Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 5C4 *

CA distance fluctuations for 2609171238041353664

--- 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
GLU 103 1.27 ALA 1 -0.49 HIS 38

ILE 102 1.14 PRO 2 -0.40 GLU 39

SER 9 0.84 GLU 3 -0.46 GLU 39

PHE 11 0.60 LEU 4 -0.24 GLU 3

SER 9 0.55 LEU 5 -0.24 SER 37

PHE 11 0.32 GLY 6 -0.58 GLU 3

PHE 11 0.23 GLY 7 -0.64 PRO 2

ALA 109 0.21 PRO 8 -0.76 PRO 2

ALA 109 0.20 SER 9 -0.93 PRO 2

SER 145 0.17 VAL 10 -0.96 PRO 2

PRO 165 0.18 PHE 11 -0.89 PRO 2

PRO 165 0.15 LEU 12 -0.82 PRO 2

PRO 165 0.17 PHE 13 -0.70 PRO 2

PRO 165 0.13 PRO 14 -0.64 PRO 2

PRO 165 0.10 PRO 15 -0.57 PRO 2

PRO 2 0.11 LYS 16 -0.52 PRO 2

PRO 2 0.13 PRO 17 -0.48 PRO 2

PRO 2 0.10 LYS 18 -0.44 PRO 2

PRO 2 0.07 ASP 19 -0.47 PRO 2

PRO 2 0.08 THR 20 -0.48 ALA 1

PRO 2 0.09 LEU 21 -0.44 ALA 1

PRO 2 0.07 MET 22 -0.42 ALA 1

PRO 2 0.05 ILE 23 -0.42 ALA 1

PRO 2 0.04 SER 24 -0.41 ALA 1

SER 170 0.04 ARG 25 -0.44 ALA 1

SER 170 0.06 THR 26 -0.47 ALA 1

SER 170 0.06 PRO 27 -0.51 ALA 1

LEU 168 0.09 GLU 28 -0.55 PRO 2

PRO 165 0.11 VAL 29 -0.62 PRO 2

LEU 168 0.14 THR 30 -0.66 PRO 2

LEU 168 0.15 CYS 31 -0.73 PRO 2

LEU 168 0.18 VAL 32 -0.73 PRO 2

ALA 109 0.18 VAL 33 -0.75 PRO 2

ALA 109 0.22 VAL 34 -0.69 PRO 2

ALA 109 0.25 ASP 35 -0.60 PRO 2

ALA 109 0.22 VAL 36 -0.55 PRO 2

LYS 110 0.23 SER 37 -0.42 PRO 2

LYS 110 0.23 HIS 38 -0.49 ALA 1

LYS 110 0.22 GLU 39 -0.49 ALA 1

LYS 110 0.20 ASP 40 -0.40 ALA 1

LYS 110 0.20 PRO 41 -0.44 ALA 1

LYS 110 0.18 GLU 42 -0.48 ALA 1

LYS 110 0.16 VAL 43 -0.57 ALA 1

LYS 110 0.14 LYS 44 -0.60 ALA 1

LYS 110 0.13 PHE 45 -0.66 ALA 1

LYS 110 0.11 ASN 46 -0.68 ALA 1

LEU 168 0.09 TRP 47 -0.69 ALA 1

LEU 168 0.08 TYR 48 -0.69 ALA 1

LEU 168 0.06 VAL 49 -0.65 ALA 1

PRO 2 0.05 ASP 50 -0.65 ALA 1

GLY 111 0.06 GLY 51 -0.68 ALA 1

GLY 111 0.06 VAL 52 -0.61 ALA 1

GLY 111 0.08 GLU 53 -0.61 ALA 1

GLY 111 0.08 VAL 54 -0.58 ALA 1

GLY 111 0.09 HIS 55 -0.54 ALA 1

GLY 172 0.09 ASN 56 -0.52 ALA 1

GLY 172 0.10 ALA 57 -0.56 ALA 1

GLY 172 0.12 LYS 58 -0.52 ALA 1

