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

* EXSA_mono1 *

CA distance fluctuations for 2401041300303831936

--- 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
VAL 130 0.32 MET 1 -0.15 GLY 210

HIS 16 0.28 GLN 2 -0.15 GLY 210

VAL 130 0.23 GLY 3 -0.17 GLY 210

LYS 10 0.28 ALA 4 -0.09 TYR 209

LYS 10 0.28 LYS 5 -0.07 ARG 91

ARG 257 0.30 SER 6 -0.10 PHE 84

ARG 258 0.28 LEU 7 -0.12 MET 136

ARG 258 0.28 GLY 8 -0.11 PRO 135

VAL 211 0.26 ARG 9 -0.11 PRO 135

ALA 4 0.28 LYS 10 -0.02 LYS 28

ARG 258 0.23 GLN 11 -0.02 LYS 28

ARG 274 0.22 ILE 12 -0.02 LYS 28

LYS 5 0.26 THR 13 -0.02 LYS 28

ASN 278 0.27 SER 14 -0.02 LYS 28

MET 1 0.27 CYS 15 -0.01 LYS 28

MET 1 0.29 HIS 16 -0.01 ARG 74

MET 1 0.26 TRP 17 -0.01 ALA 111

MET 1 0.25 ASN 18 -0.01 ALA 113

MET 1 0.22 ILE 19 -0.01 ALA 113

MET 1 0.21 PRO 20 -0.01 PRO 153

MET 1 0.19 THR 21 -0.01 PRO 153

GLY 210 0.18 PHE 22 -0.01 ARG 168

GLY 210 0.20 GLU 23 -0.01 PRO 107

GLY 210 0.22 TYR 24 -0.01 PRO 107

GLY 210 0.25 ARG 25 -0.01 CYS 15

GLY 210 0.27 VAL 26 -0.01 SER 14

GLY 210 0.29 ASN 27 -0.01 TRP 77

GLY 210 0.35 LYS 28 -0.03 PRO 79

GLY 210 0.31 GLU 29 -0.01 GLN 11

GLY 210 0.22 GLU 30 -0.02 ARG 168

GLY 210 0.21 GLY 31 -0.02 LYS 28

GLY 210 0.18 VAL 32 -0.02 ARG 168

GLY 210 0.18 TYR 33 -0.02 ARG 168

ASN 278 0.17 VAL 34 -0.02 ARG 168

ASN 278 0.18 LEU 35 -0.02 ARG 168

ASN 278 0.21 LEU 36 -0.01 ARG 168

MET 1 0.22 GLU 37 -0.01 PHE 151

MET 1 0.21 GLY 38 -0.02 ALA 113

MET 1 0.19 GLU 39 -0.02 ALA 113

MET 1 0.18 LEU 40 -0.02 ARG 168

GLY 210 0.16 THR 41 -0.02 ARG 168

GLY 210 0.17 VAL 42 -0.03 ARG 168

GLY 210 0.16 GLN 43 -0.03 ARG 168

GLY 210 0.16 ASP 44 -0.04 ARG 168

GLY 210 0.14 ILE 45 -0.04 ARG 168

GLY 210 0.12 ASP 46 -0.05 ARG 168

GLY 210 0.13 SER 47 -0.05 ARG 168

GLY 210 0.14 THR 48 -0.04 ARG 168

GLY 210 0.14 PHE 49 -0.04 ARG 168

ASN 278 0.14 CYS 50 -0.03 ARG 168

ASN 278 0.15 LEU 51 -0.03 ARG 168

ASN 278 0.16 ALA 52 -0.02 ARG 168

ASN 278 0.18 PRO 53 -0.02 ARG 168

ASN 278 0.16 GLY 54 -0.02 ARG 168

ASN 278 0.14 GLU 55 -0.02 ARG 168

GLY 210 0.14 LEU 56 -0.02 ARG 168

GLY 210 0.15 LEU 57 -0.03 ARG 168

GLY 210 0.15 PHE 58 -0.03 ARG 168

GLY 210 0.18 VAL 59 -0.03 ARG 168

GLY 210 0.19 ARG 60 -0.03 ARG 168

GLY 210 0.23 ARG 61 -0.02 ARG 168

GLY 210 0.22 GLY 62 -0.02 ARG 168

GLY 210 0.22 SER 63 -0.02 ARG 168

GLY 210 0.20 TYR 64 -0.02 ARG 168

GLY 210 0.19 VAL 65 -0.02 ARG 168

GLY 210 0.19 VAL 66 -0.02 ARG 168

MET 1 0.18 SER 67 -0.01 ARG 168

MET 1 0.20 THR 68 -0.01 ALA 113

