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

* *

CA distance fluctuations for 250309233605806127

--- normal mode 17 ---

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 210 0.77 SER 96 -0.25 LYS 101

VAL 197 0.69 VAL 97 -0.23 GLN 100

VAL 197 0.79 PRO 98 -0.43 VAL 172

VAL 197 0.69 SER 99 -0.34 THR 256

VAL 197 0.86 GLN 100 -0.23 VAL 97

VAL 197 0.81 LYS 101 -0.25 SER 96

VAL 197 0.84 THR 102 -0.16 SER 96

VAL 197 0.88 TYR 103 -0.14 PRO 152

LEU 201 0.94 GLN 104 -0.21 ASN 268

ASN 200 0.93 GLY 105 -0.21 PRO 152

GLU 198 1.05 SER 106 -0.18 ALA 129

GLU 198 1.06 SER 106 -0.18 ALA 129

GLU 198 1.08 TYR 107 -0.16 ALA 129

LEU 201 1.10 GLY 108 -0.24 PRO 128

LEU 201 1.01 PHE 109 -0.17 THR 155

LEU 201 1.04 ARG 110 -0.25 ILE 255

LEU 201 0.97 LEU 111 -0.44 ILE 255

LEU 201 1.02 GLY 112 -0.42 VAL 203

LEU 201 0.88 PHE 113 -0.46 VAL 203

LEU 201 0.82 LEU 114 -0.41 ASP 228

LEU 201 0.71 HIS 115 -0.34 ARG 202

LEU 201 0.58 SER 116 -0.46 GLU 198

LEU 201 0.45 VAL 122 -0.76 GLU 198

LEU 201 0.38 THR 123 -0.75 GLU 198

LEU 201 0.49 CYS 124 -0.50 GLU 198

LEU 201 0.60 THR 125 -0.38 GLU 198

LEU 201 0.69 TYR 126 -0.28 ASP 228

LEU 201 0.71 SER 127 -0.28 ASP 228

LEU 201 0.82 PRO 128 -0.30 ASP 228

LEU 201 0.75 ALA 129 -0.26 ASP 228

GLU 286 0.88 LEU 130 -0.23 ASP 228

LEU 201 0.69 ASN 131 -0.24 ASP 228

GLU 285 0.58 LYS 132 -0.23 ASP 228

LEU 201 0.54 MET 133 -0.26 GLY 112

LEU 201 0.45 PHE 134 -0.43 GLU 198

LEU 201 0.36 CYS 135 -0.57 GLU 198

GLU 221 0.25 GLN 136 -0.83 GLU 198

GLU 221 0.27 LEU 137 -0.84 GLU 198

GLU 221 0.35 ALA 138 -0.80 GLU 198

GLU 221 0.37 LYS 139 -0.79 GLU 198

GLU 221 0.37 LYS 139 -0.79 GLU 198

GLU 221 0.41 THR 140 -0.48 GLU 198

LEU 201 0.44 CYS 141 -0.43 ARG 202

LEU 201 0.60 PRO 142 -0.54 ARG 202

LEU 201 0.71 VAL 143 -0.63 VAL 203

LEU 201 0.92 GLN 144 -0.54 VAL 203

LEU 201 0.95 LEU 145 -0.56 TYR 220

LEU 201 1.16 TRP 146 -0.43 TYR 220

LEU 201 1.17 VAL 147 -0.30 PRO 222

LEU 201 1.26 ASP 148 -0.26 PRO 128

LEU 201 1.14 SER 149 -0.17 PRO 128

GLU 198 1.24 THR 150 -0.24 PRO 153

GLU 198 1.44 PRO 151 -0.30 LEU 265

GLU 198 1.64 PRO 152 -0.44 ASP 259

GLU 198 1.66 PRO 152 -0.41 ASP 259

GLU 198 1.88 PRO 153 -0.31 ASP 259

GLU 198 1.86 PRO 153 -0.34 GLU 221

GLU 198 1.63 GLY 154 -0.59 GLU 221

GLU 198 1.66 GLY 154 -0.64 GLU 221

GLU 198 1.53 THR 155 -0.47 GLU 221

GLU 198 1.29 ARG 156 -0.38 LEU 145

VAL 197 1.38 VAL 157 -0.42 LEU 145

VAL 197 1.69 ARG 158 -0.37 GLN 144

VAL 197 1.43 ALA 159 -0.40 LEU 111

VAL 197 1.04 MET 160 -0.29 LEU 111

