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

* *

CA distance fluctuations for 2503091508403830875

--- normal mode 31 ---

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
ASP 184 1.16 HIS 88 -0.90 PRO 191

SER 183 1.03 HIS 89 -0.96 ARG 209

LEU 114 0.95 HIS 90 -1.21 ARG 209

LEU 114 0.94 HIS 91 -0.80 SER 95

LEU 114 0.81 HIS 92 -1.35 MET 246

LEU 114 0.79 HIS 93 -1.15 ARG 249

LEU 114 0.80 SER 94 -0.84 ARG 249

THR 256 1.17 SER 95 -0.80 HIS 91

THR 256 1.58 SER 96 -0.38 HIS 89

ILE 254 1.34 VAL 97 -1.13 THR 211

PHE 270 1.69 PRO 98 -0.88 ASN 210

LYS 291 1.53 SER 99 -1.19 ASN 263

LYS 291 1.68 GLN 100 -1.70 ASN 263

LYS 291 1.29 LYS 101 -1.04 ASN 263

PRO 222 1.25 THR 102 -0.90 SER 166

PRO 222 1.18 TYR 103 -0.77 PRO 152

PRO 222 1.31 GLN 104 -0.69 LEU 130

PRO 222 0.94 GLY 105 -0.94 PRO 152

LEU 188 0.83 SER 106 -1.04 PRO 152

LEU 188 0.99 TYR 107 -0.92 ALA 129

PRO 222 1.25 GLY 108 -0.94 ALA 129

LEU 188 1.23 PHE 109 -0.99 ALA 129

PRO 222 1.48 ARG 110 -1.19 LEU 130

GLU 221 1.71 LEU 111 -1.52 ASN 131

LEU 188 1.36 GLY 112 -1.29 ASN 131

ARG 290 1.58 PHE 113 -1.03 GLY 226

CYS 238 1.68 LEU 114 -0.85 GLY 226

ARG 290 1.22 HIS 115 -0.91 THR 140

GLU 287 1.42 SER 116 -0.92 SER 185

LEU 188 0.97 GLY 117 -0.92 SER 185

GLY 199 0.90 THR 118 -0.92 SER 185

GLY 199 1.00 ALA 119 -0.69 SER 185

GLY 199 1.09 LYS 120 -0.61 SER 185

ASN 200 1.15 SER 121 -0.55 SER 185

GLY 199 1.22 VAL 122 -0.81 SER 185

CYS 141 1.58 THR 123 -0.90 SER 185

LEU 289 1.20 CYS 124 -1.19 LYS 139

GLU 286 1.33 THR 125 -1.13 SER 185

ARG 290 1.44 TYR 126 -1.05 SER 185

ASN 288 1.48 SER 127 -0.95 GLY 112

LYS 291 1.42 PRO 128 -1.18 SER 227

LYS 291 1.05 ALA 129 -1.27 VAL 147

ARG 249 1.40 LEU 130 -1.19 ARG 110

LYS 291 1.63 ASN 131 -1.52 LEU 111

LEU 289 1.58 LYS 132 -0.97 SER 185

LEU 289 1.76 MET 133 -1.19 SER 185

LEU 289 1.36 PHE 134 -1.29 SER 185

GLY 199 1.24 CYS 135 -1.42 SER 185

GLY 199 1.52 GLN 136 -1.34 SER 185

LEU 114 1.56 LEU 137 -1.33 SER 185

GLU 198 1.65 ALA 138 -0.85 SER 185

GLY 199 1.60 LYS 139 -1.19 CYS 124

ASN 200 1.67 THR 140 -0.91 HIS 115

THR 123 1.58 CYS 141 -1.20 SER 185

LEU 188 1.38 PRO 142 -1.03 ALA 159

LEU 188 1.54 VAL 143 -1.30 ILE 255

LEU 188 1.52 GLN 144 -1.31 THR 256

LEU 188 1.60 LEU 145 -1.42 THR 256

LEU 188 1.42 TRP 146 -1.16 ALA 129

LEU 188 1.22 VAL 147 -1.27 ALA 129

LEU 188 1.14 ASP 148 -1.10 ALA 129

GLY 187 0.91 SER 149 -1.27 ASP 228

GLY 187 0.85 THR 150 -1.42 CYS 229

GLY 187 1.04 PRO 151 -1.20 ASP 228

GLY 187 1.27 PRO 152 -1.04 SER 106

GLY 187 1.54 PRO 153 -0.58 GLN 100

GLY 187 0.99 GLY 154 -1.06 THR 230

VAL 147 0.90 THR 155 -1.47 THR 230

SER 96 1.06 ARG 156 -1.79 THR 230

