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

* 9pap priemra opcion *

CA distance fluctuations for 240110225601577892

--- normal mode 16 ---

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
ASN 212 0.67 ILE 1 -0.73 GLY 119

ASN 184 0.60 PRO 2 -0.67 GLY 194

ASN 184 0.64 GLU 3 -0.87 GLY 194

ASN 184 0.86 TYR 4 -0.52 GLY 194

ASN 184 0.66 VAL 5 -0.35 GLY 194

ASN 184 0.77 ASP 6 -0.32 TYR 166

ASN 184 0.58 TRP 7 -0.28 TYR 203

ASN 184 0.69 ARG 8 -0.24 TYR 203

ASN 184 0.72 GLN 9 -0.28 ILE 171

ASN 184 0.56 LYS 10 -0.32 ILE 125

ASN 184 0.50 GLY 11 -0.33 ILE 125

ASN 184 0.47 ALA 12 -0.37 ILE 125

LYS 106 0.43 VAL 13 -0.35 ALA 163

PRO 15 0.42 THR 14 -0.34 ALA 162

GLN 9 0.48 PRO 15 -0.31 ALA 162

TYR 4 0.46 VAL 16 -0.22 VAL 133

TYR 4 0.36 LYS 17 -0.29 VAL 161

TYR 4 0.34 ASN 18 -0.24 SER 205

LYS 139 0.28 GLN 19 -0.27 SER 205

LYS 139 0.36 GLY 20 -0.21 SER 205

LYS 139 0.38 SER 21 -0.18 SER 205

LYS 139 0.31 CYS 22 -0.23 SER 205

ALA 137 0.30 GLY 23 -0.25 SER 205

LYS 139 0.23 SER 24 -0.34 SER 205

ASN 175 0.26 TRP 26 -0.48 SER 205

LYS 174 0.24 ALA 27 -0.43 SER 205

SER 176 0.27 PHE 28 -0.40 SER 205

LYS 174 0.36 SER 29 -0.49 SER 205

LYS 174 0.38 ALA 30 -0.53 SER 205

LYS 174 0.29 VAL 31 -0.43 SER 205

LYS 174 0.38 VAL 32 -0.38 GLN 47

ALA 76 0.41 THR 33 -0.38 VAL 130

LYS 106 0.46 ILE 34 -0.50 TYR 208

LYS 106 0.45 GLU 35 -0.42 VAL 130

LYS 106 0.46 GLY 36 -0.42 VAL 130

LYS 106 0.50 ILE 37 -0.35 GLN 114

LYS 106 0.71 ILE 38 -0.33 GLN 114

LYS 106 0.51 LYS 39 -0.37 GLN 128

LYS 10 0.51 ILE 40 -0.35 GLN 114

LYS 106 0.42 ARG 41 -0.30 GLN 114

LYS 106 0.59 THR 42 -0.27 GLN 114

LYS 106 0.47 GLY 43 -0.32 GLN 114

ALA 105 0.49 ASN 44 -0.29 GLN 114

LYS 106 0.40 LEU 45 -0.35 VAL 130

GLY 79 0.34 ASN 46 -0.35 VAL 130

GLY 79 0.25 GLN 47 -0.40 VAL 130

GLN 9 0.23 TYR 48 -0.39 PHE 207

TYR 4 0.20 SER 49 -0.37 SER 205

TYR 4 0.21 GLU 50 -0.39 SER 205

TYR 4 0.19 GLN 51 -0.33 SER 205

TYR 4 0.19 GLU 52 -0.30 SER 205

ARG 8 0.19 LEU 53 -0.33 SER 205

LYS 139 0.19 LEU 54 -0.30 SER 205

LYS 139 0.17 ASP 55 -0.31 TYR 78

ARG 98 0.33 CYS 56 -0.34 TYR 78

ARG 98 0.29 ASP 57 -0.26 PRO 115

ARG 98 0.31 ARG 58 -0.28 GLN 77

ARG 98 0.29 ARG 59 -0.24 TYR 116

ARG 98 0.24 SER 60 -0.27 PRO 115

ARG 98 0.21 TYR 61 -0.23 TYR 116

ALA 137 0.21 GLY 62 -0.23 SER 205

ALA 137 0.26 CYS 63 -0.21 SER 205

ALA 137 0.24 ASN 64 -0.19 TYR 116

ALA 137 0.21 GLY 65 -0.25 THR 204

ARG 98 0.18 GLY 66 -0.31 SER 205

ALA 160 0.25 TYR 67 -0.41 SER 205

ALA 162 0.32 PRO 68 -0.47 SER 205

ALA 162 0.28 TRP 69 -0.41 PRO 115

LYS 174 0.25 SER 70 -0.36 PRO 115

