0.60 LEU 166 -0.91 SER 132

ASP 21 0.63 THR 167 -1.11 SER 132

ASP 21 0.54 ASP 168 -0.87 SER 132

ASP 63 0.51 THR 169 -0.64 SER 132

LYS 78 0.47 THR 170 -0.44 LYS 131

ASP 21 0.39 LYS 171 -0.39 SER 132

ASP 21 0.43 PHE 172 -0.49 SER 132

ALA 148 0.44 THR 173 -0.35 SER 132

ALA 148 0.46 GLY 174 -0.18 GLU 135

ALA 148 0.51 SER 175 -0.21 MET 1

ALA 148 0.41 HIS 176 -0.19 MET 1

ALA 148 0.41 LYS 177 -0.42 SER 132

ALA 148 0.58 GLU 178 -0.38 GLU 135

ALA 148 0.46 ARG 179 -0.29 MET 1

ASP 21 0.32 PHE 180 -0.29 SER 132

ASP 21 0.48 ASP 181 -0.50 SER 132

ASP 21 0.58 PRO 182 -0.57 SER 132

ASP 21 0.73 SER 183 -0.65 GLU 145

ASP 21 0.59 GLY 184 -0.51 GLY 146

ASP 21 0.51 LYS 185 -0.41 GLU 145

PRO 22 0.29 GLY 186 -0.34 VAL 202

ALA 148 0.36 LYS 187 -0.44 MET 1

ALA 148 0.42 GLY 188 -0.52 MET 1

ALA 148 0.30 LYS 189 -0.48 MET 1

ALA 148 0.21 ALA 190 -0.38 MET 1

ASN 12 0.19 GLY 191 -0.32 ASP 25

ALA 148 0.19 ARG 192 -0.27 GLY 41

ALA 148 0.27 VAL 193 -0.25 ASP 25

ALA 148 0.36 ASP 194 -0.27 MET 1

ALA 148 0.27 LEU 195 -0.24 ASP 25

ALA 148 0.27 VAL 196 -0.19 GLY 41

ASP 21 0.29 ASP 197 -0.20 SER 132

ASP 21 0.33 GLU 198 -0.22 SER 132

ASP 21 0.27 SER 199 -0.37 SER 159

ASP 21 0.19 GLY 200 -0.40 SER 159

ASP 21 0.19 TYR 201 -0.65 SER 159

THR 162 0.20 VAL 202 -0.52 ILE 158

ASP 21 0.14 SER 203 -0.36 GLY 41

VAL 193 0.14 GLY 204 -0.39 GLY 41

VAL 193 0.14 TYR 205 -0.49 GLU 40

VAL 193 0.14 LYS 206 -0.43 GLU 40

PRO 7 0.11 HIS 207 -0.50 GLU 40

PRO 7 0.09 ALA 208 -0.55 GLU 40

PRO 7 0.11 GLY 209 -0.57 GLU 40

PRO 7 0.14 THR 210 -0.70 SER 159

PRO 7 0.16 TYR 211 -0.61 SER 159

PRO 7 0.15 ASP 212 -0.55 SER 159

ASP 21 0.16 GLN 213 -0.58 SER 159

ASP 21 0.16 LYS 214 -0.40 SER 159

ASP 21 0.18 VAL 215 -0.29 GLY 41

SER 132 0.20 GLN 216 -0.30 GLY 41

SER 132 0.25 GLY 217 -0.33 GLY 41

SER 132 0.27 GLY 218 -0.33 GLY 41

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 2403041038051524752

--- normal mode 11 ---

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

* *