VAL 197 0.73 ALA 161 -0.26 LEU 111

VAL 197 0.63 ILE 162 -0.25 GLY 245

ASN 288 0.49 TYR 163 -0.40 MET 246

LEU 289 0.62 LYS 164 -0.32 MET 246

ASN 288 0.66 GLN 165 -0.53 ARG 249

LEU 289 0.60 SER 166 -0.51 GLY 244

ASN 288 0.53 GLN 167 -0.69 GLY 244

ASN 288 0.51 HIS 168 -0.66 GLY 244

LEU 289 0.49 MET 169 -0.43 GLY 244

VAL 197 0.52 THR 170 -0.26 GLY 244

ASN 288 0.50 GLU 171 -0.22 GLY 244

ASN 288 0.50 GLU 171 -0.21 PRO 98

ASN 288 0.40 VAL 172 -0.43 PRO 98

ARG 249 0.43 VAL 173 -0.33 HIS 168

MET 246 0.32 ARG 174 -0.35 HIS 168

SER 185 0.23 ARG 175 -0.38 HIS 168

SER 185 0.21 CYS 176 -0.48 HIS 168

GLU 221 0.19 PRO 177 -0.49 GLU 198

SER 185 0.24 HIS 178 -0.66 GLU 198

SER 185 0.35 HIS 179 -0.69 GLU 198

SER 185 0.26 GLU 180 -0.51 GLU 198

GLY 187 0.29 ARG 181 -0.62 GLU 198

GLY 187 0.37 CYS 182 -0.83 GLU 198

CYS 182 0.37 SER 185 -0.67 VAL 197

GLU 221 0.39 ASP 186 -0.93 VAL 197

CYS 182 0.37 GLY 187 -0.60 VAL 197

PRO 153 0.38 LEU 188 -0.43 VAL 197

VAL 216 0.39 ALA 189 -0.32 LEU 201

VAL 216 0.42 PRO 190 -0.45 LEU 201

PRO 153 0.28 PRO 191 -0.44 LEU 201

ARG 213 0.28 GLN 192 -0.35 LEU 201

ARG 213 0.27 GLN 192 -0.35 LEU 201

LEU 289 0.26 HIS 193 -0.21 LEU 201

LEU 289 0.26 LEU 194 -0.23 GLU 198

THR 253 0.36 ILE 195 -0.55 ARG 196

GLU 221 0.42 ARG 196 -0.55 ILE 195

ARG 158 1.69 VAL 197 -0.93 ASP 186

PRO 153 1.88 GLU 198 -0.96 ALA 276

ASP 148 0.66 GLY 199 -0.36 ARG 181

SER 106 0.95 ASN 200 -0.49 CYS 182

ASP 228 1.34 LEU 201 -0.57 GLY 187

GLU 198 0.89 ARG 202 -0.75 ILE 232

GLU 198 0.63 VAL 203 -0.81 ILE 232

GLU 198 0.63 GLU 204 -0.45 ILE 232

PRO 190 0.37 TYR 205 -0.46 ILE 195

VAL 197 0.48 LEU 206 -0.28 VAL 143

SER 96 0.48 ASP 207 -0.28 LEU 201

SER 96 0.71 ASP 208 -0.23 GLN 144

SER 96 0.68 ARG 209 -0.34 LEU 201

SER 96 0.77 ASN 210 -0.26 LEU 201

SER 96 0.62 THR 211 -0.25 SER 99

VAL 197 0.42 PHE 212 -0.26 PRO 98

VAL 197 0.55 ARG 213 -0.33 PRO 98

VAL 197 0.58 HIS 214 -0.22 GLN 144

VAL 197 0.85 SER 215 -0.30 GLN 144

VAL 197 0.81 VAL 216 -0.43 VAL 143

VAL 197 1.05 VAL 217 -0.38 GLN 144

GLU 198 0.95 VAL 218 -0.44 THR 231

GLU 198 1.32 PRO 219 -0.47 THR 230

GLU 198 1.38 TYR 220 -0.63 THR 230

GLU 198 1.12 GLU 221 -0.64 GLY 154

GLU 198 1.13 GLU 221 -0.64 GLY 154

GLU 198 1.12 PRO 222 -0.31 TRP 146

LEU 201 0.99 PRO 223 -0.29 GLY 154

LEU 201 0.91 GLU 224 -0.32 GLY 154

LEU 201 0.99 VAL 225 -0.22 GLY 154

LEU 201 1.17 GLY 226 -0.32 ARG 202

LEU 201 1.24 SER 227 -0.37 LEU 114

LEU 201 1.34 ASP 228 -0.41 LEU 114

LEU 201 1.16 CYS 229 -0.37 TYR 220

