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

* *

CA distance fluctuations for 2503091518343888681

--- normal mode 24 ---

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
LEU 264 1.05 HIS 88 -1.44 SER 261

LEU 264 0.76 HIS 89 -1.33 SER 261

LEU 264 0.84 HIS 90 -1.21 SER 261

LEU 264 0.85 HIS 91 -1.12 GLN 144

LEU 264 0.94 HIS 92 -1.13 GLN 144

LEU 264 0.92 HIS 93 -1.17 GLN 144

LEU 264 0.95 SER 94 -1.18 GLN 144

SER 106 0.85 SER 95 -1.07 GLY 262

SER 106 0.94 SER 96 -1.30 GLY 262

GLY 105 0.91 VAL 97 -1.68 GLY 262

GLY 105 1.05 PRO 98 -1.79 GLY 262

TYR 103 1.20 SER 99 -1.29 GLY 262

ASN 235 1.19 GLN 100 -1.05 GLY 262

GLU 271 1.63 LYS 101 -0.89 GLY 262

ASN 235 1.12 THR 102 -0.94 GLY 226

SER 99 1.20 TYR 103 -1.23 GLY 226

ASN 235 0.89 GLN 104 -1.37 GLY 226

SER 99 1.09 GLY 105 -1.43 GLY 226

SER 96 0.94 SER 106 -1.40 VAL 225

SER 99 0.63 TYR 107 -1.42 VAL 225

SER 99 0.58 GLY 108 -1.58 VAL 225

ASN 235 0.69 PHE 109 -1.07 VAL 225

TYR 234 0.76 ARG 110 -0.89 GLY 226

CYS 141 0.77 LEU 111 -1.16 THR 253

THR 230 0.28 GLY 112 -1.68 THR 253

THR 256 0.21 PHE 113 -1.30 GLU 271

VAL 143 0.21 LEU 114 -1.12 TRP 146

ILE 255 0.44 HIS 115 -0.95 ASP 228

LYS 101 0.59 SER 116 -1.03 ASP 228

LYS 101 0.59 GLY 117 -1.19 ASP 228

LYS 101 0.74 THR 118 -1.33 ASP 228

LYS 101 0.66 ALA 119 -1.42 ASP 228

LYS 101 0.69 LYS 120 -1.55 ASP 228

CYS 182 0.75 SER 121 -1.63 ASP 228

ILE 255 0.78 VAL 122 -1.67 ASP 228

ILE 255 1.02 THR 123 -1.78 ASP 228

ILE 255 1.11 CYS 124 -1.48 ASP 228

ILE 255 0.92 THR 125 -1.26 ASP 228

ASN 268 0.91 TYR 126 -1.00 ASP 228

LYS 101 0.87 SER 127 -0.87 ASP 228

LYS 101 0.70 PRO 128 -0.64 ASP 228

LYS 101 0.68 ALA 129 -0.69 SER 166

LYS 101 1.03 LEU 130 -0.69 ASP 228

THR 102 1.02 ASN 131 -0.74 GLY 112

LYS 101 1.24 LYS 132 -0.86 ASP 228

ASN 268 1.25 MET 133 -0.99 ASP 228

LYS 101 1.07 PHE 134 -1.24 ASP 228

ILE 255 1.05 CYS 135 -1.43 ASP 228

ILE 255 1.03 GLN 136 -1.50 ASP 228

LEU 264 1.08 LEU 137 -1.35 ASP 228

ILE 255 1.19 ALA 138 -1.28 SER 227

ILE 255 1.40 LYS 139 -1.46 ASP 228

ILE 255 1.50 THR 140 -1.37 SER 227

ILE 255 1.60 CYS 141 -1.28 CYS 229

VAL 157 0.84 PRO 142 -1.40 VAL 272

GLU 224 0.56 VAL 143 -1.59 ALA 161

GLU 224 0.54 GLN 144 -1.92 ALA 161

GLU 224 0.31 LEU 145 -1.79 ALA 159

ASP 259 0.34 TRP 146 -1.12 LEU 114

ASP 259 0.52 VAL 147 -1.10 GLY 199

SER 261 0.62 ASP 148 -1.42 GLU 224

SER 261 0.68 SER 149 -1.33 GLU 224

SER 261 0.60 THR 150 -1.47 GLY 199

ASP 259 0.56 PRO 151 -1.06 GLY 199

GLY 262 0.71 PRO 152 -0.89 GLY 199

GLY 262 0.67 PRO 153 -0.87 LEU 201

HIS 233 0.70 GLY 154 -0.71 ASN 210

HIS 233 0.86 THR 155 -0.66 ASN 210

HIS 233 0.76 ARG 156 -0.69 ASN 210

