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

* 2QLE *

CA distance fluctuations for 240228055824920786

--- normal mode 8 ---

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
LYS 101 0.12 GLY 1 -0.56 ASN 206

LYS 101 0.11 GLU 2 -0.59 ASN 206

ARG 67 0.10 GLU 3 -0.68 ASN 206

ARG 67 0.08 LEU 4 -0.70 ASN 206

VAL 106 0.08 PHE 5 -0.71 ASN 206

ASP 111 0.08 THR 6 -0.74 ASN 206

ASP 111 0.15 GLY 7 -0.85 ASN 206

ASP 111 0.13 VAL 8 -0.93 ASN 206

VAL 8 0.12 VAL 9 -0.86 ASN 206

LYS 38 0.09 PRO 10 -0.88 ASN 206

LEU 39 0.08 ILE 11 -0.67 ASN 206

LEU 39 0.06 LEU 12 -0.56 ASN 206

LEU 39 0.08 VAL 13 -0.37 ASN 206

LYS 152 0.07 GLU 14 -0.26 ASN 206

LYS 152 0.16 LEU 15 -0.14 ASN 206

LYS 152 0.22 ASP 16 -0.11 LYS 120

LYS 152 0.30 GLY 17 -0.10 ASP 16

LYS 152 0.37 ASP 18 -0.09 SER 25

LYS 152 0.39 VAL 19 -0.09 SER 25

GLN 151 0.43 ASN 20 -0.08 LEU 214

GLN 151 0.40 GLY 21 -0.07 LYS 42

GLN 151 0.34 HIS 22 -0.09 VAL 213

LYS 152 0.31 LYS 23 -0.08 ILE 44

LYS 152 0.25 PHE 24 -0.12 SER 25

LYS 152 0.19 SER 25 -0.12 PHE 24

LYS 152 0.19 SER 25 -0.12 PHE 24

LYS 152 0.13 VAL 26 -0.11 ASN 206

LYS 152 0.05 SER 27 -0.26 ASN 206

LYS 152 0.05 SER 27 -0.26 ASN 206

LEU 41 0.08 GLY 28 -0.38 ASN 206

LEU 41 0.12 GLU 29 -0.62 ASN 206

GLU 216 0.06 GLY 30 -0.77 ASN 206

LEU 39 0.09 GLU 31 -0.84 ASN 206

PHE 217 0.11 GLY 32 -0.71 ASN 206

VAL 9 0.10 ASP 33 -0.74 ASN 206

VAL 62 0.10 ALA 34 -0.61 ASN 206

ASP 111 0.10 THR 35 -0.63 ASN 206

ASP 111 0.09 TYR 36 -0.59 PRO 205

VAL 62 0.09 GLY 37 -0.49 ASN 206

GLY 32 0.11 LYS 38 -0.56 ASN 206

GLU 31 0.09 LEU 39 -0.54 ASN 206

GLU 216 0.09 THR 40 -0.70 ASP 204

GLU 216 0.09 THR 40 -0.70 ASP 204

GLU 29 0.12 LEU 41 -0.45 ASN 206

VAL 213 0.16 LYS 42 -0.45 GLY 30

LEU 201 0.07 PHE 43 -0.24 GLU 31

GLU 136 0.09 ILE 44 -0.22 PRO 10

LYS 208 0.19 CYS 45 -0.15 GLU 31

LYS 208 0.14 THR 46 -0.14 PRO 10

LYS 208 0.24 THR 47 -0.10 GLU 31

LYS 208 0.41 GLY 48 -0.15 VAL 8

LYS 208 0.50 LYS 49 -0.15 GLU 31

LYS 208 0.38 LEU 50 -0.15 THR 40

LYS 208 0.37 PRO 51 -0.12 THR 40

LYS 208 0.34 VAL 52 -0.13 LEU 214

PRO 205 0.37 PRO 53 -0.15 LEU 215

PRO 205 0.26 TRP 54 -0.18 LEU 214

PRO 205 0.25 PRO 55 -0.15 PHE 217