GLY 172 0.14 THR 59 -0.53 ALA 1

GLY 172 0.16 LYS 60 -0.50 PRO 2

GLY 172 0.17 PRO 61 -0.46 PRO 2

LYS 110 0.20 ARG 62 -0.48 PRO 2

GLY 172 0.22 GLU 63 -0.47 PRO 2

LYS 110 0.26 GLU 64 -0.43 PRO 2

LYS 110 0.29 GLN 65 -0.45 PRO 2

LYS 110 0.35 TYR 66 -0.38 PRO 2

LYS 110 0.34 ASN 67 -0.38 PRO 2

LYS 110 0.30 SER 68 -0.47 ALA 1

LYS 110 0.27 THR 69 -0.44 PRO 2

LYS 110 0.24 TYR 70 -0.49 PRO 2

LYS 110 0.22 ARG 71 -0.57 PRO 2

LYS 110 0.18 VAL 72 -0.59 PRO 2

LEU 168 0.17 VAL 73 -0.61 PRO 2

LEU 168 0.14 SER 74 -0.61 PRO 2

LEU 168 0.12 VAL 75 -0.58 PRO 2

LEU 168 0.10 LEU 76 -0.59 ALA 1

LEU 168 0.08 THR 77 -0.54 ALA 1

LEU 168 0.06 VAL 78 -0.55 ALA 1

LEU 168 0.05 LEU 79 -0.51 ALA 1

PRO 2 0.06 HIS 80 -0.49 ALA 1

PRO 2 0.06 GLN 81 -0.48 ALA 1

PRO 2 0.06 ASP 82 -0.53 ALA 1

PRO 2 0.08 TRP 83 -0.55 ALA 1

PRO 2 0.10 LEU 84 -0.50 ALA 1

PRO 2 0.09 ASN 85 -0.51 ALA 1

PRO 2 0.10 GLY 86 -0.56 ALA 1

PRO 2 0.08 LYS 87 -0.60 ALA 1

PRO 2 0.08 GLU 88 -0.69 ALA 1

PRO 165 0.08 TYR 89 -0.71 ALA 1

LEU 168 0.09 LYS 90 -0.80 ALA 1

LEU 168 0.11 CYS 91 -0.80 ALA 1

ALA 109 0.11 LYS 92 -0.84 ALA 1

ALA 109 0.14 VAL 93 -0.78 ALA 1

ALA 109 0.14 SER 94 -0.70 ALA 1

ALA 109 0.17 ASN 95 -0.60 ALA 1

LYS 110 0.17 LYS 96 -0.49 ALA 1

ALA 109 0.19 ALA 97 -0.49 ALA 1

ALA 109 0.17 LEU 98 -0.65 ALA 1

PHE 11 0.17 PRO 99 -0.62 ALA 1

ALA 109 0.14 ALA 100 -0.82 ALA 1

ALA 109 0.13 PRO 101 -0.88 ALA 1

ALA 109 0.14 ILE 102 -1.03 PRO 2

PRO 165 0.11 GLU 103 -1.04 ALA 1

PRO 165 0.12 LYS 104 -0.98 PRO 2

PRO 2 0.10 THR 105 -0.87 ALA 1

PRO 2 0.12 ILE 106 -0.75 ALA 1

PRO 2 0.12 SER 107 -0.66 ALA 1

PRO 2 0.13 LYS 108 -0.58 ALA 1

PRO 2 0.17 ALA 109 -0.55 ALA 1

PRO 2 0.16 LYS 110 -0.53 ALA 1

PRO 2 0.17 GLY 111 -0.46 ALA 1

PRO 2 0.16 GLN 112 -0.41 ALA 1

PRO 2 0.16 PRO 113 -0.41 ALA 1

PRO 2 0.18 ARG 114 -0.36 ALA 1

PRO 2 0.17 GLU 115 -0.34 ALA 1

PRO 2 0.19 PRO 116 -0.33 ALA 1

PRO 2 0.20 GLN 117 -0.29 PRO 2

PRO 2 0.20 VAL 118 -0.29 PRO 2

PRO 2 0.21 TYR 119 -0.26 PRO 2

PRO 2 0.21 THR 120 -0.25 PRO 2

PRO 2 0.23 LEU 121 -0.23 PRO 2

