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

* *

CA distance fluctuations for 2503091509563839815

--- normal mode 20 ---

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 263 0.88 HIS 88 -0.67 LEU 264

ASN 263 0.86 HIS 89 -0.54 LEU 264

ASN 263 0.99 HIS 90 -0.50 LEU 264

ASN 263 0.99 HIS 91 -0.41 GLN 104

ASN 263 1.05 HIS 92 -0.38 GLN 104

ASN 263 1.02 HIS 93 -0.41 GLN 104

ASN 263 1.00 SER 94 -0.48 GLN 104

ASN 263 0.79 SER 95 -0.55 THR 155

ASN 263 0.84 SER 96 -0.54 GLN 104

THR 256 0.95 VAL 97 -0.55 GLN 104

ASN 263 0.95 PRO 98 -0.69 GLN 104

ASN 263 0.75 SER 99 -0.68 TYR 103

THR 256 0.83 GLN 100 -0.58 GLY 262

ASN 263 0.56 LYS 101 -0.75 GLY 262

VAL 157 0.63 THR 102 -0.75 GLY 262

GLY 105 1.11 TYR 103 -1.12 GLY 262

ASP 148 0.42 GLN 104 -1.53 GLY 262

TYR 103 1.11 GLY 105 -1.58 LEU 265

GLY 266 0.55 SER 106 -1.00 THR 256

GLY 154 0.63 TYR 107 -1.15 THR 256

ASP 148 1.32 GLY 108 -1.13 GLY 262

GLY 105 1.06 PHE 109 -0.83 GLY 262

TYR 103 0.76 ARG 110 -0.65 GLY 262

LEU 257 0.80 LEU 111 -0.53 GLY 262

LEU 257 0.96 GLY 112 -0.42 GLY 262

ILE 255 1.12 PHE 113 -0.42 GLY 266

LEU 257 1.05 LEU 114 -0.48 LEU 264

LEU 257 1.23 HIS 115 -0.40 LEU 264

LEU 257 1.42 SER 116 -0.32 LEU 264

LEU 257 1.31 GLY 117 -0.36 LEU 264

LEU 257 1.24 THR 118 -0.36 LEU 264

LEU 257 1.10 ALA 119 -0.43 LEU 264

LEU 257 0.99 LYS 120 -0.47 LEU 264

LEU 257 0.91 SER 121 -0.56 LEU 264

LEU 257 0.98 VAL 122 -0.55 LEU 264

LEU 257 0.87 THR 123 -0.63 LEU 264

ILE 255 1.01 CYS 124 -0.58 LEU 264

LEU 257 1.17 THR 125 -0.45 LEU 264

LEU 257 1.31 TYR 126 -0.32 LEU 264

LEU 257 1.53 SER 127 -0.31 GLY 262

LEU 257 1.64 PRO 128 -0.38 GLY 262

LEU 257 1.69 ALA 129 -0.38 GLY 262

LEU 257 1.45 LEU 130 -0.36 GLY 262

LEU 257 1.32 ASN 131 -0.39 GLY 262

LEU 257 1.22 LYS 132 -0.32 GLY 262

ILE 255 1.27 MET 133 -0.35 LEU 264

LEU 257 1.06 PHE 134 -0.41 LEU 264

ILE 255 0.95 CYS 135 -0.55 LEU 264

ASN 263 0.93 GLN 136 -0.63 LEU 264

ASN 263 1.00 LEU 137 -0.71 LEU 264

ASN 263 1.02 ALA 138 -0.85 LEU 264

ASN 263 0.93 LYS 139 -0.83 LEU 264

ASN 263 0.89 THR 140 -0.87 LEU 264

ILE 255 1.02 CYS 141 -0.73 LEU 264

ILE 255 1.00 PRO 142 -0.74 GLY 266

ILE 255 1.09 VAL 143 -0.76 GLY 266

THR 155 0.82 GLN 144 -0.72 GLY 266

THR 155 0.64 LEU 145 -0.78 GLY 266

THR 155 0.62 TRP 146 -0.58 THR 256

GLY 108 0.76 VAL 147 -0.88 THR 256

GLY 108 1.32 ASP 148 -0.89 THR 256

GLY 108 0.65 SER 149 -1.12 THR 256

GLY 154 0.58 THR 150 -1.25 THR 256

GLY 154 0.82 PRO 151 -1.64 THR 256

GLY 154 0.60 PRO 152 -1.65 THR 256

GLU 221 0.20 PRO 153 -1.51 ARG 156

LEU 265 1.28 GLY 154 -0.69 LEU 257

SER 227 1.23 THR 155 -0.65 ASN 210

VAL 217 1.52 ARG 156 -1.51 PRO 153