SER 96 1.38 VAL 157 -1.62 THR 231

SER 96 1.57 ARG 158 -1.41 THR 231

SER 96 1.51 ALA 159 -1.24 VAL 143

SER 96 1.27 MET 160 -0.96 VAL 143

LEU 194 0.98 ALA 161 -1.13 SER 185

LEU 194 1.23 ILE 162 -1.01 SER 185

LEU 194 1.37 TYR 163 -1.05 SER 185

LEU 194 1.29 LYS 164 -1.03 SER 185

LEU 194 1.03 GLN 165 -0.93 ASP 281

LEU 194 0.87 SER 166 -0.90 THR 102

LEU 194 0.83 GLN 167 -0.81 ASP 281

LEU 194 0.90 HIS 168 -0.89 ASP 281

LEU 194 0.93 MET 169 -0.84 SER 185

LEU 114 0.83 THR 170 -0.82 ARG 249

LEU 114 0.84 GLU 171 -1.42 ARG 249

LEU 114 0.98 VAL 172 -1.11 ARG 249

LEU 114 1.15 VAL 173 -1.04 GLY 262

LEU 114 1.18 ARG 174 -1.01 SER 185

LEU 114 1.52 ARG 175 -0.87 SER 185

LEU 114 1.44 CYS 176 -0.80 SER 185

LEU 114 1.33 PRO 177 -0.87 GLY 187

LEU 114 1.43 HIS 178 -0.81 GLY 187

LEU 114 1.54 HIS 179 -0.65 SER 185

LEU 114 1.35 GLU 180 -0.93 ASP 186

LEU 114 1.23 ARG 181 -1.10 ASP 186

LEU 114 1.29 CYS 182 -0.70 LEU 194

HIS 89 1.03 SER 183 -0.96 MET 237

HIS 88 1.16 ASP 184 -0.87 MET 237

LEU 114 0.32 SER 185 -1.80 VAL 274

LEU 201 1.66 ASP 186 -1.11 LEU 194

VAL 225 1.66 GLY 187 -0.87 PRO 177

ILE 232 1.75 LEU 188 -0.58 ARG 181

LYS 139 1.49 ALA 189 -0.71 SER 261

LEU 114 1.43 PRO 190 -0.76 PRO 191

LEU 114 1.65 PRO 191 -0.90 HIS 88

LEU 114 1.62 GLN 192 -0.71 HIS 90

LEU 114 1.62 HIS 193 -0.81 GLY 262

ILE 251 1.85 LEU 194 -1.11 ASP 186

LEU 252 1.64 ILE 195 -0.93 ASP 186

VAL 272 1.40 ARG 196 -0.52 SER 183

LEU 114 1.21 VAL 197 -0.71 PRO 223

ALA 138 1.65 GLU 198 -1.22 PRO 223

LYS 139 1.60 GLY 199 -0.97 PRO 223

THR 140 1.67 ASN 200 -0.74 GLU 221

ASP 186 1.66 LEU 201 -0.64 GLU 221

THR 140 1.07 ARG 202 -0.70 SER 261

LEU 289 0.92 VAL 203 -0.72 SER 261

LEU 114 0.90 GLU 204 -1.14 SER 261

LEU 114 1.00 TYR 205 -1.20 GLY 262

ASP 184 0.96 LEU 206 -1.41 SER 261

ASP 184 0.91 ASP 207 -1.10 GLN 100

LEU 114 0.79 ASP 208 -1.17 GLN 100

LEU 114 0.71 ARG 209 -1.21 HIS 90

LEU 114 0.67 ASN 210 -1.01 VAL 97

LEU 114 0.72 THR 211 -1.13 VAL 97

LEU 114 0.77 PHE 212 -0.90 ARG 249

LEU 114 0.87 ARG 213 -1.03 GLN 100

LEU 114 0.99 HIS 214 -1.18 GLY 262

LEU 114 0.96 SER 215 -1.46 GLY 262

SER 96 1.01 VAL 216 -1.08 GLY 262

SER 96 1.08 VAL 217 -1.08 THR 230

LEU 188 1.00 VAL 218 -0.97 THR 230

LEU 188 1.16 PRO 219 -0.91 THR 230

ARG 110 1.32 TYR 220 -0.95 CYS 229

LEU 111 1.71 GLU 221 -0.88 GLY 199

LEU 111 1.48 PRO 222 -0.83 GLY 199

ASP 148 1.11 PRO 223 -1.22 GLU 198

GLY 187 1.37 GLU 224 -0.63 PRO 128

GLY 187 1.66 VAL 225 -0.92 PRO 128

GLY 187 1.36 GLY 226 -1.18 PRO 128

GLY 187 1.29 SER 227 -1.18 PRO 128

GLY 187 0.93 ASP 228 -1.27 SER 149

LEU 188 1.05 CYS 229 -1.42 THR 150

LEU 188 1.01 THR 230 -1.79 ARG 156