PRO 2 0.22 PRO 122 -0.22 PRO 2

PRO 2 0.24 PRO 123 -0.20 PRO 2

ALA 1 0.26 SER 124 -0.18 PRO 2

ALA 1 0.25 ARG 125 -0.17 PRO 2

ALA 1 0.28 ASP 126 -0.16 PRO 2

ALA 1 0.27 GLU 127 -0.17 PRO 2

ALA 1 0.24 LEU 128 -0.17 PRO 2

ALA 1 0.26 THR 129 -0.16 PRO 2

ALA 1 0.26 LYS 130 -0.17 PRO 2

ALA 1 0.23 ASN 131 -0.18 PRO 2

ALA 1 0.23 GLN 132 -0.20 PRO 2

ALA 1 0.24 VAL 133 -0.21 PRO 2

PRO 2 0.25 SER 134 -0.22 PRO 2

PRO 2 0.23 LEU 135 -0.24 PRO 2

PRO 2 0.24 THR 136 -0.25 PRO 2

PRO 2 0.22 CYS 137 -0.27 PRO 2

PRO 2 0.24 LEU 138 -0.27 PRO 2

PRO 2 0.23 VAL 139 -0.30 PRO 2

PRO 2 0.24 LYS 140 -0.29 PRO 2

PRO 2 0.23 GLY 141 -0.30 ALA 1

PRO 2 0.21 PHE 142 -0.35 ALA 1

PRO 2 0.20 TYR 143 -0.39 ALA 1

PRO 2 0.19 PRO 144 -0.44 ALA 1

PRO 2 0.22 SER 145 -0.43 PRO 2

PRO 2 0.18 ASP 146 -0.46 PRO 2

PRO 2 0.18 ILE 147 -0.41 PRO 2

PRO 2 0.16 ALA 148 -0.40 PRO 2

PRO 2 0.17 VAL 149 -0.36 PRO 2

PRO 2 0.16 GLU 150 -0.34 PRO 2

PRO 2 0.16 TRP 151 -0.31 PRO 2

PRO 2 0.13 GLU 152 -0.30 PRO 2

PRO 2 0.13 SER 153 -0.28 PRO 2

PRO 2 0.11 ASN 154 -0.27 PRO 2

PRO 2 0.10 GLY 155 -0.29 PRO 2

PRO 2 0.10 GLN 156 -0.30 PRO 2

PRO 2 0.11 PRO 157 -0.31 PRO 2

PRO 2 0.15 GLU 158 -0.29 PRO 2

PRO 2 0.16 ASN 159 -0.30 PRO 2

PRO 2 0.19 ASN 160 -0.28 PRO 2

PRO 2 0.21 TYR 161 -0.29 PRO 2

PRO 2 0.25 LYS 162 -0.30 PRO 2

PRO 2 0.25 THR 163 -0.32 PRO 2

PRO 2 0.30 THR 164 -0.31 PRO 2

PRO 2 0.30 PRO 165 -0.35 PRO 2

PRO 2 0.28 PRO 166 -0.36 PRO 2

PRO 2 0.32 VAL 167 -0.31 PRO 2

PRO 2 0.31 LEU 168 -0.31 PRO 2

PRO 2 0.30 ASP 169 -0.26 PRO 2

PRO 2 0.31 SER 170 -0.23 PRO 2

PRO 2 0.27 ASP 171 -0.26 ALA 1

PRO 2 0.27 GLY 172 -0.30 ALA 1

PRO 2 0.25 SER 173 -0.32 ALA 1

PRO 2 0.26 PHE 174 -0.33 PRO 2

PRO 2 0.27 PHE 175 -0.31 PRO 2

PRO 2 0.27 LEU 176 -0.31 PRO 2

PRO 2 0.27 TYR 177 -0.28 PRO 2

PRO 2 0.24 SER 178 -0.29 PRO 2

PRO 2 0.25 LYS 179 -0.27 PRO 2

PRO 2 0.22 LEU 180 -0.27 PRO 2

PRO 2 0.22 THR 181 -0.24 PRO 2

PRO 2 0.20 VAL 182 -0.24 PRO 2

PRO 2 0.19 ASP 183 -0.22 PRO 2

ALA 1 0.20 LYS 184 -0.20 PRO 2

PRO 2 0.18 SER 185 -0.20 PRO 2

PRO 2 0.17 ARG 186 -0.22 PRO 2