GLN 151 0.23 THR 56 -0.10 LEU 214

LYS 152 0.21 LEU 57 -0.09 LEU 41

LYS 152 0.13 VAL 58 -0.10 LEU 41

LYS 152 0.13 THR 59 -0.11 LEU 41

LYS 152 0.17 THR 60 -0.11 ASN 206

LYS 152 0.11 PHE 61 -0.21 ASN 206

GLY 32 0.10 VAL 62 -0.38 ASN 206

LEU 119 0.08 GLN 63 -0.37 ASN 206

LYS 120 0.09 CYS 64 -0.47 ASN 206

ALA 34 0.10 PHE 65 -0.52 ASN 206

THR 91 0.07 SER 66 -0.44 ASN 206

GLU 3 0.10 ARG 67 -0.49 ASN 206

TYR 176 0.11 TYR 68 -0.44 ASN 206

TYR 176 0.10 PRO 69 -0.47 ASN 206

TYR 176 0.13 ASP 70 -0.50 ASN 206

TYR 176 0.14 HIS 71 -0.44 ASN 206

TYR 176 0.17 MET 72 -0.40 ASN 206

TYR 176 0.16 LYS 73 -0.46 ASN 206

THR 91 0.20 ARG 74 -0.41 ASN 206

TYR 176 0.22 HIS 75 -0.36 ASN 206

THR 91 0.18 ASP 76 -0.41 ASN 206

THR 91 0.20 PHE 77 -0.37 ASN 206

LYS 101 0.16 PHE 78 -0.41 ASN 206

LYS 101 0.14 LYS 79 -0.50 ASN 206

LYS 101 0.17 SER 80 -0.46 ASN 206

LYS 120 0.18 ALA 81 -0.43 ASN 206

LYS 120 0.14 MET 82 -0.52 ASN 206

LYS 120 0.12 PRO 83 -0.55 ASN 206

LYS 120 0.17 GLU 84 -0.47 ASN 206

LYS 120 0.17 GLY 85 -0.42 ASN 206

LYS 120 0.23 TYR 86 -0.33 ASN 206

LYS 120 0.28 VAL 87 -0.24 ASN 206

LEU 119 0.28 GLN 88 -0.19 ASN 206

LYS 101 0.39 GLU 89 -0.11 ASN 206

TYR 100 0.37 ARG 90 -0.13 TYR 176

LYS 152 0.47 THR 91 -0.13 THR 102

GLN 151 0.37 ILE 92 -0.10 GLU 118

GLN 151 0.42 PHE 93 -0.13 ALA 173

GLN 151 0.35 PHE 94 -0.09 ARG 162

GLN 151 0.35 LYS 95 -0.08 ILE 122

GLN 151 0.39 ASP 96 -0.08 ARG 162

GLN 151 0.40 ASP 97 -0.10 ARG 162

GLN 151 0.45 GLY 98 -0.10 ILE 122

GLN 151 0.46 ASN 99 -0.08 ASP 16

LYS 152 0.43 TYR 100 -0.10 ASP 16

LYS 152 0.48 LYS 101 -0.13 GLU 118

LYS 152 0.36 THR 102 -0.13 THR 91

LEU 119 0.37 ARG 103 -0.12 ASN 206

LEU 119 0.23 ALA 104 -0.21 ASN 206

GLU 118 0.22 GLU 105 -0.28 ASN 206

LEU 119 0.13 VAL 106 -0.38 ASN 206

GLU 118 0.13 LYS 107 -0.47 ASN 206

GLY 7 0.09 PHE 108 -0.58 ASN 206

GLY 7 0.10 GLU 109 -0.58 ASN 206

GLY 7 0.12 GLY 110 -0.68 ASN 206

GLY 7 0.15 ASP 111 -0.77 ASN 206

GLY 7 0.10 THR 112 -0.74 ASN 206

GLY 7 0.10 LEU 113 -0.62 ASN 206

ASN 115 0.08 VAL 114 -0.50 ASN 206

GLY 32 0.10 ASN 115 -0.36 ASN 206

ASP 16 0.15 ARG 116 -0.28 ASN 206

GLU 105 0.20 ILE 117 -0.17 ASN 206