LEU 188 1.39 THR 231 -1.62 VAL 157

LEU 188 1.75 ILE 232 -1.20 ARG 158

LEU 188 1.45 HIS 233 -0.67 SER 185

LEU 289 1.37 TYR 234 -0.81 SER 185

VAL 272 1.62 ASN 235 -0.93 SER 183

VAL 272 1.72 CYS 236 -0.98 SER 185

LEU 114 1.56 MET 237 -0.96 SER 183

LEU 114 1.68 CYS 238 -1.28 SER 185

LEU 114 1.42 ASN 239 -1.63 SER 185

LEU 114 1.42 ASN 239 -1.63 SER 185

LEU 114 1.22 SER 240 -1.50 SER 185

LEU 114 1.26 SER 240 -1.52 SER 185

LEU 114 1.17 SER 241 -1.38 SER 185

LEU 114 1.21 SER 241 -1.38 SER 185

LEU 114 1.29 CYS 242 -1.20 SER 185

LEU 114 1.30 CYS 242 -1.21 SER 185

LEU 114 1.20 MET 243 -0.98 SER 185

LEU 114 1.20 MET 243 -0.99 SER 185

LEU 114 1.25 GLY 244 -0.87 SER 185

LEU 114 1.25 GLY 244 -0.83 SER 185

LEU 114 1.38 GLY 245 -1.04 HIS 92

LEU 114 1.40 GLY 245 -1.03 HIS 92

LEU 114 1.34 MET 246 -1.35 HIS 92

LEU 114 1.34 MET 246 -1.34 HIS 92

LEU 114 1.21 ASN 247 -1.14 HIS 92

LEU 130 1.19 ARG 248 -1.23 SER 185

LEU 130 1.40 ARG 249 -1.42 GLU 171

LEU 194 1.28 PRO 250 -1.20 SER 185

LEU 194 1.85 ILE 251 -1.23 SER 185

ILE 195 1.64 LEU 252 -1.15 SER 185

ILE 195 1.49 THR 253 -1.09 SER 185

VAL 97 1.34 ILE 254 -1.00 VAL 143

SER 96 1.56 ILE 255 -1.30 VAL 143

SER 96 1.58 THR 256 -1.42 LEU 145

SER 96 1.26 LEU 257 -1.34 THR 230

SER 96 0.98 GLU 258 -1.41 THR 230

TYR 107 0.73 ASP 259 -1.17 THR 230

VAL 147 0.63 SER 260 -1.12 THR 230

TYR 107 0.61 SER 261 -1.41 LEU 206

TYR 107 0.41 GLY 262 -1.46 SER 215

TYR 107 0.59 ASN 263 -1.70 GLN 100

SER 96 0.65 LEU 264 -1.17 GLN 100

LEU 188 0.85 LEU 265 -0.95 THR 230

SER 96 0.99 GLY 266 -1.06 LEU 145

SER 96 0.98 ARG 267 -1.01 LEU 145

LEU 188 1.22 ASN 268 -0.68 SER 185

TYR 234 1.22 SER 269 -0.81 SER 166

PRO 98 1.69 PHE 270 -0.95 SER 185

ILE 195 1.52 GLU 271 -1.02 SER 185

CYS 236 1.72 VAL 272 -1.19 SER 185

LEU 289 1.37 ARG 273 -1.50 SER 185

LEU 114 1.32 VAL 274 -1.80 SER 185

LEU 114 1.17 CYS 275 -1.51 SER 185

GLY 199 1.24 ALA 276 -1.10 SER 185

GLY 199 1.18 CYS 277 -0.95 SER 185

GLY 199 1.15 PRO 278 -1.16 SER 185

GLY 199 1.02 GLY 279 -0.97 SER 185

GLY 199 0.90 ARG 280 -0.91 SER 185

GLY 199 0.86 ASP 281 -0.97 SER 185

GLY 199 0.96 ARG 282 -0.88 SER 185

GLY 199 0.85 ARG 283 -0.84 SER 185

GLY 199 0.82 THR 284 -0.82 SER 185

CYS 275 1.06 GLU 285 -0.61 SER 185

THR 125 1.33 GLU 286 -0.51 SER 185

SER 116 1.42 GLU 287 -0.59 SER 185

SER 127 1.48 ASN 288 -0.45 SER 185

MET 133 1.76 LEU 289 -0.18 SER 185

PHE 113 1.58 ARG 290 -0.30 LYS 120

GLN 100 1.68 LYS 291 -0.42 LYS 120

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 2503091508403830875

--- normal mode 31 ---

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

* *