HIS 233 1.78 VAL 157 -1.07 ASN 210

TYR 234 1.47 ARG 158 -1.25 ASN 210

LEU 264 1.36 ALA 159 -1.79 LEU 145

LEU 264 1.67 MET 160 -1.74 ILE 232

LEU 264 1.38 ALA 161 -1.92 GLN 144

LEU 264 1.18 ILE 162 -1.66 GLN 144

LEU 264 1.00 TYR 163 -1.40 GLN 144

LEU 264 0.84 LYS 164 -1.25 GLN 144

LEU 264 0.72 GLN 165 -1.14 GLN 144

LEU 264 0.49 SER 166 -1.23 GLY 262

ASN 247 0.68 GLN 167 -1.19 GLY 262

LEU 264 0.81 HIS 168 -1.19 GLN 144

LEU 264 0.81 MET 169 -1.34 GLN 144

LEU 264 0.89 THR 170 -1.26 GLN 144

LEU 264 0.99 GLU 171 -1.28 GLN 144

LEU 264 1.17 VAL 172 -1.37 GLN 144

LEU 264 1.29 VAL 173 -1.39 GLN 144

LEU 264 1.19 ARG 174 -1.25 GLN 144

LEU 264 1.13 ARG 175 -1.04 THR 231

LEU 264 0.99 CYS 176 -1.05 SER 261

LEU 264 0.87 PRO 177 -1.22 SER 261

LEU 264 0.85 HIS 178 -1.17 SER 261

LEU 264 0.99 HIS 179 -1.06 SER 261

LEU 264 0.95 GLU 180 -1.13 SER 261

LEU 264 0.80 ARG 181 -1.31 SER 261

GLY 199 0.92 CYS 182 -1.27 SER 261

GLY 199 0.95 SER 183 -1.14 SER 261

GLY 199 1.16 ASP 184 -0.98 SER 227

LEU 264 0.96 SER 185 -1.09 SER 227

LEU 264 0.80 ASP 186 -1.50 ASN 235

HIS 88 0.87 GLY 187 -1.35 SER 227

LEU 264 0.92 LEU 188 -1.11 THR 230

LEU 264 1.07 ALA 189 -1.24 THR 230

LEU 264 1.07 PRO 190 -1.16 THR 230

LEU 264 1.00 PRO 191 -1.11 THR 230

LEU 264 1.09 GLN 192 -1.14 THR 230

LEU 264 1.31 HIS 193 -1.28 THR 231

LEU 264 1.36 LEU 194 -1.28 THR 231

LEU 264 1.34 ILE 195 -1.45 THR 231

LEU 264 1.10 ARG 196 -1.49 THR 230

ARG 158 1.32 VAL 197 -1.62 THR 230

ARG 158 0.98 GLU 198 -1.52 PRO 223

ASP 184 1.16 GLY 199 -1.57 PRO 222

ASP 184 0.71 ASN 200 -1.74 GLU 221

ASP 186 0.75 LEU 201 -1.43 GLU 221

LYS 139 0.54 ARG 202 -0.96 GLU 221

LEU 264 0.52 VAL 203 -1.18 THR 230

ASN 263 0.78 GLU 204 -1.01 THR 230

ASN 263 1.08 TYR 205 -1.18 THR 230

ASN 263 1.32 LEU 206 -1.01 THR 231

LEU 264 1.22 ASP 207 -1.05 GLN 144

LEU 264 1.09 ASP 208 -1.09 GLN 144

LEU 264 0.87 ARG 209 -0.98 GLN 144

HIS 91 0.83 ASN 210 -1.25 ARG 158

LEU 264 0.97 THR 211 -1.14 GLN 144

LEU 264 1.12 PHE 212 -1.16 GLN 144

LEU 264 1.37 ARG 213 -1.39 ILE 232

LEU 264 1.56 HIS 214 -1.41 ILE 232

LEU 264 1.51 SER 215 -1.48 ILE 232

ASN 263 1.15 VAL 216 -1.51 THR 231

GLU 258 0.70 VAL 217 -0.94 GLN 144

HIS 233 1.05 VAL 218 -0.96 ASN 210

HIS 233 1.01 PRO 219 -0.93 ASN 210

HIS 233 0.81 TYR 220 -0.90 ASN 200

GLU 224 0.66 GLU 221 -1.74 ASN 200

PRO 153 0.43 PRO 222 -1.57 GLY 199

PRO 153 0.41 PRO 223 -1.52 GLU 198

ILE 232 0.80 GLU 224 -1.42 ASP 148

ILE 232 0.65 VAL 225 -1.58 GLY 108

ILE 232 0.57 GLY 226 -1.43 GLY 105

SER 261 0.75 SER 227 -1.44 LYS 139

SER 261 0.93 ASP 228 -1.78 THR 123

SER 261 0.26 CYS 229 -1.65 HIS 233

GLU 224 0.43 THR 230 -1.62 VAL 197