LEU 265 1.10 VAL 157 -1.40 PRO 219

ASN 263 1.17 ARG 158 -1.38 GLY 266

ASN 263 1.33 ALA 159 -0.94 GLY 266

ASN 263 1.64 MET 160 -0.63 GLY 266

ASN 263 1.60 ALA 161 -0.47 GLN 104

THR 256 1.73 ILE 162 -0.45 GLN 104

THR 256 1.41 TYR 163 -0.32 GLN 104

THR 256 1.23 LYS 164 -0.26 GLN 104

THR 256 1.06 GLN 165 -0.23 GLN 104

GLU 258 1.01 SER 166 -0.28 TYR 103

GLU 258 1.08 GLN 167 -0.26 GLN 104

THR 256 1.06 HIS 168 -0.31 GLN 104

THR 256 1.17 MET 169 -0.37 GLN 104

THR 256 1.03 THR 170 -0.41 GLN 104

ASN 263 1.12 GLU 171 -0.39 GLN 104

ASN 263 1.31 VAL 172 -0.44 GLN 104

ASN 263 1.43 VAL 173 -0.41 LEU 264

ASN 263 1.37 ARG 174 -0.56 LEU 264

ASN 263 1.24 ARG 175 -0.65 LEU 264

ASN 263 1.10 CYS 176 -0.59 LEU 264

ASN 263 1.01 PRO 177 -0.63 LEU 264

ASP 259 1.06 HIS 178 -0.69 LEU 264

ASN 263 1.04 HIS 179 -0.77 LEU 264

ASN 263 1.07 GLU 180 -0.79 LEU 264

ASP 259 1.00 ARG 181 -0.82 LEU 264

ASP 259 1.04 CYS 182 -0.88 LEU 264

ASP 259 0.97 SER 183 -1.01 LEU 264

ASN 263 0.94 ASP 184 -1.05 LEU 264

ASN 263 0.96 SER 185 -1.16 LEU 264

ASN 263 0.89 ASP 186 -1.31 LEU 264

ASN 263 0.84 GLY 187 -1.40 LEU 264

ASN 263 0.91 LEU 188 -1.39 LEU 264

ASN 263 1.09 ALA 189 -1.18 LEU 264

ASN 263 1.11 PRO 190 -1.05 LEU 264

ASN 263 1.11 PRO 191 -0.95 LEU 264

ASN 263 1.24 GLN 192 -0.79 LEU 264

ASN 263 1.41 HIS 193 -0.82 LEU 264

ASN 263 1.43 LEU 194 -0.73 LEU 264

ASN 263 1.44 ILE 195 -0.79 LEU 264

ASN 263 1.24 ARG 196 -0.99 LEU 264

ASN 263 1.06 VAL 197 -1.08 LEU 264

ASN 263 0.90 GLU 198 -1.21 LEU 264

THR 155 0.82 GLY 199 -1.34 LEU 264

ASN 263 0.71 ASN 200 -1.40 LEU 264

ASN 263 0.65 LEU 201 -1.62 LEU 264

ASN 263 0.62 ARG 202 -1.43 LEU 264

ASN 263 0.84 VAL 203 -1.29 LEU 264

ASN 263 0.92 GLU 204 -1.15 LEU 264

ASN 263 1.15 TYR 205 -1.01 LEU 264

ASN 263 1.18 LEU 206 -0.81 LEU 264

ASN 263 1.20 ASP 207 -0.69 LEU 264

ASN 263 1.06 ASP 208 -0.59 GLN 104

ASN 263 0.85 ARG 209 -0.54 THR 155

ASN 263 0.77 ASN 210 -0.65 THR 155

ASN 263 0.97 THR 211 -0.59 ILE 255

ASN 263 1.13 PHE 212 -0.52 GLN 104

ASN 263 1.39 ARG 213 -0.57 GLN 104

ASN 263 1.59 HIS 214 -0.61 GLY 266

ASN 263 1.60 SER 215 -0.80 GLY 266

ASN 263 1.34 VAL 216 -1.05 GLY 266

ARG 156 1.52 VAL 217 -1.38 GLY 266

ARG 156 0.84 VAL 218 -1.46 GLY 266

LEU 265 0.74 PRO 219 -1.43 GLY 266

LEU 265 1.31 TYR 220 -1.02 GLY 266

LEU 265 1.00 GLU 221 -0.82 LEU 264

THR 155 0.69 PRO 222 -0.90 THR 256

THR 155 0.95 PRO 223 -0.70 THR 256

THR 155 1.13 GLU 224 -0.74 LEU 264

THR 155 1.11 VAL 225 -0.63 LEU 264

THR 155 1.22 GLY 226 -0.55 LEU 264

THR 155 1.23 SER 227 -0.57 LEU 264

THR 155 1.02 ASP 228 -0.55 THR 256

THR 155 0.95 CYS 229 -0.60 GLY 266