LEU 201 0.93 THR 230 -0.63 TYR 220

LEU 201 0.78 THR 231 -0.63 VAL 203

LEU 201 0.56 ILE 232 -0.81 VAL 203

GLU 221 0.52 HIS 233 -0.68 ARG 202

GLU 221 0.41 TYR 234 -0.57 VAL 203

GLU 221 0.44 ASN 235 -0.32 PHE 113

GLU 221 0.30 TYR 236 -0.40 GLU 198

SER 185 0.33 MET 237 -0.56 GLU 198

SER 185 0.31 CYS 238 -0.59 GLU 198

SER 185 0.31 CYS 238 -0.59 GLU 198

GLU 221 0.23 ASN 239 -0.67 GLU 198

ILE 195 0.28 SER 240 -0.51 GLU 198

THR 211 0.20 SER 241 -0.60 GLU 198

GLU 221 0.18 CYS 242 -0.62 GLU 198

THR 211 0.17 MET 243 -0.55 GLN 167

ASN 288 0.16 GLY 244 -0.69 GLN 167

THR 211 0.21 GLY 245 -0.62 HIS 168

ARG 174 0.32 MET 246 -0.53 GLN 165

THR 211 0.24 ASN 247 -0.53 GLN 167

VAL 173 0.27 GLN 248 -0.43 GLU 198

VAL 173 0.43 ARG 249 -0.53 GLN 165

ASN 288 0.48 PRO 250 -0.24 GLU 198

VAL 197 0.47 ILE 251 -0.27 MET 246

VAL 197 0.68 LEU 252 -0.21 LEU 111

VAL 197 0.86 THR 253 -0.32 LEU 111

VAL 197 1.13 ILE 254 -0.28 LEU 111

VAL 197 1.42 ILE 255 -0.44 LEU 111

VAL 197 1.41 THR 256 -0.34 SER 99

VAL 197 1.23 LEU 257 -0.29 LEU 145

VAL 197 1.12 GLU 258 -0.26 LEU 145

GLU 198 1.27 ASP 259 -0.44 PRO 152

GLU 198 1.28 SER 260 -0.30 GLU 221

GLU 198 1.08 SER 261 -0.34 PRO 152

VAL 197 1.00 GLY 262 -0.27 PRO 152

GLU 198 0.99 ASN 263 -0.39 PRO 152

VAL 197 1.04 LEU 264 -0.33 PRO 152

GLU 198 1.03 LEU 265 -0.36 PRO 152

VAL 197 1.03 GLY 266 -0.22 SER 99

VAL 197 1.09 ARG 267 -0.32 SER 99

VAL 197 1.00 ASN 268 -0.21 GLN 104

VAL 197 1.01 ASN 268 -0.21 GLN 104

VAL 197 0.93 SER 269 -0.17 GLN 104

VAL 197 0.68 PHE 270 -0.27 LEU 111

VAL 197 0.53 GLU 271 -0.20 LEU 111

VAL 197 0.53 GLU 271 -0.20 LEU 111

GLU 285 0.43 VAL 272 -0.24 GLY 112

GLU 285 0.34 ARG 273 -0.41 GLU 198

GLU 221 0.22 VAL 274 -0.58 GLU 198

LEU 201 0.21 CYS 275 -0.75 GLU 198

GLU 221 0.20 ALA 276 -0.96 GLU 198

LEU 201 0.28 CYS 277 -0.91 GLU 198

LEU 201 0.39 PRO 278 -0.67 GLU 198

LEU 201 0.47 GLY 279 -0.65 GLU 198

LEU 201 0.41 ARG 280 -0.70 GLU 198

LEU 201 0.42 ASP 281 -0.59 GLU 198

LEU 201 0.54 ARG 282 -0.44 GLU 198

LEU 201 0.55 ARG 283 -0.47 GLU 198

LEU 201 0.48 THR 284 -0.47 GLU 198

LEU 130 0.67 GLU 285 -0.31 GLU 198

LEU 130 0.88 GLU 286 -0.25 GLU 198

LEU 130 0.63 GLU 287 -0.32 GLU 198

GLN 165 0.66 ASN 288 -0.25 GLU 198

LEU 130 0.80 LEU 289 -0.12 GLU 198

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 8th, 2025.

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

*** ***

CA distance fluctuations for 250309233605806127

--- normal mode 17 ---

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

* *