LYS 152 0.26 GLU 118 -0.13 LYS 101

ARG 103 0.37 LEU 119 -0.09 TYR 100

LYS 152 0.43 LYS 120 -0.11 ASP 16

LYS 152 0.44 GLY 121 -0.10 ASP 16

GLN 151 0.49 ILE 122 -0.10 GLY 98

GLN 151 0.50 ASP 123 -0.08 TYR 139

GLN 151 0.42 PHE 124 -0.11 TYR 139

GLN 151 0.40 LYS 125 -0.11 TYR 139

GLN 151 0.36 GLU 126 -0.11 ALA 200

PRO 205 0.40 ASP 127 -0.12 ALA 200

PRO 205 0.38 GLY 128 -0.13 TYR 139

PRO 205 0.42 ASN 129 -0.15 TYR 139

PRO 205 0.37 ILE 130 -0.14 TYR 139

PRO 205 0.37 LEU 131 -0.13 ALA 200

PRO 205 0.46 GLY 132 -0.14 ALA 200

PRO 205 0.51 HIS 133 -0.17 TYR 137

PRO 205 0.54 LYS 134 -0.17 ALA 200

PRO 205 0.51 LEU 135 -0.18 TYR 139

PRO 205 0.57 GLU 136 -0.21 GLN 198

PRO 205 0.46 TYR 137 -0.18 PHE 217

PRO 205 0.31 ASN 138 -0.27 ALA 200

PRO 205 0.21 TYR 139 -0.21 GLN 198

PRO 205 0.16 ASN 140 -0.22 GLN 198

ALA 200 0.10 SER 141 -0.22 GLY 168

ALA 200 0.10 SER 141 -0.22 GLY 168

LYS 208 0.07 HIS 142 -0.14 GLY 168

TYR 36 0.06 ASN 143 -0.11 GLY 168

PHE 159 0.14 VAL 144 -0.11 ASN 206

PHE 159 0.24 TYR 145 -0.12 ASN 206

TYR 176 0.28 ILE 146 -0.17 ASN 206

TYR 176 0.35 MET 147 -0.18 ASN 206

TYR 176 0.34 ALA 148 -0.20 ASN 206

THR 91 0.43 ASP 149 -0.16 ASN 206

ASP 123 0.38 LYS 150 -0.19 ASN 206

ASP 123 0.50 GLN 151 -0.13 ASN 206

LYS 101 0.48 LYS 152 -0.15 ASN 206

ILE 122 0.36 ASN 153 -0.24 ASN 206

THR 91 0.37 GLY 154 -0.23 ASN 206

THR 91 0.35 ILE 155 -0.20 ASN 206

TYR 176 0.50 LYS 156 -0.13 ASN 206

TYR 176 0.27 VAL 157 -0.11 ASN 206

ASN 192 0.25 ASN 158 -0.10 GLN 178

TYR 145 0.24 PHE 159 -0.06 LEU 41

ASN 192 0.17 LYS 160 -0.06 ALA 104

PRO 205 0.18 ILE 161 -0.07 PHE 93

PRO 205 0.26 ARG 162 -0.12 GLN 171

PRO 205 0.32 HIS 163 -0.17 GLN 198

PRO 205 0.41 ASN 164 -0.20 GLN 198

PRO 205 0.49 ILE 165 -0.18 GLN 198

PRO 205 0.61 GLU 166 -0.19 GLN 198

PRO 205 0.55 ASP 167 -0.18 GLN 198

PRO 205 0.50 GLY 168 -0.22 SER 141

PRO 205 0.43 SER 169 -0.16 SER 141

PRO 205 0.37 VAL 170 -0.15 SER 141

PRO 205 0.35 GLN 171 -0.13 SER 141

PRO 205 0.26 LEU 172 -0.11 ARG 162

GLN 151 0.26 ALA 173 -0.13 PHE 93

GLN 151 0.29 ASP 174 -0.08 GLU 118

LYS 156 0.30 HIS 175 -0.08 LEU 41

LYS 156 0.50 TYR 176 -0.13 ARG 90

