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

* *

CA distance fluctuations for 2503091509563839815

--- normal mode 19 ---

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 289 0.83 HIS 88 -0.35 LYS 291

LEU 289 0.73 HIS 89 -0.36 LYS 291

LEU 289 0.71 HIS 90 -0.36 LYS 291

LEU 289 0.62 HIS 91 -0.41 LYS 291

LEU 289 0.57 HIS 92 -0.37 LYS 291

LEU 289 0.49 HIS 93 -0.45 LYS 291

LEU 289 0.47 SER 94 -0.54 LYS 291

ARG 290 0.39 SER 95 -0.62 LYS 291

LEU 289 0.38 SER 96 -0.66 LYS 291

LEU 289 0.37 VAL 97 -0.63 LYS 291

LEU 289 0.41 PRO 98 -0.67 LYS 291

LEU 289 0.33 SER 99 -0.71 LYS 291

LEU 289 0.35 GLN 100 -0.75 ASN 288

LEU 289 0.25 LYS 101 -0.78 ASN 288

LEU 289 0.29 THR 102 -0.80 ASN 288

LEU 289 0.31 TYR 103 -0.82 LYS 291

LEU 289 0.36 GLN 104 -0.82 LYS 291

LEU 289 0.35 GLY 105 -0.92 LYS 291

LEU 289 0.37 SER 106 -0.97 LYS 291

LEU 289 0.46 TYR 107 -0.87 LYS 291

LEU 289 0.41 GLY 108 -0.82 LYS 291

LEU 289 0.50 PHE 109 -0.74 LYS 291

LEU 289 0.50 ARG 110 -0.68 ASN 288

LEU 289 0.59 LEU 111 -0.69 ASN 288

LEU 289 0.64 GLY 112 -0.60 ASN 288

PRO 142 0.96 PHE 113 -0.59 ASN 288

PRO 142 0.85 LEU 114 -0.59 ARG 290

LEU 289 0.71 HIS 115 -0.57 ARG 290

LEU 289 0.60 SER 116 -0.53 GLU 285

LEU 289 0.65 GLY 117 -0.48 ARG 290

LEU 289 0.64 THR 118 -0.48 GLU 285

LEU 289 0.74 ALA 119 -0.35 GLU 285

LEU 289 0.81 LYS 120 -0.30 GLU 285

LEU 289 0.96 SER 121 -0.31 VAL 197

LEU 289 0.93 VAL 122 -0.41 GLU 285

LEU 289 1.03 THR 123 -0.42 GLU 285

HIS 233 0.95 CYS 124 -0.65 THR 140

LEU 289 0.77 THR 125 -0.63 GLU 285

LEU 289 0.62 TYR 126 -0.70 CYS 141

PRO 142 0.48 SER 127 -0.85 ASN 288

PRO 142 0.37 PRO 128 -0.94 ASN 288

PRO 142 0.30 ALA 129 -1.17 ASN 288

PRO 142 0.30 LEU 130 -1.37 ASN 288

LEU 289 0.37 ASN 131 -1.15 ASN 288

LEU 289 0.48 LYS 132 -0.93 ASN 288

LEU 289 0.65 MET 133 -0.95 CYS 141

LEU 289 0.71 PHE 134 -0.73 CYS 141

LEU 289 0.89 CYS 135 -0.55 CYS 141

LEU 289 1.00 GLN 136 -0.47 VAL 197

LEU 289 1.08 LEU 137 -0.51 VAL 197

LEU 289 1.23 ALA 138 -0.84 VAL 197

LEU 289 1.21 LYS 139 -0.76 VAL 197

LEU 289 1.32 THR 140 -0.74 PRO 142

HIS 233 1.32 CYS 141 -0.95 MET 133

PHE 113 0.96 PRO 142 -1.08 GLU 198

LEU 289 0.83 VAL 143 -0.69 THR 140

LEU 289 0.79 GLN 144 -0.53 ASN 288

LEU 289 0.73 LEU 145 -0.63 ILE 232

LEU 289 0.62 TRP 146 -0.61 LYS 291

LEU 289 0.56 VAL 147 -0.72 LYS 291

LEU 289 0.47 ASP 148 -0.78 LYS 291

LEU 289 0.52 SER 149 -0.82 LYS 291

LEU 289 0.62 THR 150 -0.79 LYS 291

LEU 289 0.62 PRO 151 -0.82 LYS 291

LEU 289 0.64 PRO 152 -0.85 LYS 291

LEU 289 0.74 PRO 153 -0.78 LYS 291

LEU 289 0.77 GLY 154 -0.75 LYS 291

LEU 289 0.73 THR 155 -0.75 LYS 291

LEU 289 0.79 ARG 156 -0.78 HIS 233