PRO 2 0.18 TRP 187 -0.22 PRO 2

PRO 2 0.18 GLN 188 -0.20 PRO 2

PRO 2 0.16 GLN 189 -0.21 PRO 2

PRO 2 0.16 GLY 190 -0.22 PRO 2

PRO 2 0.15 ASN 191 -0.23 PRO 2

PRO 2 0.15 VAL 192 -0.25 PRO 2

PRO 2 0.16 PHE 193 -0.26 PRO 2

PRO 2 0.15 SER 194 -0.28 PRO 2

PRO 2 0.17 CYS 195 -0.30 PRO 2

PRO 2 0.15 SER 196 -0.33 PRO 2

PRO 2 0.16 VAL 197 -0.35 PRO 2

PRO 2 0.14 MET 198 -0.38 PRO 2

PRO 2 0.15 HIS 199 -0.40 ALA 1

PRO 2 0.13 GLU 200 -0.42 ALA 1

PRO 2 0.14 ALA 201 -0.39 ALA 1

PRO 2 0.13 LEU 202 -0.36 ALA 1

PRO 2 0.11 HIS 203 -0.35 ALA 1

PRO 2 0.09 ASN 204 -0.37 ALA 1

PRO 2 0.11 HIS 205 -0.39 ALA 1

PRO 2 0.12 TYR 206 -0.36 ALA 1

PRO 2 0.14 THR 207 -0.32 ALA 1

PRO 2 0.14 GLN 208 -0.31 PRO 2

PRO 2 0.16 LYS 209 -0.28 PRO 2

PRO 2 0.16 SER 210 -0.26 PRO 2

PRO 2 0.18 LEU 211 -0.25 PRO 2

PRO 2 0.17 SER 212 -0.23 PRO 2

PRO 2 0.18 LEU 213 -0.21 PRO 2

PRO 2 0.18 SER 214 -0.20 PRO 2

PRO 2 0.17 PRO 215 -0.19 PRO 2

PRO 2 0.18 GLY 216 -0.18 PRO 2

PRO 2 0.18 LYS 217 -0.17 PRO 2

HIS 38 0.47 ALA 1 -1.04 GLU 103

GLU 39 0.35 PRO 2 -1.03 ILE 102

GLU 39 0.38 GLU 3 -0.79 SER 9

PRO 2 0.29 LEU 4 -0.56 PHE 11

PRO 2 0.22 LEU 5 -0.56 SER 9

GLU 3 0.55 GLY 6 -0.35 PHE 11

PRO 2 0.67 GLY 7 -0.25 PHE 11

PRO 2 0.84 PRO 8 -0.20 ALA 109

PRO 2 1.07 SER 9 -0.19 ALA 109

PRO 2 1.12 VAL 10 -0.17 PRO 165

PRO 2 1.03 PHE 11 -0.18 PRO 165

PRO 2 0.95 LEU 12 -0.15 PRO 165

PRO 2 0.81 PHE 13 -0.17 PRO 165

ALA 1 0.74 PRO 14 -0.13 PRO 165

ALA 1 0.67 PRO 15 -0.10 PRO 165

ALA 1 0.60 LYS 16 -0.09 PRO 165

ALA 1 0.56 PRO 17 -0.09 PRO 2

ALA 1 0.52 LYS 18 -0.07 PRO 2

ALA 1 0.56 ASP 19 -0.05 LYS 162

ALA 1 0.58 THR 20 -0.05 PRO 2

ALA 1 0.52 LEU 21 -0.06 PRO 2

ALA 1 0.50 MET 22 -0.04 PRO 2

ALA 1 0.50 ILE 23 -0.03 SER 170

ALA 1 0.49 SER 24 -0.03 SER 170

ALA 1 0.52 ARG 25 -0.05 SER 170

ALA 1 0.56 THR 26 -0.06 SER 170

ALA 1 0.61 PRO 27 -0.06 LEU 168

ALA 1 0.66 GLU 28 -0.09 LEU 168

ALA 1 0.74 VAL 29 -0.11 PRO 165

PRO 2 0.76 THR 30 -0.13 PRO 165

PRO 2 0.85 CYS 31 -0.14 LEU 168

PRO 2 0.85 VAL 32 -0.17 LEU 168