MET 1 0.19 LYS 69 -0.02 PRO 153

MET 1 0.22 GLY 70 -0.01 ALA 113

MET 1 0.23 LYS 71 -0.01 ALA 113

MET 1 0.26 ASP 72 -0.01 ALA 113

MET 1 0.24 SER 73 -0.01 ALA 113

MET 1 0.25 ARG 74 -0.01 HIS 16

ASN 278 0.22 ILE 75 -0.01 LYS 28

ASN 278 0.21 LEU 76 -0.02 LYS 28

GLY 210 0.21 TRP 77 -0.02 LYS 28

GLY 210 0.20 ILE 78 -0.02 LYS 28

GLY 210 0.25 PRO 79 -0.03 LYS 28

GLY 210 0.21 LEU 80 -0.02 SER 6

GLY 210 0.25 SER 81 -0.06 SER 6

VAL 208 0.15 ALA 82 -0.09 SER 6

PHE 84 0.12 GLN 83 -0.11 GLY 3

GLN 83 0.12 PHE 84 -0.10 SER 6

GLY 210 0.10 LEU 85 -0.07 SER 6

GLY 210 0.04 GLN 86 -0.10 GLY 3

MET 136 0.05 GLY 87 -0.11 GLY 3

GLY 210 0.04 PHE 88 -0.08 SER 6

GLY 210 0.03 VAL 89 -0.11 LYS 179

MET 136 0.04 GLN 90 -0.12 LYS 179

MET 136 0.03 ARG 91 -0.11 LYS 179

SER 166 0.02 PHE 92 -0.14 LYS 179

ARG 163 0.03 GLY 93 -0.18 LYS 179

ARG 163 0.02 ALA 94 -0.21 LYS 179

ASP 271 0.02 LEU 95 -0.16 LYS 179

ASP 271 0.03 LEU 96 -0.15 LYS 179

GLN 164 0.02 SER 97 -0.18 LYS 179

ASP 271 0.02 GLU 98 -0.15 LYS 179

GLY 210 0.03 VAL 99 -0.13 LYS 179

GLY 210 0.03 GLU 100 -0.13 LYS 179

GLY 210 0.03 ARG 101 -0.13 LYS 179

GLY 210 0.05 CYS 102 -0.11 GLU 193

GLY 210 0.04 ASP 103 -0.11 GLU 193

GLY 210 0.06 GLU 104 -0.09 GLU 193

GLY 210 0.07 PRO 105 -0.09 ARG 168

GLY 210 0.09 VAL 106 -0.08 ARG 168

GLY 210 0.12 PRO 107 -0.06 ARG 168

GLY 210 0.15 GLY 108 -0.05 ARG 168

GLY 210 0.14 ILE 109 -0.05 ARG 168

GLY 210 0.13 ILE 110 -0.05 ARG 168

GLY 210 0.12 ALA 111 -0.04 ARG 168

GLY 210 0.11 PHE 112 -0.04 LYS 179

ALA 275 0.11 ALA 113 -0.04 LYS 179

ALA 275 0.13 ALA 114 -0.03 LYS 179

ALA 275 0.12 THR 115 -0.04 LYS 179

ALA 275 0.13 PRO 116 -0.04 LYS 179

ASP 271 0.12 LEU 117 -0.04 LYS 179

ARG 274 0.13 LEU 118 -0.03 LYS 179

ALA 275 0.15 ALA 119 -0.02 LYS 179

ALA 275 0.16 GLY 120 -0.02 LYS 179

ARG 274 0.15 CYS 121 -0.01 ARG 91

ARG 274 0.18 VAL 122 -0.01 LYS 28

ALA 275 0.20 LYS 123 -0.01 LYS 28

ARG 274 0.20 GLY 124 -0.01 LYS 28

ARG 274 0.21 LEU 125 -0.01 LYS 28

ARG 274 0.24 LYS 126 -0.01 LYS 28

ARG 274 0.26 GLU 127 -0.01 LYS 28

ARG 274 0.29 LEU 128 -0.01 LYS 28

ARG 274 0.31 LEU 129 -0.02 LYS 28

ASN 278 0.34 VAL 130 -0.01 LYS 28

ARG 274 0.36 HIS 131 -0.02 ARG 9

ARG 274 0.42 GLU 132 -0.05 ARG 9

ARG 274 0.35 HIS 133 -0.07 ARG 9

ARG 274 0.30 PRO 134 -0.09 GLY 8

PHE 259 0.27 PRO 135 -0.11 GLY 8

LEU 223 0.21 MET 136 -0.12 LEU 7

ARG 274 0.19 LEU 137 -0.06 ARG 9

ARG 274 0.19 ALA 138 -0.04 ARG 9

LEU 223 0.14 CYS 139 -0.07 LEU 7

ASP 271 0.12 LEU 140 -0.06 LEU 7

ARG 274 0.15 LYS 141 -0.02 SER 6