LEU 289 0.80 VAL 157 -0.85 HIS 233

LEU 289 0.78 ARG 158 -0.70 HIS 233

LEU 289 0.79 ALA 159 -0.52 ASN 288

LEU 289 0.72 MET 160 -0.52 ASN 288

LEU 289 0.67 ALA 161 -0.53 ASN 288

LEU 289 0.54 ILE 162 -0.54 ASN 288

LEU 289 0.46 TYR 163 -0.52 ASN 288

ARG 290 0.36 LYS 164 -0.66 ASN 288

ARG 290 0.52 GLN 165 -0.54 ASN 288

ARG 290 0.54 SER 166 -0.53 ASN 288

ARG 290 0.66 GLN 167 -0.40 ASN 288

ARG 290 0.57 HIS 168 -0.40 ASN 288

ARG 290 0.46 MET 169 -0.49 ASN 288

ARG 290 0.46 THR 170 -0.49 LYS 291

LEU 289 0.48 GLU 171 -0.40 LYS 291

LEU 289 0.60 VAL 172 -0.41 LYS 291

LEU 289 0.68 VAL 173 -0.38 ASN 288

LEU 289 0.80 ARG 174 -0.31 ASN 288

LEU 289 0.89 ARG 175 -0.25 ASN 288

LEU 289 0.85 CYS 176 -0.21 ARG 196

LEU 289 0.88 PRO 177 -0.18 ARG 196

LEU 289 0.98 HIS 178 -0.24 VAL 197

LEU 289 1.06 HIS 179 -0.30 VAL 197

LEU 289 1.03 GLU 180 -0.22 ARG 196

LEU 289 1.07 ARG 181 -0.22 VAL 197

LEU 289 1.19 CYS 182 -0.30 VAL 197

LEU 289 1.27 SER 183 -0.30 VAL 197

LEU 289 1.34 ASP 184 -0.43 VAL 197

LEU 289 1.32 SER 185 -0.36 VAL 197

LEU 289 1.42 ASP 186 -0.41 VAL 197

LEU 289 1.35 GLY 187 -0.31 PRO 142

LEU 289 1.25 LEU 188 -0.34 PRO 142

LEU 289 1.18 ALA 189 -0.33 PRO 142

LEU 289 1.10 PRO 190 -0.31 LYS 291

LEU 289 1.10 PRO 191 -0.24 LYS 291

LEU 289 0.97 GLN 192 -0.27 LYS 291

LEU 289 0.98 HIS 193 -0.32 ASN 288

LEU 289 0.95 LEU 194 -0.34 ASN 288

LEU 289 0.99 ILE 195 -0.40 ASN 288

LEU 289 1.09 ARG 196 -0.45 CYS 236

LEU 289 1.04 VAL 197 -0.87 ASN 235

LEU 289 1.25 GLU 198 -1.08 PRO 142

LEU 289 1.32 GLY 199 -0.33 PRO 142

LEU 289 1.22 ASN 200 -0.69 HIS 233

LEU 289 1.25 LEU 201 -0.59 HIS 233

LEU 289 1.12 ARG 202 -0.72 HIS 233

LEU 289 1.10 VAL 203 -0.79 HIS 233

LEU 289 1.02 GLU 204 -0.63 HIS 233

LEU 289 0.99 TYR 205 -0.48 HIS 233

LEU 289 0.87 LEU 206 -0.52 LYS 291

LEU 289 0.81 ASP 207 -0.50 LYS 291

LEU 289 0.71 ASP 208 -0.58 LYS 291

LEU 289 0.67 ARG 209 -0.59 LYS 291

LEU 289 0.57 ASN 210 -0.65 LYS 291

LEU 289 0.55 THR 211 -0.61 LYS 291

LEU 289 0.64 PHE 212 -0.53 LYS 291

LEU 289 0.67 ARG 213 -0.52 LYS 291

LEU 289 0.79 HIS 214 -0.47 LYS 291

LEU 289 0.83 SER 215 -0.50 LYS 291

LEU 289 0.93 VAL 216 -0.61 HIS 233

VAL 197 1.02 VAL 217 -0.83 HIS 233

VAL 197 1.03 VAL 218 -1.07 HIS 233

LEU 289 0.92 PRO 219 -0.91 HIS 233

LEU 289 0.85 TYR 220 -1.01 ILE 232

LEU 289 0.91 GLU 221 -0.87 ILE 232

LEU 289 0.82 PRO 222 -0.69 ILE 232

LEU 289 0.84 PRO 223 -0.65 ARG 290

LEU 289 0.90 GLU 224 -0.70 ARG 290

LEU 289 0.83 VAL 225 -0.78 ARG 290

LEU 289 0.78 GLY 226 -0.88 ARG 290

LEU 289 0.81 SER 227 -0.81 ARG 290

LEU 289 0.71 ASP 228 -0.80 ARG 290

LEU 289 0.77 CYS 229 -0.67 ARG 290

LEU 289 0.88 THR 230 -0.57 GLU 198