PRO 2 0.86 VAL 33 -0.18 ALA 109

PRO 2 0.78 VAL 34 -0.22 ALA 109

PRO 2 0.66 ASP 35 -0.25 ALA 109

PRO 2 0.61 VAL 36 -0.22 ALA 109

PRO 2 0.45 SER 37 -0.23 ILE 106

ALA 1 0.47 HIS 38 -0.23 LYS 110

ALA 1 0.46 GLU 39 -0.22 THR 105

ALA 1 0.42 ASP 40 -0.20 LYS 110

ALA 1 0.48 PRO 41 -0.20 LYS 110

ALA 1 0.53 GLU 42 -0.17 LYS 110

ALA 1 0.65 VAL 43 -0.16 LYS 110

ALA 1 0.69 LYS 44 -0.14 LYS 110

ALA 1 0.77 PHE 45 -0.12 LYS 110

ALA 1 0.80 ASN 46 -0.10 LYS 110

ALA 1 0.81 TRP 47 -0.09 LEU 168

ALA 1 0.81 TYR 48 -0.07 LEU 168

ALA 1 0.76 VAL 49 -0.06 LEU 168

ALA 1 0.76 ASP 50 -0.05 LEU 168

ALA 1 0.79 GLY 51 -0.06 LEU 168

ALA 1 0.70 VAL 52 -0.06 GLY 111

ALA 1 0.71 GLU 53 -0.07 GLY 111

ALA 1 0.67 VAL 54 -0.07 GLY 111

ALA 1 0.63 HIS 55 -0.09 GLY 111

ALA 1 0.61 ASN 56 -0.09 GLY 172

ALA 1 0.66 ALA 57 -0.10 LEU 168

ALA 1 0.62 LYS 58 -0.12 GLY 172

ALA 1 0.62 THR 59 -0.14 GLY 172

ALA 1 0.57 LYS 60 -0.16 GLY 172

ALA 1 0.52 PRO 61 -0.17 LYS 110

PRO 2 0.54 ARG 62 -0.20 LYS 110

PRO 2 0.53 GLU 63 -0.22 LYS 110

PRO 2 0.48 GLU 64 -0.26 LYS 110

PRO 2 0.50 GLN 65 -0.29 LYS 110

PRO 2 0.43 TYR 66 -0.35 LYS 110

PRO 2 0.42 ASN 67 -0.34 ALA 109

ALA 1 0.46 SER 68 -0.30 LYS 110

PRO 2 0.48 THR 69 -0.27 ALA 109

PRO 2 0.55 TYR 70 -0.24 LYS 110

PRO 2 0.65 ARG 71 -0.22 ALA 109

PRO 2 0.67 VAL 72 -0.18 ALA 109

PRO 2 0.70 VAL 73 -0.17 LEU 168

ALA 1 0.71 SER 74 -0.14 LEU 168

ALA 1 0.69 VAL 75 -0.12 LEU 168

ALA 1 0.70 LEU 76 -0.10 LEU 168

ALA 1 0.64 THR 77 -0.08 LEU 168

ALA 1 0.65 VAL 78 -0.06 LEU 168

ALA 1 0.60 LEU 79 -0.05 LEU 168

ALA 1 0.58 HIS 80 -0.03 SER 170

ALA 1 0.57 GLN 81 -0.03 PRO 2

ALA 1 0.63 ASP 82 -0.03 LEU 168

ALA 1 0.66 TRP 83 -0.05 PRO 2

ALA 1 0.60 LEU 84 -0.06 PRO 2

ALA 1 0.60 ASN 85 -0.06 PRO 2

ALA 1 0.67 GLY 86 -0.07 PRO 2

ALA 1 0.71 LYS 87 -0.05 PRO 2

ALA 1 0.82 GLU 88 -0.05 PRO 165

ALA 1 0.86 TYR 89 -0.07 PRO 165

ALA 1 0.97 LYS 90 -0.09 PRO 165

ALA 1 0.97 CYS 91 -0.11 PRO 165

ALA 1 1.00 LYS 92 -0.11 ALA 109

ALA 1 0.92 VAL 93 -0.13 ALA 109

ALA 1 0.79 SER 94 -0.14 ALA 109

ALA 1 0.65 ASN 95 -0.16 ALA 109