ARG 274 0.12 ILE 142 -0.02 SER 6

ASP 271 0.09 GLU 143 -0.05 SER 6

ASP 271 0.10 GLU 144 -0.03 SER 6

ARG 274 0.11 LEU 145 -0.03 LYS 179

GLY 210 0.09 LEU 146 -0.04 LYS 179

ASP 271 0.07 MET 147 -0.07 LYS 179

ASP 271 0.09 LEU 148 -0.06 LYS 179

GLY 210 0.09 PHE 149 -0.06 LYS 179

GLY 210 0.07 ALA 150 -0.08 LYS 179

ASP 271 0.06 PHE 151 -0.09 LYS 179

ASP 271 0.07 SER 152 -0.07 LYS 179

GLY 210 0.07 PRO 153 -0.08 LYS 179

GLY 210 0.08 GLN 154 -0.07 LYS 179

GLY 210 0.07 GLY 155 -0.08 LYS 179

GLY 210 0.06 PRO 156 -0.10 LYS 179

GLY 210 0.08 LEU 157 -0.08 ARG 172

GLY 210 0.09 LEU 158 -0.07 LYS 179

GLY 210 0.06 MET 159 -0.10 LYS 179

GLY 210 0.06 SER 160 -0.10 ARG 172

GLY 210 0.09 VAL 161 -0.08 ARG 168

GLY 210 0.08 LEU 162 -0.07 ARG 172

GLY 210 0.04 ARG 163 -0.12 ARG 172

SER 207 0.06 GLN 164 -0.13 ARG 168

SER 207 0.10 LEU 165 -0.07 GLY 3

SER 207 0.03 SER 166 -0.09 GLY 3

GLN 90 0.02 ASN 167 -0.10 GLY 3

GLN 90 0.03 ARG 168 -0.13 GLN 164

LYS 28 0.06 HIS 169 -0.10 GLY 3

LYS 28 0.08 VAL 170 -0.11 GLY 3

MET 136 0.04 GLU 171 -0.11 GLY 3

PRO 135 0.06 ARG 172 -0.12 ARG 163

LYS 28 0.10 LEU 173 -0.10 GLY 3

SER 81 0.08 GLN 174 -0.11 GLY 3

PRO 135 0.07 LEU 175 -0.14 GLY 93

PRO 135 0.09 PHE 176 -0.16 ALA 94

PRO 135 0.11 MET 177 -0.13 ALA 94

PRO 135 0.12 GLU 178 -0.16 ALA 94

PRO 135 0.10 LYS 179 -0.21 ALA 94

PRO 135 0.11 HIS 180 -0.18 ALA 94

PRO 135 0.14 TYR 181 -0.14 ALA 94

PRO 134 0.14 LEU 182 -0.16 ALA 94

PRO 134 0.12 ASN 183 -0.17 ALA 94

LYS 10 0.12 GLU 184 -0.14 ALA 94

ARG 9 0.12 TRP 185 -0.13 ALA 94

ARG 9 0.13 LYS 186 -0.11 ALA 94

LYS 28 0.14 LEU 187 -0.11 NMA 278

LYS 28 0.13 SER 188 -0.11 NMA 278

ARG 9 0.11 ASP 189 -0.11 ALA 94

LYS 28 0.11 PHE 190 -0.11 ALA 94

LYS 28 0.12 SER 191 -0.10 NMA 278

LYS 28 0.10 ARG 192 -0.11 SER 97

ARG 9 0.08 GLU 193 -0.14 SER 97

LYS 28 0.08 PHE 194 -0.12 SER 97

LYS 28 0.08 GLY 195 -0.12 ARG 101

LYS 28 0.10 MET 196 -0.10 NMA 278

LYS 28 0.12 GLY 197 -0.11 NMA 278

LYS 28 0.14 LEU 198 -0.12 NMA 278

LYS 28 0.17 THR 199 -0.13 NMA 278

LYS 28 0.15 THR 200 -0.12 NMA 278

LYS 28 0.15 PHE 201 -0.12 NMA 278

LYS 28 0.20 LYS 202 -0.14 NMA 278

LYS 28 0.22 GLU 203 -0.14 NMA 278

LYS 28 0.19 LEU 204 -0.12 NMA 278

LYS 28 0.21 PHE 205 -0.13 NMA 278

LYS 28 0.27 GLY 206 -0.15 NMA 278

LYS 28 0.31 SER 207 -0.14 NMA 278

LYS 28 0.24 VAL 208 -0.14 GLY 3

LYS 28 0.25 TYR 209 -0.16 GLY 3

LYS 28 0.35 GLY 210 -0.17 GLY 3

LYS 28 0.28 VAL 211 -0.17 NMA 278

LYS 28 0.23 SER 212 -0.16 NMA 278

LYS 28 0.19 PRO 213 -0.14 NMA 278