LYS 174 0.29 ALA 71 -0.35 SER 205

LYS 174 0.36 LEU 72 -0.32 GLN 112

LYS 174 0.28 GLN 73 -0.34 GLN 114

ILE 34 0.29 LEU 74 -0.29 GLN 114

ILE 34 0.42 VAL 75 -0.31 GLN 112

ILE 38 0.45 ALA 76 -0.24 CYS 95

THR 42 0.40 GLN 77 -0.30 CYS 56

THR 42 0.41 TYR 78 -0.40 CYS 95

ILE 38 0.46 GLY 79 -0.40 ASN 212

ASN 44 0.27 ILE 80 -0.48 ASN 212

TYR 4 0.20 HIS 81 -0.54 ASN 212

TYR 4 0.17 TYR 82 -0.51 ASN 212

TYR 4 0.19 ARG 83 -0.37 ASN 212

TYR 86 0.15 ASN 84 -0.42 ASN 212

TYR 4 0.13 THR 85 -0.48 ASN 212

TYR 4 0.15 TYR 86 -0.40 ASN 212

TYR 4 0.16 PRO 87 -0.32 SER 205

TYR 4 0.20 TYR 88 -0.31 SER 205

LYS 139 0.21 GLU 89 -0.26 SER 205

LYS 139 0.25 GLY 90 -0.26 SER 205

LYS 139 0.23 VAL 91 -0.22 SER 205

LYS 139 0.20 GLN 92 -0.22 TYR 78

LYS 139 0.17 ARG 93 -0.28 TYR 78

TYR 61 0.17 TYR 94 -0.32 TYR 78

ARG 58 0.20 CYS 95 -0.40 TYR 78

CYS 56 0.24 ARG 96 -0.37 ASN 212

CYS 56 0.26 SER 97 -0.44 ASN 212

CYS 56 0.33 ARG 98 -0.42 ASN 212

ARG 58 0.23 GLU 99 -0.43 ASN 212

CYS 56 0.17 LYS 100 -0.51 ASN 212

CYS 56 0.16 GLY 101 -0.60 ASN 212

ASN 44 0.23 PRO 102 -0.71 ASN 212

ASN 44 0.31 TYR 103 -0.69 ASN 212

ASN 44 0.36 ALA 104 -0.72 ASN 212

ASN 44 0.49 ALA 105 -0.72 ASN 212

ILE 38 0.71 LYS 106 -0.57 TYR 103

ILE 37 0.48 THR 107 -0.45 ALA 105

ASN 127 0.46 ASP 108 -0.46 ALA 105

VAL 164 0.32 GLY 109 -0.34 ALA 105

ILE 173 0.32 VAL 110 -0.39 ALA 105

ILE 187 0.29 ARG 111 -0.36 ALA 105

ILE 189 0.29 GLN 112 -0.40 ILE 34

ILE 189 0.30 VAL 113 -0.40 GLN 114

ILE 189 0.27 GLN 114 -0.40 VAL 113

TYR 203 0.26 PRO 115 -0.42 GLU 3

VAL 150 0.29 TYR 116 -0.52 GLU 3

LYS 190 0.33 ASN 117 -0.61 GLU 3

ASN 212 0.38 GLN 118 -0.68 GLU 3

ASN 212 0.45 GLY 119 -0.78 GLU 3

ASN 212 0.46 ALA 120 -0.52 ASN 117

ASN 212 0.46 LEU 121 -0.42 GLU 3

ASN 212 0.54 LEU 122 -0.45 GLU 3

ASN 212 0.66 TYR 123 -0.48 ASN 117

ASN 212 0.69 SER 124 -0.38 GLY 36

ASN 212 0.63 ILE 125 -0.37 ALA 12

ASN 212 0.71 ALA 126 -0.31 SER 196

ASN 212 0.87 ASN 127 -0.29 GLY 43

ASN 212 0.59 GLN 128 -0.39 GLY 36

VAL 164 0.52 PRO 129 -0.32 ALA 12

TYR 208 0.45 VAL 130 -0.42 GLU 35

TYR 208 0.34 SER 131 -0.38 SER 29

PHE 207 0.31 VAL 132 -0.46 SER 29

ASN 212 0.21 VAL 133 -0.40 ALA 160

ASN 212 0.22 LEU 134 -0.27 ARG 191

ASN 212 0.19 GLN 135 -0.33 ARG 191

ASN 212 0.22 ALA 136 -0.21 ARG 191

GLY 23 0.30 ALA 137 -0.24 ARG 191

SER 21 0.31 GLY 138 -0.30 ARG 191

SER 21 0.38 LYS 139 -0.19 ARG 191

ASN 212 0.24 ASP 140 -0.16 ARG 191

ASN 212 0.26 PHE 141 -0.16 TYR 144

TYR 4 0.28 GLN 142 -0.18 ALA 136

TYR 4 0.35 LEU 143 -0.13 ALA 137

TYR 4 0.39 TYR 144 -0.16 PHE 141

TYR 4 0.58 ARG 145 -0.11 ALA 136