GLU 224 0.64 THR 231 -1.51 VAL 216

GLU 224 0.80 ILE 232 -1.77 ALA 161

VAL 157 1.78 HIS 233 -1.65 CYS 229

THR 256 1.81 TYR 234 -1.20 CYS 229

ILE 254 1.60 ASN 235 -1.50 ASP 186

ILE 254 1.42 TYR 236 -1.15 CYS 229

LEU 264 1.27 MET 237 -1.09 SER 227

LEU 264 1.14 CYS 238 -1.10 ASP 228

ASN 239 1.35 ASN 239 -1.17 ASP 228

ASN 239 1.35 ASN 239 -1.17 ASP 228

LEU 264 0.90 SER 240 -1.11 ASP 228

LEU 264 0.96 SER 240 -1.10 ASP 228

LEU 264 0.85 SER 241 -1.08 ASP 228

LEU 264 0.88 SER 241 -1.05 ASP 228

LEU 264 0.89 CYS 242 -1.04 ASP 228

LEU 264 0.90 CYS 242 -1.02 ASP 228

LEU 264 0.83 MET 243 -1.01 SER 261

LEU 264 0.84 MET 243 -1.00 SER 261

LEU 264 0.88 GLY 244 -1.05 SER 261

LEU 264 0.87 GLY 244 -1.08 SER 261

LEU 264 1.00 GLY 245 -1.03 GLN 144

LEU 264 0.99 GLY 245 -1.01 GLN 144

LEU 264 1.00 MET 246 -1.09 VAL 143

LEU 264 1.00 MET 246 -1.09 VAL 143

LEU 264 0.87 ASN 247 -0.93 GLN 144

LEU 264 0.83 ARG 248 -0.97 ASP 228

LYS 101 0.83 ARG 249 -1.08 VAL 143

LYS 101 1.03 PRO 250 -1.23 VAL 143

LYS 101 1.06 ILE 251 -1.54 VAL 143

LYS 101 0.99 LEU 252 -1.61 GLY 112

TYR 236 1.42 THR 253 -1.68 GLY 112

ASN 235 1.60 ILE 254 -1.26 GLY 262

CYS 141 1.60 ILE 255 -1.27 GLY 262

TYR 234 1.81 THR 256 -0.91 GLY 262

TYR 234 1.32 LEU 257 -0.59 GLY 226

TYR 234 1.05 GLU 258 -0.63 LYS 101

TYR 234 0.98 ASP 259 -0.59 ASN 210

HIS 233 0.61 SER 260 -0.82 ASN 210

ASP 228 0.93 SER 261 -1.44 HIS 88

PRO 152 0.71 GLY 262 -1.79 PRO 98

SER 215 1.47 ASN 263 -0.60 GLY 226

MET 160 1.67 LEU 264 -0.84 GLY 226

ASN 235 1.08 LEU 265 -0.98 GLY 226

ASN 235 1.23 GLY 266 -1.02 GLY 226

ASN 235 1.49 ARG 267 -0.80 GLY 226

ASN 235 1.35 ASN 268 -0.94 GLY 262

ASN 235 1.51 SER 269 -1.06 GLY 262

ASN 235 1.09 PHE 270 -1.42 GLY 112

LYS 101 1.63 GLU 271 -1.45 GLY 112

LYS 101 1.34 VAL 272 -1.40 PRO 142

LYS 101 1.19 ARG 273 -1.14 ASP 228

LYS 101 1.05 VAL 274 -1.26 ASP 228

LYS 101 0.91 CYS 275 -1.31 ASP 228

CYS 182 0.91 ALA 276 -1.39 ASP 228

LYS 101 0.89 CYS 277 -1.51 ASP 228

LYS 101 0.97 PRO 278 -1.45 ASP 228

LYS 101 0.88 GLY 279 -1.44 ASP 228

LYS 101 0.93 ARG 280 -1.34 ASP 228

LYS 101 1.04 ASP 281 -1.24 ASP 228

LYS 101 1.08 ARG 282 -1.15 ASP 228

LYS 101 0.98 ARG 283 -1.13 ASP 228

LYS 101 1.10 THR 284 -1.06 ASP 228

LYS 101 1.25 GLU 285 -0.98 ASP 228

LYS 101 1.18 GLU 286 -0.92 ASP 228

LYS 101 1.01 GLU 287 -0.84 ASP 228

LYS 101 1.11 ASN 288 -0.82 ASP 228

LYS 101 1.00 LEU 289 -0.80 ASP 228

LYS 101 0.86 ARG 290 -0.70 ASP 228

LYS 101 0.51 LYS 291 -0.66 ASP 228

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 2503091518343888681

--- normal mode 24 ---

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

* *