THR 155 0.95 THR 230 -0.85 GLY 266

THR 155 0.94 THR 231 -0.91 GLY 266

ASN 263 0.78 ILE 232 -1.11 GLY 266

ASN 263 0.87 HIS 233 -0.95 GLY 266

ASN 263 1.07 TYR 234 -0.89 GLY 266

ASN 263 1.12 ASN 235 -0.87 LEU 264

ASN 263 1.21 CYS 236 -0.74 LEU 264

ASN 263 1.18 MET 237 -0.80 LEU 264

ASN 263 1.15 CYS 238 -0.66 LEU 264

ASN 263 1.07 ASN 239 -0.55 LEU 264

ASN 263 1.07 ASN 239 -0.55 LEU 264

ASN 263 1.01 SER 240 -0.42 LEU 264

ASN 263 1.07 SER 240 -0.42 LEU 264

ASP 259 1.00 SER 241 -0.45 LEU 264

ASN 263 0.99 SER 241 -0.41 LEU 264

ASP 259 1.00 CYS 242 -0.51 LEU 264

ASN 263 1.02 CYS 242 -0.49 LEU 264

ASP 259 1.03 MET 243 -0.46 LEU 264

ASP 259 1.00 MET 243 -0.43 LEU 264

ASN 263 1.01 GLY 244 -0.44 LEU 264

ASN 263 1.01 GLY 244 -0.45 LEU 264

ASN 263 1.14 GLY 245 -0.47 LEU 264

ASN 263 1.14 GLY 245 -0.47 LEU 264

ASN 263 1.16 MET 246 -0.38 LEU 264

ASN 263 1.16 MET 246 -0.38 LEU 264

ASN 263 1.03 ASN 247 -0.34 LEU 264

ASN 263 0.98 ARG 248 -0.30 LEU 264

ASN 263 1.02 ARG 249 -0.22 LEU 264

THR 256 1.10 PRO 250 -0.21 GLN 104

THR 256 1.34 ILE 251 -0.28 GLN 104

THR 256 1.37 LEU 252 -0.33 GLN 104

ASN 263 1.27 THR 253 -0.49 GLY 266

ASN 263 1.16 ILE 254 -0.71 GLN 104

MET 133 1.27 ILE 255 -1.25 SER 261

ILE 162 1.73 THR 256 -1.65 PRO 152

ALA 129 1.69 LEU 257 -0.80 SER 261

GLN 167 1.08 GLU 258 -0.40 PRO 153

HIS 178 1.06 ASP 259 -0.16 SER 106

GLU 204 0.72 SER 260 -1.35 THR 256

GLU 221 0.29 SER 261 -1.25 ILE 255

LEU 206 0.64 GLY 262 -1.53 GLN 104

MET 160 1.64 ASN 263 -0.62 THR 155

LYS 101 0.29 LEU 264 -1.62 LEU 201

TYR 220 1.31 LEU 265 -1.58 GLY 105

TYR 103 0.60 GLY 266 -1.46 VAL 218

VAL 157 0.79 ARG 267 -0.85 GLN 104

VAL 157 0.88 ASN 268 -0.62 GLY 262

ASN 263 0.90 SER 269 -0.53 GLY 262

ASN 263 0.95 PHE 270 -0.41 GLY 262

ASN 263 0.96 GLU 271 -0.35 GLY 262

ASN 263 1.07 VAL 272 -0.34 GLY 266

ASN 263 1.00 ARG 273 -0.37 LEU 264

ASN 263 1.03 VAL 274 -0.50 LEU 264

ASN 263 0.92 CYS 275 -0.48 LEU 264

ASP 259 0.95 ALA 276 -0.52 LEU 264

LEU 257 0.94 CYS 277 -0.45 LEU 264

LEU 257 1.04 PRO 278 -0.43 LEU 264

LEU 257 1.15 GLY 279 -0.38 LEU 264

LEU 257 1.13 ARG 280 -0.32 LEU 264

LEU 257 1.14 ASP 281 -0.28 LEU 264

LEU 257 1.30 ARG 282 -0.24 LEU 264

LEU 257 1.35 ARG 283 -0.21 GLY 262

LEU 257 1.25 THR 284 -0.20 GLY 262

LEU 257 1.29 GLU 285 -0.23 GLY 262

LEU 257 1.47 GLU 286 -0.27 GLY 262

LEU 257 1.37 GLU 287 -0.25 GLY 262

LEU 257 1.26 ASN 288 -0.25 GLY 262

LEU 257 1.37 LEU 289 -0.29 GLY 262

LEU 257 1.39 ARG 290 -0.30 GLY 262

LEU 257 1.24 LYS 291 -0.28 GLY 262

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 20 ---

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

* *