TYR 4 0.59 GLY 146 -0.07 ALA 136

GLY 167 0.51 GLY 147 -0.10 ILE 187

GLY 147 0.43 ILE 148 -0.13 PRO 15

ASN 212 0.34 PHE 149 -0.18 ASN 169

ASN 195 0.48 VAL 150 -0.47 ASN 169

ASN 195 0.28 GLY 151 -0.38 ASN 169

ASN 212 0.22 PRO 152 -0.42 ASN 169

ASN 212 0.20 CYS 153 -0.46 ARG 191

ASN 212 0.16 GLY 154 -0.45 ARG 191

ASN 212 0.16 ASN 155 -0.41 GLU 3

ASN 212 0.14 LYS 156 -0.34 GLU 3

ASN 212 0.17 VAL 157 -0.28 GLU 3

ASN 212 0.16 ASP 158 -0.21 VAL 157

PRO 68 0.22 HIS 159 -0.22 THR 204

PRO 68 0.29 ALA 160 -0.40 VAL 133

PRO 68 0.30 VAL 161 -0.29 LYS 17

TYR 208 0.39 ALA 162 -0.34 THR 14

TYR 208 0.43 ALA 163 -0.35 VAL 13

PRO 129 0.52 VAL 164 -0.34 ALA 163

ASN 212 0.52 GLY 165 -0.30 GLY 198

ASN 212 0.52 TYR 166 -0.32 ASP 6

GLU 183 0.63 GLY 167 -0.46 GLY 192

ASN 212 0.53 PRO 168 -0.68 GLY 192

ASN 212 0.48 ASN 169 -0.47 VAL 150

ASN 212 0.46 TYR 170 -0.23 CYS 200

ASN 212 0.48 ILE 171 -0.28 GLN 9

ASN 212 0.46 LEU 172 -0.19 ILE 171

TYR 208 0.40 ILE 173 -0.27 LYS 174

PRO 129 0.42 LYS 174 -0.27 ILE 173

SER 29 0.36 ASN 175 -0.20 LEU 202

TYR 4 0.36 SER 176 -0.27 VAL 133

TYR 4 0.39 TRP 177 -0.25 GLY 178

TYR 4 0.48 GLY 178 -0.25 TRP 177

TYR 4 0.66 THR 179 -0.15 GLY 20

TYR 4 0.61 GLY 180 -0.14 ASP 158

TYR 4 0.55 TRP 181 -0.13 ASP 158

TYR 4 0.59 GLY 182 -0.09 GLN 135

TYR 4 0.79 GLU 183 -0.08 PRO 87

TYR 4 0.86 ASN 184 -0.12 GLU 89

TYR 4 0.62 GLY 185 -0.14 LEU 134

TYR 4 0.54 TYR 186 -0.16 PRO 15

TYR 4 0.44 ILE 187 -0.13 PRO 15

ASN 212 0.41 ARG 188 -0.17 PRO 15

ASN 212 0.39 ILE 189 -0.19 LYS 174

ASN 212 0.38 LYS 190 -0.44 ASN 169

ASN 212 0.42 ARG 191 -0.59 VAL 199

ASN 212 0.36 GLY 192 -0.72 GLU 3

GLY 147 0.38 THR 193 -0.60 GLU 3

VAL 150 0.40 GLY 194 -0.87 GLU 3

VAL 150 0.48 ASN 195 -0.70 GLU 3

VAL 150 0.38 SER 196 -0.67 GLU 3

VAL 150 0.34 TYR 197 -0.56 GLU 3

VAL 150 0.30 GLY 198 -0.58 GLU 3

VAL 150 0.45 VAL 199 -0.59 ARG 191

ASN 212 0.22 CYS 200 -0.50 ARG 191

ASN 212 0.19 GLY 201 -0.45 GLU 3

VAL 150 0.26 LEU 202 -0.37 GLU 3

PRO 115 0.26 TYR 203 -0.47 GLU 3

VAL 150 0.21 THR 204 -0.41 SER 29

VAL 150 0.20 SER 205 -0.53 ALA 30

ILE 189 0.28 SER 206 -0.49 ALA 30

VAL 132 0.31 PHE 207 -0.47 ALA 30

VAL 130 0.45 TYR 208 -0.50 ILE 34

VAL 164 0.38 PRO 209 -0.47 ALA 105

ASN 127 0.55 VAL 210 -0.48 ALA 105

ASN 127 0.61 LYS 211 -0.64 ALA 105

ASN 127 0.87 ASN 212 -0.72 ALA 104

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.

*** 9pap priemra opcion ***

CA distance fluctuations for 240110225601577892

--- normal mode 16 ---

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

* 9pap priemra opcion *