ALA 1 0.50 LYS 96 -0.17 ALA 109

ALA 1 0.49 ALA 97 -0.20 PHE 11

ALA 1 0.66 LEU 98 -0.18 PHE 11

ALA 1 0.56 PRO 99 -0.18 PHE 11

ALA 1 0.83 ALA 100 -0.13 PHE 13

ALA 1 0.98 PRO 101 -0.13 ALA 109

ALA 1 1.22 ILE 102 -0.13 ALA 109

ALA 1 1.27 GLU 103 -0.11 PRO 165

ALA 1 1.20 LYS 104 -0.12 PRO 165

ALA 1 1.06 THR 105 -0.09 PRO 165

ALA 1 0.91 ILE 106 -0.09 PRO 165

ALA 1 0.79 SER 107 -0.08 PRO 2

ALA 1 0.69 LYS 108 -0.09 PRO 2

ALA 1 0.65 ALA 109 -0.12 PRO 2

ALA 1 0.62 LYS 110 -0.11 PRO 2

ALA 1 0.53 GLY 111 -0.12 PRO 2

ALA 1 0.48 GLN 112 -0.12 PRO 2

ALA 1 0.48 PRO 113 -0.12 PRO 2

ALA 1 0.43 ARG 114 -0.14 PRO 2

ALA 1 0.41 GLU 115 -0.13 PRO 2

ALA 1 0.39 PRO 116 -0.15 PRO 2

ALA 1 0.35 GLN 117 -0.16 PRO 2

ALA 1 0.34 VAL 118 -0.16 PRO 2

ALA 1 0.31 TYR 119 -0.17 PRO 2

ALA 1 0.30 THR 120 -0.17 PRO 2

PRO 2 0.27 LEU 121 -0.19 PRO 2

PRO 2 0.26 PRO 122 -0.19 PRO 2

PRO 2 0.25 PRO 123 -0.20 PRO 2

PRO 2 0.22 SER 124 -0.22 PRO 2

PRO 2 0.21 ARG 125 -0.21 PRO 2

PRO 2 0.19 ASP 126 -0.23 PRO 2

PRO 2 0.21 GLU 127 -0.22 PRO 2

PRO 2 0.21 LEU 128 -0.20 PRO 2

PRO 2 0.20 THR 129 -0.21 PRO 2

PRO 2 0.21 LYS 130 -0.21 PRO 2

PRO 2 0.23 ASN 131 -0.19 PRO 2

PRO 2 0.25 GLN 132 -0.19 PRO 2

PRO 2 0.25 VAL 133 -0.20 PRO 2

PRO 2 0.27 SER 134 -0.21 PRO 2

PRO 2 0.29 LEU 135 -0.19 PRO 2

PRO 2 0.30 THR 136 -0.20 PRO 2

PRO 2 0.32 CYS 137 -0.18 PRO 2

PRO 2 0.32 LEU 138 -0.20 PRO 2

ALA 1 0.36 VAL 139 -0.18 PRO 2

ALA 1 0.35 LYS 140 -0.19 PRO 2

ALA 1 0.36 GLY 141 -0.18 PRO 2

ALA 1 0.42 PHE 142 -0.16 PRO 2

ALA 1 0.47 TYR 143 -0.15 PRO 2

ALA 1 0.52 PRO 144 -0.15 PRO 2

ALA 1 0.50 SER 145 -0.17 PRO 2

ALA 1 0.54 ASP 146 -0.14 PRO 2

ALA 1 0.49 ILE 147 -0.13 PRO 2

ALA 1 0.46 ALA 148 -0.12 PRO 2

ALA 1 0.41 VAL 149 -0.14 PRO 2

PRO 2 0.40 GLU 150 -0.12 PRO 2

PRO 2 0.36 TRP 151 -0.12 PRO 2

ALA 1 0.35 GLU 152 -0.10 PRO 2

ALA 1 0.32 SER 153 -0.10 PRO 2

ALA 1 0.32 ASN 154 -0.08 PRO 2

ALA 1 0.35 GLY 155 -0.07 PRO 2

ALA 1 0.35 GLN 156 -0.07 PRO 2

PRO 2 0.36 PRO 157 -0.08 PRO 2

PRO 2 0.34 GLU 158 -0.11 PRO 2

PRO 2 0.36 ASN 159 -0.12 PRO 2