THR 91 0.40 GLN 177 -0.09 ASN 158

THR 91 0.40 GLN 178 -0.13 ASN 206

LYS 101 0.33 ASN 179 -0.21 ASN 206

LYS 101 0.32 THR 180 -0.24 ASN 206

LYS 101 0.32 THR 180 -0.24 ASN 206

LYS 120 0.28 PRO 181 -0.31 ASN 206

LYS 120 0.28 ILE 182 -0.32 ASN 206

LYS 120 0.24 GLY 183 -0.38 ASN 206

ILE 122 0.29 ASP 184 -0.36 ASN 206

ILE 122 0.24 GLY 185 -0.43 ASN 206

ILE 122 0.28 PRO 186 -0.39 ASN 206

LYS 101 0.25 VAL 187 -0.38 ASN 206

THR 91 0.24 LEU 188 -0.37 ASN 206

THR 91 0.28 LEU 189 -0.30 ASN 206

TYR 176 0.26 PRO 190 -0.29 ASN 206

TYR 176 0.28 ASP 191 -0.24 ASN 206

TYR 176 0.29 ASN 192 -0.19 ASN 206

TYR 176 0.20 HIS 193 -0.20 ASN 206

PHE 159 0.17 TYR 194 -0.19 ASN 206

PHE 159 0.10 LEU 195 -0.22 ASN 206

TYR 36 0.08 SER 196 -0.18 ASN 206

TYR 36 0.08 SER 196 -0.18 ASN 206

TYR 36 0.08 SER 196 -0.18 ASN 206

GLY 32 0.08 THR 197 -0.18 ASN 206

THR 40 0.07 GLN 198 -0.22 ASN 138

SER 141 0.08 VAL 199 -0.23 ASN 138

LYS 42 0.10 ALA 200 -0.27 ASN 138

TYR 139 0.15 LEU 201 -0.25 LYS 38

TYR 139 0.14 SER 202 -0.29 LYS 38

GLU 136 0.32 LYS 203 -0.48 THR 40

GLU 136 0.25 ASP 204 -0.72 GLU 31

GLU 166 0.61 PRO 205 -0.86 VAL 8

GLU 166 0.46 ASN 206 -0.93 VAL 8

GLU 166 0.32 GLU 207 -0.63 GLU 31

LYS 49 0.50 LYS 208 -0.45 VAL 8

LYS 208 0.33 ARG 209 -0.29 VAL 8

LYS 208 0.38 ASP 210 -0.25 VAL 8

GLU 136 0.16 HIS 211 -0.26 GLU 31

GLU 136 0.12 MET 212 -0.29 THR 40

LYS 42 0.16 VAL 213 -0.38 THR 40

LYS 42 0.14 LEU 214 -0.28 ASP 204

LYS 42 0.14 LEU 214 -0.28 ASP 204

GLU 29 0.08 LEU 215 -0.43 ASP 204

THR 40 0.09 GLU 216 -0.33 ASP 204

GLY 32 0.11 PHE 217 -0.36 ASN 206

GLY 37 0.08 VAL 218 -0.33 ASN 206

GLY 37 0.08 VAL 218 -0.33 ASN 206

THR 35 0.09 THR 219 -0.35 ASN 206

THR 35 0.09 THR 219 -0.35 ASN 206

TYR 176 0.11 ALA 220 -0.31 ASN 206

TYR 176 0.11 ALA 221 -0.27 ASN 206

TYR 176 0.14 GLY 222 -0.22 ASN 206

TYR 176 0.18 ILE 223 -0.28 ASN 206

TYR 176 0.16 THR 224 -0.31 ASN 206

TYR 176 0.20 HIS 225 -0.30 ASN 206

TYR 176 0.19 GLY 226 -0.34 ASN 206

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.

*** 2QLE ***

CA distance fluctuations for 240228055824920786

--- normal mode 8 ---

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

* 2QLE *