ARG 9 0.19 ARG 214 -0.14 NMA 278

ARG 9 0.24 ALA 215 -0.16 NMA 278

ARG 9 0.22 TRP 216 -0.14 NMA 278

LYS 10 0.18 ILE 217 -0.12 NMA 278

LYS 10 0.21 SER 218 -0.11 NMA 278

LYS 10 0.24 GLU 219 -0.12 NMA 278

PRO 135 0.22 ARG 220 -0.10 GLY 3

PRO 135 0.19 ARG 221 -0.11 ALA 94

PRO 134 0.23 ILE 222 -0.09 ALA 94

PRO 134 0.27 LEU 223 -0.09 GLY 3

PRO 134 0.21 TYR 224 -0.11 ALA 94

PRO 134 0.21 ALA 225 -0.11 ALA 94

PRO 134 0.26 HIS 226 -0.08 ALA 94

PRO 134 0.23 GLN 227 -0.08 ALA 94

PRO 134 0.18 LEU 228 -0.11 ALA 94

PRO 134 0.20 LEU 229 -0.09 ALA 94

PRO 134 0.21 LEU 230 -0.07 ALA 94

PRO 134 0.16 ASN 231 -0.08 ALA 94

PRO 134 0.13 SER 232 -0.10 ALA 94

PRO 134 0.13 ASP 233 -0.10 ALA 94

PRO 134 0.13 MET 234 -0.12 ALA 94

GLU 132 0.14 SER 235 -0.11 ALA 94

GLU 132 0.17 ILE 236 -0.10 ALA 94

GLU 132 0.15 VAL 237 -0.12 ALA 94

PRO 134 0.13 ASP 238 -0.13 ALA 94

PRO 134 0.16 ILE 239 -0.13 ALA 94

PRO 134 0.16 ALA 240 -0.12 ALA 94

PRO 134 0.14 MET 241 -0.14 ALA 94

PRO 134 0.13 GLU 242 -0.16 ALA 94

PRO 134 0.16 ALA 243 -0.14 ALA 94

PRO 134 0.15 GLY 244 -0.15 ALA 94

PRO 134 0.16 PHE 245 -0.12 ALA 94

LYS 10 0.15 SER 246 -0.12 ALA 94

GLU 132 0.15 SER 247 -0.11 ALA 94

GLU 132 0.17 GLN 248 -0.10 ALA 94

GLU 132 0.18 SER 249 -0.09 ALA 94

SER 6 0.18 TYR 250 -0.09 ALA 94

GLU 132 0.19 PHE 251 -0.09 ALA 94

GLU 132 0.21 THR 252 -0.08 ALA 94

GLU 132 0.22 GLN 253 -0.07 ALA 94

SER 6 0.24 SER 254 -0.08 NMA 278

GLU 132 0.24 TYR 255 -0.07 ALA 94

GLU 132 0.26 ARG 256 -0.06 ALA 94

SER 6 0.30 ARG 257 -0.11 NMA 278

SER 6 0.29 ARG 258 -0.13 LYS 276

GLU 132 0.32 PHE 259 -0.09 LYS 276

GLU 132 0.31 GLY 260 -0.06 ALA 215

GLU 132 0.28 CYS 261 -0.05 ALA 94

GLU 132 0.25 THR 262 -0.06 ALA 94

GLU 132 0.23 PRO 263 -0.07 ALA 94

GLU 132 0.21 SER 264 -0.07 ALA 94

GLU 132 0.24 ARG 265 -0.05 ALA 94

GLU 132 0.27 SER 266 -0.05 ALA 94

GLU 132 0.22 ARG 267 -0.06 ALA 94

GLU 132 0.22 GLN 268 -0.04 ALA 94

GLU 132 0.27 GLY 269 -0.03 ALA 94

GLU 132 0.32 LYS 270 -0.02 CYS 261

GLU 132 0.37 ASP 271 -0.03 CYS 261

GLU 132 0.35 GLU 272 -0.04 ALA 215

GLU 132 0.36 CYS 273 -0.05 ALA 215

GLU 132 0.42 ARG 274 -0.05 VAL 211

GLU 132 0.39 ALA 275 -0.08 ALA 215

GLU 132 0.32 LYS 276 -0.13 VAL 211

GLU 132 0.33 ASN 277 -0.12 VAL 211

GLU 132 0.35 ASN 278 -0.13 VAL 211

VAL 130 0.31 NMA 278 -0.17 VAL 211

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.

*** EXSA_mono1 ***

CA distance fluctuations for 2401041300303831936

--- normal mode 9 ---

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

* EXSA_mono1 *