PRO 2 0.33 ASN 160 -0.16 PRO 2

PRO 2 0.34 TYR 161 -0.18 PRO 2

PRO 2 0.36 LYS 162 -0.21 PRO 2

PRO 2 0.38 THR 163 -0.21 PRO 2

PRO 2 0.37 THR 164 -0.25 PRO 2

PRO 2 0.41 PRO 165 -0.25 PRO 2

PRO 2 0.41 PRO 166 -0.23 PRO 2

PRO 2 0.37 VAL 167 -0.26 PRO 2

ALA 1 0.36 LEU 168 -0.26 PRO 2

ALA 1 0.31 ASP 169 -0.25 PRO 2

ALA 1 0.27 SER 170 -0.25 PRO 2

ALA 1 0.31 ASP 171 -0.22 PRO 2

ALA 1 0.36 GLY 172 -0.21 PRO 2

ALA 1 0.39 SER 173 -0.20 PRO 2

ALA 1 0.39 PHE 174 -0.21 PRO 2

ALA 1 0.36 PHE 175 -0.22 PRO 2

PRO 2 0.36 LEU 176 -0.22 PRO 2

PRO 2 0.34 TYR 177 -0.22 PRO 2

PRO 2 0.35 SER 178 -0.20 PRO 2

PRO 2 0.32 LYS 179 -0.21 PRO 2

PRO 2 0.32 LEU 180 -0.18 PRO 2

PRO 2 0.29 THR 181 -0.19 PRO 2

PRO 2 0.28 VAL 182 -0.16 PRO 2

PRO 2 0.26 ASP 183 -0.16 PRO 2

PRO 2 0.24 LYS 184 -0.17 PRO 2

PRO 2 0.24 SER 185 -0.15 PRO 2

PRO 2 0.26 ARG 186 -0.14 PRO 2

PRO 2 0.26 TRP 187 -0.15 PRO 2

PRO 2 0.24 GLN 188 -0.15 PRO 2

PRO 2 0.25 GLN 189 -0.13 PRO 2

PRO 2 0.26 GLY 190 -0.13 PRO 2

PRO 2 0.28 ASN 191 -0.12 PRO 2

ALA 1 0.29 VAL 192 -0.12 PRO 2

PRO 2 0.31 PHE 193 -0.13 PRO 2

ALA 1 0.33 SER 194 -0.12 PRO 2

ALA 1 0.35 CYS 195 -0.13 PRO 2

ALA 1 0.39 SER 196 -0.11 PRO 2

ALA 1 0.41 VAL 197 -0.12 PRO 2

ALA 1 0.46 MET 198 -0.10 PRO 2

ALA 1 0.47 HIS 199 -0.11 PRO 2

ALA 1 0.50 GLU 200 -0.09 PRO 2

ALA 1 0.46 ALA 201 -0.10 PRO 2

ALA 1 0.43 LEU 202 -0.10 PRO 2

ALA 1 0.42 HIS 203 -0.08 PRO 2

ALA 1 0.44 ASN 204 -0.06 PRO 2

ALA 1 0.46 HIS 205 -0.08 PRO 2

ALA 1 0.43 TYR 206 -0.09 PRO 2

ALA 1 0.39 THR 207 -0.10 PRO 2

ALA 1 0.37 GLN 208 -0.11 PRO 2

ALA 1 0.34 LYS 209 -0.13 PRO 2

ALA 1 0.31 SER 210 -0.13 PRO 2

ALA 1 0.29 LEU 211 -0.14 PRO 2

PRO 2 0.27 SER 212 -0.14 PRO 2

PRO 2 0.25 LEU 213 -0.15 PRO 2

PRO 2 0.24 SER 214 -0.15 PRO 2

PRO 2 0.23 PRO 215 -0.14 PRO 2

PRO 2 0.21 GLY 216 -0.15 PRO 2

PRO 2 0.20 LYS 217 -0.15 PRO 2

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** 5C4 ***

CA distance fluctuations for 2609171238041353664

--- normal mode 8 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 5C4 *