LEU 289 0.93 THR 231 -0.67 GLU 198

CYS 141 1.31 ILE 232 -1.01 TYR 220

CYS 141 1.32 HIS 233 -1.07 VAL 218

LEU 289 1.11 TYR 234 -0.86 PRO 142

LEU 289 1.14 ASN 235 -0.87 VAL 197

LEU 289 1.01 CYS 236 -0.63 VAL 197

LEU 289 1.09 MET 237 -0.51 VAL 197

LEU 289 0.96 CYS 238 -0.34 VAL 197

LEU 289 0.86 ASN 239 -0.31 VAL 197

LEU 289 0.87 ASN 239 -0.31 VAL 197

LEU 289 0.70 SER 240 -0.30 CYS 141

LEU 289 0.71 SER 240 -0.34 CYS 141

LEU 289 0.74 SER 241 -0.24 VAL 197

LEU 289 0.68 SER 241 -0.25 CYS 141

LEU 289 0.81 CYS 242 -0.24 VAL 197

LEU 289 0.78 CYS 242 -0.22 VAL 197

LEU 289 0.74 MET 243 -0.19 VAL 197

LEU 289 0.70 MET 243 -0.17 VAL 197

LEU 289 0.70 GLY 244 -0.15 VAL 197

LEU 289 0.70 GLY 244 -0.15 VAL 197

LEU 289 0.72 GLY 245 -0.22 ASN 288

LEU 289 0.73 GLY 245 -0.21 ASN 288

LEU 289 0.65 MET 246 -0.28 ASN 288

LEU 289 0.65 MET 246 -0.28 ASN 288

LEU 289 0.60 ASN 247 -0.22 CYS 141

LEU 289 0.55 ARG 248 -0.28 CYS 141

ARG 290 0.51 ARG 249 -0.32 CYS 141

LEU 289 0.47 PRO 250 -0.48 ASN 288

LEU 289 0.54 ILE 251 -0.57 ASN 288

LEU 289 0.52 LEU 252 -0.71 ASN 288

LEU 289 0.64 THR 253 -0.65 ASN 288

LEU 289 0.58 ILE 254 -0.67 ASN 288

LEU 289 0.65 ILE 255 -0.63 ASN 288

LEU 289 0.61 THR 256 -0.67 LYS 291

LEU 289 0.63 LEU 257 -0.72 LYS 291

LEU 289 0.62 GLU 258 -0.78 LYS 291

LEU 289 0.63 ASP 259 -0.83 LYS 291

LEU 289 0.69 SER 260 -0.81 LYS 291

LEU 289 0.61 SER 261 -0.87 LYS 291

LEU 289 0.61 GLY 262 -0.82 LYS 291

LEU 289 0.51 ASN 263 -0.89 LYS 291

LEU 289 0.49 LEU 264 -0.87 LYS 291

LEU 289 0.49 LEU 265 -0.87 LYS 291

LEU 289 0.47 GLY 266 -0.80 LYS 291

LEU 289 0.47 ARG 267 -0.72 LYS 291

LEU 289 0.47 ASN 268 -0.77 ASN 288

LEU 289 0.48 SER 269 -0.82 ASN 288

LEU 289 0.50 PHE 270 -0.89 ASN 288

LEU 289 0.49 GLU 271 -0.85 ASN 288

LEU 289 0.63 VAL 272 -0.72 CYS 141

LEU 289 0.65 ARG 273 -0.59 CYS 141

LEU 289 0.81 VAL 274 -0.47 CYS 141

LEU 289 0.80 CYS 275 -0.34 CYS 141

LEU 289 0.86 ALA 276 -0.33 VAL 197

LEU 289 0.78 CYS 277 -0.34 GLU 285

LEU 289 0.74 PRO 278 -0.55 GLU 285

LEU 289 0.67 GLY 279 -0.54 GLU 285

LEU 289 0.56 ARG 280 -0.36 GLU 285

LEU 289 0.51 ASP 281 -0.52 GLU 285

LEU 289 0.47 ARG 282 -1.18 GLU 285

LEU 289 0.39 ARG 283 -0.49 GLU 285

LEU 289 0.29 THR 284 -0.39 CYS 141

GLU 287 0.27 GLU 285 -1.18 ARG 282

HIS 233 0.26 GLU 286 -0.42 ASN 288

GLU 285 0.27 GLU 287 -0.33 CYS 141

THR 284 0.25 ASN 288 -1.37 LEU 130

ASP 186 1.42 LEU 289 -0.14 LYS 291

GLN 167 0.66 ARG 290 -0.88 GLY 226

LYS 120 0.20 LYS 291 -0.97 SER 106

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 2503091509563839815

--- normal mode 19 ---

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

* *